|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
45-149 |
1.87e-76 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 249.24 E-value: 1.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 45 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 124
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 41322914 125 RNDDIADGNPKLTLGLIWTIILHFQ 149
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
42-160 |
1.41e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 241.47 E-value: 1.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 121
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322914 122 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 160
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
42-158 |
6.00e-72 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 237.19 E-value: 6.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 121
Cdd:cd21236 12 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKL 91
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322914 122 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 158
Cdd:cd21236 92 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
162-267 |
7.10e-72 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 236.07 E-value: 7.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 162 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 241
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 41322914 242 PEDVDVPQPDEKSIITYVSSLYDAMP 267
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
163-267 |
2.67e-66 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 220.34 E-value: 2.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 242
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 41322914 243 EDVDVPQPDEKSIITYVSSLYDAMP 267
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
42-159 |
1.72e-63 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 212.59 E-value: 1.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 121
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 41322914 122 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 159
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
163-267 |
3.01e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.43 E-value: 3.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 242
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 41322914 243 EDVDVPQPDEKSIITYVSSLYDAMP 267
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
161-267 |
1.70e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 177.93 E-value: 1.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 161 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 240
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 41322914 241 DPEDVDVPQPDEKSIITYVSSLYDAMP 267
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
47-150 |
1.20e-50 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 175.65 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 47 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 125
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 41322914 126 NDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
42-146 |
1.16e-47 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 167.54 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 120
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 41322914 121 LVNIRNDDIADGNPKLTLGLIWTIIL 146
Cdd:cd21246 91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
163-263 |
9.06e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 161.43 E-value: 9.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 242
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 41322914 243 EDVDVPQPDEKSIITYVSSLY 263
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
46-263 |
4.04e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 175.90 E-value: 4.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 46 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 122
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLFNAII 201
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 202 HRHKPLLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLY 263
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
43-150 |
2.19e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.92 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 43 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 118
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 41322914 119 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
163-263 |
6.17e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 6.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 242
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 41322914 243 EDVDVPQPDEKSIITYVSSLY 263
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
42-146 |
7.39e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 156.30 E-value: 7.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLrHRQVK 120
Cdd:cd21193 11 EERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKVR 89
|
90 100
....*....|....*....|....*.
gi 41322914 121 LVNIRNDDIADGNPKLTLGLIWTIIL 146
Cdd:cd21193 90 LENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
43-150 |
7.64e-44 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 156.19 E-value: 7.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 43 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 115
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 41322914 116 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
162-267 |
3.51e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 148.62 E-value: 3.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 162 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 241
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 41322914 242 PEDVDVPQPDEKSIITYVSSLYDAMP 267
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
150-265 |
7.16e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 147.89 E-value: 7.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 150 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 229
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322914 230 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 265
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1318-1897 |
3.12e-40 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 164.72 E-value: 3.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1318 QEYVDLRTHYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ---LAEAHAQAKAQAERE 1393
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1394 AKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG 1473
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL----EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1474 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAE 1553
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1554 RRLR--QAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQeehvavAQLREEAERRAQQQAEAERAREEA 1631
Cdd:COG1196 449 EEEAelEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE------AEADYEGFLEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1632 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1711
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1712 RLAAEQELIRLRAETEQGEqqrqLLEEELARLQREAAAATQKRqeLEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ 1791
Cdd:COG1196 603 LVASDLREADARYYVLGDT----LLGRTLVAARLEAALRRAVT--LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1792 RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 1871
Cdd:COG1196 677 AEAELE----ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
570 580
....*....|....*....|....*.
gi 41322914 1872 RLAEDEAFQRRRLEEQAAQHKADIEE 1897
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
42-146 |
5.13e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 146.32 E-value: 5.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 120
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 41322914 121 LVNIRNDDIADGNPKLTLGLIWTIIL 146
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
42-146 |
5.73e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 143.27 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 120
Cdd:cd21317 26 DEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKVH 105
|
90 100
....*....|....*....|....*.
gi 41322914 121 LVNIRNDDIADGNPKLTLGLIWTIIL 146
Cdd:cd21317 106 LENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
45-146 |
9.92e-39 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 141.37 E-value: 9.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 45 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 123
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 41322914 124 IRNDDIADGNPKLTLGLIWTIIL 146
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
43-150 |
1.18e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 141.51 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 43 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 120
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 41322914 121 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
159-263 |
1.83e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.91 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 159 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 238
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 41322914 239 LLDPEDVDVPQPDEKSIITYVSSLY 263
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
47-148 |
1.90e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.61 E-value: 1.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 47 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 124
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 41322914 125 RNDDIADGNPKLTLGLIWTIILHF 148
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
159-263 |
6.72e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.42 E-value: 6.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 159 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 238
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 41322914 239 LLDPEDVDVPQPDEKSIITYVSSLY 263
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1355-1977 |
1.01e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 156.64 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1355 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAKELQQRMQEevvRREEAAVdaqQQKRSIQEELQQLrqss 1433
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELKEELKE---LEAELLL---LKLRELEAELEEL---- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1434 EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEAterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1513
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEE-------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1514 KRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALEtaQRSAEAELQSKRASFAEKT 1593
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1594 AQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEA 1673
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1674 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQREAAAA 1750
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1751 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAkRQRQLAEEDAAR 1830
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL-LGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1831 QRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSEL 1910
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1911 ERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSnaEDTLRsKEQAELEAARQR 1977
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD--LEELE-RELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1685-2253 |
3.18e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 155.09 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1764
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1765 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEE---DAARQRAEAERVLAE 1841
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEeleEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1842 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKgLVEDTL 1921
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1922 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE 2001
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2002 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2076
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2077 QSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQA 2156
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2157 EQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFS 2236
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 41322914 2237 VRVQMEELSKLKARIEA 2253
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
162-263 |
3.54e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 137.30 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 162 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 241
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 41322914 242 PEDVDVPQPDEKSIITYVSSLY 263
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
42-150 |
8.82e-37 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 136.21 E-value: 8.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 120
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 41322914 121 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1445-2053 |
2.15e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.40 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1445 EAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASR 1524
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1525 VKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEH 1604
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1605 VAVAQLreeaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE 1684
Cdd:COG1196 341 ELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1764
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1765 RAEMEVLLAskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL--AEEAKRQRQLAEEDAARQRAEAERVLAEK 1842
Cdd:COG1196 490 AARLLLLLE--AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1843 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLR 1922
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1923 QRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEE 2002
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 41322914 2003 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2053
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1482-2117 |
3.98e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 151.63 E-value: 3.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1482 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQRKRqaevelasrVKAEAEAAREKQRALQALEE-------LRLQAEE 1551
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAERYRELKEELKEleaelllLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1552 AERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEA 1631
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1632 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1711
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-----------AELAEAEEALLEAEAELAEAEEELEELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1712 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ 1791
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1792 RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAiGEATRLKTEAEIALKEKEAENERLR 1871
Cdd:COG1196 468 LLEEAA----LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA-GLRGLAGAVAVLIGVEAAYEAALEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1872 RLAEDEAFQRRRLEEQAAQhkadIEERLAQLRkasdseLERQKGLVEDTLRQRRQVEEEILALKASFekAAAGKAELELE 1951
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAA----AIEYLKAAK------AGRATFLPLDKIRARAALAAALARGAIGA--AVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1952 LGRIRSNAEDTL--RSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2029
Cdd:COG1196 611 ADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2030 ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAA 2109
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
....*...
gi 41322914 2110 QSRRQVEE 2117
Cdd:COG1196 771 RLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1343-2055 |
8.77e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 151.45 E-value: 8.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1422
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1423 Q----EELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEATERQRGGAEGELQALRA--RAEEAEAQKRQA 1496
Cdd:PTZ00121 1192 ElrkaEDARKAEAARKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeEARMAHFARRQA 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1497 QEEAERLRRQVQ-DESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEvERARQVQVALETAQ 1575
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK-KKAEEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1576 rsAEAELQSKRASFAEKTAQLERSLQEEHvavaqlreeaerraqqqaeaerareeaerelerwQLKANEAlrlRLQAEEV 1655
Cdd:PTZ00121 1350 --AEAEAAADEAEAAEEKAEAAEKKKEEA----------------------------------KKKADAA---KKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1656 AQQKSLAQaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQ 1734
Cdd:PTZ00121 1391 KKADEAKK------------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1735 LLEEelarlQREAAAATQKRQEL-EAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEaEAGRFRELAEEAARLRAl 1813
Cdd:PTZ00121 1452 KAEE-----AKKAEEAKKKAEEAkKADEAKKKAE-------EAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK- 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1814 AEEAKRQRQLAEEDAARQRAEA----ERVLAEKLAAIGEATRL--KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1887
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAkkaeEKKKADELKKAEELKKAeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1888 AAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRrqveEEILALKASFEKAAAGKAELELELGRIRS-----NAEDT 1962
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1963 LRSKEQA--ELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQES 2036
Cdd:PTZ00121 1674 KKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDE 1753
|
730
....*....|....*....
gi 41322914 2037 ARQLQLAQEAAQKRLQAEE 2055
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEE 1772
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
166-267 |
1.18e-35 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 132.55 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 166 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 244
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 41322914 245 VDVPQPDEKSIITYVSSLYDAMP 267
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
147-263 |
4.02e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 132.10 E-value: 4.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 147 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQA 226
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322914 227 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 263
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
46-151 |
7.27e-34 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 128.34 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 46 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 122
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHFQIS 151
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1709-2341 |
7.59e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.92 E-value: 7.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1709 AQQRL-AAEQELIRLRAETEQgeqqrqlLEEELARLQREAAAAtQKRQELEAELAKVRAEMEVLLASKARAEEEsrstse 1787
Cdd:COG1196 177 AERKLeATEENLERLEDILGE-------LERQLEPLERQAEKA-ERYRELKEELKELEAELLLLKLRELEAELE------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1788 kskqrleaeagrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1867
Cdd:COG1196 243 --------------ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1868 ERLRRLAEDEA---FQRRRLEEQAAQHKADIEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAG 1944
Cdd:COG1196 309 ERRRELEERLEeleEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1945 KAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE 2024
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2025 ARRLRERAEQESARQLQLAQEAAQKR---LQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEAR 2101
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLlllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2102 VQA---------------EREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQA 2166
Cdd:COG1196 548 LQNivveddevaaaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2167 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSK 2246
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2247 LKARIEAENRALILRDKDNTQRFLQEEAEKMKQvAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK----MQA 2322
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnLLA 786
|
650
....*....|....*....
gi 41322914 2323 VQEATRLKAEAELLQQQKE 2341
Cdd:COG1196 787 IEEYEELEERYDFLSEQRE 805
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
47-150 |
6.04e-33 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 125.09 E-value: 6.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 47 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 124
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 41322914 125 RNDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
162-260 |
1.50e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 123.69 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 162 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 241
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 41322914 242 PEDVDVPQPDEKSIITYVS 260
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
47-150 |
1.72e-32 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 123.58 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 47 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 125
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 41322914 126 NDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
163-263 |
1.87e-32 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 123.67 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 242
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 41322914 243 EDVDVPQPDEKSIITYVSSLY 263
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
42-146 |
4.88e-32 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 124.39 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 120
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 41322914 121 LVNIRNDDIADGNPKLTLGLIWTIIL 146
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
150-265 |
3.30e-31 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 120.33 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 150 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 229
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322914 230 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 265
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
166-267 |
5.25e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 119.29 E-value: 5.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 166 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 244
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 41322914 245 VDVPQPDEKSIITYVSSLYDAMP 267
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
166-268 |
1.41e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.49 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 166 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 243
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 41322914 244 DVDVPQPDEKSIITYVSSLYDAMPR 268
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
162-260 |
1.66e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.01 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 162 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 241
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 41322914 242 PEDVDVPQPDEKSIITYVS 260
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
43-152 |
1.86e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 118.07 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 43 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 118
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 41322914 119 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 152
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
168-263 |
4.16e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 116.68 E-value: 4.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 168 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 246
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 41322914 247 VPQPDEKSIITYVSSLY 263
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
46-148 |
4.99e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 116.81 E-value: 4.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 46 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHF 148
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
898-975 |
1.27e-29 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 114.24 E-value: 1.27e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 898 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 975
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1681-2464 |
2.58e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 130.26 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1681 GKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1760
Cdd:PTZ00121 1098 GKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEE--ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1761 LAKvRAEmevllasKARAEEESRSTSEKSKqrleaeagrfrelAEEAARlralAEEAKRQRQLAEEDAARQRAEAERvlA 1840
Cdd:PTZ00121 1174 DAK-KAE-------AARKAEEVRKAEELRK-------------AEDARK----AEAARKAEEERKAEEARKAEDAKK--A 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1841 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRleeqaAQHKADIEERLAQLRKASdselERQKGLVEDT 1920
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ-----AAIKAEEARKADELKKAE----EKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1921 LRQRRQVEEeilalkasfekaAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAA 2000
Cdd:PTZ00121 1298 AEEKKKADE------------AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2001 EEEAARQRKAALEEVERLKAKVEEARR---LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2077
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2078 SvlDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQsaeeqaqaraqaqaaaekLRKEAEQEAARRAQAE 2157
Cdd:PTZ00121 1446 A--DEAK--KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE------------------AKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2158 QAALRQKQAADAEMEKHKKFAEQTlrQKAQVEQELTTLRLQLEETDHQKNLLDEELQrlKAEATEAARQRSQVEEELFSV 2237
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2238 RVQMEELSKL-KARIEAENRALILRDKDNTQRFLQEEAEKMKqvAEEAARlsvaAQEAARLRQLAEEDLAQQRALAEKML 2316
Cdd:PTZ00121 1580 LRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2317 KEKMQAVQEATRLKAEAEllqQQKELAQEqARRLQEDKEQMAQQLAEETQgfqrtlEAERQRQLEMSAEAERLKlrVAEM 2396
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAE---EDKKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKK--AEEL 1721
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2397 SRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvTLVQTLEIQRQQSDHDAERLREAIAELEREKE 2464
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
148-265 |
4.56e-29 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 114.41 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 148 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAF 227
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322914 228 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 265
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1318-2031 |
1.47e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.09 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1318 QEYVDLRTHYSELT-TLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqAKAQAEREAKE 1396
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1397 LQQRMQEEVVRREeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1476
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1477 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1556
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1557 RQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL- 1635
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1636 ---------------ERWQLKANEALRLRLQA----------EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQ 1690
Cdd:TIGR02168 518 lsgilgvlselisvdEGYEAAIEAALGGRLQAvvvenlnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1691 RELA------------------------------EQELEKQRQL-----------------------AEGTAQQRLAAEQ 1717
Cdd:TIGR02168 598 EGFLgvakdlvkfdpklrkalsyllggvlvvddlDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1718 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRL 1793
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1794 EAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAeialKEKEAENERLRRL 1873
Cdd:TIGR02168 758 ELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1874 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAGKAELELELG 1953
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1954 RIRSNAE--DTLRSKEQAELEAARQR------QLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK----AK 2021
Cdd:TIGR02168 912 ELRRELEelREKLAQLELRLEGLEVRidnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAA 991
|
810
....*....|
gi 41322914 2022 VEEARRLRER 2031
Cdd:TIGR02168 992 IEEYEELKER 1001
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
166-265 |
3.20e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.22 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 166 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 244
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 41322914 245 VDVPQPDEKSIITYVSSLYDA 265
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1542-2172 |
3.34e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.82 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1542 LEELRLQAEEAERRLRQAEVERARQVQVALeTAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLreeaerraqqq 1621
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAEL----------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1622 aeaerareeaerelerwqlkanEALRLRLQAEEvaqqkslaqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQ 1701
Cdd:COG1196 270 ----------------------EELRLELEELE---------------------------LELEEAQAEEYELLAELARL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1702 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmevLLASKARAEEE 1781
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1782 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1861
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1862 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKA 1941
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1942 AAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAK 2021
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2022 VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEAR 2101
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322914 2102 VQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEME 2172
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1110-1820 |
4.57e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 4.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1110 RAHEEQLKEAQAVpATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLl 1189
Cdd:COG1196 216 RELKEELKELEAE-LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1190 erwqavlaqtdvrQRELEQLGRQLRYYRESadplgawLQDARRRQEQIQAmpladsqavreqlrQEQALLEEIERHGEKV 1269
Cdd:COG1196 294 -------------LAELARLEQDIARLEER-------RRELEERLEELEE--------------ELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1270 EECQrfakqyinaikdyelqlvtykaqlepvaspakkpkvqsgsesviqeyvdlrthyselttltsqyikfisETLRRME 1349
Cdd:COG1196 340 EELE---------------------------------------------------------------------EELEEAE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1350 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmQEEVVRREEAAVDAQQQKRSIQEELQQL 1429
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1430 RQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRrqvQD 1509
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE---GF 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1510 ESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASF 1589
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1590 AEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA----NEALRLRLQAEEVAQQKSLAQAE 1665
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGS 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1666 AEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR 1745
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1746 EAAAATQ-------KRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLralaEEAK 1818
Cdd:COG1196 747 LLEEEALeelpeppDLEELERELERLEREIEALGPVNLLAIEE-----------YEELEERYDFLSEQREDL----EEAR 811
|
..
gi 41322914 1819 RQ 1820
Cdd:COG1196 812 ET 813
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1355-2417 |
6.54e-28 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 125.32 E-value: 6.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1355 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAE--REAKELQQRMQEEVVRREEAaVDAQQQKRSIQEELQQLRQ 1431
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAElhTEAVQRRQQLDQELAERRQT-VESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1432 SSEA-----EIQAKARQAEAAERSRlrieeeirVVRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERLRRQ 1506
Cdd:NF041483 162 ESQArrlldESRAEAEQALAAARAE--------AERLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1507 VQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQaeEAERRLRQAEVERARQVQVALETAqrsaeaelqSKR 1586
Cdd:NF041483 227 ASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA---------AKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1587 ASFAEKT-AQLERSLQEEhvaVAQL-REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQA 1664
Cdd:NF041483 296 LASAESAnEQRTRTAKEE---IARLvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1665 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQGEQQRQLLEEELARL 1743
Cdd:NF041483 373 AEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1744 QREAAAATQK-----RQELEAELAKVRAEMEVLLAsKARAE-EESRSTSEKSKQRLEAEAGR----FRELAE-------- 1805
Cdd:NF041483 453 RAEAVAEGERirgeaRREAVQQIEEAARTAEELLT-KAKADaDELRSTATAESERVRTEAIErattLRRQAEetlertra 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1806 EAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLAEKLA-AIGEATRLKTEAE-------IALKEKEAENERLRRLAED 1876
Cdd:NF041483 532 EAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEerltaaeEALADARAEAERIRREAAE 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1877 EAfqrRRLEEQAAqhkadieERLAQLRKASDSELERQKGLVEDTLRQRRqVEEEILALKASFEKAAagkaelelELGRIR 1956
Cdd:NF041483 612 ET---ERLRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAAR-AEGENVAVRLRSEAAA--------EAERLK 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1957 SNAEDTlRSKEQAELEAARQRqlaaeeerrrrEAEERVQKSLAAEEEAARQRKaalEEVERLKAKVEEARRLRERAEQES 2036
Cdd:NF041483 673 SEAQES-ADRVRAEAAAAAER-----------VGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERERAREQS 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2037 ARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEaarraaeeaeearvQAEREAAQSRRQVE 2116
Cdd:NF041483 738 EELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQE--------------QAEEEIAGLRSAAE 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2117 EAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEaarraqaeqaalRQKQAADAEMEKHKKFAEQTLRQkAQVEQElttlR 2196
Cdd:NF041483 804 HAAERTRTEAQEEADRVRSDAYAERERASEDAN------------RLRREAQEETEAAKALAERTVSE-AIAEAE----R 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2197 LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVR----VQMEELSKLKARIEAENRALILRDKDNTQRFLQE 2272
Cdd:NF041483 867 LRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARA 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2273 EAEKMKQVAEEAAR--LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmqavqEATRLKAEAELLQQQKELAQEQARRL 2350
Cdd:NF041483 947 EAERVRADAAAQAEqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEA-----ERVKAEAAAEAERLRTEAREEADRTL 1021
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 2351 QEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQrfRKQAEEI 2417
Cdd:NF041483 1022 DEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAA--RKEAERI 1086
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1726-2610 |
1.21e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 124.87 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1726 TEQGEQQRQLLEEELARLQREAAAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1803
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1804 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlAEKLAAIGEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 1881
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1882 RRLEEQaaqHKADIEERLAQLRKASDSelerqkglvedtlrqrRQVEEeilalkasfekaaAGKAELELELGRIRsNAED 1961
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1962 TLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQ 2041
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2042 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTlqqeqsvldqlrgeaeaarraaeeaeearVQAEREAAQSRRQVEEAERL 2121
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKK-----------------------------ADAAKKKAEEAKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2122 KQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2201
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2202 TDHQknlldEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARiEAENRALILRDKDNtqrfLQEEAEKMKQVA 2281
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADE----AKKKAEEAKKKA 1499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2282 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKeQM 2357
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-NM 1578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2358 AQQLAEETQgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVtlvqt 2437
Cdd:PTZ00121 1579 ALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK----- 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2438 leiqrqqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLlqetqalqqsflsEKDSLLQRErfiEQEK 2517
Cdd:PTZ00121 1647 ---------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-------------KAAEALKKE---AEEA 1701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2518 AKLEQL---FQDEVAKAQqlreEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEE 2594
Cdd:PTZ00121 1702 KKAEELkkkEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
890
....*....|....*.
gi 41322914 2595 NQRLREQLQLLEEQHR 2610
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRR 1793
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
46-148 |
2.04e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 109.11 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 46 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHF 148
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
150-265 |
2.65e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 109.40 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 150 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 229
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322914 230 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 265
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
46-151 |
1.12e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.81 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 46 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHFQIS 151
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1403-2120 |
1.25e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.40 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1403 EEVVrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL 1482
Cdd:PTZ00121 1030 EELT--EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1483 RARAEEaEAQKRQAQEEAERLRRqvqdeSQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQ-AEEAERRLRQAEV 1561
Cdd:PTZ00121 1108 TGKAEE-ARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1562 ERARQVQVALETaqRSAEaelQSKRASFAEKtAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1641
Cdd:PTZ00121 1182 RKAEEVRKAEEL--RKAE---DARKAEAARK-AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1642 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELI 1720
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKKaDAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1721 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE-----A 1795
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelkkaA 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1796 EAGRFRELAEEAARLRALAEEAKRQRQLAEE-DAARQRAEAERVlAEKLAAIGEATRLKTEAEIALKEKEAENErLRRLA 1874
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADE-AKKKA 1492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1875 EDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGR 1954
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAKK 1571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1955 IRSNAEDTLRSKEQA-ELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE--EVERLKAKVEE----ARR 2027
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkKVEQLKKKEAEekkkAEE 1651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2028 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAERE 2107
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
730
....*....|...
gi 41322914 2108 AAQSRRQVEEAER 2120
Cdd:PTZ00121 1732 AEEAKKEAEEDKK 1744
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
150-265 |
1.38e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.50 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 150 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 229
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322914 230 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 265
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1488-2470 |
2.89e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.93 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1488 EAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEVELASRVKAE--AEAAREKQRALQALEELRLQAE-EAERRLR 1557
Cdd:NF041483 73 QAEQLLRNAQIQADQLRadaerelRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1558 QAEVERARQVQVA---LETAQRSAEAELQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeAERAREEAERE 1634
Cdd:NF041483 153 WAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE--------------------AESARAEAEAI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1635 LERWQLKANEALR-LRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrl 1713
Cdd:NF041483 213 LRRARKDAERLLNaASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQE---AEEALREARAEAEKVVAE-- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1714 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKS 1789
Cdd:NF041483 288 AKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1790 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVlAEKLAAIG----------------EATRLK 1853
Cdd:NF041483 368 KAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ-AEQLKGAAkddtkeyraktvelqeEARRLR 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1854 TEAEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIE------------------ERLAQLRKASDSEL 1910
Cdd:NF041483 447 GEAEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADelrstataeservrteaiERATTLRRQAEETL 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1911 ERQKGLVEdtlRQRRQVEEEILALKASFEKAA------------AGKAELELELGRIRSNAEDTLRSKEQAELEaarqrq 1978
Cdd:NF041483 527 ERTRAEAE---RLRAEAEEQAEEVRAAAERAArelreeteraiaARQAEAAEELTRLHTEAEERLTAAEEALAD------ 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1979 laaeeerrrreaeervqkslaAEEEAARQRKAALEEVERLKAKV-EEARRLRERAEQESARqlqLAQEAAQKRLQAEEKA 2057
Cdd:NF041483 598 ---------------------ARAEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAER---LRTEAAADASAARAEG 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2058 HAFAVQQKEQELQQTLQQEQSVLDqlrgeaeaarraaeeaEEARVQAEREAAQSRRQVEEAERLKQSAEEQAqaraqaqa 2137
Cdd:NF041483 654 ENVAVRLRSEAAAEAERLKSEAQE----------------SADRVRAEAAAAAERVGTEAAEALAAAQEEAA-------- 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2138 aaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAEQTL-RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRL 2216
Cdd:NF041483 710 ------------------------RRRREAEETLGSARAEADQEReRAREQSEELLASARKRVEEAQAEAQRLVEEADRR 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2217 KAEATEAARQRSQ-VEEELFSVRVQM-EELSKLkaRIEAENRAlilrdkDNTQRFLQEEAEKMKqvAEEAARLSVAAQEA 2294
Cdd:NF041483 766 ATELVSAAEQTAQqVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SDAYAERERASEDA 835
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2295 ARLRQLAEEDLAQQRALAEKMLKEkmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEA 2374
Cdd:NF041483 836 NRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAA 912
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2375 ERQRQL--EMSAEAERLKLRV-AEMSRAQARAEEDAQRFRKQAEEIGEKL--HRTELATQEKVTLVQTLEIQRQQSDH-- 2447
Cdd:NF041483 913 AQADRLigEATSEAERLTAEArAEAERLRDEARAEAERVRADAAAQAEQLiaEATGEAERLRAEAAETVGSAQQHAERir 992
|
1050 1060
....*....|....*....|....*
gi 41322914 2448 -DAERLR-EAIAELEREKEKLQQEA 2470
Cdd:NF041483 993 tEAERVKaEAAAEAERLRTEAREEA 1017
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
42-150 |
1.22e-25 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 104.84 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHR- 117
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTKv 94
|
90 100 110
....*....|....*....|....*....|...
gi 41322914 118 QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21247 95 PVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1105-1858 |
1.59e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.55 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1105 AEEVLRAHE-EQLKEAQAVPATLPELEATKASLKKlRAQ----AEAQQPTFDALR-DELRGAQEVGERLQQRHGERDVEV 1178
Cdd:PTZ00121 1136 AEDARKAEEaRKAEDAKRVEIARKAEDARKAEEAR-KAEdakkAEAARKAEEVRKaEELRKAEDARKAEAARKAEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1179 ERWR----ERVAQLLERWQAVLAQTD-VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVR--EQ 1251
Cdd:PTZ00121 1215 EEARkaedAKKAEAVKKAEEAKKDAEeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDE 1294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1252 LR--QEQALLEEIERHGEKVEECQRFAKQYINAIKDYELqlVTYKAQLEPVASPAKKPKVQSGSESViqeyvDLRTHYSE 1329
Cdd:PTZ00121 1295 AKkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEA-----EAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1330 LTTLTSQYIKFISETLRRMEEEERLAEQ--QRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAKELQQRmQEEVVR 1407
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKK-AEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1408 REEAAVDAQQQKRSiqEELQQlrqsseaeiqaKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGElQALRARAE 1487
Cdd:PTZ00121 1446 ADEAKKKAEEAKKA--EEAKK-----------KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKK 1511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1488 EAEAQKRQAQEEAERLRRqvqdeSQRKRQAEvelasrvkaEAEAAREKQRAlqalEELRlQAEEAERRLRQAEVERARQV 1567
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKK-----AEEAKKAD---------EAKKAEEKKKA----DELK-KAEELKKAEEKKKAEEAKKA 1572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1568 QVALETAQRSAE--AELQSKRASFAEKTAQLERSLQEEHVAvaqlreeaerraqqqaeaerareeaerelerwqlKANEA 1645
Cdd:PTZ00121 1573 EEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAK----------------------------------KAEEA 1618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1646 lrlRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRElaeqELEKQRQLAEGTAQQRLAAEQELIRLRAE 1725
Cdd:PTZ00121 1619 ---KIKAEELKKAEEEKKKVEQLK------------KKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1726 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAElakVRAEMEVllaskARAEEESRSTSEKSKQRLEAEAGRFRELAE 1805
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE---KKKAEEL-----KKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1806 EAARLRALAEEAKRQRQLAEEdaarQRAEAERVLAEKLAAIGEATRLKTEAEI 1858
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
50-147 |
2.19e-25 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 103.16 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 50 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 125
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 41322914 126 NDDIADGnPKLTLGLIWTIILH 147
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
168-263 |
2.81e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.00 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 168 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 246
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 41322914 247 VPQPDEKSIITYVSSLY 263
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
150-265 |
3.70e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 103.23 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 150 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 229
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322914 230 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 265
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1685-2523 |
9.64e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.77 E-value: 9.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1764
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1765 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1844
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1845 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrRLEEQAAQHKADIEERLAQLrkaSDSELERQKGLVEDTLRQR 1924
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1925 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdtlrsKEQAELEAARQRQLaaeeerrrreaeervqkSLAAEEEA 2004
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD-----------------AAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2005 ARQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQ 2064
Cdd:TIGR02168 487 LQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2065 KEQELQQTLQQEQSVLDQ-LRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEE-------AERLKQSAEEQAQARAQAQ 2136
Cdd:TIGR02168 567 QNELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2137 AAAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRL 2216
Cdd:TIGR02168 647 IVTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2217 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEnralilrdkdntqrfLQEEAEKMKQVAEEAARLSVAAQEAAR 2296
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE---------------LTELEAEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2297 LRQLAEEDLAQQRALAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtleae 2375
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2376 rqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA 2455
Cdd:TIGR02168 849 -----ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2456 IAELEREKEKLQQEAKLLQlkseemQTVQQEQLLQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2523
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
162-268 |
1.24e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.21 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 162 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 238
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 41322914 239 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 268
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1407-2252 |
1.86e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.61 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1407 RREEAavdaQQQKRSIQEELQQL---RQSSEAEIQAKARQAEAAERSRlRIEEEIRvvrlqleaterqrggaEGELQALR 1483
Cdd:TIGR02168 173 RRKET----ERKLERTRENLDRLediLNELERQLKSLERQAEKAERYK-ELKAELR----------------ELELALLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1484 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLR--QAEV 1561
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1562 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLErSLQEEHVAVAQLREeaerraqqqaeaerareeaerelERWQLK 1641
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELE-----------------------ELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1642 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIR 1721
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1722 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGR 1799
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1800 FRELAEEAARLRALAEEAKRQR--QLAEEDAARQRAEAErvlAEKLAAIGEATRLkteAEIALKEKEAENERLRRLAEDE 1877
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGRlqAVVVENLNAAKKAIA---FLKQNELGRVTFL---PLDSIKGTEIQGNDREILKNIE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1878 AFQR--RRLEEQAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILALKASFEKAAAG----KAELELE 1951
Cdd:TIGR02168 599 GFLGvaKDLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTN 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1952 LGRI-RSNAEDTLRSK-EQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2029
Cdd:TIGR02168 670 SSILeRRREIEELEEKiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2030 ERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAA 2109
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2110 QSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVE 2189
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 2190 QELTTLRLQLEETDHQKNLLDEELQRLKAEA---TEAARQRSQVEEELFSVRVQMEELSKLKARIE 2252
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIdnlQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
166-266 |
1.98e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 100.62 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 166 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 245
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 41322914 246 DVPQPDEKSIITYVSSLYDAM 266
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
47-150 |
2.28e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.44 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 47 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 122
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1859-2523 |
2.43e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1859 ALKEKEAENERLRRLaEDEAF----QRRRLEEQAAQ------HKADIEERLAQLRKASDSELERQKGLVEdtlRQRRQVE 1928
Cdd:COG1196 177 AERKLEATEENLERL-EDILGelerQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELE---AELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1929 EEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR 2008
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2009 KAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQkeqelqqtlqqeqsvldqlrgeae 2088
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL------------------------ 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2089 aarraaeeaeearVQAEREAAQSRRQVEEAERLKQSAeeqaqaraqaqaaaeklrkeaeqeaarraqaeqaaLRQKQAAD 2168
Cdd:COG1196 389 -------------LEALRAAAELAAQLEELEEAEEAL-----------------------------------LERLERLE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2169 AEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK 2248
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2249 ARIEAENRA-LILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2327
Cdd:COG1196 501 ADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2328 RLKAEAELLQQQKELAQEQARRL----QEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARA 2403
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2404 EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTV 2483
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 41322914 2484 QQEQLLQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2523
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERE-LERLEREIEAL 779
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
164-263 |
5.26e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 99.56 E-value: 5.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 164 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 243
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 41322914 244 D-VDVPQPDEKSIITYVSSLY 263
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1105-1905 |
2.64e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 110.15 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1105 AEEVLRAHEEQLKEAQAvpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1184
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1185 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIER 1264
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1265 hgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQyikfISET 1344
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1345 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-------------------EAKE--LQQRMQE 1403
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegyeAAIEaaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1404 EVVRREEAAVDAQQ---QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQ 1480
Cdd:TIGR02168 550 VVVENLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKLRKALSYLLG 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1481 ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAevelASRVKAEAEAAREKQRalQALEELRLQAEEAERRLR--Q 1558
Cdd:TIGR02168 624 GVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGV----ITGGSAKTNSSILERR--REIEELEEKIEELEEKIAelE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1559 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEehvaVAQLREEAERRAQQQAEAERAREEAERELERW 1638
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1639 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1718
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1719 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEA 1795
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEG 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1796 EAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIGEATRLkteaeiALKEKEAENERLRRLa 1874
Cdd:TIGR02168 934 LEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL- 1005
|
810 820 830
....*....|....*....|....*....|.
gi 41322914 1875 edeafqrrrleeqaAQHKADIEERLAQLRKA 1905
Cdd:TIGR02168 1006 --------------TAQKEDLTEAKETLEEA 1022
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
163-267 |
3.55e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.17 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 242
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 41322914 243 EDVDVPQPDEKSIITYVSSLYDAMP 267
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
163-263 |
3.91e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 96.73 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 242
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 41322914 243 EDVDVPQ-PDEKSIITYVSSLY 263
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1020-1588 |
3.07e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1020 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1099
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1100 RGTQGAEEVLRAHEEQLKEAQAvpATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVE 1179
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1180 RWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAmpladsqAVREQLRQEQALL 1259
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1260 EEIERHGEKVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLtsqyik 1339
Cdd:COG1196 470 EEAALLEAALAE----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1340 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvrreEAAVDAQQQK 1419
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI----GAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1420 RSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1499
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1500 AERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALE--TAQRS 1577
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdlEELER 767
|
570
....*....|.
gi 41322914 1578 AEAELQSKRAS 1588
Cdd:COG1196 768 ELERLEREIEA 778
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
46-151 |
4.15e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.76 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 46 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHFQIS 151
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
163-261 |
4.16e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 93.84 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 241
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 41322914 242 PEDVDVPQPDEKSIITYVSS 261
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
46-151 |
4.87e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.77 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 46 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHFQIS 151
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
797-863 |
6.26e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.94 E-value: 6.26e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 797 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 863
Cdd:pfam17902 1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1107-2390 |
3.74e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.98 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1107 EVLRAheeQLKEAQAVPATLPELEAT----KASLKKLRAQAEAQQPTFDALRdELRGAQEVGERLQQRHGERDVeverwr 1182
Cdd:NF041483 46 EVLRA---KLHEARRSLASRPAYDGAdigyQAEQLLRNAQIQADQLRADAER-ELRDARAQTQRILQEHAEHQA------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1183 ervaqlleRWQAVLAQTDV--RQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQ----LRQEQ 1256
Cdd:NF041483 116 --------RLQAELHTEAVqrRQQLDQELAERRQTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQalaaARAEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1257 ALLEEIERH--GEKVEECQRFAKQYI-NAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqeyvDLRTHYSELTTL 1333
Cdd:NF041483 188 ERLAEEARQrlGSEAESARAEAEAILrRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESD-----QARRQAAELSRA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1334 TSQyikfisetlrRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAhaqAKAQAEREAKELQQRMQEEVVRREEAav 1413
Cdd:NF041483 263 AEQ----------RMQEAEEALREARAEAEKVVAEAKEAAAKQLASAES---ANEQRTRTAKEEIARLVGEATKEAEA-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1414 daqqqkrsIQEELQQLRQSSEAEiqAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRARAEEAEAQK 1493
Cdd:NF041483 328 --------LKAEAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1494 RQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRA--LQALEELRLQAEEAE--RRLRQAEVER----AR 1565
Cdd:NF041483 389 RAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAktVELQEEARRLRGEAEqlRAEAVAEGERirgeAR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1566 QVQVA-LETAQRSAEAELQSKRASFAE----KTAQLERSLQEEHVAVAQLREEAERRaqqqaeaerareeaereLERWQl 1640
Cdd:NF041483 469 REAVQqIEEAARTAEELLTKAKADADElrstATAESERVRTEAIERATTLRRQAEET-----------------LERTR- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1641 kaNEALRLRLQAEEVAQqkslAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAegTAQQRLA-AEQEL 1719
Cdd:NF041483 531 --AEAERLRAEAEEQAE----EVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLT--AAEEALAdARAEA 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1720 IRLRAET-EQGEQQRQLLEEELARLQREAAAATQK-RQELEAELAKVRAEME---VLLASKARAE-EESRSTSEKSKQRL 1793
Cdd:NF041483 603 ERIRREAaEETERLRTEAAERIRTLQAQAEQEAERlRTEAAADASAARAEGEnvaVRLRSEAAAEaERLKSEAQESADRV 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1794 EAEAGRFRE-LAEEAAR-LRALAEEAKRQRQLAEE--DAARQRAEAERVLA-----EKLA--------AIGEATRLKTEA 1856
Cdd:NF041483 683 RAEAAAAAErVGTEAAEaLAAAQEEAARRRREAEEtlGSARAEADQERERAreqseELLAsarkrveeAQAEAQRLVEEA 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1857 E------IALKEKEAENER-----LRRLAEDEAFQRRrleeQAAQHKADIEERLAQL---RKASDSELERQKGlVEDTLR 1922
Cdd:NF041483 763 DrratelVSAAEQTAQQVRdsvagLQEQAEEEIAGLR----SAAEHAAERTRTEAQEeadRVRSDAYAERERA-SEDANR 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1923 QRRQVEEEILALKASFEKAAAG--------KAELELELGRIRSNAEDTLRSKEQ--------AELEAARQRQLAAEEERR 1986
Cdd:NF041483 838 LRREAQEETEAAKALAERTVSEaiaeaerlRSDASEYAQRVRTEASDTLASAEQdaartradAREDANRIRSDAAAQADR 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1987 RREAEERVQKSLAAE--EEAARQRKAALEEVERLKAK--------VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2056
Cdd:NF041483 918 LIGEATSEAERLTAEarAEAERLRDEARAEAERVRADaaaqaeqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEAER 997
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2057 AHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQAraqaq 2136
Cdd:NF041483 998 VKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQA----- 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2137 aaaeklrkeaeqeaarraqaeqaalrQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTlrlqleetdhqknlLDEELQRL 2216
Cdd:NF041483 1073 --------------------------DTMVGAARKEAERIVAEATVEGNSLVEKARTD--------------ADELLVGA 1112
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2217 KAEATeAARQRSQveeelfsvrvqmeelsKLKARIEAENRALilrdkdnTQRFLQEEAEKMKQVAEEAARLSVAAQEaar 2296
Cdd:NF041483 1113 RRDAT-AIRERAE----------------ELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEE--- 1165
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2297 lrQLAEEDLAQQRALAE---KMLKEKMQAVQEATRLKAEAEllqQQKELAQEQARRLQEDKEQMAQQLAEETqgfQRTLE 2373
Cdd:NF041483 1166 --QLAEAEAKAKELVSDansEASKVRIAAVKKAEGLLKEAE---QKKAELVREAEKIKAEAEAEAKRTVEEG---KRELD 1237
|
1370
....*....|....*..
gi 41322914 2374 AERQRQLEMSAEAERLK 2390
Cdd:NF041483 1238 VLVRRREDINAEISRVQ 1254
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2080-2692 |
7.25e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 7.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2080 LDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERlkqsaeeqaqaraQAQAAAEKLRKEAEQEAARRAQAEQA 2159
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-------------AELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2160 ALRQKQAADAEMEKHKKFAEQtlrQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRV 2239
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2240 QMEELsklkARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2319
Cdd:COG1196 366 ALLEA----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2320 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtLEAERQRQLEMSAEAERLklrvaemsRA 2399
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----AAARLLLLLEAEADYEGF--------LE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2400 QARAEEDAQRFRKQAEEIGEKLHRTELAtqEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEE 2479
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVEAAY--EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2480 MQTVQQEQLLQETQALQQSFLSEKDSLLQReRFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEA 2559
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYY-VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2560 RRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATK------TLPNG 2633
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEReelleeLLEEE 745
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322914 2634 RDALDGPAAEAEPEHSFDGLRRKVSA--QRLQEAG---ILSAEELQRLAQGHTTVDElaRREDV 2692
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERleREIEALGpvnLLAIEEYEELEERYDFLSE--QREDL 807
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1105-1905 |
2.77e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 100.13 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1105 AEEVLRAHE--EQLKEAQAVPATLpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDveverwr 1182
Cdd:TIGR02168 209 AEKAERYKElkAELRELELALLVL-RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1183 ERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQALLEEi 1262
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE-LAELEEKLEELKEELESLEA- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1263 erhgeKVEECQrfakqyiNAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDlrthySELTTLTSQYIKFIS 1342
Cdd:TIGR02168 359 -----ELEELE-------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevVRREEAAvdAQQQKRSI 1422
Cdd:TIGR02168 422 EIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQ--LQARLDSL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1423 QEELQQLRQSSEAEIQAKArqaeaaerSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALRARAEEAEAQKRQAQE 1498
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLK--------NQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1499 EAERLRR-------------QVQDESQRKRQAEVE--LASRVKAEAEAarekQRALQALEELRLQAEEAERRLRQAEVER 1563
Cdd:TIGR02168 567 QNELGRVtflpldsikgteiQGNDREILKNIEGFLgvAKDLVKFDPKL----RKALSYLLGGVLVVDDLDNALELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1564 ARQVQVALET-----------AQRSAEAELQSKRASFAE---KTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERARE 1629
Cdd:TIGR02168 643 PGYRIVTLDGdlvrpggvitgGSAKTNSSILERRREIEEleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1630 EAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTA 1709
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1710 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKS 1789
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1790 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAE--- 1866
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidn 940
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 41322914 1867 -NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 1905
Cdd:TIGR02168 941 lQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
167-264 |
3.71e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.56 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 167 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 245
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 41322914 246 DVPQPDEKSIITYVSSLYD 264
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1335-2065 |
4.06e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 99.66 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1335 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVD 1414
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1415 AQQQKRSIQEELQQLRQSSEAEIQA-----KARQAEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAE 1487
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESskqeiEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1488 EAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS--RVKAEAEAAREKQRALQALEELRLQAEEAE-RRLRQAEVERA 1564
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKkKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1565 RQVQVALETAQR-SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKAN 1643
Cdd:pfam02463 391 KLKEEELELKSEeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1644 EALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELI 1720
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1721 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG-R 1799
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIlK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1800 FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAF 1879
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1880 QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA 1959
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1960 EDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2039
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740
....*....|....*....|....*....
gi 41322914 2040 LQLAQE---AAQKRLQAEEKAHAFAVQQK 2065
Cdd:pfam02463 871 ELLLKEeelEEQKLKDELESKEEKEKEEK 899
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
163-263 |
5.20e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 88.17 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 242
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 41322914 243 EDVDV--PQPDEKSIITYVSSLY 263
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1343-1902 |
7.61e-20 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 98.45 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDA 1415
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1416 QQQKRSIQEELQQLRQ-----------SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1473
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1474 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELrLQAEEAE 1553
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1554 RRLRQAeVERA----------------------------RQVQVALETAQRSAEAELQSKRASFAEK--------TAQLE 1597
Cdd:COG4913 474 ERWRGA-IERVlggfaltllvppehyaaalrwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfRAWLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1598 RSLQEE--HVAV---AQLREEA----ERRAQQQAEAERAREEAERELERWQL-KANEALRLRLQAEEVAQQKSLAQAEAE 1667
Cdd:COG4913 553 AELGRRfdYVCVdspEELRRHPraitRAGQVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1668 KQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQ 1744
Cdd:COG4913 633 LEAL----------EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1745 REAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1824
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1825 EEDAARQRAEAERVLAE--------------KLAAIGE-ATRLKTEAEIALKEKEAENERLRRLAEDEAFQrrRLEEQAA 1889
Cdd:COG4913 779 RARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVA--DLLSKLR 856
|
650
....*....|...
gi 41322914 1890 QHKADIEERLAQL 1902
Cdd:COG4913 857 RAIREIKERIDPL 869
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
163-262 |
3.11e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 85.61 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 242
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 41322914 243 ED-VDVPQPDEKSIITYVSSL 262
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
159-264 |
3.42e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 85.77 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 159 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 238
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 41322914 239 LLDPEDV-DVPQPDEKSIITYVSSLYD 264
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
166-262 |
4.66e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.06 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 166 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 241
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 41322914 242 PEDVDVPQPDEKSIITYVSSL 262
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1309-1957 |
8.01e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.11 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1309 VQSGSESVIQEYVDLRTHySELTTLTSQyIKFISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQ 1378
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLH-ERLNGLESE-LAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1379 laeahaqAKAQAEREAKELQQRMQEEVVRREEaavdaqqqkrsIQEELQQLRQSSE---AEIQAKARQAEAAERSRLRIE 1455
Cdd:PRK02224 266 -------TIAETEREREELAEEVRDLRERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1456 EEIRVVRLQLEATERQRGGAEGELQALRARAEEaeaqkrqAQEEAERLRRQVQdesqrkrqaevelasrvkaEAEAAREK 1535
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEE-------LREEAAELESELE-------------------EAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1536 QRAlqALEELRLQAEEAERRLRQAEVERArqvqvalETAQRSaeAELQSKRASFAEKTAQLERSLQEEHVAVAQlreeae 1615
Cdd:PRK02224 382 RRE--EIEELEEEIEELRERFGDAPVDLG-------NAEDFL--EELREERDELREREAELEATLRTARERVEE------ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1616 rraqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRQRELAE 1695
Cdd:PRK02224 445 ---------------------------AEALLEAGKCPECGQP---------------VEGSPHVETIEEDRERVEELEA 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1696 qELEKQRqLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1775
Cdd:PRK02224 483 -ELEDLE-EEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1776 ARAEEEsrstSEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAARQRAEAervLAEKLAAIGEatrLKTE 1855
Cdd:PRK02224 561 AEAEEE----AEEAREEVAELNSKLAELKERIESLERIRT------LLAAIADAEDEIER---LREKREALAE---LNDE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1856 AEIALKEKeaeNERLRRLAEDeaFQRRRLEE------QAAQHKADIEERLAQLRKASDsELERQKGLVE------DTLRQ 1923
Cdd:PRK02224 625 RRERLAEK---RERKRELEAE--FDEARIEEaredkeRAEEYLEQVEEKLDELREERD-DLQAEIGAVEneleelEELRE 698
|
650 660 670
....*....|....*....|....*....|....*
gi 41322914 1924 RR-QVEEEILALKASFEKAaagkAELELELGRIRS 1957
Cdd:PRK02224 699 RReALENRVEALEALYDEA----EELESMYGDLRA 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1793-2626 |
1.15e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 94.74 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1793 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLAEKLAAIGEATRlKTEAE 1857
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1858 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILAL 1934
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1935 KASFEKAAAGKAELELELgrirsnaEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2014
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2015 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEqelqqtlqqeqsvLDQLRGEAEAARR 2092
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-------------LKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2093 AAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQAraqaqaaaeklrkeaeqeaarraqaeqaaLRQKQAADAEME 2172
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-----------------------------LQARLDSLERLQ 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2173 KHKKFAEQTLRQKAQVEQELTTLR---LQLEETDHQ-----KNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEEL 2244
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSGLSGILgvlSELISVDEGyeaaiEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2245 SKLKARIEAENRALILRDKDNTQRFLqeeaekmKQVAEEAARLSVAAQeaARLRQLA-EEDLAQQRALAEKMLKEKMQAV 2323
Cdd:TIGR02168 579 DSIKGTEIQGNDREILKNIEGFLGVA-------KDLVKFDPKLRKALS--YLLGGVLvVDDLDNALELAKKLRPGYRIVT 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2324 QEATRL--------------------KAEAELLQQQKELAQEQARRLQ---EDKEQMAQQLAEETQGFQRTLEAERQRQL 2380
Cdd:TIGR02168 650 LDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQIS 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2381 EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELE 2460
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2461 REKEKLQQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQR 2540
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEE 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2541 QQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEqhrAALAHSEEVT 2620
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIE 964
|
....*.
gi 41322914 2621 ASQVAA 2626
Cdd:TIGR02168 965 DDEEEA 970
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
48-148 |
1.19e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 84.17 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 48 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 123
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 41322914 124 IRNDDIADGNPKLTLGLIWTIILHF 148
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
49-146 |
3.64e-18 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 82.77 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 49 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 124
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 41322914 125 RNDDI-ADGNPKLTLGLIWTIIL 146
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1892-2693 |
3.80e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.28 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1892 KADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfEKAAAGKAELELELGRIRSNAEDTLRSKEQAEL 1971
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA--KKTETGKAEEARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1972 EAARQrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQEAAQKRl 2051
Cdd:PTZ00121 1137 EDARK------------------------AEEARKAEDAKRVEIAR---KAEDARKAEEARKAEDAKKAEAARKAEEVR- 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2052 QAEEKAHAFAVQQKEQELQQTLQQEqsvLDQLRgeaeaarraaEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQA 2131
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERK---AEEAR----------KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2132 RAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ--KQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEETDHQKnll 2209
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEekKKADEAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKA--- 1331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2210 dEELQRlKAEATEAARQRSQVEEElfsvrVQMEELSKLKARIEAenralilrDKDNTQRfLQEEAEKMKQVAEEAARLSV 2289
Cdd:PTZ00121 1332 -DAAKK-KAEEAKKAAEAAKAEAE-----AAADEAEAAEEKAEA--------AEKKKEE-AKKKADAAKKKAEEKKKADE 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2290 AAQEAARLRQLAEEdlaqqralaekmLKEKMQAVQEATRLKAEAEllqqQKELAQEQARRLQEDKEqmaqqlAEETQgfQ 2369
Cdd:PTZ00121 1396 AKKKAEEDKKKADE------------LKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKK------ADEAK--K 1451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2370 RTLEAERQRQLEMSAEAERlklrVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvQTLEIQRQQSDHDA 2449
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAK----KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKA 1524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2450 ERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQALQQSFLSEKD---SLLQRERFIEQEKAKLEQLF-- 2524
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMkl 1600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2525 --QDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQL 2602
Cdd:PTZ00121 1601 yeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2603 QLLEEQHR----AALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRlQEAGILSAEELQRLAQ 2678
Cdd:PTZ00121 1681 KKAEEDEKkaaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKI 1759
|
810
....*....|....*
gi 41322914 2679 GHTTVDELARREDVR 2693
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIR 1774
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1343-2111 |
7.30e-18 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 92.20 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEerlAEQQRAEERERLAEV-----EAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQ 1417
Cdd:NF041483 524 ETLERTRAE---AERLRAEAEEQAEEVraaaeRAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARA 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1418 Q----KRSIQEELQQLRQSSEAEIQAKARQAE----------AAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQAL 1482
Cdd:NF041483 601 EaeriRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESAD 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1483 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASrvkAEAEAAREKQRALQALEELrlqAEEAERRLRQAEVE 1562
Cdd:NF041483 681 RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGS---ARAEADQERERAREQSEEL---LASARKRVEEAQAE 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1563 RARQVQvalETAQRSAEAelqskrASFAEKTAQLERSlqeehvAVAQLREEAERraqqqaeaerareeaerelerwqlka 1642
Cdd:NF041483 755 AQRLVE---EADRRATEL------VSAAEQTAQQVRD------SVAGLQEQAEE-------------------------- 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1643 nEALRLRLQAEEVAQQksLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRL 1722
Cdd:NF041483 794 -EIAGLRSAAEHAAER--TRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERL 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1723 RAETEQGEQQ-------------------RQLLEEELARLQREAAA-----ATQKRQELEAELAKVRAEMEVLLASKARA 1778
Cdd:NF041483 868 RSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAqadrlIGEATSEAERLTAEARAEAERLRDEARAE 947
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1779 EEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAERVLAEklaAIGEATRLKTEAEi 1858
Cdd:NF041483 948 AERVRADAAAQAEQLIAEA------TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE---AAAEAERLRTEAR- 1014
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1859 alkekeAENERLRRLAEDEAFQRRRleEQAAQHKADIEERLAQLRK-ASDSELERQKGLVE-----DTLRQRRQVEEEIL 1932
Cdd:NF041483 1015 ------EEADRTLDEARKDANKRRS--EAAEQADTLITEAAAEADQlTAKAQEEALRTTTEaeaqaDTMVGAARKEAERI 1086
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1933 ALKASFE------KAAAGKAELELELGR----IRSNAEDtLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEE 2002
Cdd:NF041483 1087 VAEATVEgnslveKARTDADELLVGARRdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEE 1165
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2003 EAARQRKAALEEVERLK--------AKVEEARRLRERAEQESArqlQLAQEAAQKRLQAEEKAHAFAVQQKEQelqqtlq 2074
Cdd:NF041483 1166 QLAEAEAKAKELVSDANseaskvriAAVKKAEGLLKEAEQKKA---ELVREAEKIKAEAEAEAKRTVEEGKRE------- 1235
|
810 820 830
....*....|....*....|....*....|....*..
gi 41322914 2075 qeqsvLDQLrgeaeAARRAAEEAEEARVQAEREAAQS 2111
Cdd:NF041483 1236 -----LDVL-----VRRREDINAEISRVQDVLEALES 1262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1361-1905 |
7.41e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 91.90 E-value: 7.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1361 EERERLAEVEAALEKQRQLAEAHAQAkaqaeREAKElqqrmQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAK 1440
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEAL-----EDARE-----QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1441 ARQAEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRA--------RAEEAEAQKRQAQEEAERLRRQVQDESQ 1512
Cdd:COG4913 289 RLELLEAELEELR--AELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1513 RKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQV------ALETAQRSAEAELQSKR 1586
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleaeiaSLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1587 ASFAEKTAQLERSLQ--EEHVAVAQLReeaerraqqqaeaerareeaerelERWQLKANEAL---RLRL--------QAE 1653
Cdd:COG4913 447 DALAEALGLDEAELPfvGELIEVRPEE------------------------ERWRGAIERVLggfALTLlvppehyaAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1654 EVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG- 1729
Cdd:COG4913 503 RWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAGq 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1730 --------------------------EQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1783
Cdd:COG4913 583 vkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1784 STS--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRL 1852
Cdd:COG4913 663 VASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1853 KTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 1905
Cdd:COG4913 743 ARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
163-262 |
5.30e-17 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 79.51 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 242
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 41322914 243 ED-VDVPQPDEKSIITYVSSL 262
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1489-2371 |
5.47e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 89.26 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1489 AEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQ 1568
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1569 VALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL 1648
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1649 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1728
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1729 GEQQRQLLeEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAA 1808
Cdd:pfam02463 403 EEKEAQLL-LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1809 RLRALAEEAKRQRQlaEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1888
Cdd:pfam02463 482 LQEQLELLLSRQKL--EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1889 AQHKADIEERLAQLRKASDSeLERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 1968
Cdd:pfam02463 560 VEERQKLVRALTELPLGARK-LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1969 AELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2048
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2049 KRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQ 2128
Cdd:pfam02463 719 AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2129 AQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNL 2208
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2209 LDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAarls 2288
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN---- 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2289 vaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGF 2368
Cdd:pfam02463 955 --------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
...
gi 41322914 2369 QRT 2371
Cdd:pfam02463 1027 VSI 1029
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
167-264 |
7.88e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.15 E-value: 7.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 167 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 245
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 41322914 246 DVPQPDEKSIITYVSSLYD 264
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1417-2360 |
1.18e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.20 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1417 QQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA----- 1491
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1492 QKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAR------EKQRALQALEELRLQAEEAERrlrQAEVERAR 1565
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEL---EAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1566 QVQVALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQaeaerareeaerelerwqlka 1642
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL--------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1643 nEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIR 1721
Cdd:TIGR02169 367 -EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1722 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAG 1798
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHG 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1799 RFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLAEKLAAigeatrlktEAEIALKEKEAENER---LRRLAE 1875
Cdd:TIGR02169 526 TVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1876 DEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELeRQKGLVEDTLRQRRQVEEEILALKAS--FEKAAAgkaeleLELG 1953
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRMVTLEGelFEKSGA------MTGG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1954 RIRSNAEDTLRSKEQAELEAARQRqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2033
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2034 Q-----ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAeeaeearvqAEREA 2108
Cdd:TIGR02169 716 RkigeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---------NDLEA 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2109 AQSRRQVEEAERLKQSAEeqaqaraqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQV 2188
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2189 EQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENraliLRDKDNTQR 2268
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSELKAK 925
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2269 fLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2348
Cdd:TIGR02169 926 -LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
970
....*....|..
gi 41322914 2349 RLQEDKEQMAQQ 2360
Cdd:TIGR02169 1004 AILERIEEYEKK 1015
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
165-276 |
2.02e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 78.11 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 165 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 244
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 41322914 245 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 276
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
967-1602 |
3.04e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.65 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 967 HHYQQLLQSLeqgAQEESRCQRCISELKDIRLQLEA-CETRTVHRLRLPLDKEPARECAQRIAEQQK-AQAEVEGLGKGV 1044
Cdd:TIGR02168 284 EELQKELYAL---ANEISRLEQQKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEeLKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1045 ARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSlSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVP 1123
Cdd:TIGR02168 361 EELEAElEELESRLEELEEQLETLRSKVAQLELQIASLNN-EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1124 ATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQ----T 1199
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1200 DVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQampLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQY 1279
Cdd:TIGR02168 520 GILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAA---KKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1280 INAIKDYELQLVTYKAQLEPVASP---------------AKKPKVQSGSESVIQEYVDLRTHYS--------ELTTL-TS 1335
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRR 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1336 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAE----AHAQAKAQAEREAKElQQRMQEEVVRREEA 1411
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEelsrQISALRKDLARLEAE-VEQLEERIAQLSKE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1412 AVDAQQQKRSIQEELQQLRQsseaeiqakarQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1491
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEE-----------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1492 QKRQAQEEAERLRRQVQDESQRKRQAEVELASrvkaeaeaarekqrALQALEELRLQAEEAERRLRQAEVERArQVQVAL 1571
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIES--------------LAAEIEELEELIEELESELEALLNERA-SLEEAL 889
|
650 660 670
....*....|....*....|....*....|.
gi 41322914 1572 ETAqRSAEAELQSKRASFAEKTAQLERSLQE 1602
Cdd:TIGR02168 890 ALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1340-1827 |
3.09e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 85.97 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1340 FISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQ-RMQEEVVRREEAAVDAQQQ 1418
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1419 KRSIQEELQQLRQSSEA------EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG-GAEGELQALRARAEEAEA 1491
Cdd:COG4717 127 LLPLYQELEALEAELAElperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1492 QKRQAQEEAERLRRQVQDESQRKRQAEVELAsRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVAL 1571
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELE-AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1572 ETAqrsAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQ 1651
Cdd:COG4717 286 LAL---LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1652 AEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQ 1731
Cdd:COG4717 363 LQLEELEQEIAALLAEAGV-----------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1732 qrqlLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlaskaraeEESRSTSEKSKQRLEAEAgRFRELAEEAARLR 1811
Cdd:COG4717 430 ----LEEELEELEEELEELEEELEELREELAELEAELEQL--------EEDGELAELLQELEELKA-ELRELAEEWAALK 496
|
490
....*....|....*.
gi 41322914 1812 ALAEEAKRQRQLAEED 1827
Cdd:COG4717 497 LALELLEEAREEYREE 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
970-1879 |
3.93e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.28 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 970 QQLLQSLEQGAQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1049
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1050 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRGTQG----AEEVLRAHEEQLKEAQ 1120
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1121 AVPATL-PELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavlaqt 1199
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1200 dvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAmpladsqavreqlrqeqalleEIERHGEKVEECQRFAKQY 1279
Cdd:TIGR02169 390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1280 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQR 1359
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1360 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKelqQRMQEEVVRREEAAVDAQQQKRS-------------IQEEL 1426
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1427 QQLRQSSEA----------EIQAKARQA-----------EAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1481
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvEFDPKYEPAfkyvfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1482 LRARAEEAEAQKRQAQEEA-ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEE----LRLQAEEAERRL 1556
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeekLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1557 RQAEVERarqvqvaletaqrsaeAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelE 1636
Cdd:TIGR02169 747 SSLEQEI----------------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------S 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1637 RWQLKANEalrLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAE 1716
Cdd:TIGR02169 792 RIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1717 QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAE 1796
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDP 939
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1797 AGRFRELAEEAARLRALAEEAKR-QRQLAEEDAARQRA--EAERVLAEKLAAIGEATRLKTEAEiALKEKEAENERLRRL 1873
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKRE 1018
|
....*.
gi 41322914 1874 AEDEAF 1879
Cdd:TIGR02169 1019 VFMEAF 1024
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
168-263 |
6.25e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 76.63 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 168 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 246
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 41322914 247 VPQPDEKSIITYVSSLY 263
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
165-264 |
8.62e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 76.16 E-value: 8.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 165 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 244
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 41322914 245 VDV--PQPDEKSIITYVSSLYD 264
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
165-268 |
1.40e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 75.47 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 165 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 244
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 41322914 245 VDV--PQPDEKSIITYVSSLYDAMPR 268
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1378-1748 |
1.59e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 84.02 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1378 QLAEAHAQAKAQAEREAKELQQRMQEEVVRreeaavdaqQQKRSIQEELQQLRQSSEAEiqaKARQAEA-------AERS 1450
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1451 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEVELASRVK-AEA 1529
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1530 EAAREKQRALQALEELRLQAEEA-ERRLRQAEVERARqvqvaletaqrsaeaELQSKRASFAEKTAQLERSLQEEhvava 1608
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1609 qlreeaerraqqqaeAERAREEAERELE-RWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQa 1687
Cdd:pfam17380 470 ---------------EERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE- 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1688 vrQRELAEQELEKQRQLAE--GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1748
Cdd:pfam17380 534 --RRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
45-144 |
2.25e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 74.87 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 45 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 119
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 41322914 120 KLVNIRNDDIADGNPKLTLGLIWTI 144
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1694-2480 |
3.17e-15 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 83.34 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1694 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQREA-AAATQKRQELEAELAKVRAEMEV 1770
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1771 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLaekLAAIGE 1848
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1849 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRleeQAAQHKADIEERLAQlrkasdselerqkglVEDTLRQRRQVE 1928
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARR---QAAELSRAAEQRMQE---------------AEEALREARAEA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1929 EEILAlkasfekaaagkaelelelgrirsnaedtlrskeQAELEAARQrqlaaeeerrrreaeervqksLAAEEEAARQR 2008
Cdd:NF041483 282 EKVVA----------------------------------EAKEAAAKQ---------------------LASAESANEQR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2009 -KAALEEVERLKAK-VEEARRLRERAEQESArqlQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQlrge 2086
Cdd:NF041483 307 tRTAKEEIARLVGEaTKEAEALKAEAEQALA---DARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTK---- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2087 aeaarraaeeaeearvQAEREAAQSRRQVEEAERLkqsaeeqaqaraqaqaaaeklRKeaeqeaarRAQAEQAALRQKQA 2166
Cdd:NF041483 380 ----------------ASEDAKATTRAAAEEAERI---------------------RR--------EAEAEADRLRGEAA 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2167 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEElQRLKAEATEAARQR-----SQVEEELFSVRVQM 2241
Cdd:NF041483 415 DQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEG-ERIRGEARREAVQQieeaaRTAEELLTKAKADA 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2242 EELSKL------KARIEAENRALILRDK-DNTQRFLQEEAEKMKQVAEEAAR--LSVAAQEAARLRQLAEEDLAQQRAla 2312
Cdd:NF041483 494 DELRSTataeseRVRTEAIERATTLRRQaEETLERTRAEAERLRAEAEEQAEevRAAAERAARELREETERAIAARQA-- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2313 ekmlkekmQAVQEATRLKAEAELLQQQKELAQEQARrlqEDKEQMAQQLAEETQGfQRTLEAERQRQLEMSAEAERLKLR 2392
Cdd:NF041483 572 --------EAAEELTRLHTEAEERLTAAEEALADAR---AEAERIRREAAEETER-LRTEAAERIRTLQAQAEQEAERLR 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2393 ---VAEMSRAQARAEEDAQRFRKQAEEIGEKLH----------RTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAEL 2459
Cdd:NF041483 640 teaAADASAARAEGENVAVRLRSEAAAEAERLKseaqesadrvRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETL 719
|
810 820
....*....|....*....|.
gi 41322914 2460 EREKEKLQQEAKLLQLKSEEM 2480
Cdd:NF041483 720 GSARAEADQERERAREQSEEL 740
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4046-4084 |
3.74e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.74e-15
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 4046 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4084
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1018-1592 |
4.16e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.04 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1018 EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISL 1097
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1098 VIRGTQGAEEvlraheEQLKEaqavpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVE 1177
Cdd:COG4913 331 QIRGNGGDRL------EQLER---------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1178 VERWRERVAQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVRE--QLRQE 1255
Cdd:COG4913 396 LEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEliEVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1256 QALLEE-IER--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsviqeyvdlrth 1326
Cdd:COG4913 473 EERWRGaIERvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG------------ 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1327 ysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAKAQAE 1391
Cdd:COG4913 539 --KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1392 REAKELQQRMQeEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAErsrlrIEEEIRvvrlQLEAterq 1471
Cdd:COG4913 617 AELAELEEELA-EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE-----LEAELE----RLDA---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1472 rggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL-ASRVKAEAEAAREKQRALQALEELRlqAE 1550
Cdd:COG4913 683 ---SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERF--AA 757
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 41322914 1551 EAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEK 1592
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
42-147 |
1.27e-14 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 72.70 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIAL 111
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 41322914 112 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 147
Cdd:cd21219 72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2245-2760 |
1.28e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2245 SKLKARI-EAENR-----------ALILRDKDNTQRFLQEEAEKmkqvAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL 2311
Cdd:COG1196 168 SKYKERKeEAERKleateenlerlEDILGELERQLEPLERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2312 AEKMLKEkmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqRTLEAERQRQLEM------SAE 2385
Cdd:COG1196 244 LEAELEE---LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEerrrelEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2386 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2465
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2466 LQQEAKLLQLKSEEMQtvqqeqllqetqALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQM 2545
Cdd:COG1196 398 LAAQLEELEEAEEALL------------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2546 EQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLRE-------QLQLLEEQHRAALAHSEE 2618
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavaVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2619 VtASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSAEELQRLAQGHTTVDELARREDVRHYLQG 2698
Cdd:COG1196 546 A-ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 2699 RSSIA-----GLLLKATNEKLSVYAALQRQLLSPGTALILLEAQAASGFLLDPVRNRRLTVNEAVKE 2760
Cdd:COG1196 625 RTLVAarleaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
622-811 |
1.29e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.95 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 622 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 701
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 702 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 781
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 41322914 782 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 811
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3727-3765 |
1.41e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.41e-14
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 3727 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3765
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1105-2053 |
1.48e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1105 AEEVLRAHEEQLKEAQAVpatLPELEATKASLKKLRAQAEaqqpTFDALRDELRGAqEVGERLQQrhgerdveverWRER 1184
Cdd:TIGR02169 175 ALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAE----RYQALLKEKREY-EGYELLKE-----------KEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1185 VAQLlerwQAVLAQTDVRQRELEQLGRQLRyyrESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIER 1264
Cdd:TIGR02169 236 ERQK----EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1265 hgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsESVIQEYVDLRTHYSELttltsqyikfiset 1344
Cdd:TIGR02169 309 ---SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDL-------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1345 lrrmeeeerlaeqqraeeRERLAEVEAALEKQRQlaeahaqaKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRsiqE 1424
Cdd:TIGR02169 370 ------------------RAELEEVDKEFAETRD--------ELKDYREKLEKLKREINELKRELDRLQEELQRLS---E 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1425 ELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqrggAEGELQALRARAEEAEAQKRQAQEEAERLR 1504
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKK------------------QEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1505 RqvqdesqRKRQAEVELAsRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQS 1584
Cdd:TIGR02169 483 K-------ELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVV 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1585 KRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQqkslaqa 1664
Cdd:TIGR02169 555 EDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE------- 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1665 eaekqkeeaereARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA------EQELIRLRAETEQGEQQRQLLEE 1738
Cdd:TIGR02169 628 ------------DIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGIlfsrsePAELQRLRERLEGLKRELSSLQS 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1739 ELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEE---ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1815
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1816 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT-EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 1894
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1895 IEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE--QAELE 1972
Cdd:TIGR02169 856 IENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELS 934
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1973 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQ----RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2048
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
....*
gi 41322914 2049 KRLQA 2053
Cdd:TIGR02169 1015 KKREV 1019
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2809-2847 |
1.49e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.49e-14
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 2809 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 2847
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1639-2482 |
1.97e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1639 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1714
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1715 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1792
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1793 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLAEKLAaigeatrLKTEAEIALKEKEAENERLRR 1872
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINE-------LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1873 LAEDEAFQRRRLEEQAAQHkADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEIlalkasfEKAAAGKAELELEL 1952
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEY-DRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1953 GRIrsnaedtlRSKEQAELEAARQRQLAAEEERRRREAEERVQksLAAEEEAARqrkAALEEVERLKAKVEEARRLRERA 2032
Cdd:TIGR02169 531 GSV--------GERYATAIEVAAGNRLNNVVVEDDAVAKEAIE--LLKRRKAGR---ATFLPLNKMRDERRDLSILSEDG 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2033 EQESARQLqlaqeaaqkrLQAEEK-AHAFAVQQKEQELQQTLQQEQSVLDQLR------------GEAEAARRAAEEAEE 2099
Cdd:TIGR02169 598 VIGFAVDL----------VEFDPKyEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtlegelfeksGAMTGGSRAPRGGIL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2100 ARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAE 2179
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2180 QTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLkaEATEAARQRSQVEEELFSVRvqmEELSKLKARIEAENRALi 2259
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQKL- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2260 lrdkdNTQRFLQEEAEKMKQVAEEaARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQ 2339
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2340 KELAQEQARRLQEDKEQMAQQlaeetqgfqrtLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGE 2419
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-----EEELSLE 954
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2420 KLHRTELATQEKvtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2482
Cdd:TIGR02169 955 DVQAELQRVEEE---IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
48-148 |
2.30e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.95 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 48 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 119
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 41322914 120 KLVNIRNDDIADGNPKLTLGLIWTIILHF 148
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
165-266 |
2.46e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 72.04 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 165 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 244
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 41322914 245 -VDVPQPDEKSIITYVSSLYDAM 266
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3468-3506 |
2.73e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 2.73e-14
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 3468 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 3506
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
163-263 |
3.17e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 72.03 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 242
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 41322914 243 ED-VDVPQPDEKSIITYVSSLY 263
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1109-1585 |
3.19e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.43 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1109 LRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRH---GERDVEVERWRERV 1185
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1186 AQlLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAW-LQDARRRQEQIQamplADSQAVREQLRQEQALLEEIER 1264
Cdd:COG4717 153 ER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ----QRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1265 HGEKVEEcQRFAKQYINAIKDYELQLVTYKAQLEPVAspakkpkVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISET 1344
Cdd:COG4717 228 ELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLG-------LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1345 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrrEEAAVDAQQQKRSIQE 1424
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE-----LEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1425 ELQQLRQSSEAEIQAKARQAEAAErsrlRIEEEIRVVRLQLEA--TERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1502
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1503 LRRQVQDESQRKRQaevelasrvkaeAEAAREKQRALQALEELRLQAEEAERRLRqaeveRARQVQVALETAQRSAEAEL 1582
Cdd:COG4717 451 LREELAELEAELEQ------------LEEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYREER 513
|
...
gi 41322914 1583 QSK 1585
Cdd:COG4717 514 LPP 516
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1385-2470 |
3.44e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.83 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1385 QAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQqlrqsSEAEIQAKARQAEAAERSRLRIEEEIrvvrlq 1464
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEAEEMRARLAARKQELEEI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1465 leaterqrggaegeLQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEVELASRVKAEAEAAREKQRALQALEE 1544
Cdd:pfam01576 77 --------------LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAARQKLQLEKVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1545 LRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKT-AQLERSLQEEHVAVAQLREEAERRAQQQAE 1623
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1624 AERAREEAERELE--RWQLKANE----ALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK-AEEQAVRQRELAEQ 1696
Cdd:pfam01576 220 LQEQIAELQAQIAelRAQLAKKEeelqAALARLEEETAQKNNALKKIRELEAQISELQEDLESERaARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1697 ELEKQRQLAEGT-----AQQRLAA--EQELIRLR----AETEQGEQQRQ-----------LLEEELARLQREAAAATQKR 1754
Cdd:pfam01576 300 ELEALKTELEDTldttaAQQELRSkrEQEVTELKkaleEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKANLEKAK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1755 QELEAELAKVRAEMEVLLASKaraeeesrSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE--AKRQRQLAEEDAARQR 1832
Cdd:pfam01576 380 QALESENAELQAELRTLQQAK--------QDSEHKRKKLEGQLQELQARLSESERQRAELAEklSKLQSELESVSSLLNE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1833 AEAERV-LAEKLAAIG-----------EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdieeRLA 1900
Cdd:pfam01576 452 AEGKNIkLSKDVSSLEsqlqdtqellqEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1901 QLRKasdsELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLrskeqaeLEAARQRQLA 1980
Cdd:pfam01576 528 DMKK----KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLV 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1981 AEEERRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahaf 2060
Cdd:pfam01576 597 SNLEKKQKKF-----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAE------ 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2061 avqqkeqelqqtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSaeeqaqaraqaqAAAE 2140
Cdd:pfam01576 666 -------------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA------------TEDA 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2141 KLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKKfaeQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEA 2220
Cdd:pfam01576 715 KLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQI 786
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2221 TEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMkQVAEEAARLSVAAQEAARLRQL 2300
Cdd:pfam01576 787 DAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDE 865
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2301 AEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEA----ER 2376
Cdd:pfam01576 866 LADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESArqqlER 945
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2377 Q------RQLEMSAEAE-RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDA 2449
Cdd:pfam01576 946 QnkelkaKLQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQA 1025
|
1130 1140
....*....|....*....|.
gi 41322914 2450 ERLREAIAELEREKEKLQQEA 2470
Cdd:pfam01576 1026 EKGNSRMKQLKRQLEEAEEEA 1046
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1105-1608 |
3.48e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1105 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRaqaeaqqptfDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1184
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1185 VAQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQA 1257
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1258 LLEEIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESVIQEYVDLRTHYSELTTLtsqy 1337
Cdd:PRK02224 385 EIEELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT---- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1338 ikfISETLRRMEEEERLAEQ-------QRAEERERLAEVEAALEKQRQLAEAHAQAKAQaereakelqqrmQEEVVRREE 1410
Cdd:PRK02224 435 ---LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE------------VEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1411 AAVDAQQQKRSIqEELQQLRQSSEAEIqakARQAEAAERSRLRIEE-EIRVVRLQLEATERQRGGAEGELQALRARAEEA 1489
Cdd:PRK02224 500 RAEDLVEAEDRI-ERLEERREDLEELI---AERRETIEEKRERAEElRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1490 EAQKRQAQ--EEAERLRR--QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEA--ERRLRQAEVER 1563
Cdd:PRK02224 576 ELNSKLAElkERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDK 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 41322914 1564 AR----QVQVALETAQRSAE-AELQSKRASFAEKTAQLErSLQEEHVAVA 1608
Cdd:PRK02224 656 ERaeeyLEQVEEKLDELREErDDLQAEIGAVENELEELE-ELRERREALE 704
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1073-1602 |
5.74e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1073 LTLGKLEQVRSLSAiylEKLKTISLVIRGTQGAEEVLRAHEEQlKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDA 1152
Cdd:PRK02224 159 LQLGKLEEYRERAS---DARLGVERVLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1153 LRDElrgAQEVGErlqqRHGERDVEVERWRERVAQLlerwQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDARR 1232
Cdd:PRK02224 235 TRDE---ADEVLE----EHEERREELETLEAEIEDL----RETIAET---EREREELAEEVRDLRERLEELEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1233 RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1312
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1313 SESVIQEYVDlrthySELTTLTSQYiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAER 1392
Cdd:PRK02224 381 DRREEIEELE-----EEIEELRERF-GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE-----RVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1393 EAKELQQRMQE-EVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---------EIQAKARQAEAAERSRLRIEEEIRVVR 1462
Cdd:PRK02224 450 EAGKCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEveerleraeDLVEAEDRIERLEERREDLEELIAERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1463 LQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS--RVKAEAEAAREKQRALQ 1540
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIE 609
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1541 ALEELR--LQAEEAERRLRQAEV-ERARQVQVALETAqrsAEAELQSKRASFAEKTAQLERSLQE 1602
Cdd:PRK02224 610 RLREKReaLAELNDERRERLAEKrERKRELEAEFDEA---RIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1069-1934 |
6.04e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 79.34 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1069 SELELTLGKLEQVRslsaiylEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATK--ASLKKLRAQAEAQ 1146
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1147 QPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLaQTDVR--QRELEQLGRQLRYYRESadplg 1224
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGelEAEIASLERSIAEKERE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1225 awLQDARRRQEQIQAmpladsqavreqlrQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPA 1304
Cdd:TIGR02169 317 --LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1305 KKPKvqsgsesviQEYVDLRTHYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA 1384
Cdd:TIGR02169 381 AETR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1385 QAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ 1464
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLS-----------KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1465 LEATERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDESQRKRQaeVELASRVKA------EAEAAREK 1535
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEA--IELLKRRKAgratflPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1536 QRALQALEE-----LRLQAEEAERRLRQA--EVERARQVQVALETAQR--------SAEAELQSKRA-----SFAEKTAQ 1595
Cdd:TIGR02169 587 RRDLSILSEdgvigFAVDLVEFDPKYEPAfkYVFGDTLVVEDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1596 LERSLQEEHVAVAqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQaEEVAQQKSLAQAEAEKQKEEAER 1675
Cdd:TIGR02169 667 LFSRSEPAELQRL----------------------------RERLEGLKRELSSLQ-SELRRIENRLDELSQELSDASRK 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1676 EARRRGKAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQgeqqrqlLEEELARLQreAAAATQKRQ 1755
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSS-LEQEIENVKSELKELEARIEE-------LEEDLHKLE--EALNDLEAR 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1756 ELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1835
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1836 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---ERLAQL--RKASDSEL 1910
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIedPKGEDEEI 946
|
890 900
....*....|....*....|....
gi 41322914 1911 ERQKGLVEDTLRQRRQVEEEILAL 1934
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1330-2224 |
7.54e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 78.68 E-value: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1330 LTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAkAQAEREAKELQQRMQEEV 1405
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQAQIAELRAQL-AKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1406 VRREEAavdaQQQKRSIQEELQQLRQSSEAEIQAKARqaeaAERSRLRIEEEIRVVRLQLEATErqrgGAEGELQALRAR 1485
Cdd:pfam01576 257 AQKNNA----LKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1486 AE-EAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAsrvkaeaEAAREKQRALQALEELRlQAEEAERRLRQAEVERA 1564
Cdd:pfam01576 325 REqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1565 RQVQVALETAQRSAEAELQSKRASFAEktAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANE 1644
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1645 ALRlrlqAEEVAQQKSLAQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRA 1724
Cdd:pfam01576 475 ELL----QEETRQKLNLSTRLRQL---------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1725 ETEQGEQQRQLLEEELARLQREAAAATQKRQELEAElakvraeMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEAG 1798
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA-------YDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQK 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1799 RFRELaeeaarlraLAEEAKRQRQLAEEdaaRQRAEAERVLAEKLA-----AIGEATRLKTEAEIALKEKEAENERLRRL 1873
Cdd:pfam01576 605 KFDQM---------LAEEKAISARYAEE---RDRAEAEAREKETRAlslarALEEALEAKEELERTNKQLRAEMEDLVSS 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1874 AEDEAFQ-------RRRLEEQAAQHKADIEERLAQLRKASDSEL-------------------------ERQKGLVedtl 1921
Cdd:pfam01576 673 KDDVGKNvhelersKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnmqalkaqferdlqardeqgeEKRRQLV---- 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1922 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE 2001
Cdd:pfam01576 749 KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQS 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2002 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSV 2079
Cdd:pfam01576 829 KESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELL 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2080 LDQLRgeaeaARRAAEEAEEARVQAEREAAQSRRQV-EEAERLKQSAEEQAQARAQAQAAAEKLR-KEAEQEAARRAQAE 2157
Cdd:pfam01576 909 NDRLR-----KSTLQVEQLTTELAAERSTSQKSESArQQLERQNKELKAKLQEMEGTVKSKFKSSiAALEAKIAQLEEQL 983
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2158 QAALRQKQAADA--------------EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQK---NLLDEELQRLKAEA 2220
Cdd:pfam01576 984 EQESRERQAANKlvrrtekklkevllQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAsraNAARRKLQRELDDA 1063
|
....
gi 41322914 2221 TEAA 2224
Cdd:pfam01576 1064 TESN 1067
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
163-260 |
7.55e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.49 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 241
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPgLCPDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 41322914 242 PEDVDVPQPDEKSIITYVS 260
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1063-1816 |
1.38e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.09 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1063 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTIslvirgtQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRA 1141
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSL-------HGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1142 QAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQlgRQLRYYRESAD 1221
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1222 PLGAWLQDARRRQEQI---QAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYElQLVTYKAQLE 1298
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1299 pvaspAKKPKVQSGSesviqeyvdlrthySELTTLTSQYIKFISETLRRMEEEERLAeqqRAEERERLAEVEAALekQRQ 1378
Cdd:TIGR00618 390 -----TLTQKLQSLC--------------KELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAEL--CAA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1379 LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAE-AAERSRLRIEEE 1457
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGP 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1458 IRVVRLQLEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDESQRKRQAEVELASRVKAEAE 1530
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSeedvYHQLTSERKQRASLKEQMQEIQQSFSILtqcDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1531 AAREKQRALQAlEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK--------RASFAEKTAQLERSLQE 1602
Cdd:TIGR00618 606 AEDMLACEQHA-LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehalsiRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1603 EHVAVAQLREEAER---RAQQQAEAERAREEAERELERWQLkANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArr 1679
Cdd:TIGR00618 685 MQSEKEQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE-- 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1680 rgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKR 1754
Cdd:TIGR00618 762 ----AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRL 837
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322914 1755 QELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1816
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1713-2481 |
1.97e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 77.52 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1713 LAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEkskQR 1792
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELE---SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1793 LEAEAGRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEIAL-KEKEAENERL 1870
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1871 RRL---AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKglvedtlrQRRQVEEEILALKASFEKAAAGKAE 1947
Cdd:pfam01576 162 SEFtsnLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK--------AKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1948 LELELgrirsnaedtlrSKEQAELEAARQRqlaaeeerrrreaeervqkslaAEEEAArQRKAALEEVERLKAKVEEarr 2027
Cdd:pfam01576 234 LRAQL------------AKKEEELQAALAR----------------------LEEETA-QKNNALKKIRELEAQISE--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2028 LRERAEQESArqlQLAQEAAQKRLQAEEkahafavqqkeqelqqtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAERE 2107
Cdd:pfam01576 276 LQEDLESERA---ARNKAEKQRRDLGEE------------------------LEALKTELEDTLDTTAAQQELRSKREQE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2108 AAQSRRQVEEAERLKQSAEEqaqaraqaqaaaeKLRKEAEQEAARRAQAeqaaLRQKQAADAEMEKHKKFAEQtlrQKAQ 2187
Cdd:pfam01576 329 VTELKKALEEETRSHEAQLQ-------------EMRQKHTQALEELTEQ----LEQAKRNKANLEKAKQALES---ENAE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2188 VEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALilrDKD--- 2264
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDvss 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2265 ------NTQRFLQEEAekmKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLqq 2338
Cdd:pfam01576 466 lesqlqDTQELLQEET---RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL-- 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2339 qkELAQEQARRLQEDKEQMAQQLAEETQGFQR---------------TLEAERQRQLEMSAEAERLKLR--VAEMSRAQA 2401
Cdd:pfam01576 541 --EALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrlqqelddlLVDLDHQRQLVSNLEKKQKKFDqmLAEEKAISA 618
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2402 RAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA-------IAELEREKEKLQQEAKLLQ 2474
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknVHELERSKRALEQQVEEMK 698
|
....*..
gi 41322914 2475 LKSEEMQ 2481
Cdd:pfam01576 699 TQLEELE 705
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
163-263 |
2.74e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 68.90 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 242
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 41322914 243 ED-VDVPQPDEKSIITYVSSLY 263
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2179-2474 |
3.26e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 76.32 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2179 EQTLRQKAQVEQELTTLRLQLEETDHQKNLlDEELQRLKAEATEAARQRSQVEEELFSV--RVQMEELSKLK-------A 2249
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2250 RIEAENRALILRDKDNTQRFLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2329
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2330 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDaQR 2409
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-KR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2410 FRKQAEEIGEKLHRTELAT--------QEKVTLVQTLEIQRQQSDHDAERLREaiAELEREKEKLQQEAKLLQ 2474
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEErkqamieeERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEMEERRRIQ 555
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3061-3099 |
5.01e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.81 E-value: 5.01e-13
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 3061 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 3099
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
66-145 |
6.31e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.00 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 66 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 137
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 41322914 138 LGLIWTII 145
Cdd:cd21223 105 LALLWRII 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1682-1898 |
7.61e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 73.64 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1761
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1762 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1837
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322914 1838 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1898
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
50-151 |
1.93e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 66.88 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 50 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHFQIS 151
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1697-2478 |
2.49e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.85 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1697 ELEKQRQLAEGTAQQRLAAEQELIRLRAE----TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvll 1772
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1773 askaRAEEESRSTSEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEedaarqraeaervLAEKLAAIGEATRL 1852
Cdd:TIGR00618 251 ----AQEEQLKKQQLLKQLRARIE-----ELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1853 KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR-RQVEEEI 1931
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1932 LALKASFEKAAAGKAELELELGRIrsNAEDTLRSKEQAELEAAR-QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2010
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2011 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQEaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQlrgeaEAA 2090
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT-----YAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2091 RRAAEEAEEARVQAEREAAQSRRqvEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEqeaarraqaeqaalRQKQAADAE 2170
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLK--EQMQEIQQSFSILTQCDNRSKEDIPNLQNITV--------------RLQDLTEKL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2171 MEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQrLKAEATEAARQRsqVEEELFSVRVQMEELSKLKar 2250
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA-LHALQLTLTQER--VREHALSIRVLPKELLASR-- 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2251 ieaenralilrdkdntQRFLQEEAEKMKQVAEEAARLsvaAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK 2330
Cdd:TIGR00618 679 ----------------QLALQKMQSEKEQLTYWKEML---AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2331 AEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRF 2410
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2411 RKQAEEIGEKLHRTELATQEKVTLVQTLeiqRQQSDHDAERLReaiaeleREKEKLQQEAKLLQLKSE 2478
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSATLGEI---THQLLKYEECSK-------QLAQLTQEQAKIIQLSDK 877
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
165-260 |
3.03e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 65.87 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 165 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 243
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPgLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 41322914 244 DVDVPQPDEKSIITYVS 260
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1317-2064 |
3.05e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.83 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1317 IQEYVDLRTHYSELTTLTSQYikFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKE 1396
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARE-SD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1397 LQQRMQ--EEVVRREEAAVDAQQQKRSIQEELQQL----RQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLeaTER 1470
Cdd:COG3096 325 LEQDYQaaSDHLNLVQTALRQQEKIERYQEDLEELterlEEQEEVVEEAAEQLAEAEARLE-AAEEEVDSLKSQL--ADY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1471 QRGgaegeLQALRARAeeaeAQKRQAQEEAERLRRQVQDESQRKRQAEVELAsRVKAEAEAAREKQRALqaleELRLQ-A 1549
Cdd:COG3096 402 QQA-----LDVQQTRA----IQYQQAVQALEKARALCGLPDLTPENAEDYLA-AFRAKEQQATEEVLEL----EQKLSvA 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1550 EEAERRLRQA---------EVERARQVQVALETAQRSAEAELQSKRAS-FAEKTAQLERSLQEEHVAVAQLRE---EAER 1616
Cdd:COG3096 468 DAARRQFEKAyelvckiagEVERSQAWQTARELLRRYRSQQALAQRLQqLRAQLAELEQRLRQQQNAERLLEEfcqRIGQ 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1617 RAQQQAEAERAREEAERELERWQLKANEAL--RLRLQAEEV---AQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQR 1691
Cdd:COG3096 548 QLDAAEELEELLAELEAQLEELEEQAAEAVeqRSELRQQLEqlrARIKELAARAPAWL------------AAQDALERLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1692 ELAEQELEKQRQLAEgTAQQRLAAEQELIRLRaetEQGEQQRQLLEEELARLQREAAAATQKRQEL-------------- 1757
Cdd:COG3096 616 EQSGEALADSQEVTA-AMQQLLEREREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALaerlggvllseiyd 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1758 ----------EA------------ELAKVRAEMEVLL-----------------ASKARAEEESRSTSEKSKQRlEAEAG 1798
Cdd:COG3096 692 dvtledapyfSAlygparhaivvpDLSAVKEQLAGLEdcpedlyliegdpdsfdDSVFDAEELEDAVVVKLSDR-QWRYS 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1799 RFREL-----AEEAARLRALAEEAKR-QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEnerlRR 1872
Cdd:COG3096 771 RFPEVplfgrAAREKRLEELRAERDElAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQR----RS 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1873 LAEDEAFQRRRLEEQAAQHKADIEERLAQLRKAsdseLERQKGLVEDTLRQRRQVEEEIL--ALKASFEKAAAGKA--EL 1948
Cdd:COG3096 847 ELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL----LPQANLLADETLADRLEELREELdaAQEAQAFIQQHGKAlaQL 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1949 ELELGRIRSNAE--DTLrskeQAELEAARQRQlaAEEERRRREAEERVQKSLA-AEEEAARQRKAALEEVERLKAKVEEA 2025
Cdd:COG3096 923 EPLVAVLQSDPEqfEQL----QADYLQAKEQQ--RRLKQQIFALSEVVQRRPHfSYEDAVGLLGENSDLNEKLRARLEQA 996
|
810 820 830
....*....|....*....|....*....|....*....
gi 41322914 2026 RRLRERAeQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2064
Cdd:COG3096 997 EEARREA-REQLRQAQAQYSQYNQVLASLKSSRDAKQQT 1034
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1721-2275 |
3.54e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1721 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1800
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1801 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKE---AENERLRRLA 1874
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1875 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAEL 1948
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1949 ELELGRIRSNAEDtLRSKE---QAELEAARQR-----------------QLAAEEERRRREAEERVQKS-LAAEEEAARQ 2007
Cdd:PRK02224 411 EDFLEELREERDE-LREREaelEATLRTARERveeaealleagkcpecgQPVEGSPHVETIEEDRERVEeLEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2008 RKAALEE-VERLKAKVEEARRLRERAEQESArqlqLAQEAAQKRLQAEEKahafavQQKEQELQQTLQQEQSVLDQLRGE 2086
Cdd:PRK02224 490 EVEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEK------RERAEELRERAAELEAEAEEKREA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2087 AEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSaeeqaqaraqaqaaaeklrkeaeQEAARRAQAEQAALRQKQA 2166
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL-----------------------LAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2167 ADAEMEKHKKFAEQTLRQ-KAQVEQELTTLRlqLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELS 2245
Cdd:PRK02224 617 ALAELNDERRERLAEKRErKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
570 580 590
....*....|....*....|....*....|.
gi 41322914 2246 KLKARIEA-ENRALILRDkdntqrfLQEEAE 2275
Cdd:PRK02224 695 ELRERREAlENRVEALEA-------LYDEAE 718
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4315-4353 |
4.21e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.21e-12
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 4315 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4353
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
165-264 |
4.50e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.05 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 165 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 240
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 41322914 241 DPEDVdVPQPDEKSIITYVSSLYD 264
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1360-2296 |
5.63e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.68 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1360 AEERERLaeVEAALEKQRQLAEAHAQAkaqaeREAKELQQRMQEEVvrreeaavdAQQQKRsiQEELQQLRQSSE---AE 1436
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQL-----AEEQYRLVEMAREL---------EELSAR--ESDLEQDYQAASdhlNL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1437 IQAKARQAEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrKRQ 1516
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1517 AEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAElqskrasfaEKTAQL 1596
Cdd:COG3096 404 ALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---------AARRQF 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1597 ERSLQeehvAVAQLREEAERRaqqqaeaerareeaerelERWQlKANEALR----LRLQAEEVAQQKSlaqaeaekqkee 1672
Cdd:COG3096 475 EKAYE----LVCKIAGEVERS------------------QAWQ-TARELLRryrsQQALAQRLQQLRA------------ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1673 aerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQREAAAATQ 1752
Cdd:COG3096 520 ------QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1753 KRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ 1822
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1823 LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAE-----------IALKEKEAENERLRRL----------------AE 1875
Cdd:COG3096 666 PGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYfsalygparhaIVVPDLSAVKEQLAGLedcpedlyliegdpdsFD 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1876 DEAFQRRRLEEQAAQHKADI------------------EERLAQLRKASDSELERQKGLVEDTLRQRRQVE--EEILALK 1935
Cdd:COG3096 746 DSVFDAEELEDAVVVKLSDRqwrysrfpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQafSQFVGGH 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1936 ASFEKAAAGKAELElELGRIRSNAEDTLRSKEQAE------LEAARQR---------QLAAEEERRRREAEERVQKSLAA 2000
Cdd:COG3096 826 LAVAFAPDPEAELA-ALRQRRSELERELAQHRAQEqqlrqqLDQLKEQlqllnkllpQANLLADETLADRLEELREELDA 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2001 EEEAAR---QRKAALEEVERLkakveeARRLRERAEQESARQLQLAQ-EAAQKRLQAEEKAHAFAVQQKE----QELQQT 2072
Cdd:COG3096 905 AQEAQAfiqQHGKALAQLEPL------VAVLQSDPEQFEQLQADYLQaKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2073 LQQEQSVLDQLRgeaeaarraaeeaeEARVQAEREAAQSRRQVEEA-ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAA 2151
Cdd:COG3096 979 LGENSDLNEKLR--------------ARLEQAEEARREAREQLRQAqAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2152 RRAqaeqaalrqkqAADAEMEkhkkfaEQTLRQKAQVEQELTTLRLqleetdhQKNLLDEELQRLKAEATEAARQRSQVE 2231
Cdd:COG3096 1045 LGV-----------QADAEAE------ERARIRRDELHEELSQNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2232 EELFSVRvqmEELSKLKARIEAENRalILRDKD-----NTQRFLQEEAEKMKQVAEE---AARLSVAAQEAAR 2296
Cdd:COG3096 1101 RDYKQER---EQVVQAKAGWCAVLR--LARDNDverrlHRRELAYLSADELRSMSDKalgALRLAVADNEHLR 1168
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
165-265 |
6.03e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 65.07 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 165 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 244
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 41322914 245 VdVPQPDEKSIITYVSSLYDA 265
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3137-3175 |
6.86e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 6.86e-12
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 3137 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 3175
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1105-1836 |
7.37e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.29 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1105 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQ--RHGERdveVERWR 1182
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK---IERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1183 ERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLRQEQALLEEI 1262
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1263 ERHGEKVEECQRFAKQYINAIKDYELQLVT-------YKAQ-------LEPVASPAKKPKVQSGSESVIQEYVDLRTHYS 1328
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEEVLELEQklsvadaARRQfekayelVCKIAGEVERSQAWQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1329 ELTTLTSQYiKFISETLRRMEEEERLAEQ------QRAEERERLAEVEAALEKQR----QLAEAHAQAKAQAEREAKELQ 1398
Cdd:COG3096 513 RLQQLRAQL-AELEQRLRQQQNAERLLEEfcqrigQQLDAAEELEELLAELEAQLeeleEQAAEAVEQRSELRQQLEQLR 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1399 QRMQEeVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaERSRLRIEEEIRVVRLQLEATER---QRGGA 1475
Cdd:COG3096 592 ARIKE-LAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQALESQIErlsQPGGA 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1476 E-GELQALRAR-----------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQR 1513
Cdd:COG3096 670 EdPRLLALAERlggvllseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVF 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1514 KRQaEVELASRVKAE---------------AEAAREKQralqaLEELRLQAEE-----AERRLRQAEVER---------A 1564
Cdd:COG3096 750 DAE-ELEDAVVVKLSdrqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1565 RQVQVALETaqrSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRA-------QQQAEAERAREEAERELER 1637
Cdd:COG3096 824 GHLAVAFAP---DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1638 WQLKANEALR-LRLQAEEVAQ-QKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLA 1714
Cdd:COG3096 901 ELDAAQEAQAfIQQHGKALAQlEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLG 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1715 AEQELI-RLRAETEQGEQQRQLLEEELARLQREAAAATQKR--------------QELEAELakvrAEMEVLLAskARAE 1779
Cdd:COG3096 981 ENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAE 1054
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1780 EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1836
Cdd:COG3096 1055 ERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2733-2771 |
7.49e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.49e-12
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 2733 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2771
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3970-4008 |
9.94e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 9.94e-12
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 3970 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4008
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3803-3841 |
1.05e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.05e-11
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 3803 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3841
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1692-2542 |
1.96e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.97 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1692 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAeME 1769
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1770 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1849
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1850 TRLktEAEIALKEKEAENERLRRLAEDEafQRRRLEEQ---------------AAQH--KADIEERLAQLRKASDSELER 1912
Cdd:pfam01576 267 REL--EAQISELQEDLESERAARNKAEK--QRRDLGEElealkteledtldttAAQQelRSKREQEVTELKKALEEETRS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1913 QKGLVEDTLRQRRQVEEEilaLKASFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEAARQRQlaaeeerrrrE 1989
Cdd:pfam01576 343 HEAQLQEMRQKHTQALEE---LTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEHKRK----------K 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1990 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARqlqLAQEAAQKRLQaeekahafaVQQKEQEL 2069
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKDVSSLESQ---------LQDTQELL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2070 QQTLQQEQSVLDQLRgeaeaarraaeeaeearvQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQE 2149
Cdd:pfam01576 478 QEETRQKLNLSTRLR------------------QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2150 AARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLeetDHQKNLL----------DEELQRLKAE 2219
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVsnlekkqkkfDQMLAEEKAI 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2220 ATEAARQRSQVEEE-------LFSVRVQMEELSKLKARIEAENRAL------ILRDKDNTQRFLQEeAEKMKQVAEeaar 2286
Cdd:pfam01576 617 SARYAEERDRAEAEareketrALSLARALEEALEAKEELERTNKQLraemedLVSSKDDVGKNVHE-LERSKRALE---- 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2287 lsvaaQEAARLR-QLAE-EDLAQQRALAEKMLKEKMQAvqeatrLKAEAEL-LQQQKELAQEQARRLQEDKEQMAQQLAE 2363
Cdd:pfam01576 692 -----QQVEEMKtQLEElEDELQATEDAKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLVKQVRELEAELED 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2364 ETQgfQRTLEAERQRQLEMsaEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQ 2443
Cdd:pfam01576 761 ERK--QRAQAVAAKKKLEL--DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLK 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2444 QSDHDAERLREAIAELEREKEKLQQEAKLLQlksEEMQtvqqeqllqetqalqqSFLSEKDSLLQRERFIEQEKAKLEQL 2523
Cdd:pfam01576 837 NLEAELLQLQEDLAASERARRQAQQERDELA---DEIA----------------SGASGKSALQDEKRRLEARIAQLEEE 897
|
890
....*....|....*....
gi 41322914 2524 FQDEVAKAQQLREEQQRQQ 2542
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKST 916
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1477-2055 |
2.20e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1477 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAevELASRVKAEAEAAREKQRALQALEELRLQAEEA--ER 1554
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1555 RLRQAEVERARQVQVALETA---QRSAEAELQSKRASFAEKTAQLERSLQEehvavaqlreeaerraqqqAEAERAREEA 1631
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------------------LEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1632 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE--REARRRGKAEEQAVRQRELA---EQELEKQRQLAE 1706
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAaelESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1707 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR---AEMEVLLA---------- 1773
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqp 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1774 ----SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAARQRAEAERVLAEKLAAIG 1847
Cdd:PRK02224 461 vegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1848 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---------ERLAQLRKASDSELERQKGLVE 1918
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1919 ------DTLRQRRqveEEILALKASFEKAAAGKAELElelgriRSNAEDTLR--SKEQAELEAARQRqlaaeeerrrrea 1990
Cdd:PRK02224 621 lnderrERLAEKR---ERKRELEAEFDEARIEEARED------KERAEEYLEqvEEKLDELREERDD------------- 678
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1991 eerVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2055
Cdd:PRK02224 679 ---LQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2162-2364 |
2.47e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2162 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEEL---FSVR 2238
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaelLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2239 VQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2318
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 41322914 2319 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEE 2364
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1410-1610 |
2.52e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1410 EAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA 1489
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1490 EAQKRQAQEEAERLRRQVQdesQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEVERA 1564
Cdd:COG4942 96 RAELEAQKEELAELLRALY---RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 41322914 1565 RQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1610
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1158-1581 |
2.76e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 70.37 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1158 RGAQEvgERLQQRHGERDVEVERWR---------ERVAQLLERW-------------QAVLAQTDVR----QRELEQLGR 1211
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRrselERELAQHRA 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1212 QLRYYRESADPLGAWLQDARRRQEQiqAMPLADSQAvreqlrqeQALLEEIERHGEKVEECQRFAKQYINAIkdyelqlv 1291
Cdd:COG3096 858 QEQQLRQQLDQLKEQLQLLNKLLPQ--ANLLADETL--------ADRLEELREELDAAQEAQAFIQQHGKAL-------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1292 tykAQLEPVASPAKKPKVQSgsESVIQEYVDLrthySELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEE--R 1363
Cdd:COG3096 920 ---AQLEPLVAVLQSDPEQF--EQLQADYLQA----KEQQRRLKQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEklR 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1364 ERLAEVEAALEKQRQLAEAHAQAKAQAereakelQQRMQEEVVRREEAavdaQQQKRSIQEELQQLrqsseaEIQAKARQ 1443
Cdd:COG3096 991 ARLEQAEEARREAREQLRQAQAQYSQY-------NQVLASLKSSRDAK----QQTLQELEQELEEL------GVQADAEA 1053
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1444 AEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQ 1516
Cdd:COG3096 1054 EERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERRL 1133
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1517 AEVELasrvkaeaeaarekqrALQALEELRLQAEEAERRLRQAeVERARQVQVALETAQRSAEAE 1581
Cdd:COG3096 1134 HRREL----------------AYLSADELRSMSDKALGALRLA-VADNEHLRDALRLSEDPRRPE 1181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1128-1509 |
3.04e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1128 ELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWqavlAQTDVRQRELE 1207
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI----AQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1208 QLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQAlleEIERHGEKVEECQRFAKQYINAIKDYE 1287
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1288 LQLVTYKAQLEpvaspaKKPKVQSGSESVIQEYvdlrthyselttltsqyikfiSETLRRMEEEERLAEQQRAEERERLA 1367
Cdd:TIGR02168 838 RRLEDLEEQIE------ELSEDIESLAAEIEEL---------------------EELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1368 EVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAA 1447
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1448 ERSRLRIEEEI-RVVRLQLEATErqrggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1509
Cdd:TIGR02168 971 RRRLKRLENKIkELGPVNLAAIE--------EYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1430-2056 |
3.45e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.25 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1430 RQSSEAEIQAKARQAEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1503
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1504 RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAeLQ 1583
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1584 SKRASFAEKTAQLERSLQEEHVA-VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1662
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1663 QAEAEKQKEEAEREARRRGKAEEQAV-RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelA 1741
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE--L 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1742 RLQREAAAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1815
Cdd:pfam12128 526 ELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1816 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 1895
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1896 EERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEkaaagkAELELELGRIRSN--AEDTLRSKEQAELEA 1973
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSGAKAELKALET 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1974 ARQRQLAAEEERRRREAEERVQ-KSLAAEEEAARQRKAA------------LEEVERLKAKVEEARRLRERAEQESARQl 2040
Cdd:pfam12128 755 WYKRDLASLGVDPDVIAKLKREiRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAISELQQQLARL- 833
|
650
....*....|....*.
gi 41322914 2041 qlaQEAAQKRLQAEEK 2056
Cdd:pfam12128 834 ---IADTKLRRAKLEM 846
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
43-142 |
7.51e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 62.44 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 43 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 114
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 41322914 115 RHRQVKLVNIRNDDIADGNPKLTLGLIW 142
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1786-2523 |
8.06e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1786 SEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEEDaaRQRAEAERVLAEKLAAIgEATRLKTEAEIALKEK-- 1863
Cdd:TIGR02169 170 RKKEKALEELE-----EVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKea 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1864 -EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAA 1942
Cdd:TIGR02169 242 iERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1943 AGKAELELELGRIRSNAEDtlrSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR---KAALEEVERLK 2019
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2020 AKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAA 2090
Cdd:TIGR02169 399 REINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2091 RraaeeaeearvQAEREAAQSRRQVEEAE-RLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA 2169
Cdd:TIGR02169 479 D-----------RVEKELSKLQRELAEAEaQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2170 EME-----------------KHKKFAEQTLRQKAQVEQELTTLRLQLEE--TDHQKNLLDEELQRlkAEATEAARQRSQV 2230
Cdd:TIGR02169 548 RLNnvvveddavakeaiellKRRKAGRATFLPLNKMRDERRDLSILSEDgvIGFAVDLVEFDPKY--EPAFKYVFGDTLV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2231 EEELFSVRVQMeelskLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRA 2310
Cdd:TIGR02169 626 VEDIEAARRLM-----GKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL--SSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2311 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLK 2390
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2391 LRVAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEA 2470
Cdd:TIGR02169 779 EALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2471 KLLQLKSEEMQTVQQEQLLQETQalqqsfLSEKDSLLQRERfiEQEKAKLEQL 2523
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRD------LESRLGDLKKER--DELEAQLREL 901
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1363-1888 |
8.65e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 68.73 E-value: 8.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1363 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR 1442
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1443 QAEAAERSRLRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEV 1519
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1520 ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERS 1599
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1600 LQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARR 1679
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1680 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEA 1759
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1760 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1839
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 41322914 1840 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1888
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1336-1975 |
9.09e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.61 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1336 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDA 1415
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1416 QQQKRSIQEELQQLRQ---SSEAEIQA-KARQAEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1485
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1486 --AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEVELASrVKAEAEAAREKQRALQAleelrlQAEEAERRLRQAEVE 1562
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEITG-LTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1563 RARQVQvALETAQRSAEAELQSKRASFAEKTAQLERSLQeehVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1642
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1643 NEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1713
Cdd:pfam15921 391 KE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1714 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRQELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1789
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1790 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLAEKLAAIGEATRL-KTEAEIALKEK 1863
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1864 EAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASDSELERQKGL--VEDTLRQRRQVEEEILALKAS 1937
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDYEVLKRN 682
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 41322914 1938 F----EKAAAGKAELELELGRIRSNAE---DTLRSKEQAELEAAR 1975
Cdd:pfam15921 683 FrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMK 727
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1685-2118 |
9.85e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR--------QLLEEELARLQREAAAATQKRQE 1756
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1757 L--------------EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR----------- 1811
Cdd:COG4913 364 LeallaalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparll 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1812 ----ALAEEAKRQR----------QLAEEDAARQRAeAERVL-------------AEKLAAIGEATRLKTEAEIALKEKE 1864
Cdd:COG4913 444 alrdALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLggfaltllvppehYAAALRWVNRLHLRGRLVYERVRTG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1865 AENERLRRLAED-------------EAFQRRRLEEQAAQHKADIEERLAQLRKA-------SDSELERQKG--------- 1915
Cdd:COG4913 523 LPDPERPRLDPDslagkldfkphpfRAWLEAELGRRFDYVCVDSPEELRRHPRAitragqvKGNGTRHEKDdrrrirsry 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1916 -LVEDTLRQRRQVEEEILALKASFEKAAAGKAELelelgrirsnaedtlrskeQAELEAARQRQLAAEEERRRREAEERV 1994
Cdd:COG4913 603 vLGFDNRAKLAALEAELAELEEELAEAEERLEAL-------------------EAELDALQERREALQRLAEYSWDEIDV 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1995 QkSLAAEEEAARQRKAALE----EVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQ 2070
Cdd:COG4913 664 A-SAEREIAELEAELERLDassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 41322914 2071 QTLQQEQSVLDQLRGEAEAARRAAEEA--EEARVQAEREAAQSRRQVEEA 2118
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELREnlEERIDALRARLNRAEEELERA 792
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1317-1815 |
1.09e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1317 IQEYVDLRTHYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKE 1396
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1397 LQQRMQeevvrreeAAVDAQQqkrSIQEELQQlrqsSEAEIQAKARQAEAAErsrlRIEEEIRVVRlqlEATERQrggae 1476
Cdd:PRK04863 326 LEQDYQ--------AASDHLN---LVQTALRQ----QEKIERYQADLEELEE----RLEEQNEVVE---EADEQQ----- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1477 gelqalraraEEAEAQKRQAQEEAERLRRQVQD-----ESQRKR----QAEVELASRVKA-------EAEAAREKQRALQ 1540
Cdd:PRK04863 379 ----------EENEARAEAAEEEVDELKSQLADyqqalDVQQTRaiqyQQAVQALERAKQlcglpdlTADNAEDWLEEFQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1541 A-LEELRLQAEEAERRLRQAEvERARQVQVALETAQRSAeAELQSKRASfaEKTAQLERSLQEEHVAVAQLreeaerraq 1619
Cdd:PRK04863 449 AkEQEATEELLSLEQKLSVAQ-AAHSQFEQAYQLVRKIA-GEVSRSEAW--DVARELLRRLREQRHLAEQL--------- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1620 qqaeaeRAREEAERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELE 1699
Cdd:PRK04863 516 ------QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---------------------DEDELEQLQEELEARLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1700 KQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQREAAAATQKRQELEAELAKvraemevlLASKA 1776
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------LLERE 640
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 41322914 1777 RAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1815
Cdd:PRK04863 641 RELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1533-1885 |
1.16e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 68.23 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1533 REKQRALQALEELRLQaEEAERRLRqaEVERARQvqvaLETAQRSAEAELQSKRASFAEKtaqlERSLQEEHvavaqlre 1612
Cdd:pfam17380 287 RQQQEKFEKMEQERLR-QEKEEKAR--EVERRRK----LEEAEKARQAEMDRQAAIYAEQ----ERMAMERE-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1613 eaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRrgKAEEQAVRQRE 1692
Cdd:pfam17380 348 --------------------RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1693 LaeQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQ-QRQLLEEELARLQREAAAATQKRQ-------ELEAELAKV 1764
Cdd:pfam17380 406 I--LEEERQRKIQQ--------QKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1765 RAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLAE 1841
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 41322914 1842 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1885
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1682-2059 |
1.40e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1761
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELE-AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1762 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE------EDAARQRAEA 1835
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEeeleqlENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1836 ERVLAEKLAAIGEATRLKTEAEIAL------------------------------KEKEAENERLRRLAEDEAFQRRRLE 1885
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSllsliltiagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1886 EQAAQHKADIEERLAQLRKASDSELERQKGLVE-DTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDTLR 1964
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1965 SKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQL 2042
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQ 476
|
410
....*....|....*..
gi 41322914 2043 AQEAAQKRLQAEEKAHA 2059
Cdd:COG4717 477 ELEELKAELRELAEEWA 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1685-1922 |
1.43e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAaatqkrqELEAELAKV 1764
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELA-------RLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1765 RAEMEVLLASKARAEEESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1840
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREierlERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1841 EKLAAIGEATRLKTEAEIALKEKEAENERLRRlaedeafQRRRLEeqaaQHKADIEERLAQLRKAsdseLERQKGLVEDT 1920
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEA-------EIASLE----RRKSNIPARLLALRDA----LAEALGLDEAE 459
|
..
gi 41322914 1921 LR 1922
Cdd:COG4913 460 LP 461
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1329-1546 |
1.44e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 66.82 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1329 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAEREA 1394
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1395 KELQQRMQEEVVRRE-EAAVDAQQQKRsiQEELQQlrqssEAEIQAKARQAEAAERSRLRIEEEirvvrlqLEATERQRg 1473
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANA--EREVQR-----QLEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1474 gAEGELQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1546
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1520-2055 |
1.46e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 67.96 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1520 ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVE-RARQVQVALETAQRSAEAELQSKRAS---------- 1588
Cdd:COG3899 713 RRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppasa 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1589 FAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEK 1668
Cdd:COG3899 793 RAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLA 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1669 QKEEAEREARRrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1748
Cdd:COG3899 873 LAAAAAAAAAA---AALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAA 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1749 AATQKRQELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1828
Cdd:COG3899 950 AAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALA 1016
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1829 ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDS 1908
Cdd:COG3899 1017 AALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAA 1096
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1909 ELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRR 1988
Cdd:COG3899 1097 LAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALA 1176
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1989 EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2055
Cdd:COG3899 1177 ALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1881-2618 |
1.74e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 67.69 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1881 RRRLEEQAA--QHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSN 1958
Cdd:pfam02463 155 RLEIEEEAAgsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1959 AEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2038
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2039 QLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRgeaeaarraaeeaeearvQAEREAAQSRRQV 2115
Cdd:pfam02463 315 KLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK------------------LQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2116 EEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2195
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2196 RLQLEEtdhqKNLLDEELQRLKAEATEAARQRSQVEEElfSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAE 2275
Cdd:pfam02463 457 ELKLLK----DELELKKSEDLLKETQLVKLQEQLELLL--SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2276 KmkqvaeEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ----EQARRLQ 2351
Cdd:pfam02463 531 L------GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSiavlEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2352 EDKEQMAQQLAEETQGFQRTLEAERQRQLEMSaeaERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2431
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2432 VTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQalQQSFLSEKDSLLQRER 2511
Cdd:pfam02463 682 QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ--KIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2512 FIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGvrrkqEELQQLEQQRRQQEELL 2591
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL-----EEEQLLIEQEEKIKEEE 834
|
730 740
....*....|....*....|....*..
gi 41322914 2592 AEENqRLREQLQLLEEQHRAALAHSEE 2618
Cdd:pfam02463 835 LEEL-ALELKEEQKLEKLAEEELERLE 860
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1105-1606 |
2.15e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.67 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1105 AEEVLRAHEEQLKEAQAVPATL-PELEATKASLKKLRAQAEAqqptfdalrdeLRGAQEVGERLQQRHGERDVEVERWRE 1183
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELrQQLEQLRARIKELAARAPA-----------WLAAQDALERLREQSGEALADSQEVTA 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1184 RVAQLLERWQAVLAQTD---VRQRELEQLGRQLRYYRESADP--------LGAWL----------QDA----RRRQEQIQ 1238
Cdd:COG3096 631 AMQQLLEREREATVERDelaARKQALESQIERLSQPGGAEDPrllalaerLGGVLlseiyddvtlEDApyfsALYGPARH 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1239 AMPLADSQAVREQLRQEQALLEE---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKV 1309
Cdd:COG3096 711 AIVVPDLSAVKEQLAGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEEL 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1310 QSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQ 1389
Cdd:COG3096 791 RAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLD 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1390 AEREAKELQQRMQEEVV---------RREEAAVD---AQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERSRLRIE 1455
Cdd:COG3096 868 QLKEQLQLLNKLLPQANlladetladRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAK 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1456 EEIRVVRLQLEATE--RQR------GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKA 1527
Cdd:COG3096 948 EQQRRLKQQIFALSevVQRrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS 1027
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1528 EAEAAREKQRALQALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--KRASFAEKTAQLER 1598
Cdd:COG3096 1028 RDAKQQTLQELEQELEELGVQAdAEAEERARirrdelHEELSQNRSRRSQLEKQLTRCEAEMDSlqKRLRKAERDYKQER 1107
|
....*...
gi 41322914 1599 SLQEEHVA 1606
Cdd:COG3096 1108 EQVVQAKA 1115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
924-1544 |
3.05e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 924 EEQRQALHSLELHYQAFLRDSQDAggfgpeDRLMAEREYgscsHHYQQLLQSLEQGAQEESRCQRcisELKDIRLQLEAC 1003
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERL------AELEYLRAA----LRLWFAQRRLELLEAELEELRA---ELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1004 ETRtvhrlrlpldkeparecaQRIAEQQKAQAEVEGLGKGVARLSAeaekvlalpepspaaptLRSELELTLGKLEQVRS 1083
Cdd:COG4913 315 EAR------------------LDALREELDELEAQIRGNGGDRLEQ-----------------LEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1084 LSAIYLEKLKTISLVIRGTqgaeevlrahEEQLKEAQA-VPATLPELEATKASLKKLRAQAEAQqptFDALRDELRGAQE 1162
Cdd:COG4913 360 RRARLEALLAALGLPLPAS----------AEEFAALRAeAAALLEALEEELEALEEALAEAEAA---LRDLRRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1163 VGERLQQRHGERDVEVERWRERVAQLL--------------------ERWQAVLaqtdvrQRELEQLGRQL----RYYRE 1218
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeERWRGAI------ERVLGGFALTLlvppEHYAA 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1219 SAdplgAWLQDARRRQE-QIQAMPLADSQAVREQLrQEQALLEEIERhgeKVEECQRFAKQYINAIKDYELqlvtykaql 1297
Cdd:COG4913 501 AL----RWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLDF---KPHPFRAWLEAELGRRFDYVC--------- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1298 epVASPAkkpkvqsgsesviqeyvDLRTHYSELTT--LTSQyikfiSETLRRMEEEERL---------AEQQRAEERERL 1366
Cdd:COG4913 564 --VDSPE-----------------ELRRHPRAITRagQVKG-----NGTRHEKDDRRRIrsryvlgfdNRAKLAALEAEL 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1367 AEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmqEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeAEIQAKARQAEA 1446
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1447 AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE--AERLRRQVQDESQRKRQAEVElASR 1524
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERELRENLE-ERI 775
|
650 660
....*....|....*....|
gi 41322914 1525 VKAEAEAAREKQRALQALEE 1544
Cdd:COG4913 776 DALRARLNRAEEELERAMRA 795
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4391-4429 |
3.16e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.72 E-value: 3.16e-10
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 4391 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 4429
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1742-2479 |
3.40e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.92 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1742 RLQREAAAATQKRQELEAELAKVRAEMEVLLASKA-------RAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL- 1813
Cdd:TIGR00618 53 KLPRRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIyrvhrtlRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVi 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1814 -------AEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR 1883
Cdd:TIGR00618 133 hdllkldYKTFTRVVLLPQGEFAQflkAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1884 LEEQAAQHKADIEERLAQLRKASDSELERQKGLVE--DTLRQRRQVEEEILALKASFEKAAAGKAELEL---ELGRIRSN 1958
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEEtqeRINRARKA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1959 AEDTLRSKEQAELEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2038
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRA-----KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2039 QLQLAQeaaqkrlQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEA 2118
Cdd:TIGR00618 368 REISCQ-------QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2119 ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQ------------------ 2180
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscihpnparqdi 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2181 -----TLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEA-------ARQRSQVEEELFSVRVQMEEL---- 2244
Cdd:TIGR00618 521 dnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsfsilTQCDNRSKEDIPNLQNITVRLqdlt 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2245 ---SKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQE---------AARLRQLAEEDLAQQRA 2310
Cdd:TIGR00618 601 eklSEAEDMLACEQHALLrkLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqervrehALSIRVLPKELLASRQL 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2311 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEdkeqmaQQLAEETQGFQRTLEAERQRQLEMSAEAER-- 2388
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE------IENASSSLGSDLAAREDALNQSLKELMHQArt 754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2389 -LKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAtQEKVTLVQTLEIQRQQ-----------SDHDAERLREAI 2456
Cdd:TIGR00618 755 vLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEIGQeipsdedilnlQCETLVQEEEQF 833
|
810 820
....*....|....*....|...
gi 41322914 2457 AELEREKEKLQQEAKLLQLKSEE 2479
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYEE 856
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
49-145 |
3.73e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 60.28 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 49 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 114
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 41322914 115 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 145
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
526-715 |
4.23e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.85 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 526 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 602
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 603 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 679
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 41322914 680 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 715
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1106-1296 |
5.51e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.46 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1106 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1185
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1186 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1264
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|..
gi 41322914 1265 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1296
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1355-1553 |
6.88e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.44 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1355 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREeaavdAQQQKrsiQEELQQLRQSS 1433
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1434 EAEIQAKARQAEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDESQR 1513
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41322914 1514 KRQAEV-ELASRVKAEAEAAREKQRALQALEELRLQAEEAE 1553
Cdd:PRK09510 218 KAAAEAkAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1701-1915 |
8.67e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1701 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEE 1780
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1781 ESRSTSEKSKQRLEA--EAGRFRELA--------EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1850
Cdd:COG4942 98 ELEAQKEELAELLRAlyRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1851 RLKTEAEIALKE----KEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKASDSELERQKG 1915
Cdd:COG4942 178 ALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERTPA 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1107-1884 |
1.13e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1107 EVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqptfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERva 1186
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1187 qlLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLRQEQALLE----EI 1262
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1263 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKK-------PKVQSGSESVIQEYVDLRTHYSELTT 1332
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1333 LTSQYikfisETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQA-------EREAKELQ 1398
Cdd:PRK04863 518 LRMRL-----SELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1399 QRMQEEVVRREE--AAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATErQRGGAE 1476
Cdd:PRK04863 593 ARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSE 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1477 GE-LQALRARA--------------EEA-------------------EAQKRQAQE-----------------------E 1499
Cdd:PRK04863 672 DPrLNALAERFggvllseiyddvslEDApyfsalygparhaivvpdlSDAAEQLAGledcpedlyliegdpdsfddsvfS 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1500 AERLRRQV-QDESQRK----RQAEVELASRvkaeaeAAREKQralqaLEELRLQAEEAERRLRQAEVERaRQVQVALETA 1574
Cdd:PRK04863 752 VEELEKAVvVKIADRQwrysRFPEVPLFGR------AAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAF 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1575 QR------------SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlKA 1642
Cdd:PRK04863 820 SRfigshlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA----DR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1643 NEALRLRLQAEEVAQQkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQ--------------LAEG 1707
Cdd:PRK04863 896 VEEIREQLDEAEEAKR-FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDyQQAQQTQRDAKQqafaltevvqrrahFSYE 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1708 TAQQRLAAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRQELEAELAK--VRAEMEV 1770
Cdd:PRK04863 975 DAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGA 1054
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1771 LLASKARAEE---------ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAARQRAEAER 1837
Cdd:PRK04863 1055 EERARARRDElharlsanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERR 1133
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1838 VLAEKLAAiGEATRLKTEAEI---ALKEKEAENERLR---RLAEDEAFQRRRL 1884
Cdd:PRK04863 1134 LHRRELAY-LSADELRSMSDKalgALRLAVADNEHLRdvlRLSEDPKRPERKV 1185
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2272-2713 |
1.37e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2272 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2348
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2349 RLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKlRVAEMSRAQ--ARAEE--DAQRFRKQAEEIGEKLHRT 2424
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdaKKAEAvkKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2425 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQalQQSFLSEKD 2504
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKADEAKKKAEEA--KKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2505 SLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvaSMEEARRRQHEAEEGVRRKQEELQQLEQqr 2584
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK--KKEEAKKKADAAKKKAEEKKKADEAKKK-- 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2585 rqqeellAEENQRLREQLQLLEEQHRAA---LAHSEEVTASQVAATKtlpngrdaldgpaaeAEPEHSFDGLRRKVSAQR 2661
Cdd:PTZ00121 1400 -------AEEDKKKADELKKAAAAKKKAdeaKKKAEEKKKADEAKKK---------------AEEAKKADEAKKKAEEAK 1457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 41322914 2662 LQEAGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLLLKATNEK 2713
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
42-148 |
1.51e-09 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 58.75 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 42 DERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDYLR 115
Cdd:cd21222 9 EAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELME 88
|
90 100 110
....*....|....*....|....*....|...
gi 41322914 116 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 148
Cdd:cd21222 89 DAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1371-1595 |
1.66e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 63.29 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1371 AALEKQRQLAEAHAQAKAQAEREAKELQQrmQEEVvrREEAAVDAQQQKRSIQEELQ---QLRQSSEAEIQAKARQAEAA 1447
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAaqeQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1448 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEVELASRVK 1526
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1527 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1595
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1345-1559 |
1.71e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1345 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQE 1424
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1425 ---ELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1501
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1502 RLRRQVqdesQRKRQAEVELASRVKAEAEAAREKQRALQALEEL--RLQAEEAERRLRQA 1559
Cdd:COG4942 189 ALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTP 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1106-1765 |
1.74e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.43 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1106 EEVLRAHEEQLKE-----AQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVER 1180
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1181 WRERV-------AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARR-RQEQIQAmPLADSQAVReQL 1252
Cdd:pfam01576 417 LQARLseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQElLQEETRQ-KLNLSTRLR-QL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1253 RQEQALLEEieRHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESVIQEY------- 1320
Cdd:pfam01576 495 EDERNSLQE--QLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLeekaaay 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1321 ------------------VDLRTHYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlAEVEAALEKQRQLAEA 1382
Cdd:pfam01576 569 dklektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR-AEAEAREKETRALSLA 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1383 HA-----QAKAQAEREAKELQQRMQEEVVRR----------EEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR----- 1442
Cdd:pfam01576 643 RAleealEAKEELERTNKQLRAEMEDLVSSKddvgknvhelERSKRALEQQVEEMKTQLEELEDELQATEDAKLRlevnm 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1443 QA-------------EAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEAER 1502
Cdd:pfam01576 723 QAlkaqferdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKK 802
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1503 LRRQVQDesqrkRQAEVELASRVKAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEVERAR-QVQVALETAQR 1576
Cdd:pfam01576 803 LQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGASGK 877
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1577 SAeaeLQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELE-----RWQL-KANEALRLRL 1650
Cdd:pfam01576 878 SA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQksesaRQQLeRQNKELKAKL 954
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1651 QAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQELIR 1721
Cdd:pfam01576 955 QEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQ 1034
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 41322914 1722 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR 1765
Cdd:pfam01576 1035 LKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1496-2031 |
2.95e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1496 AQEEAERLRRQVQDESQRKR---QAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRqAEVERARQVQVALE 1572
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEkfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1573 TAQRSAEAELQSKRAsFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQA 1652
Cdd:PRK03918 242 ELEKELESLEGSKRK-LEEKIRELEERIEELKKEIEELEEKVKE------------------LKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1653 EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRA 1724
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1725 ETEQGEQQRQLLEEELAR--LQREAAAATQKRQELEAELAKVRAEMEVLLASKARA-------EEESR-----------S 1784
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRkelleeytaelK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1785 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAEAERVLAEKLAAIGEAT 1850
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1851 RLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SDSELERQKGLVE 1918
Cdd:PRK03918 543 SLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1919 DTLRQRRQVEEEILALKASFEKAaagKAELElELGRIRSnaEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSL 1998
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590
....*....|....*....|....*....|...
gi 41322914 1999 AAEEEAARQRKAALEEVERLKAKVEEARRLRER 2031
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1438-1659 |
2.96e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1438 QAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1517
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1518 EVELASRVKAEAEAAREKQR-ALQALEELRLQAEEAERRLRQAE-VERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1595
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 1596 LERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQK 1659
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
163-265 |
3.24e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.39 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 163 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 241
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPgLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 41322914 242 PEDVDVPQPDEKSIITYVSSLYDA 265
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1693-1924 |
3.25e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.17 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1693 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL 1772
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1773 AsKARAEEESRSTSEKSKQRLEAEAGRFRelAEEAARLRAlAEEAKRQRQLAE---EDAARQRAEAER-VLAEKLAAIGE 1848
Cdd:TIGR02794 124 A-KAKQAAEAKAKAEAEAERKAKEEAAKQ--AEEEAKAKA-AAEAKKKAEEAKkkaEAEAKAKAEAEAkAKAEEAKAKAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 1849 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR 1924
Cdd:TIGR02794 200 AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1021-1606 |
3.68e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1021 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLEklktislv 1098
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMA-------- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1099 irgtqgaeevLRAHEEQLK-EAQAVPATLPELEATKASLKKLRAQAEAQQPTFDAL-----------------RDELRGA 1160
Cdd:PRK04863 584 ----------LRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVteymqqllerereltveRDELAAR 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1161 QEV----GERLQQRHGERDveverwrERVAQLLERWQAVLAQTDVRQRELEQLGrqlrYYResadplgAWLQDARrrqeq 1236
Cdd:PRK04863 654 KQAldeeIERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YFS-------ALYGPAR----- 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1237 iQAMPLADSQAVREQLRQEQALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK- 1308
Cdd:PRK04863 711 -HAIVVPDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKr 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1309 ---VQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRM-----EEEERLAEQQRAEERERLAEVEAALEKQRQLA 1380
Cdd:PRK04863 788 ieqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQL 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1381 EAHAQAKAQAEREAKE--------LQQRM---QEEVVRREEAAVDAQQQKRSI-------------QEELQQLRQSSEae 1436
Cdd:PRK04863 868 EQAKEGLSALNRLLPRlnlladetLADRVeeiREQLDEAEEAKRFVQQHGNALaqlepivsvlqsdPEQFEQLKQDYQ-- 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1437 iQAKARQAEAaeRSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRK 1514
Cdd:PRK04863 946 -QAQQTQRDA--KQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQY 1018
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1515 RQAEVELASRVKAEAEAAREkqrALQALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--K 1585
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQE---LKQELQDLGVPAdSGAEERARarrdelHARLSANRSRRNQLEKQLTFCEAEMDNltK 1095
|
650 660
....*....|....*....|.
gi 41322914 1586 RASFAEKTAQLERSLQEEHVA 1606
Cdd:PRK04863 1096 KLRKLERDYHEMREQVVNAKA 1116
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1351-1602 |
3.74e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 63.04 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1351 EERLAEQQRaEERERLAEVEAALEKQR---QLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQ 1427
Cdd:PRK05035 456 EARQARLER-EKAAREARHKKAAEARAakdKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1428 QLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1507
Cdd:PRK05035 535 AEKQAAAAADPKKAAVAAAIARAKAKKAA-------QQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQV 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1508 QDESQRKrqaevelasrVKAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEVERARQVQVALETAQRSAEAELQSKR 1586
Cdd:PRK05035 608 AEVDPKK----------AAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAEDPKK 677
|
250
....*....|....*.
gi 41322914 1587 ASFAEKTAQLERSLQE 1602
Cdd:PRK05035 678 AAVAAAIARAKAKKAA 693
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1416-1960 |
3.87e-09 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 62.74 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1416 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1493
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1494 RQAQEEAERLRRQVQDESQRKRQAEVELASrVKAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEVERAr 1565
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1566 QVQVALETAQRS-AEAELQSKRASFA--EKTAQLERSLQEEHVAVAQLREEAERRAQQQAeaerareeaerelerwQLKA 1642
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1643 NEALRLRLQAEEVAQQKSlaqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1719
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1720 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1799
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1800 frelAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA--ENERLRRLAEDE 1877
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1878 AFQR-------------RRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAG 1944
Cdd:pfam05701 466 DSPRgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAKEG 544
|
570
....*....|....*.
gi 41322914 1945 KAELELELGRIRSNAE 1960
Cdd:pfam05701 545 KLAAEQELRKWRAEHE 560
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4313-4350 |
5.12e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 5.12e-09
10 20 30
....*....|....*....|....*....|....*...
gi 41322914 4313 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4350
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1339-1587 |
5.23e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.47 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1339 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAeREAKELQQRMQEEVVRREEAAVDAQQQ 1418
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1419 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGEL-QALRARAEEAEAQKRQAQ 1497
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAeKKARQRQELQQAREEQIE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1498 EEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1577
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
250
....*....|
gi 41322914 1578 AEAELQSKRA 1587
Cdd:pfam13868 327 RRERIEEERQ 336
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
48-147 |
5.43e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 56.74 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 48 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILH 147
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1227-1610 |
5.73e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1227 LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK 1306
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1307 PKVQSGSESVIQEYVDLRTHYSELTTLtsqyikfiSETLRRMEEEERLAEQQRAEERERL-AEVEAALEKQRQLAEAHAQ 1385
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELREL--------EEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1386 AKAQAEREAKELQQRMQEevVRREEAAVDAQQQKRSIQEELQQLRQSSEAE----------------------------- 1436
Cdd:COG4717 207 RLAELEEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1437 -------IQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQ 1508
Cdd:COG4717 285 llallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLeLLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1509 DESQRKRQAEVELASRVKAEaEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRAS 1588
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|..
gi 41322914 1589 FAEKTAQLERSLQEEHVAVAQL 1610
Cdd:COG4717 444 LEEELEELREELAELEAELEQL 465
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1741-1902 |
6.63e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.81 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1741 ARLQREAAAAtQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEAGRFRELAEEAARLRalAEEAKRQ 1820
Cdd:COG2268 206 AEAERETEIA-IAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIA--EANAERE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1821 RQLAEEDAARQR------AEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 1894
Cdd:COG2268 279 VQRQLEIAEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAI 358
|
....*...
gi 41322914 1895 IEERLAQL 1902
Cdd:COG2268 359 LLMLIEKL 366
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
158-260 |
6.69e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 158 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 236
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPgLCPDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 41322914 237 TRLLDPEDVDVPQPDEKSIITYVS 260
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1720-2025 |
7.97e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.89 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1720 IRLRA-ETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1792
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1793 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlaeklaaigeatrlkteAEIALKEKEAENERLRR 1872
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1873 LAEDEAFQRRrleeqaaqhkadieerlAQLRKASdselerQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELEL 1952
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAA------QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322914 1953 grIRSNAEDTLRSKEQAELEAARQRQLAAeeerrrreaeervQKSLAAEEEAARQRKAALE-EVERLKAKVEEA 2025
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKAAQ-------------QQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1165-1472 |
9.34e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.68 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1165 ERLQQRHGERDVEVERWRervaQLLERWQAvlaqtdvRQRELEqlgRQLRYYRESAdplgawlQDARRRQEQIQAMPLAD 1244
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1245 SQAVREQLRQEQALLE-----EIERHGEKVEECQRFAKQYINAIKDYELQLV--TYKAQLEPVASPAKKPKVQSGSESVI 1317
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1318 QEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKEL 1397
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1398 QQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAeAAERSRLRIEEEIRVVRLQLEATERQR 1472
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1356-1589 |
1.06e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.57 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1356 EQQRAEERERLAEVEAALEKQrqLAEAHAQAkAQAEREAKELQQrmQEEVVRREEAAVDAQQQKRSIQEELQQLrQSSEA 1435
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQ--LPELRKEL-EEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEA-RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1436 EIQAKARQAEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkr 1515
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1516 qaeveLASRVKAEAEAAREKQRALQALEE------LRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASF 1589
Cdd:COG3206 314 -----ILASLEAELEALQAREASLQAQLAqlearlAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1426-1979 |
1.10e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 61.80 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1426 LQQLRQSSEAEIQAKARQAEAAErsrlrieEEIRVVRLQLEATER--QRGGAEGELQALRaRAEEAEAQKRQAQEEAERL 1503
Cdd:COG3899 677 EARGPEPLEERLFELAHHLNRAG-------ERDRAARLLLRAARRalARGAYAEALRYLE-RALELLPPDPEEEYRLALL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1504 RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV-QVALETAQRSAEAEL 1582
Cdd:COG3899 749 LELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFgELALALAERLGDRRL 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1583 QSK-RASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1661
Cdd:COG3899 829 EARaLFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAA 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1662 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1741
Cdd:COG3899 909 AAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAA 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1742 RLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR 1821
Cdd:COG3899 989 AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAAL 1068
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1822 QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1901
Cdd:COG3899 1069 LAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAA 1148
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 1902 LRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQL 1979
Cdd:COG3899 1149 LLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLL 1226
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1657-1852 |
1.31e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.59 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1657 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1736
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1737 EEELARLQREAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1816
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 41322914 1817 AKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1852
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1197-1963 |
1.46e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.29 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1197 AQTDVRQRE---LEQLGRQLR---YYRESADPLGA-WLQDARRRQEQIQAMPLAdSQAVREQLRQeqALLEEIERHGEKV 1269
Cdd:pfam15921 128 AMADIRRREsqsQEDLRNQLQntvHELEAAKCLKEdMLEDSNTQIEQLRKMMLS-HEGVLQEIRS--ILVDFEEASGKKI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1270 EECQRFAKQYINA--------IKDYELQLVTYKAQLEPVAS--PAKKPKVQSGSESVIQEYVD-----LRTHYSELTTLT 1334
Cdd:pfam15921 205 YEHDSMSTMHFRSlgsaiskiLRELDTEISYLKGRIFPVEDqlEALKSESQNKIELLLQQHQDrieqlISEHEVEITGLT 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1335 SQ-------------YIKFISET--------LRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQ-AKAQAE 1391
Cdd:pfam15921 285 EKassarsqansiqsQLEIIQEQarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVLANSElTEARTE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1392 REA---------KELQQRMQEEVVRREEAAVDAQQQKR--------SIQ---------------EELQQLRQSSEAEIQA 1439
Cdd:pfam15921 365 RDQfsqesgnldDQLQKLLADLHKREKELSLEKEQNKRlwdrdtgnSITidhlrrelddrnmevQRLEALLKAMKSECQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1440 KARQAEAAERSRLRIEEEIRVVRLQLEATErqrggaegelQALRARAEEAEAqKRQAQEEAERLRRQVQDESQRKRQAeV 1519
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTK----------EMLRKVVEELTA-KKMTLESSERTVSDLTASLQEKERA-I 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1520 ELASrvkaeAEAAREKQRALQALEELR-LQAEEAERRLRQAEVErARQVQVA-----LETAQRSAEAELQ-------SKR 1586
Cdd:pfam15921 513 EATN-----AEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECE-ALKLQMAekdkvIEILRQQIENMTQlvgqhgrTAG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1587 ASFAEKtAQLERSLQEEHVAVAQLreEAERRAQQQAEAERAREEAERELERWQLKANEALRLRlQAEEVAQQ-------- 1658
Cdd:pfam15921 587 AMQVEK-AQLEKEINDRRLELQEF--KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR-AVKDIKQErdqllnev 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1659 KSLAQAEAEKQKEEAEREARRRGKAEEQAVRQREL------AEQELEKQRQL------AEGTAQQ-RLAAEQELIRLRAE 1725
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmqlksAQSELEQTRNTlksmegSDGHAMKvAMGMQKQITAKRGQ 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1726 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVraemevllaskarAEEESRSTSEkskqrLEAEAGRFRELAE 1805
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV-------------ATEKNKMAGE-----LEVLRSQERRLKE 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1806 EAARLRALAEEAkrQRQLAEEDAARQRAEAERVlaeklaaigeatRLKTEAEIALKEKEA----ENERLR-RLAEDEAFQ 1880
Cdd:pfam15921 805 KVANMEVALDKA--SLQFAECQDIIQRQEQESV------------RLKLQHTLDVKELQGpgytSNSSMKpRLLQPASFT 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1881 RRRLEEQAAQHKADIEERLAQlrkasdseleRQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAE---LELELGRIRS 1957
Cdd:pfam15921 871 RTHSNVPSSQSTASFLSHHSR----------KTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEdkgRAPSLGALDD 940
|
....*.
gi 41322914 1958 NAEDTL 1963
Cdd:pfam15921 941 RVRDCI 946
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1070-1524 |
1.67e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1070 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLK-------KLRAQ 1142
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelperleELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1143 AEAQQPTFDALRDELRGAQEVGERLQQrhgERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP 1222
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1223 LGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEecqrfakqyinAIKDYELQLVTYKAQLEPVAS 1302
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL-----------FLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1303 PAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAEA 1382
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1383 HAQAKAQAEREAKELQQRmQEEVVRREEAAVDAQQQKRSIQEELQQLRQSS-EAEIQAKARQAEAAERSRLRIEEEIRVV 1461
Cdd:COG4717 380 GVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1462 RLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAEV-ELASR 1524
Cdd:COG4717 459 EAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPPVlERASE 523
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
158-265 |
1.69e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 158 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 236
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPgLCPDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 41322914 237 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 265
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1523-2120 |
1.80e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1523 SRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1602
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1603 EHVAVAQLreeaerraqqqaeaerareeaerelerwqlkanEALRLRLQAEEVAQQKSLAqaeaekqkeeaerearrrgK 1682
Cdd:COG4913 318 LDALREEL---------------------------------DELEAQIRGNGGDRLEQLE-------------------R 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1683 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAeteQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1762
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1763 KVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGrfrelaEEAARLRALAEEAkrqrQLAEEDAARQRAeAERVL--- 1839
Cdd:COG4913 423 ELEAEIASLERRKSNIPARL----LALRDALAEALG------LDEAELPFVGELI----EVRPEEERWRGA-IERVLggf 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1840 ----------AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAED-------------EAFQRRRLEEQAAQHKADIE 1896
Cdd:COG4913 488 altllvppehYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfRAWLEAELGRRFDYVCVDSP 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1897 ERLAQLRKA-------SDSELERQKGlvedtlRQRRQVEEEILAlkasfEKAAAGKAELELELGRIRSNAEDTLRSKEQA 1969
Cdd:COG4913 568 EELRRHPRAitragqvKGNGTRHEKD------DRRRIRSRYVLG-----FDNRAKLAALEAELAELEEELAEAEERLEAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1970 ELEAARQRQLAAEEERRRREAEERVqKSLAAEEEAARQRkaalEEVERLKAKVEEARRLRERAE--QESARQLQLAQEAA 2047
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDEI-DVASAEREIAELE----AELERLDASSDDLAALEEQLEelEAELEELEEELDEL 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2048 QKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEEAER 2120
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAAALGDAVERELRENLEERIDALRARL 782
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1694-1881 |
1.96e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1694 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmevllA 1773
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE-----A 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1774 SKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVlAEKLAAIGEATRLK 1853
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAEAK 224
|
170 180
....*....|....*....|....*...
gi 41322914 1854 TEAEIALKEKEAENERLRRLAEDEAFQR 1881
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1855-2304 |
2.02e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1855 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILAL 1934
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQ---------LLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1935 KASFEKAAAGKAELElELGRIRSNAEDTLRSKEQAELEAARQRQLaaeeerrrrEAEERVQKSLAAEEEAARQRKAALEE 2014
Cdd:COG4717 145 PERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSL---------ATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2015 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAA 2094
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2095 EEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAAlRQKQAADAEMEKH 2174
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2175 KKFA------EQTLRQKAQVEQELTTLRLQLEETDHQ-KNLLDEELQRLKAEATEAARQR-SQVEEELFSVRVQMEELSK 2246
Cdd:COG4717 374 ALLAeagvedEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEElEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 2247 LKARIEAENRALILRDK-DNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEED 2304
Cdd:COG4717 454 ELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1346-1607 |
2.32e-08 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 59.67 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1346 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaqakAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1425
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLL-------LQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1426 LQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaEGELQALRARAEEAEaQKRQAQEEAERLRR 1505
Cdd:pfam15558 94 SRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALR---EQNSLQLQERLEEAC-HKRQLKEREEQKKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1506 QVQDESQR-KRQA-EVELASRVKAEAEAARE--KQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAE 1581
Cdd:pfam15558 170 QENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEER 249
|
250 260
....*....|....*....|....*.
gi 41322914 1582 LQSKRASFAEKTAQLERSLQEEHVAV 1607
Cdd:pfam15558 250 QEHKEALAELADRKIQQARQVAHKTV 275
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1682-1889 |
2.49e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAel 1761
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1762 akvRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1840
Cdd:COG4942 119 ---QPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 41322914 1841 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1889
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1685-2107 |
2.54e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1762
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1763 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--------------- 1827
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1828 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASD 1907
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1908 SELERQKGLVE-DTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDTLRSKEQAELEAARQRQLAAEEERR 1986
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1987 RREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQlQLAQEAAQKRLQAEEKAHAFAVQQK 2065
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELA-ELLQELEELKAELRELAEEWAALKL 497
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 41322914 2066 EQElqqtlqqeqsVLDQLRGeaeaarraaeeaeearvQAERE 2107
Cdd:COG4717 498 ALE----------LLEEARE-----------------EYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2278-2481 |
2.55e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2278 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQED 2353
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARriraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2354 KEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2433
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 41322914 2434 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2481
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1363-1832 |
2.59e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.42 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1363 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAqqqkrsiqeelqQLRQSSEAEIQAKAR 1442
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRA------------ALRWALAHGDAELAL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1443 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELA 1522
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1523 SRvkAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1602
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1603 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1682
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1683 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1762
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1763 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1832
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
167-262 |
2.64e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 55.77 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 167 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNL-----------------------EN 222
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 41322914 223 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 262
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
50-144 |
2.81e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 54.65 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 50 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 121
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 41322914 122 VNIRNDDIADGNPKLTLGLIWTI 144
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1343-1596 |
2.89e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 59.16 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1422
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1423 QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1502
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1503 LRRQVQDESQRKRQAEVELASRVKaEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAEL 1582
Cdd:pfam13868 206 LRAKLYQEEQERKERQKEREEAEK-KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
250
....*....|....
gi 41322914 1583 QSKRASFAEKTAQL 1596
Cdd:pfam13868 285 RMKRLEHRRELEKQ 298
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1051-1546 |
3.02e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1051 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEaqaVPATLPELE 1130
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1131 ATKASLKKLRAQAEAQQpTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLG 1210
Cdd:PRK03918 280 EKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1211 RQLRYYRE------------------SADPLGAWLQDARRRQEQIQAmPLADSQAVREQLRQEQALL----EEIERHGEK 1268
Cdd:PRK03918 359 ERHELYEEakakkeelerlkkrltglTPEKLEKELEELEKAKEEIEE-EISKITARIGELKKEIKELkkaiEELKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1269 VEECQR---------FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESviqEYVDLRTHYSELTTLTSQYIK 1339
Cdd:PRK03918 438 CPVCGRelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES---ELIKLKELAEQLKELEEKLKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1340 FISETLRRMEEE-----ERLA-----------EQQRAEERE-RLAEVEAAL-EKQRQLAEAHAQAKAQAEREAKELQQRM 1401
Cdd:PRK03918 515 YNLEELEKKAEEyeklkEKLIklkgeikslkkELEKLEELKkKLAELEKKLdELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1402 Q--EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEE-EIRVVRLQLEATERQRGGAEGE 1478
Cdd:PRK03918 595 KelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRE 674
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 1479 LQALRARAEEAEAQKRQAQEEAERLRRQVqdESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1546
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1128-1886 |
3.38e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.24 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1128 ELEATKASLKKLRAQAEAQQPTFDALRDELRgaqevgERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELE 1207
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1208 Q-LGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEEcqRFAKQYINAikdy 1286
Cdd:pfam12128 333 AfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD--KLAKIREAR---- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1287 ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYvDLRTHYSELTTLTSQYIkFISETLRRMEEEERLAEQQRAEERERL 1366
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEY-RLKSRLGELKLRLNQAT-ATPELLLQLENFDERIERAREEQEAAN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1367 AEVEAAlekQRQLAEAHAQAKAQAEReakelqqrmqeevVRREEAAVdaQQQKRSIQEELQQLRQSSEAEIQAKARQAEA 1446
Cdd:pfam12128 485 AEVERL---QSELRQARKRRDQASEA-------------LRQASRRL--EERQSALDELELQLFPQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1447 AERSRLRIEEEIRVVRLQL--EATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRRQV-----QDESQRKRQAEV 1519
Cdd:pfam12128 547 WEQSIGKVISPELLHRTDLdpEVWDGSVGG-ELNLYGVKLDLKRIDVPEWAASEEELRERLDKaeealQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1520 ELASRVKAEAEAAREKQRALQALEelrlQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQskraSFAEKTAQLERS 1599
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALK----NARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN----SLEAQLKQLDKK 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1600 LQeehvavaqlreeaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQkslaqaeaekqKEEAEREARR 1679
Cdd:pfam12128 698 HQ-------------------------------AWLEEQKEQKREARTEKQAYWQVVEG-----------ALDAQLALLK 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1680 RGKAEEQAVRQRELAEQELEKQRQLAE-GTAQQRLAA-EQELIRLRAETEQGEQQRQLLeEELARLQREaaAATQKRQEL 1757
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKRDLASlGVDPDVIAKlKREIRTLERKIERIAVRRQEV-LRYFDWYQE--TWLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1758 EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlaeeakRQRQLAEEDAARQRAEAER 1837
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATLKEDANSEQAQG 886
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 41322914 1838 VLAEKLAAiGEATRLKTEAEIALKEKEAEN-----ERLRRLAEDEAFQRRRLEE 1886
Cdd:pfam12128 887 SIGERLAQ-LEDLKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1416-1597 |
3.46e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1416 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqleaterqrggaegelqalraraEEAEAQKRQ 1495
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---------------------------LAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1496 AQEEAER-LRRQVQDESQRKRQAEvelASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER---ARQVQVAL 1571
Cdd:PRK09510 120 AEEAAKQaALKQKQAEEAAAKAAA---AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAA 196
|
170 180
....*....|....*....|....*.
gi 41322914 1572 ETAQRSAEAELQSKRASFAEKTAQLE 1597
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1682-1837 |
4.12e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1761
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1762 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EAARLRALAEEAKRQRQLAeedAARQRAEAER 1837
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEAAKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1151-1583 |
4.39e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1151 DALRDELRGAQEVGERLQQRHGERDVEVERWRE-----------RVAQLLERWQAV---LAQTDVRQRELEQLGRQLRYY 1216
Cdd:PRK04863 743 DSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEvplfgraarekRIEQLRAEREELaerYATLSFDVQKLQRLHQAFSRF 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1217 RES-------ADPLGAWLQDARRRQEQIQAMPLADSQAVR-----EQLRQEQALLEEI---------ERHGEKVEECQ-- 1273
Cdd:PRK04863 823 IGShlavafeADPEAELRQLNRRRVELERALADHESQEQQqrsqlEQAKEGLSALNRLlprlnlladETLADRVEEIReq 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1274 --------RFAKQYINAIkdyelqlvtykAQLEPVAS-----PAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKF 1340
Cdd:PRK04863 903 ldeaeeakRFVQQHGNAL-----------AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHF 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1341 -ISETLRRMEEEERLAEQQRAeereRLAEVEAALEKQRqlaEAHAQAKAQAeREAKELQQRMQEEVVRreeaavdAQQQK 1419
Cdd:PRK04863 972 sYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERTRAR---EQLRQAQAQL-AQYNQVLASLKSSYDA-------KRQML 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1420 RSIQEELQQL--RQSSEAEIQAKARQAEaaersrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1497
Cdd:PRK04863 1037 QELKQELQDLgvPADSGAEERARARRDE--------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1498 EEAE-------RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKqrALQALeelrlqaeeaerRLRQAEVERARQVQVA 1570
Cdd:PRK04863 1109 EQVVnakagwcAVLRLVKDNGVERRLHRRELAYLSADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRL 1174
|
490
....*....|...
gi 41322914 1571 LETAQRsAEAELQ 1583
Cdd:PRK04863 1175 SEDPKR-PERKVQ 1186
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1501-1977 |
6.00e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1501 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERArqvqvalETAQRSAEA 1580
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-------ELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1581 ELQSKRASFAEKTAQLERSLQEEHVAVAQLreeaerraqqqaeaERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1660
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEEL--------------EERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1661 LAQAeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEEL 1740
Cdd:COG4717 188 LATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1741 ARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ 1820
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1821 RQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEER 1898
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1899 LAQLRKASDSELERQKGLVEDTLRQR-RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQR 1977
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1348-1601 |
6.78e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.01 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1348 MEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1426
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1427 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVR-----------LQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1495
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekeeereedERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1496 ---AQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALE 1572
Cdd:pfam13868 188 rlrAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERML 267
|
250 260
....*....|....*....|....*....
gi 41322914 1573 TAQRSAEAELQSKRASFAEKTAQLERSLQ 1601
Cdd:pfam13868 268 RKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1682-2055 |
7.54e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1761
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1762 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAERVL 1839
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1840 AEKLAAIGEatrlKTEAEIALKEKEAENERLRRLaedeafqrrrleeqaaQHKADIEERLAQLRKASDSELERQKGLVED 1919
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFL----------------DQKRGHPEVKSQNGEEEVTKLKVTTKRRQG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1920 TLRQRRQVEEEilalkasfekaAAGKAELELELGRIR-SNAEdtlrsKEQAELEAARQRQLAAEEERRRREAEERVQKSL 1998
Cdd:pfam02029 229 GLSQSQEREEE-----------AEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1999 AAEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2055
Cdd:pfam02029 293 LEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1427-1594 |
8.23e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1427 QQLRQSsEAEIQAKARQAEAAERSRLRIEEeiRVVRLQLEATERQrggaegelqalrARAEEAEAQKRQAQEEA-----E 1501
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARLEREKAARE------------ARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1502 RLR-RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA 1580
Cdd:PRK05035 494 RVKaKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170
....*....|....
gi 41322914 1581 ELQSKRASFAEKTA 1594
Cdd:PRK05035 574 EVDPKKAAVAAAIA 587
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4044-4080 |
8.93e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 8.93e-08
10 20 30
....*....|....*....|....*....|....*..
gi 41322914 4044 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4080
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1356-2035 |
9.33e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.90 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1356 EQQRAEERERLAEVEAALEKQRQLAE---AHAQAKAQAEREAKELQQRMQE------------------EVVRREEAAVD 1414
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNeikALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyhnhqrTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1415 AQQQKRSIQEELQQLRQSS---EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG----------------GA 1475
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKtelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfhtlvieRQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1476 EGELQALRARAEEAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRlq 1548
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRdekkglgRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1549 aeEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLER---------SLQEEHVAVAQLREEAERRAQ 1619
Cdd:TIGR00606 482 --KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtqmeMLTKDKMDKDEQIRKIKSRHS 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1620 QQAEAERAREEAERELERW-QLKANEALRLRLQAEEVaqQKSLAQAEAEKQKEEAerearrrgkaeeqavRQRELAEQEL 1698
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAKL--NKELASLEQNKNHINN---------------ELESKEEQLS 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1699 EKQRQLAEGTAQQrlAAEQELIRLRAETEQGEQQRQLLE----------EELARLQREAAAATQKRQELEAELAKVRAEM 1768
Cdd:TIGR00606 623 SYEDKLFDVCGSQ--DEESDLERLKEEIEKSSKQRAMLAgatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1769 EVLLASKARAEEESRSTSEKSKQRLEAEAGRF-----------RELAEEAARLRALAEEAKRQRQ-LAEEDAARQRAEAE 1836
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgrqsiidlkeKEIPELRNKLQKVNRDIQRLKNdIEEQETLLGTIMPE 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1837 RVLAEKLAA-IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD------------IEERLAQLR 1903
Cdd:TIGR00606 781 EESAKVCLTdVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskielnrklIQDQQEQIQ 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1904 --KASDSELERQKGLVEDTLRQRRQVEE-------EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAA 1974
Cdd:TIGR00606 861 hlKSKTNELKSEKLQIGTNLQRRQQFEEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322914 1975 RQRQLAAEEERRRREAEERVQKSLaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2035
Cdd:TIGR00606 941 DKVNDIKEKVKNIHGYMKDIENKI--QDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1780-2065 |
1.42e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.83 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1780 EESRSTSEKSKQ----RLEAEagRFRELAEEAARlralaeEAKRQRQLAEEDAARQrAEAERvlaeKLAAIGEATRLKTE 1855
Cdd:pfam17380 279 QHQKAVSERQQQekfeKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1856 AE-----IALKEKEAENERLRR--LAEDEAFQRR--RLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTL----- 1921
Cdd:pfam17380 346 RErelerIRQEERKRELERIRQeeIAMEISRMREleRLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVemeqi 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1922 ---------RQRRQVEEEilaLKASFEKAAAGKAELELELGRIRSNAEDtlRSKEQAELEAARQRQLAAEEERRRREAEE 1992
Cdd:pfam17380 426 raeqeearqREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 1993 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHAFAVQQK 2065
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRLEAMERE 574
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1366-1778 |
1.45e-07 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 58.33 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1366 LAEVEAALEKQRQLAEAHAQAkaqaeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE----------- 1434
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1435 --------AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1506
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1507 VQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKR 1586
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1587 ASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1666
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1667 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1746
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 41322914 1747 AAAATQKRQELEAELAKVRAEMEVLLASKARA 1778
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2252-2479 |
1.83e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2252 EAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLS-----VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA 2326
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2327 TRLKAEAELLQQQK-ELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2405
Cdd:COG4913 319 DALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 2406 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE-LEREKEKLQQEAKLLQLKSEE 2479
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1483-1603 |
1.95e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.19 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1483 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqaevELASRVKAEAEAAREKQRAlqaleELRLQAE----EAERRLRQ 1558
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQER----EIETARIAEAEAELAKKKA-----EERREAEtaraEAEAAYEI 270
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 41322914 1559 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEE 1603
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAE 315
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2171-2474 |
2.01e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.34 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2171 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKAR 2250
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2251 IEAENRAL------ILRDKDNTQRFLQEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2322
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2323 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLeaerqrqlemsaeaERLKLRVAEMSRAQAR 2402
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI--------------EELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322914 2403 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2474
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1435-1567 |
2.02e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 56.21 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1435 AEIQAKARQAEAAersrlrieeeIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------R 1505
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322914 1506 QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1567
Cdd:COG1566 148 QELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1343-1565 |
2.12e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.39 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQkr 1420
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1421 siqeelqqlrqsseaeiQAKARQAEAAersrlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE- 1499
Cdd:TIGR02794 146 -----------------EEAAKQAEEE--------------AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1500 ---AERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1565
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1541-1979 |
2.15e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 57.72 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1541 ALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ---------LR 1611
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1612 EEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1691
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1692 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVL 1771
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1772 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATR 1851
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1852 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEI 1931
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 41322914 1932 LALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQL 1979
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1694-1909 |
2.29e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1694 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLA 1773
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1774 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1842
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1843 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSE 1909
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
43-150 |
2.34e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 52.70 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 43 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 115
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 41322914 116 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 150
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1369-1588 |
2.50e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.39 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1369 VEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAE 1448
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKL----EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1449 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEAERLRRQVQDESQRKRQAEVELASRVKAE 1528
Cdd:TIGR02794 114 AEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKA-KAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1529 AEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRAS 1588
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGA 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1792-1978 |
2.88e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1792 RLEAEAGRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1867
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1868 ERLRRLAEDEAF----------QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAS 1937
Cdd:COG4913 302 AELARLEAELERlearldalreELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41322914 1938 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQ 1978
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1831-2221 |
2.92e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.06 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1831 QRAEAERVLAEKLAAIgEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasDSEL 1910
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1911 ERQKglVEDTLRQRRQVEEEILALKASFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEAARQRQLAaeeerrrre 1989
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1990 aeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHafavQQKEQE 2068
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLR----QQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2069 LQQTLQQEQSVLDQLRGEAEAARRAaeeaeearvqaEREAAQSRRQVEEAERlKQSAEEQAQARAQAQAAAEKLRKEAEQ 2148
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEEQRRKIL-----------EKELEERKQAMIEEER-KRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2149 EaarraqaeqaalRQKQaadAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKNLLDEELQRLKAEAT 2221
Cdd:pfam17380 541 E------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1350-1534 |
2.95e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1350 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAKELQQRMqeevvrrEEAAVDAQQQKRSIQEELQQL 1429
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRA-------AAAAKKAAAEAKKKAEAEAAK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1430 RQSSEAEIQAKARQAEAAersrlrieeeirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1509
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKA------------------AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 41322914 1510 ESQRKRQAEVELASRVKAEAEAARE 1534
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1349-1514 |
3.32e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.01 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1349 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQ 1428
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1429 LRQSSEAEIQAKARQAEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1497
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 41322914 1498 EEAERLRRQVQDESQRK 1514
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2262-2611 |
3.43e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.67 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2262 DKDNTQRFLQEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEKmlkEKMQAVQEATRLKAEAELLQQQKE 2341
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDRQ---AAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2342 LAQEQARRLQEDKEQMAQQLAEETQGFQ--RTLEAERQRQlEMSAeAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2419
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELERLQmeRQQKNERVRQ-ELEA-ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2420 -KLHRTELATQEKVTLVQTLEIQRQqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqllqetqaLQQS 2498
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQ---QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-----------LEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2499 FLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAQQLREEQQRQqqqmeqerqrlvasmEEARRRQHEAEEGvRRKQEELQ 2578
Cdd:pfam17380 501 LEERKQAMIEEER-----KRKLLEKEMEERQKAIYEEERRREA---------------EEERRKQQEMEER-RRIQEQMR 559
|
330 340 350
....*....|....*....|....*....|...
gi 41322914 2579 QLEQQRRQQeellaEENQRLREQLQLLEEQHRA 2611
Cdd:pfam17380 560 KATEERSRL-----EAMEREREMMRQIVESEKA 587
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1681-1923 |
3.67e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.50 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1681 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqreaaaATQKRQEL 1757
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1758 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1837
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1838 VLAEKlaaigeatRLKTEAEIALKEkeaENERLRRLAEDEAFQ-RRRLEEQAAQHKADIEERLAQLRKASDSELERQKGL 1916
Cdd:pfam15709 447 AEAEK--------QRQKELEMQLAE---EQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
....*..
gi 41322914 1917 VEDTLRQ 1923
Cdd:pfam15709 516 AQEQARQ 522
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1730-1905 |
4.40e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1730 EQQRQLLEEELAR-LQREAAAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1808
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1809 RLRALAEeakrqrQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1888
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170
....*....|....*..
gi 41322914 1889 AQHKADIEERLAQLRKA 1905
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKA 236
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2307-2608 |
4.90e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2307 QQRALAEKMLKEKMQavqeatrlKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAEETQGfqrTLEAERQR-QLEMSA 2384
Cdd:pfam17380 280 HQKAVSERQQQEKFE--------KMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQA---AIYAEQERmAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2385 EAERLKLRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTELATQEKVTLV-QTLEIQRQQSDHDAERLREaIAELEREK 2463
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVrQELEAARKVKILEEERQRK-IQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2464 EKL---QQEAKLLQLK--SEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQ 2538
Cdd:pfam17380 423 EQIraeQEEARQREVRrlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2539 QRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRrqqeellaEENQRLREQLQLLEEQ 2608
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM--------EERRRIQEQMRKATEE 564
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2183-2479 |
5.47e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2183 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILR- 2261
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERf 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2262 -----DKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAE-------------------------------EDL 2305
Cdd:PRK02224 401 gdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvetieedrervEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2306 AQQRALAE---KMLKEKMQAVQEATRLKAEAELLQQQKELAQE---QARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2379
Cdd:PRK02224 481 EAELEDLEeevEEVEERLERAEDLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2380 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK-------------QAEEIGEKL-HRTELATQEKVTLVQTLEIQRQ-Q 2444
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedEIERLREKReALAELNDERRERLAEKRERKRElE 640
|
330 340 350
....*....|....*....|....*....|....*
gi 41322914 2445 SDHDAERLREAIAELEREKEKLQQEAKLLQLKSEE 2479
Cdd:PRK02224 641 AEFDEARIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2167-2367 |
5.53e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2167 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEE--- 2243
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2244 --------LSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2315
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 41322914 2316 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQG 2367
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1924-2479 |
5.76e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1924 RRQVEEEILALKaSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEERRRREAEERVQKSLAAEEE 2003
Cdd:PRK03918 147 REKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2004 AARQRKaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQL 2083
Cdd:PRK03918 225 KLEKEV---KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2084 RGEAEAARRAAEEAEEARvqaEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ 2163
Cdd:PRK03918 302 YEEYLDELREIEKRLSRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2164 KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE-----LFSVR 2238
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2239 VQMEELSKLKARIEAENRALiLRDKDNTQRFLQEEAE--KMKQVAEEAARLSvaaqeaARLRQLAEEDLAQQRALAEKML 2316
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKL-RKELRELEKVLKKESEliKLKELAEQLKELE------EKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2317 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEAERLKLRVAE 2395
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2396 msRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2475
Cdd:PRK03918 612 --KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
....
gi 41322914 2476 KSEE 2479
Cdd:PRK03918 688 RREE 691
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1324-1457 |
6.22e-07 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 54.22 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1324 RTHYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreakelQQ 1399
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEE------LL 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1400 RMQEEVVRREEAAVDAQQQKRSIQEEL----QQLRQSSEAEIQAKARQAEAA-----ERSRLRIEEE 1457
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKEERENedlnlEQLREKANEE 196
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1401-1569 |
6.31e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 55.92 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1401 MQEEVVRREEAAVDAQQQkrsiqeELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQ 1480
Cdd:COG1193 497 LPEEIIERARELLGEESI------DVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK-------E 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1481 ALRARA-EEAEAQKRQAQEEAERLRRQVQDEsqrkrqaevelasrvKAEAEAAREKQRALQALEElRLQAEEAERRLRQA 1559
Cdd:COG1193 564 EILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKAK 627
|
170
....*....|
gi 41322914 1560 EVERARQVQV 1569
Cdd:COG1193 628 PAKPPEELKV 637
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3725-3760 |
6.52e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 6.52e-07
10 20 30
....*....|....*....|....*....|....*.
gi 41322914 3725 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3760
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2320-2465 |
9.04e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.41 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2320 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLAEEtQGFQRTLEAERQRQLEMSAEAERLKL 2391
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 2392 RVAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlREAIAELEREKEK 2465
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1741-2471 |
9.80e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1741 ARLQREAAAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1817
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1818 KRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRLKTEAEIalkekEAENERLR---RLAEDEAfQRRRLEEQAAQH 1891
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRV-----QAENARLEmhfKLKEDHE-KIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1892 KADIEERLAQLRKASDSELERQKGL---VEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSkeq 1968
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1969 aeleaarQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV---EEARRLRERAEQESARQLQLAQE 2045
Cdd:pfam05483 312 -------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcslEELLRTEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2046 AAQKRLQAEEKAHAFAVQQKEQelqqtlqqeqsvLDQLRgeaeaarraaeeaeeaRVQAEREAA-QSRRQVEE-AERLKQ 2123
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE------------LEELK----------------KILAEDEKLlDEKKQFEKiAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2124 SAEEQAQARAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEME--KHKKFAEQTLRQKAQVEQELTTLRLQLEE 2201
Cdd:pfam05483 437 KEQELIFLLQA---------------------------REKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2202 TDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELskLKARIEAENRALILRDKDNTQR--FLQEEAE---K 2276
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM--LKQIENLEEKEMNLRDELESVReeFIQKGDEvkcK 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2277 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2356
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2357 MAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQ---------------ARAEEDAQRFRKQAEEIGEKL 2421
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQYDKIIEERDSEL 727
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 41322914 2422 HRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAK 2471
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1338-1581 |
9.93e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1338 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQ 1417
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1418 QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE----EAEAQK 1493
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1494 RQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALET 1573
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*...
gi 41322914 1574 AQRSAEAE 1581
Cdd:COG3883 258 AAGSAGAA 265
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4147-4175 |
1.03e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.03e-06
10 20
....*....|....*....|....*....
gi 41322914 4147 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4175
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2278-2482 |
1.04e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2278 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2357
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2358 AQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2437
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41322914 2438 LEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2482
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1351-1978 |
1.06e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.19 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1351 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAKELQQRMQEEVVRREEA 1411
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1412 AVDAQQQKRSIQEELQQLRQ-SSEAEIQAKARQAEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1486
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1487 EEAEAQKRQAQEEAERLR---RQVQDESQRKRQAEVElasrvKAEAEAAREKQRALQALEELRLQAEEaerrlRQAEVER 1563
Cdd:PRK10246 410 EVAAALAQHAEQRPLRQRlvaLHGQIVPQQKRLAQLQ-----VAIQNVTQEQTQRNAALNEMRQRYKE-----KTQQLAD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1564 ARQVqvaleTAQRSAEAELQSKRASF-AEKTAQLERSlqEEHVAVAQLREEAERRAQQQAEAERAreeaerelERWQLKa 1642
Cdd:PRK10246 480 VKTI-----CEQEARIKDLEAQRAQLqAGQPCPLCGS--TSHPAVEAYQALEPGVNQSRLDALEK--------EVKKLG- 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1643 NEALRLRLQAEEVAQQKSlaqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRL 1722
Cdd:PRK10246 544 EEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNITLQPQDDIQPW 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1723 RAETEQGEQQRQLLEEELArLQREAAAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKSKQRLEAE 1796
Cdd:PRK10246 602 LDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1797 AGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLAEKLAAIGEATrLKTEAEIALKEKEAENERlRRLAE- 1875
Cdd:PRK10246 681 QNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA-QRLQKa 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1876 ----DEAFQRRRLEEQAAQHKADIEE----RLAQLRKASDSELERQKGLVEdtlrQRRQVEEEILALKASFEKAAAGKAE 1947
Cdd:PRK10246 751 qaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QTAQALAQHQQHRPDGLDLTVTVEQ 826
|
650 660 670
....*....|....*....|....*....|....*.
gi 41322914 1948 LELEL----GRIRSNAEDTLRSKEQAELEA-ARQRQ 1978
Cdd:PRK10246 827 IQQELaqlaQQLRENTTRQGEIRQQLKQDAdNRQQQ 862
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1380-1594 |
1.11e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1380 AEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEI- 1458
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEAEIEERREELg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1459 -RVVRLQ------------------------LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1513
Cdd:COG3883 90 eRARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1514 KRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKT 1593
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
.
gi 41322914 1594 A 1594
Cdd:COG3883 250 G 250
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1038-1605 |
1.29e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1038 EGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLK 1117
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQE--QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1118 EAQAvpaTLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERlqQRHGERDVEVERWRERVAQLLERWQavla 1197
Cdd:TIGR00606 482 KAER---ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL--NHHTTTRTQMEMLTKDKMDKDEQIR---- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1198 qtDVRQRELEQLGRQLRYYRESADpLGAWLQDARRRQEQIQ------AMPLADSQAVREQLR-QEQALLEEIERHGEKVE 1270
Cdd:TIGR00606 553 --KIKSRHSDELTSLLGYFPNKKQ-LEDWLHSKSKEINQTRdrlaklNKELASLEQNKNHINnELESKEEQLSSYEDKLF 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1271 EcqrfakqyINAIKDYELQLVTYKAQLEpvaSPAKKPKVQSGSESVIQEYVDLRTHYSE----LTTLTSQYIKFISETLR 1346
Cdd:TIGR00606 630 D--------VCGSQDEESDLERLKEEIE---KSSKQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFIS 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1347 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrreeAAVDAQQQKRSIQEEL 1426
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK-------VNRDIQRLKNDIEEQE 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1427 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1506
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1507 VQDESQRKRQAEV---ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEvERARQVQVALETAQRSAEAELQ 1583
Cdd:TIGR00606 852 IQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAK-EQDSPLETFLEKDQQEKEELIS 930
|
570 580
....*....|....*....|..
gi 41322914 1584 SKRASfaEKTAQLERSLQEEHV 1605
Cdd:TIGR00606 931 SKETS--NKKAQDKVNDIKEKV 950
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1314-1550 |
1.46e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1314 ESVIQEYVDLRThySELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ---RQLAEAHAQ-AKAQ 1389
Cdd:COG3206 155 NALAEAYLEQNL--ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKlllQQLSELESQlAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1390 AEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEAtE 1469
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHPDVIALRAQIAALRAQLQQ-E 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1470 RQRGGAEGELQALRARAEEAEAQKRQAQeeaerLRRQVQDESQRkrqaEVELAsRVKAEAEAAREK-QRALQALEELRLQ 1548
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQ-----LEARLAELPEL----EAELR-RLEREVEVARELyESLLQRLEEARLA 380
|
..
gi 41322914 1549 AE 1550
Cdd:COG3206 381 EA 382
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2162-2618 |
1.54e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.97 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2162 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQ--LEETDHQKnllDEELQRLKAEATEAARQRSQVEEELFSVRV 2239
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQ---EIHIRDAHEVATSIREISCQQHTLTQHIHT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2240 QMEELSKLKARIEAENRAL-ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2318
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELdILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2319 KMQAVQEATRLKAEAE-LLQQQKELAQEQARRLQEDKEQ------------MAQQLAEETQGFQRTLEAERQRQLEMSAE 2385
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEqIHLQETRKKAVVLARLLELQEEpcplcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2386 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTelaTQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2465
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS---KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2466 LQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDsllqrerfiEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQM 2545
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER---------VREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2546 EQERQRLVASMEEARRRQHEAEEGVRRkqeELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE 2618
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDR---EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE 761
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2183-2468 |
1.55e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2183 RQKAQVEQELTTLRLQLeeTDHQknlldeelQRLKAEATEAArQRSQVEEELFSVRVQME----ELSKLKARIEAenraL 2258
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQ--------QALDVQQTRAI-QYQQAVQALERAKQLCGlpdlTADNAEDWLEE----F 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2259 ILRDKDNTQRFLQEE-----AEKMKQVAEEAARL------SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKE 2318
Cdd:PRK04863 448 QAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQ 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2319 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEEtqgfqrtLEAERQRQLEMSAEAERLKLRVAE-MS 2397
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAA 600
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 2398 RAQA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLREAIAELEREKEKLQQ 2468
Cdd:PRK04863 601 RAPAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQ 666
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1341-2248 |
1.58e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1341 ISETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreAKELQQRMQEEVVRREEAAVDaqqqkr 1420
Cdd:TIGR00606 178 IFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQIT--SKEAQLESSREIVKSYENELD------ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1421 siqeelqqlrqsseaEIQAKARQAEAAERSRLRIEEEIRvvrlQLEATERQRGGAEGELQALraRAEEAEAQKRQAQEEA 1500
Cdd:TIGR00606 249 ---------------PLKNRLKEIEHNLSKIMKLDNEIK----ALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLY 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1501 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER-ARQVQVALETAQRSAE 1579
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIqSLATRLELDGFERGPF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1580 AELQSKRASFAEKtaqleRSLQEEHVAVAQLREeaerraqqqaeaerareeaerelerwQLKANEALRLRlQAEEVAQQK 1659
Cdd:TIGR00606 388 SERQIKNFHTLVI-----ERQEDEAKTAAQLCA--------------------------DLQSKERLKQE-QADEIRDEK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1660 SLAQAEAEKqkeeaerearrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAE---------TEQGE 1730
Cdd:TIGR00606 436 KGLGRTIEL-------------KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERElskaeknslTETLK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1731 QQRQLLEEELARLQREAAAATQKRQELEAElAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL 1810
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1811 RALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEI----ALKEKEAENERLRRLAEDEAFQRRRLE 1885
Cdd:TIGR00606 580 HSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEKSSKQRAMLA 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1886 EQAAQHKADIEER---------LAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKaaagKAELELELGRIR 1956
Cdd:TIGR00606 660 GATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK----RRDEMLGLAPGR 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1957 SNAEDtLRSKEQAELEAARQRQLAAEEERRRREAEERVQ-KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2035
Cdd:TIGR00606 736 QSIID-LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2036 SaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQ 2114
Cdd:TIGR00606 815 L-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2115 VEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEK--------HKKFAEQTLRQKA 2186
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLK 973
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322914 2187 QVEQELTTLRLQLEETDHQKNLLDEELqRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK 2248
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDM-RLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE 1034
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1696-1853 |
1.75e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 54.64 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1696 QELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqrEAAAATQKRQELEAELAKVRAemevllAS 1774
Cdd:PTZ00491 647 DSLQKSVQLAiEITTKSQEAAARHQAELLEQEARGRLERQKMHDKA-----KAEEQRTKLLELQAESAAVES------SG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1775 KARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAIgEATRLK 1853
Cdd:PTZ00491 716 QSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAKAKELADI-EATKFE 791
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1330-1567 |
2.06e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1330 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAKELQQrMQEEVVR 1407
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1408 REEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggAEGELQALRAR-A 1486
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1487 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEaAREKQRALQALEELrlqAEEAERRLRQAEVERARQ 1566
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVAREL---YESLLQRLEEARLAEALT 384
|
.
gi 41322914 1567 V 1567
Cdd:COG3206 385 V 385
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1351-1598 |
2.10e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.88 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1351 EERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQAKAQaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR 1430
Cdd:pfam05667 210 ERNAAELAAAQEWEEEWNSQGL---ASRLTPEEYRKRKR-TKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1431 QSSEAEIQAK-------------ARQAEAAERS-----------RLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1486
Cdd:pfam05667 286 GSSTTDTGLTkgsrfthteklqfTNEAPAATSSpptkveteeelQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1487 EEAEAQKRQAQEEAERLRRQVQ------------DESQRKRQAEVELASRVKAEAEAAREKQRA--LQALEELRL----Q 1548
Cdd:pfam05667 366 KQVEEELEELKEQNEELEKQYKvkkktldllpdaEENIAKLQALVDASAQRLVELAGQWEKHRVplIEEYRALKEaksnK 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41322914 1549 AEEAERRLRQAEVERARQVQVAletaqrsaeAELQSKRASFAEKTAQLER 1598
Cdd:pfam05667 446 EDESQRKLEEIKELREKIKEVA---------EEAKQKEELYKQLVAEYER 486
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3930-3967 |
2.22e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.22e-06
10 20 30
....*....|....*....|....*....|....*...
gi 41322914 3930 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 3967
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1756-2413 |
2.34e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1756 ELEAELAKVRAEMEVLLAskaraEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1835
Cdd:pfam15921 246 QLEALKSESQNKIELLLQ-----QHQDRIEQLISEHEVEITG-----LTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1836 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErlaQLRKASDSELERQKG 1915
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---QLQKLLADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1916 LVEDTLRQRRQVEEEIlalkasfekaaaGKAeleLELGRIRSNAEDtlRSKEQAELEAARQrqlaaeeerrrrEAEERVQ 1995
Cdd:pfam15921 393 LSLEKEQNKRLWDRDT------------GNS---ITIDHLRRELDD--RNMEVQRLEALLK------------AMKSECQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1996 KSLAAEEEAARQRKAALEEVERLKAKVEEARR-LRERAEQESARQLQL-AQEAAQKRLQAEEKAHAFAVQQKEQELQQTL 2073
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMTLeSSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2074 QQEQSVLDQLRgeaeaaRRAAEEAEEARVQAEREAAqsRRQVEEAERLKQsaeeqaqaraqaqaaaeklrkeaeqeaarr 2153
Cdd:pfam15921 524 SRVDLKLQELQ------HLKNEGDHLRNVQTECEAL--KLQMAEKDKVIE------------------------------ 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2154 aqaeqaALRQKQAADAEM-EKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQV-- 2230
Cdd:pfam15921 566 ------ILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvn 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2231 --EEELFSVRVQMEELSKLKARIEAENRAL--ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQ---EAAR--LRQLA 2301
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQselEQTRntLKSME 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2302 EED-------LAQQRALAEK-----MLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaEETQGF 2368
Cdd:pfam15921 720 GSDghamkvaMGMQKQITAKrgqidALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQ 798
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 41322914 2369 QRTLeaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2413
Cdd:pfam15921 799 ERRL---KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
48-156 |
2.50e-06 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 50.06 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 48 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 114
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 41322914 115 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 156
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2163-2348 |
2.68e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.88 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2163 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKNLLDEELQRLKAEAteaarqrSQVEEELFSVRVQME 2242
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2243 ELSKLKARIEaenRAL-ILRDKDNT----QRFLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2314
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 41322914 2315 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2348
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1153-1584 |
3.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1153 LRDELRGAQEVGERLQQRHGERDV-EVERWRERVAQLLERwQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDAR 1231
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1232 RRQEQIQAMpladsQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLepvaSPAKKPKVQS 1311
Cdd:COG4717 126 QLLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL----SLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1312 GSESVIQEYVDLRTHYSELTTLTSQyIKFISETLRRMEEE-ERLAEQQRAEERERLAEVEAAL----------------- 1373
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEE-LEELEEELEQLENElEAAALEERLKEARLLLLIAAALlallglggsllslilti 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1374 -EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRsIQEELQQLRQSSEAEIQAKARQAEAAERSRL 1452
Cdd:COG4717 276 aGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE-LLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1453 RIEEEIRVVRLQLEATERQ----RGGAEGElQALRARAEEAEaQKRQAQEEAERLRRQVQDE-SQRKRQAEVELASRVKA 1527
Cdd:COG4717 355 EAEELEEELQLEELEQEIAallaEAGVEDE-EELRAALEQAE-EYQELKEELEELEEQLEELlGELEELLEALDEEELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1528 EAEAAREKQRALQAlEELRLQAEEAERRLRQAEVERARQVQvALETAQRSAEAELQS 1584
Cdd:COG4717 433 ELEELEEELEELEE-ELEELREELAELEAELEQLEEDGELA-ELLQELEELKAELRE 487
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1720-2607 |
3.42e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.82 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1720 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1797
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1798 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEdE 1877
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1878 AFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQkglvedtlrQRRQVEEeilalkasfeKAAAGKAELELELGRIRS 1957
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1958 NAEdtLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2037
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2038 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQL-RGEAEAARRAAEEAEEARVQAEREAAQSRRQVE 2116
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2117 EAERLKQSAEEQAQARAQAQAAAEKlRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR 2196
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2197 LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELsklkarieaenralilrdkdntQRFLQEEAEK 2276
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------------------QDLTEKLSEA 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2277 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlkekmqavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQ 2356
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA-----------LKLTALHALQLTLTQERV--REHALSIRVLPKE 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2357 MAQQlaeetqgfqrtleaerqrqlemsaeaerlklrvaemsraQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2436
Cdd:TIGR00618 674 LLAS---------------------------------------RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2437 TLEIQRQQSdhdAERLREAIAELEREKEKLQQEAKLLQlksEEMQTVQQEQLLQETQALQQSFLsekdsLLQRERFIEQE 2516
Cdd:TIGR00618 715 EYDREFNEI---ENASSSLGSDLAAREDALNQSLKELM---HQARTVLKARTEAHFNNNEEVTA-----ALQTGAELSHL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2517 KAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQ 2596
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
890
....*....|.
gi 41322914 2597 RLREQLQLLEE 2607
Cdd:TIGR00618 864 LTQEQAKIIQL 874
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1329-2062 |
3.55e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.60 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1329 ELTTLTSQYIKFIS---ETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQAEREA---KELQQRMQ 1402
Cdd:pfam07111 56 EGSQALSQQAELISrqlQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1403 EEVVRREeaavdAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSrlrieeeirvvrlqLEATERQRGGAEGELQal 1482
Cdd:pfam07111 135 EEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQLA-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1483 raraeeaeaqkrQAQEEAERLRRQVQdESQRKRQAEVELASRVKaeaeaareKQRALQALEELRLQAEEAERRLRQAEVE 1562
Cdd:pfam07111 194 ------------EAQKEAELLRKQLS-KTQEELEAQVTLVESLR--------KYVGEQVPPEVHSQTWELERQELLDTMQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1563 RARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRaqqqaeaerareeaereLERWQLKA 1642
Cdd:pfam07111 253 HLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSL-----------------LNRWREKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1643 NeALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREarrrGKAEEQAVRQRELaeqelekqrqlaegtaqQRLAAEQELIRL 1722
Cdd:pfam07111 316 F-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVT----SQSQEQAILQRAL-----------------QDKAAEVEVERM 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1723 RAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSekskQRLEAEAGRFRE 1802
Cdd:pfam07111 374 SAKGLQMELSRA--QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLS----NRLSYAVRKVHT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1803 LAEEAARLRALAEeaKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 1882
Cdd:pfam07111 448 IKGLMARKVALAQ--LRQESCPPPPPAPPVDADLSLELEQLRE--ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1883 RLEEQAAQHKADIEERLAQLRKASDSELERQKGLVED--TLRQRRQVEEEILAlKASFEKAAagkaelELELgRIRSNAE 1960
Cdd:pfam07111 524 EVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEaaSLRQELTQQQEIYG-QALQEKVA------EVET-RLREQLS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1961 DTLRskeqaeleaarqrqlaaeeerRRREAEERVQK---SLAAEEEAARQRKAALEEVERLK--AKVEEARRLRERAEQ- 2034
Cdd:pfam07111 596 DTKR---------------------RLNEARREQAKavvSLRQIQHRATQEKERNQELRRLQdeARKEEGQRLARRVQEl 654
|
730 740
....*....|....*....|....*...
gi 41322914 2035 ESARQLQLAQEAAQKRLQAEEKAHAFAV 2062
Cdd:pfam07111 655 ERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
970-1509 |
3.76e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 970 QQLLQSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIA-EQQKAQAEVEGLGKGVARLS 1048
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1049 AEAEKVLAlpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRGTQGAEEVLRAHEEQLKEAQAVpaTLPE 1128
Cdd:TIGR00618 421 DLQGQLAH----------AKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1129 LEATKASLKKLRAQAEAQQPTFDALR---------DELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQT 1199
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1200 DVRQRELEQLGRQLRYYRESADPLGAWLQDARR---RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQrfa 1276
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1277 kQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAE 1356
Cdd:TIGR00618 643 -LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1357 QQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAEREAKELQQRMQEEVV------RREEAAVDAQQQKRSIQEELQQL 1429
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAalqtgaELSHLAAEIQFFNRLREEDTHLL 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1430 RQsSEAEIQAKARQAEAAersRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1509
Cdd:TIGR00618 802 KT-LEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
48-155 |
3.83e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 49.66 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 48 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 114
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 41322914 115 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 155
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2807-2843 |
3.96e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.96e-06
10 20 30
....*....|....*....|....*....|....*..
gi 41322914 2807 IRLLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEM 2843
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1747-1978 |
4.08e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1747 AAAATQKRQELEAELAKVRAEMEVL---LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1823
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELekeLAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1824 AEEDAARQRAEAERVLAeKLAAIGEATRLKteaeiALKEKEAENERLRRLAEDEAFQRRRlEEQAAQHKADIEErLAQLR 1903
Cdd:COG4942 95 LRAELEAQKEELAELLR-ALYRLGRQPPLA-----LLLSPEDFLDAVRRLQYLKYLAPAR-REQAEELRADLAE-LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1904 KASDSELERQKglvedtlRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQ 1978
Cdd:COG4942 167 AELEAERAELE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2261-2416 |
4.38e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.03 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2261 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2337
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2338 QQKELAQEQARRLQEDKE---QMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRaqaRAEEDAQRF---- 2410
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 41322914 2411 -RKQAEE 2416
Cdd:pfam15709 512 aMKQAQE 518
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1356-1538 |
4.45e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1356 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAavdaqqqkrsiqeELQQLRQSSEA 1435
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-------------EEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1436 EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkr 1515
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE--- 166
|
170 180
....*....|....*....|...
gi 41322914 1516 qaevELASRVKAEAEAAREKQRA 1538
Cdd:COG1579 167 ----ELAAKIPPELLALYERIRK 185
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1410-1609 |
4.78e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.16 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1410 EAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvRLQLEATERQrggaeGELQALRARAEEA 1489
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ----RAAAEKAAKQ-----AEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1490 EAQKRQAQEEAErlrrqvqdesqRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL---RQAEVERARQ 1566
Cdd:TIGR02794 120 QAEEAKAKQAAE-----------AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 41322914 1567 VQValETAQRSAEAElQSKRASFAEKTAQLERSLQEEHVAVAQ 1609
Cdd:TIGR02794 189 AKA--EEAKAKAEAA-KAKAAAEAAAKAEAEAAAAAAAEAERK 228
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1682-1976 |
5.43e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 53.30 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRQE 1756
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1757 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1813
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1814 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA 1893
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDES 1777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1894 DIEERlaqlRKASDSELERQKGLVEDtlrqrrqVEEEILALKASFEKAAAGKaelelelgrirsNAEDtLRSKEQAELEA 1973
Cdd:NF012221 1778 DKPNR----QGAAGSGLSGKAYSVEG-------VAEPGSHINPDSPAAADGR------------FSEG-LTEQEQEALEG 1833
|
...
gi 41322914 1974 ARQ 1976
Cdd:NF012221 1834 ATN 1836
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3398-3430 |
5.54e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.78 E-value: 5.54e-06
10 20 30
....*....|....*....|....*....|...
gi 41322914 3398 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 3430
Cdd:pfam00681 7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1376-1504 |
5.83e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.97 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1376 QRQLAEAHAQ-AKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKArQAEAAERSRLRI 1454
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41322914 1455 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1504
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1521-1769 |
5.83e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1521 LASRVKAEAEAAREKQRALQALEElRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1600
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1601 QEEHVAVAQLREEAERRAQQQAEAerareeaerelerWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1680
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL-------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1681 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlaaeqeliRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1760
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*....
gi 41322914 1761 LAKVRAEME 1769
Cdd:COG4942 229 IARLEAEAA 237
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1714-1809 |
5.93e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.03 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1714 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1793
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 41322914 1794 EAEAGRFrELAEEAAR 1809
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
158-265 |
6.40e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 48.26 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 158 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 236
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPgLCPDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 41322914 237 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 265
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1382-1870 |
6.80e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.75 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1382 AHAQAKAQAEREAKELQQR------MQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERsrlr 1453
Cdd:PRK10929 17 AYAATAPDEKQITQELEQAkaaktpAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDnfPKLSAELRQQLNNER---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1454 ieEEIRVVRLQLEAterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRrQVQDESQRKRQAEVElASRVKAEAEaar 1533
Cdd:PRK10929 93 --DEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAR-EISDSLSQLPQQQTE-ARRQLNEIE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1534 ekqRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSA--EAELQSKRASFAEK-TAQLERSLQeehvavaql 1610
Cdd:PRK10929 158 ---RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQ--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1611 reeaerraqqqaeaerareeaerelerwqlkaneALRLRLQAEevaqqkslaqaeaekqkeeaerearrrgkaeeqavRQ 1690
Cdd:PRK10929 226 ----------------------------------ALRNQLNSQ-----------------------------------RQ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1691 RElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQK-RQELEA------ELAK 1763
Cdd:PRK10929 237 RE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlreqsqWLGV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1764 VRAEMEVLLASKARAEEESRStsekskQRLEAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLAE 1841
Cdd:PRK10929 315 SNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDA 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 41322914 1842 KLAA---------------IGEATRLK---TEAEIALKE-KEAENERL 1870
Cdd:PRK10929 384 QLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2170-2607 |
6.84e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2170 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA------EATEAARQRSQVEEELFSVRVQMEE 2243
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2244 LSKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2321
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2322 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEM 2396
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2397 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-EAKL 2472
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2473 LQLKSEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQqrqqqqmeqerqrl 2552
Cdd:PRK03918 542 KSLKKELEK--------------LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER-------------- 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2553 VASMEEARRRQHE---AEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEE 2607
Cdd:PRK03918 594 LKELEPFYNEYLElkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1685-1976 |
6.98e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.99 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRQEL 1757
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1758 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAARQRaeae 1836
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEARNQLR---- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1837 rvlaEKLAAIGEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQLRKA---SDSELERQ 1913
Cdd:pfam19220 273 ----DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEMLTKAlaaKDAALERA 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1914 KGLVEDTLRQRRQVEEEILALKASFEKAAagkAELELELGRIRSNaedtlRSKEQAELEAARQ 1976
Cdd:pfam19220 345 EERIASLSDRIAELTKRFEVERAALEQAN---RRLKEELQRERAE-----RALAQGALEIARE 399
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
623-715 |
7.40e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 623 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 702
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 41322914 703 ALQTQWSWMLQLC 715
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2161-2363 |
7.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2161 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQknLLDEELQRLKAEATEAARQRSQVEEELFSVRVQ 2240
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2241 MEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAArlrqlaeEDLAQQRAlaekmlkekm 2320
Cdd:COG4913 325 LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA-------EEFAALRA---------- 387
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 41322914 2321 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE 2363
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1899-2421 |
8.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1899 LAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELelgrirsnaedtlRSKEQAELEAARQRq 1978
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-------------LEEELEELEAELEE- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1979 laAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2058
Cdd:COG4717 114 --LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2059 AfAVQQKEQELQQTLQQEQSVLDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSA---EEQAQARAQA 2135
Cdd:COG4717 192 E-ELQDLAEELEELQQRLAELEEELE--EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaalLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2136 QAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQR 2215
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2216 LKAEATEAARQRSQVEEElfsvrVQMEELSKLKARIEAENRALIlrdkdntqRFLQEEAEKMKQVAEEAARLSvaaqeaA 2295
Cdd:COG4717 349 LQELLREAEELEEELQLE-----ELEQEIAALLAEAGVEDEEEL--------RAALEQAEEYQELKEELEELE------E 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2296 RLRQLAEEDLAQQRALAEKMLKEKMQAVQEatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE 2375
Cdd:COG4717 410 QLEELLGELEELLEALDEEELEEELEELEE-----ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 41322914 2376 RQRQLEmsaEAERLKLRVAEMSRAQARAEEDAQ-RFRKQAEEIGEKL 2421
Cdd:COG4717 485 LRELAE---EWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3098-3134 |
8.18e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 8.18e-06
10 20 30
....*....|....*....|....*....|....*..
gi 41322914 3098 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 3134
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1231-1563 |
8.99e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1231 RRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGE---KVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKP 1307
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1308 KVQSG-SESVIQEYVDlrthysELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERER---LAEVEAALEKQRQLAEAH 1383
Cdd:pfam07888 121 LAQRAaHEARIRELEE------DIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERkqlQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1384 AQAK-AQAEREAKELQqrMQEEVVRREEAAVDAQQQKRSIQEELQQLR------QSSEAEIQAKARQAEAAERSRLRIEE 1456
Cdd:pfam07888 195 QELRnSLAQRDTQVLQ--LQDTITTLTQKLTTAHRKEAENEALLEELRslqerlNASERKVEGLGEELSSMAAQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1457 EIRVVRLQLEATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREK 1535
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK 352
|
330 340
....*....|....*....|....*...
gi 41322914 1536 QRALQALEELRLQAEEAERRLRQAEVER 1563
Cdd:pfam07888 353 DCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3466-3502 |
9.20e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 9.20e-06
10 20 30
....*....|....*....|....*....|....*..
gi 41322914 3466 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEM 3502
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1018-1610 |
9.33e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1018 EPARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIyleKLKTISL 1097
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHT---RQQIEEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1098 VIRGTQGAEEVLRAHEEQLKEAQAVPATLPELeatkaslkklrAQAEAQQPTFDALRDELRG-----AQEVGERLQQRhg 1172
Cdd:PRK10246 317 NTRLQSTMALRARIRHHAAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1173 erdveveRWRERVAQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLQDARRRQEQIQAmplADSQA 1247
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1248 VREQLRQEQALLEEIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1300
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1301 ASPAKKPKVQSGSESVIQEYVDLRthySELTTLTSQYIKFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1380
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1381 EAHAQAKAQAEREAKELQQRMQEEVVRREEAAvdAQQQKRSIQEELQQLRQSSEAEIQAKARQ--AEAAERSRL--RIEE 1456
Cdd:PRK10246 596 DDIQPWLDAQEEHERQLRLLSQRHELQGQIAA--HNQQIIQYQQQIEQRQQQLLTALAGYALTlpQEDEEASWLatRQQE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1457 EIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DESQRKRQAEVE 1520
Cdd:PRK10246 674 AQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQAQ 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1521 LASRVKAEAEAAREKQRALQALEELRLQAEEAERRLrqaevERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1600
Cdd:PRK10246 754 FDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQ 828
|
650
....*....|
gi 41322914 1601 QEEHVAVAQL 1610
Cdd:PRK10246 829 QELAQLAQQL 838
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1341-1546 |
1.00e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.82 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1341 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQK 1419
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1420 RSIQEELQQLRQsseaeiqakarQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKR----- 1494
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1495 ------QAQEEAERLRRQV-QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1546
Cdd:COG1842 156 sgidsdDATSALERMEEKIeEMEARAEAAAELAAGDSLDDELAELEADSEVEDELAALK 214
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1028-1557 |
1.03e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1028 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRGTQGAEE 1107
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1108 VLRAHEEQLKEAQAVPATLPELEATKASLkklraQAEAQQpTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1187
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1188 LLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLQDARRRQEQIqamplADSQAVREQLRQEQALLEE 1261
Cdd:pfam05557 144 LKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI-----PELEKELERLREHNKHLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1262 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK------------PKVQSGSESVIQEYVDLRTHYSE 1329
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlRSPEDLSRRIEQLQQREIVLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1330 LTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL----------------------AEAHAQA 1386
Cdd:pfam05557 299 NSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgyrailesydkeltMSNYSPQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1387 KAQAEREAKELQQRMQeevVRREEAAVDAQQQKRSIQEELQQLrQSSEAEIQAKARQAEAAERSRLRIE-----EEIRVV 1461
Cdd:pfam05557 378 LLERIEEAEDMTQKMQ---AHNEEMEAQLSVAEEELGGYKQQA-QTLERELQALRQQESLADPSYSKEEvdslrRKLETL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1462 RLQLEATERQRGGAEGEL--QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRAL 1539
Cdd:pfam05557 454 ELERQRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRL 533
|
570 580
....*....|....*....|....*..
gi 41322914 1540 ---------QALEELRLQAEEAERRLR 1557
Cdd:pfam05557 534 pettstmnfKEVLDLRKELESAELKNQ 560
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1342-1592 |
1.05e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.41 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1342 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvrREEAAVDAQQQKRS 1421
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSW--EKEEKRDSRLGRYK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1422 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQ---------------------------RGG 1474
Cdd:pfam02029 130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVkdekikkekkvkyeskvfldqkrghpeVKS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1475 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK----RQAEVELASRvkaEAEAAREKQR-ALQALEEL---- 1545
Cdd:pfam02029 210 QNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKleelRRRRQEKESE---EFEKLRQKQQeAELELEELkkkr 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41322914 1546 ---RLQAEEAERRLRQAEVERarqvQVALETAQRSAEAELQSKRASFAEK 1592
Cdd:pfam02029 287 eerRKLLEEEEQRRKQEEAER----KLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1308-1523 |
1.05e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1308 KVQSGSESVIQEYVDLRTHYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1382
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1383 --HAQAKAQAEREAKELQQRMQEevvRREEAavdaqQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIrv 1460
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAPA---RREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1461 vrlqleaTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS 1523
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1773-1972 |
1.14e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.35 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1773 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLAEKLAAIGEATRL 1852
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1853 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEIL 1932
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 41322914 1933 ALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1972
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1681-2064 |
1.21e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.55 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1681 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1753
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1754 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1828
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1829 ARQRAEAERvlaeklaaiGEATRL---KTEAEIA---------LKEKEAENERLRRLAEDEAFQRRR---LEEQAAQHKA 1893
Cdd:NF033838 209 AKAKVESKK---------AEATRLekiKTDREKAeeeakrradAKLKEAVEKNVATSEQDKPKRRAKrgvLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1894 DIEErlaqlrKASDSELERQKgLVEDTLRQRRQVEEEILALKASFEKAAAGKAE------------LELELgrirsnAED 1961
Cdd:NF033838 280 ENDA------KSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEI------AES 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1962 TLRSKEqAELEAARQRQLAAEEERRRREAEERVQKSLAAE---EEAARQRKAALEEVERlkaKVEEARRLRER-AEQ-ES 2036
Cdd:NF033838 347 DVKVKE-AELELVKEEAKEPRNEEKIKQAKAKVESKKAEAtrlEKIKTDRKKAEEEAKR---KAAEEDKVKEKpAEQpQP 422
|
410 420
....*....|....*....|....*....
gi 41322914 2037 ARQLQLAQEAAQKRLQAEE-KAHAFAVQQ 2064
Cdd:NF033838 423 APAPQPEKPAPKPEKPAEQpKAEKPADQQ 451
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3932-3970 |
1.21e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.21e-05
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 3932 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 3970
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
45-144 |
1.27e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 47.27 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 45 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 120
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 41322914 121 LVNIRNDDIADGNPKLTLGLIWTI 144
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1696-2084 |
1.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1696 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR--EAAAATQKRQELEAELAKVRAEMEvlla 1773
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1774 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEaervlaeklaaigEATRLK 1853
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA-------------ELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1854 TEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVedtlrqrrQVEEEILA 1933
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL--------FLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1934 LKASF---EKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2010
Cdd:COG4717 288 LLFLLlarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2011 ALEEVERL--KAKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEKA-HAFAVQQKEQELQQTLQQEQSVLDQLR 2084
Cdd:COG4717 368 LEQEIAALlaEAGVEDEEELRAALEQaEEYQELKEELEELEEQLEELLGElEELLEALDEEELEEELEELEEELEELE 445
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1785-2056 |
1.41e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1785 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA-EIALKEK 1863
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1864 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfeKAAA 1943
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA---EREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1944 GKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAK-V 2022
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270
....*....|....*....|....*....|....
gi 41322914 2023 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2056
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE 290
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1355-1783 |
1.52e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.06 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1355 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1434
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1435 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1514
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1515 RQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTA 1594
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1595 QLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE 1674
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1675 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1754
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 41322914 1755 QELEAELAKVRAEMEVLLASKARAEEESR 1783
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2178-2612 |
1.58e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2178 AEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRLKAEATEAARQRSQVEEELfSVRVQMEELSKLKARIEAENRA 2257
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2258 LI-LRDKDNTQRFLQEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2336
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2337 QQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARAEEDAQRFRKQAE 2415
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2416 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllqETQAL 2495
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---------IAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2496 QQSFLSEKDSLLQRERFIEQEKAKLEQLfqdEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVrrkqe 2575
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL----- 448
|
410 420 430
....*....|....*....|....*....|....*..
gi 41322914 2576 elqqleqqrrqqeellaeenQRLREQLQLLEEQHRAA 2612
Cdd:COG4717 449 --------------------EELREELAELEAELEQL 465
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1682-1897 |
1.60e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.10 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ-------------LLEEEL 1740
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVikagarpdnsaviAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1741 ARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1820
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1821 RQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1897
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2273-2432 |
1.64e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2273 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2352
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2353 DKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2432
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1432-1645 |
1.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1432 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1509
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1510 ESQRKRQAEV-------------ELASRVKAEAEAAREKQRALQALEELRLQAEEAerrlrQAEVERARQVQVALETAQR 1576
Cdd:COG3883 93 RALYRSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1577 SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1645
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2103-2475 |
1.86e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2103 QAEREAAQSRRQVEEAE-RLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQT 2181
Cdd:COG4717 92 ELQEELEELEEELEELEaELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2182 LRQKAQ------------VEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQmEELSKLKA 2249
Cdd:COG4717 172 LAELQEeleelleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2250 RIEAENRALILRDKDNTQRFLQEE---------------AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLaqQRALAEK 2314
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEEL--EELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2315 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGfqrTLEAERQRQLEMSAEAERLKLRVA 2394
Cdd:COG4717 329 GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV---EDEEELRAALEQAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2395 EMSR--AQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTL---------EIQRQQSDHDAERLREAIAELEREK 2463
Cdd:COG4717 406 ELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELreelaeleaELEQLEEDGELAELLQELEELKAEL 485
|
410
....*....|..
gi 41322914 2464 EKLQQEAKLLQL 2475
Cdd:COG4717 486 RELAEEWAALKL 497
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2003-2347 |
2.13e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2003 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2074
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2075 qeqsvLDQLRgEAEAARRAAEEAEEARVQAEREAAQSR--RQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQeaAr 2152
Cdd:pfam17380 362 -----LERIR-QEEIAMEISRMRELERLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE--A- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2153 raqaeqaalRQKQAADAEMEKhkkfaeqtlrqkaqvEQELTTLRLQLEETDHQknlldeeLQRLKAEATEAARQRSQVEE 2232
Cdd:pfam17380 433 ---------RQREVRRLEEER---------------AREMERVRLEEQERQQQ-------VERLRQQEEERKRKKLELEK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2233 ElfsvrvqmeelSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALA 2312
Cdd:pfam17380 482 E-----------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
330 340 350
....*....|....*....|....*....|....*....
gi 41322914 2313 EKMLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2347
Cdd:pfam17380 551 RRRIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1366-1460 |
2.19e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.11 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1366 LAEVEAALEKQRQLAEAHAQAKAQAEREAkelqQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR-QSSEAEIQAKARQA 1444
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 41322914 1445 EAAERSRLRI---EEEIRV 1460
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
48-155 |
2.29e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 47.31 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 48 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 114
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 41322914 115 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 155
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1343-1580 |
2.38e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAEREAKelqqrmqeevvrreeAAVDAQQ 1417
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAK---------------AAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1418 QKRSIQEELQQLRQSSEAEIQAKARqAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqalRARAEEAEAQKRQAQ 1497
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAK-AKAAALAKQKREGTEEVTEEEKAAAKAKAAAAA------KAKAAALAKQKREGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1498 EEAERlrrqvQDESQRKRQAEVELASRVKAEAeAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1577
Cdd:PRK07735 151 EEVTE-----EEEETDKEKAKAKAAAAAKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
...
gi 41322914 1578 AEA 1580
Cdd:PRK07735 225 QGN 227
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1356-1483 |
2.42e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 49.50 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1356 EQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAKELQQRMQEEVVrreeaavdaQQQKRSIQEELQQLRQSSE 1434
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEaAEQERKLLEEQQRELEQKL---------EDQERSYEEHLRQLKEKME 247
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 41322914 1435 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1483
Cdd:cd16269 248 EERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2170-2610 |
2.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2170 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEelfsVRVQMEELSKLKA 2249
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2250 RIEAENRALILRDKdNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqraLAEKMLKEKMQAVQEATRL 2329
Cdd:PRK03918 249 SLEGSKRKLEEKIR-ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--------FYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2330 KAEAELLQQQKELAQEQARRLQEDKEQMA--QQLAEETQGFQRTLEAERQRQLEMSAEAERLK-LRVAEMSRAQARAEED 2406
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKelEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2407 AQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---------SDHDAERLREAIAELER-EKEKLQQEAKLLQLK 2476
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRiEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2477 SEEMQTvqqeqllqetqalqQSFLSEKDSLLQRERFIEQEKA---KLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLV 2553
Cdd:PRK03918 480 KELREL--------------EKVLKKESELIKLKELAEQLKEleeKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 2554 ASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHR 2610
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
43-151 |
2.47e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 46.52 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 43 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 113
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322914 114 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 151
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1639-2057 |
2.51e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1639 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1718
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1719 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1798
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1799 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA 1878
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1879 FQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSN 1958
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1959 AEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2038
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 41322914 2039 QLQLAQEAAQKRLQAEEKA 2057
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1346-1461 |
2.55e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1346 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA-EREAKELQQRMQEEVVRREEAAVD---------A 1415
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQrqkelemqlA 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41322914 1416 QQQKR----SIQEELQQLRQSSEAEiqaKARQAEAAERsRLRIEEEIRVV 1461
Cdd:pfam15709 463 EEQKRlmemAEEERLEYQRQKQEAE---EKARLEAEER-RQKEEEAARLA 508
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1355-1516 |
2.61e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 50.67 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1355 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1434
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1435 AEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDESQRK 1514
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 41322914 1515 RQ 1516
Cdd:PRK12678 216 EE 217
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2286-2452 |
2.66e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2286 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2362
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2363 ------EETQGFQRTLEAERQRQLEMSAEAERLK-------LRVAEMSRAQAR----------AEEDAQRFRKQAEEIGE 2419
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKeillekveeeARHEAAVLIKEIEEEAK 183
|
170 180 190
....*....|....*....|....*....|....
gi 41322914 2420 klhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2452
Cdd:PRK12704 184 -----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2164-2366 |
2.72e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2164 KQAADAEMEKH----KKFAE---QTLRQ-KAQVEQELTTLRLQLEETDHQknlldeelqrlkAEATEAARQRSQVEEELF 2235
Cdd:NF012221 1549 KHAKQDDAAQNaladKERAEadrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2236 SVRVqmeELSKLKARIEA----------------ENRALILRDK-----DNTQRFLQEEAEKMKQ--------VAEEAAR 2286
Cdd:NF012221 1617 AVTK---ELTTLAQGLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2287 LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQ 2366
Cdd:NF012221 1694 SEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1227-1451 |
2.79e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1227 LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakk 1306
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1307 pKVQSGSESVIQEYVD-LRTHY-----SELTTLTSQyiKFISETLRRMEEEERLAEQQRA------EERERLAEVEAALE 1374
Cdd:COG4942 94 -ELRAELEAQKEELAElLRALYrlgrqPPLALLLSP--EDFLDAVRRLQYLKYLAPARREqaeelrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1375 KQRqlaeahaQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQsSEAEIQAKARQAEAAERSR 1451
Cdd:COG4942 171 AER-------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAA 239
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1347-1565 |
2.94e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1347 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1426
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1427 QQLRQSSEAEIQAKARQAeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1506
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 1507 VQDESQRKRQaevELASRVKAEAEAAREKQR---------ALQALEELRLQAEEAERRLRQAEVERAR 1565
Cdd:pfam05262 333 VAEDLQKTKP---QVEAQPTSLNEDAIDSSNpvyglkvvdPITNLSELVLIDLKTEVRLRESAQQTIR 397
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2185-2737 |
2.99e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2185 KAQVEQELTTLRLQLEETDHQKNLLDEELQRlkaEATEAARQRSQVEEELFSVRVQMEELSKLKAriEAENRALILRDKD 2264
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2265 NTQ-RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2339
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2340 ----KELAQEQARRLQEDKEQMaQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEmsraqaraEEDAQRFRKQAE 2415
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2416 EIGEKLHRTElatQEKVTLVQT-------LEIQ----RQQSDHDAERLREAIAELEREKEK---LQQEAKLLQLKSEEMq 2481
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQArekeihdLEIQltaiKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKEL- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2482 TVQQEQLLQETQALQQSFLSEKDsllQRERFIEQekakLEQLFQDEVakaqqlreeqqRQQQQMEQERQRLVASMEEARR 2561
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKK---QEERMLKQ----IENLEEKEM-----------NLRDELESVREEFIQKGDEVKC 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2562 RQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEE--QHRAALAHSEEVTASQVAATKTLPNGRDaLDG 2639
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLE-LEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2640 PAAEAEPEHSFDGLRRKVSAQRLQEAGIL--------SAEELQRLAQ------GHTTVDELARREDVRH----YLQGRSS 2701
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLeevekakaIADEAVKLQKeidkrcQHKIAEMVALMEKHKHqydkIIEERDS 725
|
570 580 590
....*....|....*....|....*....|....*.
gi 41322914 2702 IAGLLLKATNEKLSVYAALQRQLLSPGTALILLEAQ 2737
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1066-1506 |
3.18e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1066 TLRSELEltlGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQL-----------KEAQAVPATLPE----LE 1130
Cdd:pfam15921 437 AMKSECQ---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtlesseRTVSDLTASLQEkeraIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1131 ATKASLKKLRAQAEAQQPTFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRERVAQLLE-------RWQAVLAQTD 1200
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrTAGAMQVEKA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1201 VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQrfaKQYI 1280
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELN 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1281 NAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTHYSELTTLTSqyikfiseTLRRMEEEERLAeqqra 1360
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA----- 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1361 eererlaeVEAALEKQRQLAEAHAQAKAqaereakelqqrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQssEAEIQAK 1440
Cdd:pfam15921 726 --------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ--ELSTVAT 783
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 1441 ARQAEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQAlrarAEEAEAQKRQAQEEAeRLRRQ 1506
Cdd:pfam15921 784 EKNKMAGELEVLRSQER----RLKEKVANMEVALDKASLQF----AECQDIIQRQEQESV-RLKLQ 840
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2210-2416 |
3.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2210 DEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIlRDKDNTQRFLQEEAEKMKQVAEEAARLSV 2289
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2290 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2361
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 2362 AEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2416
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1687-2055 |
3.30e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1687 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--REAAAATQKRQELEA 1759
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1760 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAARQRAEAERvl 1839
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKS--QLADYQQAL---DVQQTRAIQYQ-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1840 aEKLAAIGEATRLKTEAEIALKEKEAenerlrrlaedeafqrrRLEEQAAQHKADIEERLaqlrkasdsELERQKGLVED 1919
Cdd:PRK04863 418 -QAVQALERAKQLCGLPDLTADNAED-----------------WLEEFQAKEQEATEELL---------SLEQKLSVAQA 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1920 TLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQR-QLAAEEERRRREAEERVQKSL 1998
Cdd:PRK04863 471 AHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNL 550
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1999 AAEEEAARQRKAALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQAEE 2055
Cdd:PRK04863 551 DDEDELEQLQEELEARLESLSESVSEA---RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1651-1827 |
3.40e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1651 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1726
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1727 EQGEQQRQLLEEELArlQREAAAATQKRQELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1801
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 41322914 1802 ELAEEAARLRALAEEAKRQRQLAEED 1827
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1235-1550 |
3.43e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1235 EQIQAMPLADSQAVREQLRQEQALLEEIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSE 1314
Cdd:PRK10929 33 EQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1315 SVIQEYVDLRTHYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAer 1392
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1393 eakelqqrMQEEVVRReEAAVDaqqqkrsiQEELQQLRQSSEAEIqakAR-QAEAAERSRLRIEEEIRVVRLQLEaTERQ 1471
Cdd:PRK10929 178 --------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQALRNQLN-SQRQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1472 RggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL---ASRVKAEA----EAAREKQRALQALEE 1544
Cdd:PRK10929 237 R------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQALNT 304
|
....*.
gi 41322914 1545 LRLQAE 1550
Cdd:PRK10929 305 LREQSQ 310
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1407-1760 |
3.81e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1407 RREEAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1486
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1487 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1566
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1567 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1646
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1647 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1726
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 41322914 1727 EQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1760
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2189-2418 |
3.95e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2189 EQELTTLRLQLEE----TDHQKNLLDEELQRLKAEATEAARQRS-----QVEEELFSVRVQMEELSKLKARI-EAENRal 2258
Cdd:COG3096 450 EQQATEEVLELEQklsvADAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRYRSQQALAQRLQQLRAQLaELEQR-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2259 iLRDKDNTQRFLQEEAEKMKQVAEEAARLsvaaqeaarlrqlaEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2338
Cdd:COG3096 528 -LRQQQNAERLLEEFCQRIGQQLDAAEEL--------------EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2339 Q-KEL---------AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQ 2408
Cdd:COG3096 593 RiKELaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
250
....*....|
gi 41322914 2409 RFRKQAEEIG 2418
Cdd:COG3096 673 RLLALAERLG 682
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1346-1554 |
4.01e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1346 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREakelQQRMQEEVVRREEAAVDAQQQKRSIQEE 1425
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRR-FEEIRLRKQRLEEE----RQRQEEEERKQRLQLQAAQERARQQQEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1426 LQQLRQsseaEIQAKaRQAEAAERSrlrieeeirvvrlqlEATERQRGGAEGELqalraraeeAEAQKRQAQ-EEAERLr 1504
Cdd:pfam15709 428 FRRKLQ----ELQRK-KQQEEAERA---------------EAEKQRQKELEMQL---------AEEQKRLMEmAEEERL- 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 41322914 1505 rqvqdESQRKRQaEVELASRVKAEAEAAREKQRALQALEELRLQAEEAER 1554
Cdd:pfam15709 478 -----EYQRQKQ-EAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1716-1865 |
4.05e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1716 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1794
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1795 AE----AGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEatrLKTEAEIALKEKEA 1865
Cdd:COG1579 96 KEieslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREE 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2275-2636 |
4.06e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2275 EKMKQVAEEaarLSVAAQEAARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARRLQED 2353
Cdd:TIGR02169 170 RKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKR-EYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2354 keqmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSraqaraEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2433
Cdd:TIGR02169 246 ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2434 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqQEQLLQETQALQQSFLSEKDSLLQRERFI 2513
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-LEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2514 EQEKAKLEQL------FQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRkqeelqqleqqRRQQ 2587
Cdd:TIGR02169 395 EKLKREINELkreldrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-----------LAAD 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 41322914 2588 EELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDA 2636
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2282-2623 |
4.10e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2282 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2361
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2362 AEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQ 2436
Cdd:pfam02463 239 IDLLQELLRDEQEEIEsskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2437 TLEIQRQQSDHDAERLREAIAELEREKeKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQE 2516
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2517 KAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvasmEEARRRQHEAEEGVR-RKQEELQQLEQQRRQQEELLAEEN 2595
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL----EEEEESIELKQGKLTeEKEELEKQELKLLKDELELKKSED 472
|
330 340
....*....|....*....|....*...
gi 41322914 2596 QRLREQLQLLEEQHRAALAHSEEVTASQ 2623
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQ 500
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4140-4168 |
4.21e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.21e-05
10 20
....*....|....*....|....*....
gi 41322914 4140 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4168
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2770-2806 |
4.21e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.21e-05
10 20 30
....*....|....*....|....*....|....*..
gi 41322914 2770 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 2806
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1322-1601 |
4.72e-05 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 49.45 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1322 DLRTHYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-AKAQAERE-A 1394
Cdd:pfam15450 226 ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdAKGQLEESqA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1395 KELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAE------AAERSRLRIEEEirVVRLQLEAT 1468
Cdd:pfam15450 304 GELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ--TLGLKLSEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1469 ERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAarekqralqaleelrl 1547
Cdd:pfam15450 382 KKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKA---------------- 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322914 1548 qaeeaerrlRQAEVERARQ--------VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQ 1601
Cdd:pfam15450 446 ---------REFEVEAMRQelaallssVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1783-1949 |
4.80e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1783 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1861
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1862 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQR--RQVEEEILALKASFE 1939
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARHEAAVLI 175
|
170
....*....|
gi 41322914 1940 KAAAGKAELE 1949
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1334-1500 |
5.38e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1334 TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQ--AKAQAEREAKELQQRMQEEVVRREE- 1410
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPn 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1411 --AAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIR-------VVRLQLEATERQRGGAEGELQA 1481
Cdd:COG3206 290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlaelpELEAELRRLEREVEVARELYES 369
|
170
....*....|....*....
gi 41322914 1482 LRARAEEAEAQKRQAQEEA 1500
Cdd:COG3206 370 LLQRLEEARLAEALTVGNV 388
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1483-1658 |
5.59e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1483 RARAEEAEAQ------KRQAQEEAERLRrQVQDESQRKRQAEVELASRVKAEAEAAReKQRalqaLEELRLQAEEAER-- 1554
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQRRLQ-QEQLERAEKMREELELEQQRRFEEIRLR-KQR----LEEERQRQEEEERkq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1555 -RLRQAEVERARQVQVA----LETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERARE 1629
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKA 490
|
170 180 190
....*....|....*....|....*....|....
gi 41322914 1630 EAERelERWQLKANEALRLRL-----QAEEVAQQ 1658
Cdd:pfam15709 491 RLEA--EERRQKEEEAARLALeeamkQAQEQARQ 522
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
47-148 |
5.71e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 45.49 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 47 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHF 148
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2255-2621 |
6.01e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2255 NRALILRDKDNTQRflQEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2329
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2330 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGF--QRTLEAERQRQLEMSAEAERLkLRVAE 2395
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2396 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2475
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2476 KSEEMQtvqqeqllqetqalqqsflsekdslLQRERFIEQEKAKLEQLFQdEVAKAQQLREEQQRQQQQMEQERQRLVAS 2555
Cdd:COG3096 505 RSQQAL-------------------------AQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322914 2556 MEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR------LREQLQLLEEQHRAALAHSEEVTA 2621
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTA 630
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2242-2369 |
6.07e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 48.34 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2242 EELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarlRQLAEEDLAQQRALAE--KMLKEK 2319
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEK 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41322914 2320 MQavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQ 2369
Cdd:cd16269 246 ME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1416-1551 |
6.11e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1416 QQQKRSIQEELQQLRQ---SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQALR 1483
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 1484 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEE 1551
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2267-2476 |
6.20e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2267 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2346
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2347 ARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERlklRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2426
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 41322914 2427 ATQEKvtlvqTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2476
Cdd:pfam13868 191 AQQEK-----AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQ 235
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1350-2058 |
6.47e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1350 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1425
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1426 LQQLR-QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ-----LEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1499
Cdd:PRK04863 378 QEENEaRAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1500 AERLRRQVQDESQRKRQAEV--ELASRVKAEAEAAREKQRALQALEELRLQAEEAER----RLRQAEVERARQVQVALET 1573
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEQayQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1574 AQRSAEaelqsKRASFAEKTAQLERSLQEEHVAvaqlreeaerrAQQQAEAERAREEAERELERWQLKANEALRLRLQAE 1653
Cdd:PRK04863 538 LLAEFC-----KRLGKNLDDEDELEQLQEELEA-----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1654 EVAQQKslaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRaetEQGEQQR 1733
Cdd:PRK04863 602 APAWLA-----------------------AQDALARLREQSGEEFEDSQDV-TEYMQQLLERERELTVER---DELAARK 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1734 QLLEEELARL-QREAAAATQKRQ-----------------------ELEAELAKVRAEMEVLLASKAR------------ 1777
Cdd:PRK04863 655 QALDEEIERLsQPGGSEDPRLNAlaerfggvllseiyddvsledapYFSALYGPARHAIVVPDLSDAAeqlagledcped 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1778 -----------------AEEESRSTSEKSKQRlEAEAGRFRE--LAEEAARlRALAEEAKRQRQLAEEDAARQRAE---- 1834
Cdd:PRK04863 735 lyliegdpdsfddsvfsVEELEKAVVVKIADR-QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREELAERYATLSFDvqkl 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1835 ------AERVLAEKLA---------AIGEATRLKTEAEIALKEKEAENERLR--------------------RLAEDEAF 1879
Cdd:PRK04863 813 qrlhqaFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHESQEQQQRsqleqakeglsalnrllprlNLLADETL 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1880 QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGRIR--- 1956
Cdd:PRK04863 893 ADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQRRahf 971
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1957 --SNAEDTLrSKEQAELEAARQRQLAAEEERRRREAE-----------ERVQKSLAAEEEAARQ-RKAALEEVE----RL 2018
Cdd:PRK04863 972 syEDAAEML-AKNSDLNEKLRQRLEQAEQERTRAREQlrqaqaqlaqyNQVLASLKSSYDAKRQmLQELKQELQdlgvPA 1050
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 41322914 2019 KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2058
Cdd:PRK04863 1051 DSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2695-2733 |
6.50e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 42.70 E-value: 6.50e-05
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 2695 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 2733
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1487-1566 |
6.65e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 49.56 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1487 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL----ASRVKAE--AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1559
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAeaqqQELVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 41322914 1560 EVERARQ 1566
Cdd:PRK11448 218 RKEITDQ 224
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2265-2732 |
6.77e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.20 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2265 NTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2344
Cdd:COG4995 7 LALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2345 EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2424
Cdd:COG4995 87 LALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2425 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLkseemqtvqqeqLLQETQALQQSFLSEKD 2504
Cdd:COG4995 167 ALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAA------------LAALLLALLALAAALLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2505 SLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQR 2584
Cdd:COG4995 235 LLLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2585 RQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQE 2664
Cdd:COG4995 315 LALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 2665 AGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLL-LKATNEKLSVYAALQRQLLSPGTALI 2732
Cdd:COG4995 395 LLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1273-1604 |
6.77e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 49.24 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1273 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTHY-SELTTLTSQyikfiSETLRRMEEE 1351
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1352 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA--------KELQQRMQEEVVRREEAAVDAQQQKRSIQ 1423
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRrnyptntyKTLELEIAESDVEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1424 EELQQLRQsSEAEIQAKarQAEAaerSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRARAEEAEAQKRQA------ 1496
Cdd:NF033838 201 RDEEKIKQ-AKAKVESK--KAEA---TRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1497 --------QEEAERLRRQVQDES----QRKRQAEVELASRVKAEAEAAREKQR-------ALQALEELRLQAEEAERRLR 1557
Cdd:NF033838 272 epatpdkkENDAKSSDSSVGEETlpspSLKPEKKVAEAEKKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDVKVK 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 41322914 1558 QAEVERARQV--QVALETAQRSAEAELQSKRA--SFAEKTAQLERSLQEEH 1604
Cdd:NF033838 352 EAELELVKEEakEPRNEEKIKQAKAKVESKKAeaTRLEKIKTDRKKAEEEA 402
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1106-1822 |
6.82e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.36 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1106 EEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqptfdaLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1184
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1185 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplGAWLQDARRRQEQIQAMpLADSQavrEQLRQEQALLEEIER 1264
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRKQ-LSKTQ---EELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1265 H-GEKV------EECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTHYSELTTLTSQY 1337
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1338 IKFISETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKeLQQRMQEEvvrreeaAVDAQ 1416
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDK-------AAEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1417 QQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1496
Cdd:pfam07111 370 VERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1497 QEEAER--LRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEEL--RLQAEEAERRLRQAEVERARQVQVAle 1572
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVA-- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1573 taqRSAEAELQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRlqa 1652
Cdd:pfam07111 527 ---QQLEQELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR--- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1653 EEVAQQKSLAQAEAEKQKEEAEREARrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE-----QELIRLRAETE 1727
Cdd:pfam07111 566 QELTQQQEIYGQALQEKVAEVETRLR-----EQLSDTKRRLNEARREQAKAVVSLRQIQHRATQekernQELRRLQDEAR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1728 QGEQQR-----QLLEEE----LARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRL 1793
Cdd:pfam07111 641 KEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSL 720
|
730 740
....*....|....*....|....*....
gi 41322914 1794 EAEAGRFRELAEEAARLRALAEEAKRQRQ 1822
Cdd:pfam07111 721 TVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2179-2482 |
7.57e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2179 EQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE--------------LFSVRVQMEEL 2244
Cdd:pfam15921 345 EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitIDHLRRELDDR 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2245 SKLKARIEAENRALILRDKDNTQR---FLQEEAEKMKQVAEEAARLSVAAQeaaRLRQLAEEDLAQQRALAEK------- 2314
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERqmaAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEELTAKKMTLESSertvsdl 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2315 --MLKEKMQAVQ----EATRLKAEAEL-LQQQKELAQE--QARRLQEDKEQMAQQLAEEtqgfQRTLEAERQRQLEMSAE 2385
Cdd:pfam15921 502 taSLQEKERAIEatnaEITKLRSRVDLkLQELQHLKNEgdHLRNVQTECEALKLQMAEK----DKVIEILRQQIENMTQL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2386 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQR-QQSDHDAERLReAIAELEREKE 2464
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvKLVNAGSERLR-AVKDIKQERD 656
|
330 340 350
....*....|....*....|....*....|....*.
gi 41322914 2465 KLQQEAKL------------------LQLKSEEMQT 2482
Cdd:pfam15921 657 QLLNEVKTsrnelnslsedyevlkrnFRNKSEEMET 692
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3801-3837 |
7.74e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 7.74e-05
10 20 30
....*....|....*....|....*....|....*..
gi 41322914 3801 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3837
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1685-2006 |
7.77e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1764
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1765 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1844
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1845 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR 1924
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1925 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEA 2004
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
..
gi 41322914 2005 AR 2006
Cdd:COG4372 368 AD 369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1407-1745 |
7.84e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1407 RREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1486
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1487 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1566
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1567 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1646
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1647 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1726
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330
....*....|....*....
gi 41322914 1727 EQGEQQRQLLEEELARLQR 1745
Cdd:COG4372 323 ELAKKLELALAILLAELAD 341
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2172-2650 |
7.88e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2172 EKHKKFAEQTLRQKAQVEQELTTLRLQL-EETDHQKNLLDEELQRLKAEATEAARQRSQV---EEELFSVRVQMEELSKL 2247
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2248 KARIEAENRAlilrdkdntQRFLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2327
Cdd:pfam12128 477 REEQEAANAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2328 RLKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA------ 2399
Cdd:pfam12128 539 FLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsare 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2400 -QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKS 2477
Cdd:pfam12128 619 kQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2478 EEMQTVQQEQLLQETQALQQSFL---SEKDSLLQR-----ERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQER 2549
Cdd:pfam12128 699 QAWLEEQKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREI 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2550 QRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE----VTASQVA 2625
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMerkaSEKQQVR 857
|
490 500 510
....*....|....*....|....*....|...
gi 41322914 2626 ATKTLPNGRD--------ALDGPAAEAEPEHSF 2650
Cdd:pfam12128 858 LSENLRGLRCemsklatlKEDANSEQAQGSIGE 890
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1343-1538 |
7.90e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEER---LAEQQRAEererlaeveaaLEKQRQLAEAHAQAKAQAEREAKELQQRMQ----------EEVVRRE 1409
Cdd:PLN03188 1052 ERLRWTEAESKwisLAEELRTE-----------LDASRALAEKQKHELDTEKRCAEELKEAMQmamegharmlEQYADLE 1120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1410 EAAVDAQQQKRSIQEELQQLRQsseAEIQAKARQAE-------AAERSRLRI--EEEIRVVRLQLEATERQ-RGGAE--- 1476
Cdd:PLN03188 1121 EKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISALKVerEKERRYLRDENKSLQAQlRDTAEavq 1197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 1477 --GELQALRARAEEA--EAQKR--QAQEEAERLRRQVqDESQRKRQAEVELASRVKAEAEAAREKQRA 1538
Cdd:PLN03188 1198 aaGELLVRLKEAEEAltVAQKRamDAEQEAAEAYKQI-DKLKRKHENEISTLNQLVAESRLPKEAIRP 1264
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1705-2201 |
7.92e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.09 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1705 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV----------RAEMEVLLAS 1774
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1775 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1854
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1855 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILAL 1934
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1935 KASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2014
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2015 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAA 2094
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2095 EEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2174
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 41322914 2175 KKFAEQTLRQKAQVEQELTTLRLQLEE 2201
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1363-1773 |
7.94e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1363 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvRREEAAVDAQQQKRSIQEELQQLRQSSEAEiqaKAR 1442
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERL-AELEAKRQAEEEAREAKAEAEQRAAELAAE---AAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1443 QAEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELA 1522
Cdd:COG3064 78 KLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1523 SRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1602
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1603 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1682
Cdd:COG3064 232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1683 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1762
Cdd:COG3064 312 AAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGI 391
|
410
....*....|.
gi 41322914 1763 KVRAEMEVLLA 1773
Cdd:COG3064 392 LAAAGGGGLLG 402
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2213-2426 |
8.16e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2213 LQRLKAEATEAARQRSQVEEElfsvrvQMEELSKLKARIEAENRALilrdkdnTQRFLQEEAEKmKQvAEEAARLSVAAQ 2292
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL-------EKERLAAQEQK-KQ-AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2293 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQGFQRT 2371
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 2372 LEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2426
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2217-2407 |
8.89e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2217 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAAR 2296
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2297 LRQLAEEDLAQQrALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGfQRTLEAER 2376
Cdd:TIGR02794 126 AKQAAEAKAKAE-AEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK-AKAEAAKA 203
|
170 180 190
....*....|....*....|....*....|.
gi 41322914 2377 QRQLEMSAEAERLKLRVAEMsRAQARAEEDA 2407
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAA-EAERKADEAE 233
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1796-1915 |
9.16e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.79 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1796 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLAEKLAAIGEATRLKTEAEIA-LKEKEAE 1866
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1867 NERLRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA---SDSE-LERQKG 1915
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKAgweADSKtLRFSKG 261
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1681-1803 |
9.41e-05 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 47.51 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1681 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATQKR 1754
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 41322914 1755 QELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1803
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1343-1837 |
9.59e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.50 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1422
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1423 QEELQQLRQSSEAEIQAKARQAEAAERSRlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1502
Cdd:COG3064 83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAE------------KAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1503 LRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAEL 1582
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1583 QSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1662
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1663 QAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1742
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1743 LQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ 1822
Cdd:COG3064 391 ILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVA 470
|
490
....*....|....*
gi 41322914 1823 LAEEDAARQRAEAER 1837
Cdd:COG3064 471 LDGGAVLADLLLLGG 485
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1685-1880 |
1.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1761
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1762 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1826
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1827 DAARQRAEAERVLAEKLAAIG-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1880
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3354-3388 |
1.07e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.07e-04
10 20 30
....*....|....*....|....*....|....*
gi 41322914 3354 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 3388
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1699-2062 |
1.20e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1699 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA--AATQKRQELEAELAKVRAEM--EVLLAS 1774
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeeEAREAKAEAEQRAAELAAEAakKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1775 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1854
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1855 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILAL 1934
Cdd:COG3064 164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1935 KASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2014
Cdd:COG3064 244 ALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAA 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 41322914 2015 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAV 2062
Cdd:COG3064 324 AGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4389-4426 |
1.20e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|....*...
gi 41322914 4389 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 4426
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
48-145 |
1.21e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 48 QKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 114
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 41322914 115 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 145
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2181-2413 |
1.24e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2181 TLRQKAQVEQELTTLRLQleetdhQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIL 2260
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2261 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2334
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 2335 LLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2413
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3970-4004 |
1.27e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.27e-04
10 20 30
....*....|....*....|....*....|....*
gi 41322914 3970 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4004
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2161-2463 |
1.31e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.75 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2161 LRQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQknlldeeLQRLKAEATEAARQRSQVEEELFSVRVQ 2240
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2241 MEELSKLKARIEAENRALILRDKDNTQRFLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2319
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2320 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAEETQGFQRT---LEAERQRQLEMSAEAERLKLRVAEM 2396
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2397 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLREaiaELEREK 2463
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1837-2608 |
1.35e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1837 RVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqHKADIEERLAQLRKASDSELERQKgl 1916
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGYELLKEK-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1917 vEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAED-TLRSKEQAELEAARQRQLAAEEERRRREAEERVQ 1995
Cdd:TIGR02169 233 -EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1996 KSLAAEEEAARQRKAALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAAQK---------RLQAEEKAHAFAVQQKE 2066
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELkeeledlraELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2067 QELQQtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAE-RLKQSAEEqaqaraqaqaaaeklrke 2145
Cdd:TIGR02169 389 DYREK--------LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEaKINELEEE------------------ 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2146 aeqeaarraqaeqaalrqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEA---TE 2222
Cdd:TIGR02169 443 ------------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQArasEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2223 AARQRSQVEEELFS----VRVQMEELSKLKAR------IEAENR--ALILRDKDNTQR---FLQEEA---------EKMK 2278
Cdd:TIGR02169 505 RVRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMR 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2279 QVAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAE 2332
Cdd:TIGR02169 585 DERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2333 AELLQQQKElaqEQARRLQEDKEQMAQQLAeetqGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK 2412
Cdd:TIGR02169 665 GILFSRSEP---AELQRLRERLEGLKRELS----SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2413 QAEEIGEKLhrtelatqekvtlvQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-----EAKLLQLKSEEMQtvQQEQ 2487
Cdd:TIGR02169 738 RLEELEEDL--------------SSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQ--AELS 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2488 LLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAE 2567
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 41322914 2568 E---GVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQ 2608
Cdd:TIGR02169 882 SrlgDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1485-1609 |
1.37e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1485 RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRalQALEELRL------QAEEAERRLRQ 1558
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQaalkqkQAEEAAAKAAA 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 41322914 1559 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ 1609
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1798-2044 |
1.40e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1798 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDE 1877
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1878 AFQRRRLEEQAAQHKADIEE------RLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELE 1951
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1952 LGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2030
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 41322914 2031 RAEQESAR-QLQLAQ 2044
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1430-1583 |
1.59e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 47.03 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1430 RQSSEAEIQAKARQAEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1507
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 1508 QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQ 1583
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1706-2110 |
1.76e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.59 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1706 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1785
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1786 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA 1865
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1866 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGK 1945
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1946 AELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2025
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2026 RRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAE 2105
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAA 512
|
....*
gi 41322914 2106 REAAQ 2110
Cdd:COG5278 513 AEAAL 517
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4279-4312 |
1.78e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.78e-04
10 20 30
....*....|....*....|....*....|....
gi 41322914 4279 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4312
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1476-1610 |
1.79e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1476 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDesqRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERR 1555
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322914 1556 LRQ--AEVERARQvQVALETAQRSAEAELQSK----RASFAEKTAQLERSLQEEHVAVAQL 1610
Cdd:pfam09787 141 IKDreAEIEKLRN-QLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1672-1835 |
1.81e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1672 EAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQElirlrAETEQGEQQRQL-LEEELARLQREAAAA 1750
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA-----YEIAEANAEREVqRQLEIAEREREIELQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1751 TQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEedAA 1829
Cdd:COG2268 296 EKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IA 370
|
....*.
gi 41322914 1830 RQRAEA 1835
Cdd:COG2268 371 EAAAKP 376
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1686-2056 |
1.84e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.72 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1686 QAVRQRELAEQELEKQRQ-------LAEGTAQQRLAAEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATQkrqelE 1758
Cdd:pfam05701 32 QTVERRKLVELELEKVQEeipeykkQSEAAEAAKAQVLEELESTKRLIEE-------LKLNLERAQTEEAQAKQ-----D 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1759 AELAKVRA-EMEVLLASKARAeeESRSTSEKSKQRLEAEAGRFRELAEEaarLRALAEEakRQRQLAEEDAARQRAEaER 1837
Cdd:pfam05701 100 SELAKLRVeEMEQGIADEASV--AAKAQLEVAKARHAAAVAELKSVKEE---LESLRKE--YASLVSERDIAIKRAE-EA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1838 VLAEKlaAIGEATRLKTEAEIALKEK---------EAENERLR----------------RLAEDEAfqrRRLEEQAA--- 1889
Cdd:pfam05701 172 VSASK--EIEKTVEELTIELIATKESlesahaahlEAEEHRIGaalareqdklnwekelKQAEEEL---QRLNQQLLsak 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1890 --QHKADIEERLAQLRKAS-----DSELERQKGLVEDTLRQRRQVEEEILALKASFE--KAAAGKAELELELGRIrsnAE 1960
Cdd:pfam05701 247 dlKSKLETASALLLDLKAElaaymESKLKEEADGEGNEKKTSTSIQAALASAKKELEevKANIEKAKDEVNCLRV---AA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1961 DTLRS---KEQAELEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAArqrKAALEEVERLKAKVEEARRLRERAE--- 2033
Cdd:pfam05701 324 ASLRSeleKEKAELASLRQREgMASIAVSSLEAELNRTKSEIALVQAKE---KEAREKMVELPKQLQQAAQEAEEAKsla 400
|
410 420 430
....*....|....*....|....*....|...
gi 41322914 2034 ----------QESARQLQLAQEAAQKRLQAEEK 2056
Cdd:pfam05701 401 qaareelrkaKEEAEQAKAAASTVESRLEAVLK 433
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1355-1486 |
2.01e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.96 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1355 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ-AKAQAERE-AKELQQRMQEEVvrrEEAAVDAQQqkrsiQEELQQLRQS 1432
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlAAAQAQLDlAQRELERYQALY---KKGAVSQQE-----LDEARAALDA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 41322914 1433 SEAEIQAkARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1486
Cdd:COG1566 160 AQAQLEA-AQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2276-2625 |
2.12e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2276 KMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALaekmLKEKMQAvqeatrlKAEAELLQQQKELAQEQARRLQEDKE 2355
Cdd:pfam02463 166 RLKRKKKEALK--KLIEETENLAELIIDLEELKLQE----LKLKEQA-------KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2356 QMAQQLAEEtqgFQRTLEAERQRQLEMSAEAErlklrvaemsrAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlV 2435
Cdd:pfam02463 233 KLNEERIDL---LQELLRDEQEEIESSKQEIE-----------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE---E 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2436 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqlLQETQALQQSFLSEKDSLLQRERFIEQ 2515
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE-----LKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2516 EKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEA-----EEGVRRKQEELQQLEQQRRQQEEL 2590
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeekkEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350
....*....|....*....|....*....|....*
gi 41322914 2591 LAEENQRLREQLQLLEEQHRAALAHSEEVTASQVA 2625
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1352-1603 |
2.21e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1352 ERLAEQQRAEERERLAEVEaalekqrqlaeahaqakaQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQE---E 1425
Cdd:pfam10174 453 ERLKEQREREDRERLEELE------------------SLKKENKDLKEKvsaLQPELTEKESSLIDLKEHASSLASsglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1426 LQQLRQSSEAEIQA-------------KARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1492
Cdd:pfam10174 515 KDSKLKSLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1493 K---------------RQAQEEAERLR--RQVQDESQRKRQAEVELASRVK-AEAEAAREKQRA--LQALEELRLQAEEA 1552
Cdd:pfam10174 595 KndkdkkiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDAT 674
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1553 ERRLRQAEV--------------ERARQVQVALETAQRSAEAELQSKRASFA--EKTAQLERSLQEE 1603
Cdd:pfam10174 675 KARLSSTQQslaekdghltnlraERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE 741
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2163-2436 |
2.22e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2163 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVR 2238
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2239 VQMEELSKL-----KARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE------DLAQ 2307
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdelraKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2308 QRALAEKMLKEKMQAVQEATRL----KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMS 2383
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRqelqQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2384 AEAERLklrvaEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2436
Cdd:pfam13868 293 RELEKQ-----IEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1070-1286 |
2.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1070 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLkklraqaEAQQPT 1149
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1150 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLGAWLQD 1229
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1230 ARRRQEQIQAMPladsQAVREQLRQEQ-ALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1286
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERIdALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1352-1516 |
2.31e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1352 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQ 1431
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1432 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1511
Cdd:PRK12678 158 ADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236
|
....*
gi 41322914 1512 QRKRQ 1516
Cdd:PRK12678 237 DARGD 241
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2162-2469 |
2.40e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.73 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2162 RQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQM 2241
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2242 EELSKLKARIEAENRAlilrdkDNTQRflqeeaekmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQ 2321
Cdd:pfam15905 132 LELTRVNELLKAKFSE------DGTQK-----------------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2322 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRqLEMSAEAERLKLRVAEMSRAQA 2401
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2402 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQE 2469
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1063-1929 |
2.45e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1063 AAPTLRsELELTLGKLEQVRSLSAIYLEKLKTISLVIRGT--------QGAEEVLRAHE-------EQLKEAQAVPATLP 1127
Cdd:TIGR00606 187 ALETLR-QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYEneldplkNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1128 ELEATKASLKKLRAQAEAQQPTFDALRDE-LRGAQEVGERLQQRHGERDVEVERWRERVaqllerwqavlaqtdvrQREL 1206
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDC-----------------QREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1207 EQLGRQLRYYRESADPL----GAWLQDARRRQEQIQAMplaDSQAVREQLRQEQALLEE---IER-----HGEKVEECQR 1274
Cdd:TIGR00606 329 EKLNKERRLLNQEKTELlveqGRLQLQADRHQEHIRAR---DSLIQSLATRLELDGFERgpfSERqiknfHTLVIERQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1275 FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK--VQSGSESVIQEYVDLRTHYSELTTLT--SQYIKFISETLRRMEE 1350
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGrtIELKKEILEKKQEELKFVIKELQQLEgsSDRILELDQELRKAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1351 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKELQQRMQEEVVRREEAAVDAQQQK---RSIQEELQ 1427
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKiksRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1428 QLRQSSEAEIQAKARQAEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-----AQKRQAQE-EAE 1501
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTR--DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdVCGSQDEEsDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1502 RLRRQVqdESQRKRQAEVELASRVKAE--AEAAREK-------QRALQALEELRLQAEEAERRLRQA------------E 1560
Cdd:TIGR00606 643 RLKEEI--EKSSKQRAMLAGATAVYSQfiTQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRLApdklksteselkK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1561 VERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQlREEAERRAQQQAEAERAREEAERELERWQL 1640
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQM 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1641 KANEALRlrlqaeEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLaaeQELI 1720
Cdd:TIGR00606 800 ELKDVER------KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT---NELK 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1721 RLRAETEQGEQQRQLLEEELARLQREA----AAATQKRQE---LEAELAKVRAEMEVLLASK----ARAEEESRSTSEKS 1789
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVqsliREIKDAKEQdspLETFLEKDQQEKEELISSKetsnKKAQDKVNDIKEKV 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1790 KQRLEAEAGRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAE------AERVLAEKLaaigeaTRL 1852
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDgkddylkqketELNTVNAQLEECEKHQEKINEDMRLMRQDidtqkiQERWLQDNL------TLR 1024
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1853 KTEAEIalkeKEAENERLRRLAedEAFQRRRLEEQAAQHKadIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEE 1929
Cdd:TIGR00606 1025 KRENEL----KEVEEELKQHLK--EMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1411-1592 |
2.48e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1411 AAVDAQQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE 1490
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1491 AQKRQA--QEEAERLRRQVQDESQRKRQAEvELASRVKAEAEAAREKQRALQA-LEELRLQAEEAERRLRQAEVERARQv 1567
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAeLAELEAELEEKKAELDEELAELEAE- 157
|
170 180
....*....|....*....|....*
gi 41322914 1568 qvaletaqrsaEAELQSKRASFAEK 1592
Cdd:COG1579 158 -----------LEELEAEREELAAK 171
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
185-262 |
2.52e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 43.06 E-value: 2.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 185 DNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 262
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2103-2469 |
2.58e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2103 QAEREAAQSRRQVEEAERLKQSAEEQAQARAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAeQTL 2182
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEE---------------------------KYKELSASSEELSEEKD-ALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2183 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRAL--IL 2260
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2261 RDKDNTQRFLQEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQ 2338
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2339 QKELAQ------EQARRLQEDKEQMAQqlaeETQGFQRTLEAERQRQLEMSAEAERLKLRVaemsraqarAEEDAQRfrk 2412
Cdd:pfam07888 278 RLQAAQltlqlaDASLALREGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERL---------QEERMER--- 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 2413 qaeeigEKLhRTELATQEKVTLVQTLEIQRQQSDhdaerLREAIAELEREKEKLQQE 2469
Cdd:pfam07888 342 ------EKL-EVELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAE 386
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2288-2566 |
2.58e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2288 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAEeTQG 2367
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLAA-ISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2368 FQRTLEAERQRQLEMSAEAERlklrvaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2447
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2448 DAE---RLREAIAE--LEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSllqrerfiEQEKAKLEQ 2522
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 41322914 2523 LFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRR-QHEA 2566
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3689-3724 |
2.89e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.89e-04
10 20 30
....*....|....*....|....*....|....*.
gi 41322914 3689 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 3724
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3429-3460 |
2.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.97e-04
10 20 30
....*....|....*....|....*....|..
gi 41322914 3429 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 3460
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2183-2481 |
3.01e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2183 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRD 2262
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2263 KDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKEL 2342
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE--REEEREAEREEIEEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2343 AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLH 2422
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 2423 RTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2481
Cdd:pfam13868 262 EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1945-2624 |
3.03e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1945 KAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE 2024
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2025 ARRLRERAEQESARQLQLAQEAAQ-KRLQAEEKAHAFAvqqkeqelqqtlqqeqsvldqlrgeaeaarraaeeaeearvQ 2103
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVLEET-----------------------------------------Q 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2104 AERE-AAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQK--QAADAEMEKHKKFAEQ 2180
Cdd:TIGR00618 284 ERINrARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllQTLHSQEIHIRDAHEV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2181 TLRQKAQVEQElTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIL 2260
Cdd:TIGR00618 364 ATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2261 RdkdntQRFLQEEAEKMKQVAEEAARLSVAAQEaaRLRQLAE-EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2339
Cdd:TIGR00618 443 C-----AAAITCTAQCEKLEKIHLQESAQSLKE--REQQLQTkEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2340 KELA---QEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2416
Cdd:TIGR00618 516 ARQDidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2417 IGEKLHRTELATQEKVTLVQTLEIQRQQSDHD----------AERLREAIAELEREKEKL----QQEAKLLQLKSEEMQT 2482
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLqdvrlhlqqcSQELALKLTALHALQLTLtqerVREHALSIRVLPKELL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2483 VQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRR 2562
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV 755
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2563 QHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLRE------QLQLLEEQHRAALAHSEEVTASQV 2624
Cdd:TIGR00618 756 LKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLreedthLLKTLEAEIGQEIPSDEDILNLQC 823
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1695-1926 |
3.28e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1695 EQELeKQRQLAEGTAQ----QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAaaatqkRQELEAELAKVRA---- 1766
Cdd:PRK10929 29 TQEL-EQAKAAKTPAQaeivEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAEL------RQQLNNERDEPRSvppn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1767 ------EMEVLLAS-------------KARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAE----EAKRQRQL 1823
Cdd:PRK10929 102 mstdalEQEILQVSsqlleksrqaqqeQDRAREISDSLSQLPQQQTEAR----RQLNEIERRLQTLGTpntpLAQAQLTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1824 AEEDAARQRAEAERVLAEKLAAIG--EATRLKteAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1901
Cdd:PRK10929 178 LQAESAALKALVDELELAQLSANNrqELARLR--SELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGD 255
|
250 260
....*....|....*....|....*
gi 41322914 1902 LRKASDSELERQKGLvEDTLRQRRQ 1926
Cdd:PRK10929 256 LPKSIVAQFKINREL-SQALNQQAQ 279
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2211-2419 |
3.44e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2211 EELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKM-----KQVAEEAA 2285
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2286 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLA 2362
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 2363 EETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2419
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2176-2343 |
3.51e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.38 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2176 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKNLLDEElqrlkAEATEAARQRSQVEEELFSVRVQMEELSKlkarieaen 2255
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALRS--------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2256 ralILRDKDNTQRFLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEA 2333
Cdd:COG3524 243 ---YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEA 316
|
170
....*....|
gi 41322914 2334 EllQQQKELA 2343
Cdd:COG3524 317 A--RQQRYLA 324
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3354-3388 |
3.52e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.77 E-value: 3.52e-04
10 20 30
....*....|....*....|....*....|....*
gi 41322914 3354 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 3388
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2178-2362 |
3.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2178 AEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAarQRSQVEEELFSVRVQME-ELSKLKARIEAENR 2256
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2257 ALilrdkdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2336
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
170 180
....*....|....*....|....*.
gi 41322914 2337 QQQKELAQEqarRLQEDKEQMAQQLA 2362
Cdd:COG3206 364 RELYESLLQ---RLEEARLAEALTVG 386
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1262-1602 |
3.62e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.87 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1262 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVaSPAKKPKVQSGSESVIQEY-VDLRTHYSELTTLTSQYIKF 1340
Cdd:COG5185 154 GEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGI-SELKKAEPSGTVNSIKESEtGNLGSESTLLEKAKEIINIE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1341 ISETLRRMEEEERLAEQQRAEERERLAEVEAAL--EKQRQLAEAHAQAKAQAEREAKELQQrmQEEVVRREEAAVDAQQQ 1418
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrlEKLGENAESSKRLNENANNLIKQFEN--TKEKIAEYTKSIDIKKA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1419 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEATERQRGGAEGElQALRARAEEAEAQKRQAQE 1498
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTA-EIEQGQESLTENLEAIKEEIENIVGE-VELSKSSEELDSFKDTIES 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1499 EAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEElrlQAEEAERRLRQAEVERARQVQVA-------L 1571
Cdd:COG5185 389 TKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATS---SNEEVSKLLNELISELNKVMREAdeesqsrL 465
|
330 340 350
....*....|....*....|....*....|.
gi 41322914 1572 ETAQRSAEAELQSKRASFAEKTAQLERSLQE 1602
Cdd:COG5185 466 EEAYDEINRSVRSKKEDLNEELTQIESRVST 496
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1606-2061 |
3.77e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.93 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1606 AVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE 1685
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1686 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR 1765
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1766 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1845
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1846 IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRR 1925
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1926 QVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 2005
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 2006 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2061
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1681-1828 |
3.86e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1681 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQREAAAATQKRQELEA 1759
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1760 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDA 1828
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLEH 506
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1682-1841 |
4.01e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.82 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRQELEA 1759
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1760 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1835
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....*.
gi 41322914 1836 ERVLAE 1841
Cdd:COG1842 207 EDELAA 212
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1349-1610 |
4.06e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1349 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAK-------ELQQRMQEEVVRREEAAVDAQQQKRS 1421
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgqgglDEEEAFLDRTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1422 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEI--RVVRLQLEATE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1498
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1499 EAERLRRQV-----QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQvqvALET 1573
Cdd:pfam02029 165 EAEEVPTENfakeeVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE---EEAE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41322914 1574 AQRSAEAELQSKRASFAEKTAQ----LERSLQEEHVAVAQL 1610
Cdd:pfam02029 242 VFLEAEQKLEELRRRRQEKESEefekLRQKQQEAELELEEL 282
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1347-1706 |
4.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1347 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1426
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1427 QQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1506
Cdd:COG4372 83 EELNE----QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1507 VQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKR 1586
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1587 ASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1666
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 41322914 1667 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE 1706
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1372-1543 |
4.13e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1372 ALEKQRQLA--------EAHAQAKAQA-EREAKEL--QQRMQEEVvrreeaavDAQQQKRsiqeELQQLRQSSEAEIQAK 1440
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARGRleRQKMHDKA--------KAEEQRT----KLLELQAESAAVESSG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1441 ARQAEA-AERSRLRIEEEirvvrlqleaterqrggAEGELQALRARAEEAEAQKrqaqeEAERLR-RQVQDESQRKRQAE 1518
Cdd:PTZ00491 716 QSRAEAlAEAEARLIEAE-----------------AEVEQAELRAKALRIEAEA-----ELEKLRkRQELELEYEQAQNE 773
|
170 180
....*....|....*....|....*
gi 41322914 1519 VELasrvkaeaeaarEKQRALQALE 1543
Cdd:PTZ00491 774 LEI------------AKAKELADIE 786
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2245-2479 |
4.14e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2245 SKLKARIEAENRALILRdkdntQRFlqeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQ 2324
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAK-----ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2325 EATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQR-----------QLEMSAEAERLKLRV 2393
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaqqaaNAEAEEEVDPKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2394 -AEMSRAQAR---AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREK-EKLQQ 2468
Cdd:PRK05035 583 aAAIARAKAKkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKaRKAAQ 662
|
250
....*....|.
gi 41322914 2469 EAKLLQLKSEE 2479
Cdd:PRK05035 663 QQANAEPEEAE 673
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1345-1509 |
4.20e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1345 LRRMEEEERLAEQQRAEERERLAEVEAA--LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1422
Cdd:pfam00038 136 LKKNHEEEVRELQAQVSDTQVNVEMDAArkLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1423 QEELQQLR---QSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqRGgaEGELQALRARAEEAEAQKRQAQEE 1499
Cdd:pfam00038 216 KEEITELRrtiQSLEIELQSLKKQKASLERQLAETEE---------------RY--ELQLADYQELISELEAELQETRQE 278
|
170
....*....|
gi 41322914 1500 AERLRRQVQD 1509
Cdd:pfam00038 279 MARQLREYQE 288
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2179-2436 |
4.47e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2179 EQTLR---QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRS------QVEEELFSVRVQmeeLSKLKA 2249
Cdd:PRK11281 66 EQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAQTLDQ---LQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2250 RIEAENRALIlrdkdnTQRFLQEEAEkmkqvaeeaARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQEATrl 2329
Cdd:PRK11281 143 DLAEYNSQLV------SLQTQPERAQ---------AALYANSQRLQQIRNLLKGGKVGGKALRPS-QRVLLQAEQALL-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2330 kaEAELLQQQKELA-----QE--QARRlqEDKEQMAQQLAEETQGFQrtlEAERQRQLEMSAEAerlklrVAEMSRAQAR 2402
Cdd:PRK11281 205 --NAQNDLQRKSLEgntqlQDllQKQR--DYLTARIQRLEHQLQLLQ---EAINSKRLTLSEKT------VQEAQSQDEA 271
|
250 260 270
....*....|....*....|....*....|....*
gi 41322914 2403 AEEDAQRFRKQAEEIGEKLHRTEL-ATQEKVTLVQ 2436
Cdd:PRK11281 272 ARIQANPLVAQELEINLQLSQRLLkATEKLNTLTQ 306
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1340-1402 |
4.50e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 46.79 E-value: 4.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322914 1340 FISETLRRmeEEERLAEQQraEERERLAEVEAALEKQRQLAEA-HAQAKAQAEREAKELQQRMQ 1402
Cdd:PLN02316 249 FLLEEKRR--ELEKLAKEE--AERERQAEEQRRREEEKAAMEAdRAQAKAEVEKRREKLQNLLK 308
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2733-2766 |
4.58e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.58e-04
10 20 30
....*....|....*....|....*....|....
gi 41322914 2733 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2766
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1360-1602 |
4.68e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1360 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLRQSSEAEIQA 1439
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEAAPKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1440 KARqaeaaersrlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEV 1519
Cdd:pfam12795 74 ILA-------------------SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1520 ELASRVKAEAEAAREKQRALQA--------LEELRLQAEEAERR--LRQAEVERARQVQVALETAQRSAEAELQSKRASF 1589
Cdd:pfam12795 135 RLNGPAPPGEPLSEAQRWALQAelaalkaqIDMLEQELLSNNNRqdLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQE 214
|
250
....*....|....
gi 41322914 1590 AEKT-AQLERSLQE 1602
Cdd:pfam12795 215 AEQAvAQTEQLAEE 228
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2210-2430 |
5.36e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.13 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2210 DEELQRLKAEATEAARQRSQveEELfsVRVQMEELSKLKARIEAENRALILRDKDNTqrflqEEAEKMKQVAEEAARLSV 2289
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEAR--KRL--VAKHGAEISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2290 AAQEAARLRQLAEEDLAQQRALAekmlkekmqavqeATRLKAEAELLQQQKELAQEQARrlQEDKEQMAQQLAEETQGfq 2369
Cdd:PRK07735 75 AKQKREGTEEVTEEEKAKAKAKA-------------AAAAKAKAAALAKQKREGTEEVT--EEEKAAAKAKAAAAAKA-- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322914 2370 RTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE 2430
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEE 198
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1363-1472 |
5.48e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 45.36 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1363 RERLAEVEAALEKQRQLAEAH-AQAKAQAEREAKELQQRMQEEVVRREEAavDAQQQKRSIQEELQQLRQSSEAEIQAKA 1441
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEkAIEAERAKAEAAEAEQELLREKQKEEEQ--MMEAQERSYQEHVKQLIEKMEAEREQLL 260
|
90 100 110
....*....|....*....|....*....|.
gi 41322914 1442 RQAEAAERSRLRIEEEIRVVRLQLEATERQR 1472
Cdd:pfam02841 261 AEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1699-1974 |
5.51e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 45.62 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1699 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1775
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1776 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1835
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1836 ErvLAEKLAAIG---EATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLRKASDS 1908
Cdd:pfam03148 159 D--LSDKKEALEideKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 1909 ELERQKGLVEDTLRQRrqVEEeilalkasFEKAaagKAELELELGRIRSNAEDTlrSKEQAELEAA 1974
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTLQEIAEL--EKNIEALEKA 287
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2277-2476 |
5.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2277 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE- 2355
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2356 ----QMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2431
Cdd:COG4717 128 lplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41322914 2432 vtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2476
Cdd:COG4717 208 ---LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1379-1585 |
5.65e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.61 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1379 LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKarqaeaaersrlrieeei 1458
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1459 rvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkrqaeveLASRVKAEAEAarekqRA 1538
Cdd:COG3524 222 -----LIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERAR-------LTGASGGDSLA-----SL 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 41322914 1539 LQALEELRLQAEEAERRLRQAeverarqvQVALETAQrsAEAELQSK 1585
Cdd:COG3524 285 LAEYERLELEREFAEKAYTSA--------LAALEQAR--IEAARQQR 321
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3764-3800 |
5.80e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.80e-04
10 20 30
....*....|....*....|....*....|....*..
gi 41322914 3764 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 3800
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2161-2325 |
5.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2161 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQ 2240
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2241 mEELSKLKARIEAENRALILRDKDnTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2320
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 41322914 2321 QAVQE 2325
Cdd:COG1579 167 ELAAK 171
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1025-1568 |
5.91e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1025 QRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQG 1104
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1105 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQE-------VGERLQQRHGERDVE 1177
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRI 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1178 VERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQA 1257
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1258 LLEEIERHGEKVEECQR---FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLT 1334
Cdd:pfam02463 605 LAQLDKATLEADEDDKRakvVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1335 SQYIKFISETLRRMEEEERlaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEA--- 1411
Cdd:pfam02463 685 AESELAKEEILRRQLEIKK--KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeek 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1412 ---AVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEE 1488
Cdd:pfam02463 763 eeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1489 AEAQKRQ--AQEEAERLrrqvQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1566
Cdd:pfam02463 843 KEEQKLEklAEEELERL----EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
..
gi 41322914 1567 VQ 1568
Cdd:pfam02463 919 IE 920
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3135-3171 |
6.93e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 6.93e-04
10 20 30
....*....|....*....|....*....|....*..
gi 41322914 3135 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEET 3171
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3061-3095 |
6.93e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 6.93e-04
10 20 30
....*....|....*....|....*....|....*
gi 41322914 3061 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 3095
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1385-1600 |
6.98e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1385 QAKAQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQEELQQLRQ------SSEAEIQAK--------ARQAEAA 1447
Cdd:PRK11637 54 QDIAAKEKSVRQQQQQrasLLAQLKKQEEAISQASRKLRETQNTLNQLNKqidelnASIAKLEQQqaaqerllAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1448 ERsrlriEEEIRVVRLQLEATERQRG------------GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1515
Cdd:PRK11637 134 FR-----QGEHTGLQLILSGEESQRGerilayfgylnqARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1516 QAEVELASRVK--AEAEAAREKQRalQALEELRLQaeeaERRLR----QAEVE-RARQVQVALEtAQRSAEAELQSKRAS 1588
Cdd:PRK11637 209 KLEQARNERKKtlTGLESSLQKDQ--QQLSELRAN----ESRLRdsiaRAEREaKARAEREARE-AARVRDKQKQAKRKG 281
|
250
....*....|..
gi 41322914 1589 FAEKTAQLERSL 1600
Cdd:PRK11637 282 STYKPTESERSL 293
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1100-1551 |
7.34e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1100 RGTQGAEEVLRAHEEQLKEAQAVPA----------------TLPELEATKASLKKLRAQAEAQQP-------TFDALrdE 1156
Cdd:PRK10246 441 RLAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqladvkTICEQEARIKDLEAQRAQLQAGQPcplcgstSHPAV--E 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1157 LRGAQEVGERlQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQ 1236
Cdd:PRK10246 519 AYQALEPGVN-QSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDD 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1237 IQamPLADSQAVRE----QLRQEQALLEEIERHGEKVEEcqrfakqyinaikdYELQLVTYKAQLEPVASPAKKPKVQSG 1312
Cdd:PRK10246 598 IQ--PWLDAQEEHErqlrLLSQRHELQGQIAAHNQQIIQ--------------YQQQIEQRQQQLLTALAGYALTLPQED 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1313 SESviqeyvdlrthySELTTltsqyikfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1392
Cdd:PRK10246 662 EEA------------SWLAT----------------RQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEET 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1393 EAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1472
Cdd:PRK10246 714 VALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1473 GGAegelQALRARAEEAEAQKRQAQEE-------AERLRRQVQDESQRKRQ---AEVELASRVKAEAEAAREKQRALQAL 1542
Cdd:PRK10246 794 QQA----QTLVTQTAQALAQHQQHRPDgldltvtVEQIQQELAQLAQQLREnttRQGEIRQQLKQDADNRQQQQALMQQI 869
|
....*....
gi 41322914 1543 EELRLQAEE 1551
Cdd:PRK10246 870 AQATQQVED 878
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1682-1978 |
7.92e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.72 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRELAEQElekQRQLAEGTAQqrlaaeqelIRLRAETEQGEQQRQLLEE--ELARLQREAAAATQKRQ-ELE 1758
Cdd:COG5185 279 RLNENANNLIKQFENT---KEKIAEYTKS---------IDIKKATESLEEQLAAAEAeqELEESKRETETGIQNLTaEIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1759 AELAKVRAEMEVLLASKARAEEESRstSEKSKQRLEAEAGRFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERV 1838
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVE--LSKSSEELDSFKDTIESTKES---LDEIPQNQRGYAQEILATLEDTLKAADRQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1839 LAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA-----QHKADIEERLAQLRKASDS---EL 1910
Cdd:COG5185 422 IEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrsvrSKKEDLNEELTQIESRVSTlkaTL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1911 ERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA--EDTLRSKEQAELEAARQRQ 1978
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELiqASNAKTDGQAANLRTAVID 571
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2163-2363 |
7.94e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2163 QKQAADAEMEKHKKFAEQT--LRQKAQVEQElttlRLQLEEtdhQKNLLDEELQRLKAEATEAARQRSQVEEElfsVRVQ 2240
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLE---KERLAAQEQKKQAEEAAKQAALKQKQAEE---AAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2241 MEELSKLKAriEAENRALilrdkdntqrflqeeAEKMKQVAEEAARLSVAAQEAarlrQLAEEdlAQQRALAEkmlkEKM 2320
Cdd:PRK09510 141 AAAAAKAKA--EAEAKRA---------------AAAAKKAAAEAKKKAEAEAAK----KAAAE--AKKKAEAE----AAA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 41322914 2321 QAVQEAtRLKAEAELLQQQKELAQEQARRlqEDKEQMAQQLAE 2363
Cdd:PRK09510 194 KAAAEA-KKKAEAEAKKKAAAEAKKKAAA--EAKAAAAKAAAE 233
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1432-1566 |
7.96e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1432 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDES 1511
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1512 QRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1566
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1489-1937 |
8.21e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.52 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1489 AEAQKRQAQEEAERLRRQVQDES-QRKRQAEVElASRVKAEAEAAREKQRALQALEElrlqAEEAERRLRQAEVERA-RQ 1566
Cdd:pfam09731 73 SAVTGESKEPKEEKKQVKIPRQSgVSSEVAEEE-KEATKDAAEAKAQLPKSEQEKEK----ALEEVLKEAISKAESAtAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1567 VQVALETAQRSAEAELQSKRASFA-EKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1645
Cdd:pfam09731 148 AKEAKDDAIQAVKAHTDSLKEASDtAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEH 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1646 LRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQqrLAAEQELIRLRAE 1725
Cdd:pfam09731 228 LDNVEEKVEKAQSLAKLVDQYKEL------------VASERIVFQQELVSIFPDIIPVLKEDNLL--SNDDLNSLIAHAH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1726 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASkaraeeesrstsEKSKQRLEAEagrfrelae 1805
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAA------------DEAQLRLEFE--------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1806 eaarlRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR-RRL 1884
Cdd:pfam09731 353 -----REREEIRESYEEKLRTELERQAEAHEEHLKDVLVE--QEIELQREFLQDIKEKVEEERAGRLLKLNELLANlKGL 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322914 1885 EEQAAQHKADIEERLA--QLRKASDSelerqkglVEDTLR------QRRQVEEEILALKAS 1937
Cdd:pfam09731 426 EKATSSHSEVEDENRKaqQLWLAVEA--------LRSTLEdgsadsRPRPLVRELKALKEL 478
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2165-2418 |
8.46e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2165 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA-----EATEAARQRSQVEEELFSVRV 2239
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLREQRH 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2240 QMEELSKLKARI-EAENRaliLRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2318
Cdd:PRK04863 511 LAEQLQQLRMRLsELEQR---LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2319 KMQAVQEATRLKAEAELLQQqkelAQEQARRLQE---DKEQMAQQLaeeTQGFQRTLEAERQRQLEMSAEAERLKLRVAE 2395
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLA----AQDALARLREqsgEEFEDSQDV---TEYMQQLLERERELTVERDELAARKQALDEE 660
|
250 260
....*....|....*....|...
gi 41322914 2396 MSRAQARAEEDAQRFRKQAEEIG 2418
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAERFG 683
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1682-1875 |
8.73e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1761
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1762 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1841
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 41322914 1842 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAE 1875
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2295-2470 |
9.09e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.38 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2295 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLAEETQG 2367
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2368 FQRTLEAERQRQLemsaeAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDh 2447
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP- 332
|
170 180
....*....|....*....|...
gi 41322914 2448 DAERLREAIAELEREKEKLQQEA 2470
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2163-2371 |
9.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2163 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRLKAEATEAAR--QRSQVEEELFSVRVQ 2240
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERREELGERARalYRSGGSVSYLDVLLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2241 MEELSKLKARIEAENRaLILRDKD--NTQRFLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2317
Cdd:COG3883 111 SESFSDFLDRLSALSK-IADADADllEELKADKAELEAKKaELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 41322914 2318 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRT 2371
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1343-1447 |
9.24e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 43.93 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQ-------AEREAKELQQRMQEEVVRREEA-- 1411
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKqkaaesaSKSLAKPERKVSQEEAKEVLQEwe 148
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322914 1412 -AVDAQQQKRsiQEELQQLRQSSEAEIQAKARQAEAA 1447
Cdd:pfam13904 149 rKKLEQQQRK--REEEQREQLKKEEEEQERKQLAEKA 183
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1258-1751 |
9.42e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1258 LLEEIERHGEKVEECQRFAKQYI---NAIKDY---ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELT 1331
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLkelIEKKDHltkELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1332 TLTSQYIKFISE---TLRRMEEEERlAEQQRAEERE-RLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvr 1407
Cdd:pfam05483 342 KAKAAHSFVVTEfeaTTCSLEELLR-TEQQRLEKNEdQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED--- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1408 reEAAVDAQQQKRSIQEELQQ-------LRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE-------------- 1466
Cdd:pfam05483 418 --EKLLDEKKQFEKIAEELKGkeqelifLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahcd 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1467 --ATERQRGGAEGELQALRARAEEAEAQKRQAQEEA--------ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1536
Cdd:pfam05483 496 klLLENKELTQEASDMTLELKKHQEDIINCKKQEERmlkqienlEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1537 RALQ---------------ALEELRLQAEEAERRLRQAEVE-RARQVQVALETAQRSA--------EAELQSKRASFAEK 1592
Cdd:pfam05483 576 RSIEyevlkkekqmkilenKCNNLKKQIENKNKNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEI 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1593 TAQLERSLQEEHVAVAQLREEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKslaqaeaekqkEE 1672
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEE---------------------VEKAKAIADEAVKLQKEIDKRCQHK-----------IA 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1673 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1751
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2264-2433 |
9.57e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.38 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2264 DNTQRFLQEEAEKMKQVAEEAarlSVAAQEAARLRQlaEEDLAQqrALAEKMLKEKMQAVQEATRLKAEAElLQQQKEla 2343
Cdd:pfam05262 202 DLKERESQEDAKRAQQLKEEL---DKKQIDADKAQQ--KADFAQ--DNADKQRDEVRQKQQEAKNLPKPAD-TSSPKE-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2344 qeqARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQlemsAEAERLKLRVAEMSRAQARAEEDAQRFRkqaEEIGEKLHR 2423
Cdd:pfam05262 272 ---DKQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR---EPVAEDLQK 339
|
170
....*....|
gi 41322914 2424 TELATQEKVT 2433
Cdd:pfam05262 340 TKPQVEAQPT 349
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2116-2437 |
9.88e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2116 EEAERLKQSAEEQAQARAQAQAAAEKLRkeaeqeAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLrqkaqvEQELTTL 2195
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIA------EYTKSIDIKKATESLEEQLAAAEAEQELEESKR------ETETGIQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2196 RLQlEETDHQKNLLDEELQRLKAEATE--AARQRSQVEEELFSVRVQMEElskLKARIEAENRALilrdKDNTQRFLQEE 2273
Cdd:COG5185 340 NLT-AEIEQGQESLTENLEAIKEEIENivGEVELSKSSEELDSFKDTIES---TKESLDEIPQNQ----RGYAQEILATL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2274 AEKMKQVAEEAARLSVAaqeaarLRQLAEEDLAQQRAL--AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEqARRLQ 2351
Cdd:COG5185 412 EDTLKAADRQIEELQRQ------IEQATSSNEEVSKLLneLISELNKVMREADEESQSRLEEAYDEINRSVRSK-KEDLN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2352 EDKEQMAQQLAEETQGFQrTLEAERQRQLE-----MSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2426
Cdd:COG5185 485 EELTQIESRVSTLKATLE-KLRAKLERQLEgvrskLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAA 563
|
330
....*....|.
gi 41322914 2427 ATQEKVTLVQT 2437
Cdd:COG5185 564 NLRTAVIDELT 574
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1346-1602 |
1.02e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1346 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREakelqqrmqeevvrREEAAVDAQQQKRSIQE 1424
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1425 ELQqLRQSSEAEIQAKARQAEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQAQEEAERLR 1504
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNHEEEVRELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1505 RQVQDESqrkRQAEV------ELAS-----RVKAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEVERA---RQ 1566
Cdd:pfam00038 149 AQVSDTQ---VNVEMdaarklDLTSalaeiRAQYEEIAAKNREEAeewyQSKLEELQQAAARNGDALRSAKEEITelrRT 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41322914 1567 VQ-------------VALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1602
Cdd:pfam00038 226 IQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQE 274
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
41-145 |
1.02e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 42.05 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 41 VDERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGR 98
Cdd:cd21294 3 INEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 41322914 99 MRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 145
Cdd:cd21294 76 NNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1372-1885 |
1.03e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1372 ALEKQRQLAEAHAQA---KAQAEREAKELQQrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---EIQAKARQAE 1445
Cdd:pfam05557 22 ELEHKRARIELEKKAsalKRQLDRESDRNQE-LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEAlnkKLNEKESQLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1446 AAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ---DESQRKRQAEVELA 1522
Cdd:pfam05557 101 DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSslaEAEQRIKELEFEIQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1523 SRV-------KAEAEAAR--EKQRALQALEE--------------LRLQAEEAERRLRQaeVERARQVQVALETAQRSAE 1579
Cdd:pfam05557 181 SQEqdseivkNSKSELARipELEKELERLREhnkhlnenienkllLKEEVEDLKRKLER--EEKYREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1580 AELQSkrasfAEKTAQ---------------LERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQ 1639
Cdd:pfam05557 259 QELQS-----WVKLAQdtglnlrspedlsrrIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLkkiedLNKK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1640 LKANEALRLRLQAEEVAQQKS-------LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA--- 1709
Cdd:pfam05557 334 LKRHKALVRRLQRRVLLLTKErdgyraiLESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1710 -QQRLAAEQELIRLRAETEQGEQQRQllEEELARLQREAaaatqkrQELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1788
Cdd:pfam05557 414 kQQAQTLERELQALRQQESLADPSYS--KEEVDSLRRKL-------ETLELERQRLREQKNELEMELERRCLQGDYDPKK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1789 SK---QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervlAEKLAAIGEATRLKTEAEIA--LKEK 1863
Cdd:pfam05557 485 TKvlhLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDD------------LEQVLRLPETTSTMNFKEVLdlRKEL 552
|
570 580
....*....|....*....|..
gi 41322914 1864 EAENERLRRLaeDEAFQRRRLE 1885
Cdd:pfam05557 553 ESAELKNQRL--KEVFQAKIQE 572
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1341-1446 |
1.05e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 44.59 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1341 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAK------AQ--AEREAKELQQRMQEEV-V 1406
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEvakiqmQQkiMEKEAEKKISEIEDEMhL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 41322914 1407 RREEAAVDAQQQKRSIQEELQQLRQSSE----AEIQAKARQAEA 1446
Cdd:cd03406 237 AREKARADAEYYRALREAEANKLKLTPEylelKKYQAIANNTKI 280
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3689-3727 |
1.13e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.23 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|....*....
gi 41322914 3689 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 3727
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1363-1568 |
1.14e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1363 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEelqQLRQSSEAEIQAKAR 1442
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAE---AASAPEAAQARERRE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1443 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqaLRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAEVELA 1522
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEE-----EERDERRRRGDREDRQAEAERGERG--RREERGRDGDDRDR 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 41322914 1523 SRVKAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEVERARQVQ 1568
Cdd:PRK12678 206 RDRREQGDRREERGRRDGGDRrGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1373-1595 |
1.19e-03 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 44.86 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1373 LEKQRQLAEAHAQAKAqAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKaRQAEAAERSRL 1452
Cdd:pfam08017 31 LERRQRDAENRSQGNV-LERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER-RQRDAENRSQG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1453 RIEEEIR---VVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEA 1529
Cdd:pfam08017 109 NVLERRQrdaENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQG 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1530 EAAREKQRAlqalEELRLQAEEAERRLRQAEVERARQVqvaLETAQRSAEAELQ----SKRASFAEKTAQ 1595
Cdd:pfam08017 189 NVLERRQRD----AENRSQGNVLERRQRDAENRSQGNV---LERRQRDAENRSQgnvlERRQRDAENKSQ 251
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2268-2480 |
1.21e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2268 RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2343
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2344 QEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARA----EEDAQRFRKQAEEIG 2418
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322914 2419 EKLHRTELATQEKVTLVQTLEIQRQQ------SDHDAERLREAIAELErEKEKLQQ------EAKLLQLKSEEM 2480
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldtemaQLRVQRLRYEDL 355
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1709-2006 |
1.23e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1709 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAA----TQKRQELEAELAKVRAEME----VLLASKARAEE 1780
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErlaeLEAKRQAEEEAREAKAEAEqraaELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1781 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA 1856
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKaeeaKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1857 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKA 1936
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1937 SFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAAR 2006
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1710-1972 |
1.27e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1710 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKS 1789
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK----EL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1790 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAARQR--------------AEAERVLAEKLAaigeatRLKTE 1855
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGG--SIDKLRKEierlewrqqtevlsPEEEKELVEKIK------ELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1856 AEIALKEKEAENERLRRLAEDEAFQrrrleEQAAQHKADIEERLAQLRKASDS------ELERQKGLVEDTLRQRRQVEE 1929
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELR-----KEAEEIHKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 41322914 1930 EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1972
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2273-2408 |
1.28e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2273 EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2348
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322914 2349 RLQEDKEQmaQQLAEetqgfqrtLEAERQRQLeMSAEAERLKLRVAEMSR----AQARAEEDAQ 2408
Cdd:PTZ00491 761 QELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1685-1828 |
1.34e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1764
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1765 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1828
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1994-2429 |
1.34e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1994 VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR--QLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQq 2071
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEER- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2072 tlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEA-ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEA 2150
Cdd:COG4717 155 --------LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2151 ARRAQAeqaalrQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQV 2230
Cdd:COG4717 227 EELEQL------ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2231 EEELFSVRVQmEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEA--ARLRQLAEEDLAQQ 2308
Cdd:COG4717 301 GKEAEELQAL-PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2309 RALAEKMLKEKMQAVQEATRLKAEAELLQQQkeLAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAER 2388
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQ--LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 41322914 2389 LKLRVAEMSRAQ--ARAEEDAQRFRKQAEEIGEKLHRTELATQ 2429
Cdd:COG4717 458 LEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2176-2630 |
1.35e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2176 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEN 2255
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2256 RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2335
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2336 LQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2415
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2416 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQAL 2495
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2496 QQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQE 2575
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 2576 ELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTL 2630
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1445-1561 |
1.39e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1445 EAAerSRLRIE-----EEIRVVRLQLEATERQRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQdesqrkrqAE 1518
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEIEKEALKKEQdEASFERLAELRDELAELEEELEALKARWE--------AE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 41322914 1519 VELASRV---KAEAEAAREKQRALQALEELRLQAEEAERRLRQAEV 1561
Cdd:COG0542 467 KELIEEIqelKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1690-2375 |
1.45e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1690 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR---QLLEEELARLQREAAAATQKRQELEAELAKVR- 1765
Cdd:PRK10246 232 EKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpQLAALSLAQPARQLRPHWERIQEQSAALAHTRq 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1766 --AEMEVLLASKARAEEESRSTSEKSKQRLEAEAG----------RFRELAEEAARLRALAEEAKRQRQlaEEDAARQRA 1833
Cdd:PRK10246 312 qiEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQslntwlaehdRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1834 EAERvlaEKLAAIGEATRLKTEAEIAlkEKEAENERLRRLaedeafqRRRLEEQAAQHkADIEERLAQLrKASDSELERQ 1913
Cdd:PRK10246 390 THAE---QKLNALPAITLTLTADEVA--AALAQHAEQRPL-------RQRLVALHGQI-VPQQKRLAQL-QVAIQNVTQE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1914 KGLVEDTLRQRRQveeeilALKASFEKAAAGKAELELElGRIRSNAEdtlrskEQAELEAARQRQLAAEEERRRreaeer 1993
Cdd:PRK10246 456 QTQRNAALNEMRQ------RYKEKTQQLADVKTICEQE-ARIKDLEA------QRAQLQAGQPCPLCGSTSHPA------ 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1994 VQKSLAAEEEAARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQT 2072
Cdd:PRK10246 517 VEAYQALEPGVNQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2073 LQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQsrRQVEEAErlKQSAEEQAQARAQAQAAAEKLRKEAEQEAAR 2152
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHN--QQIIQYQ--QQIEQRQQQLLTALAGYALTLPQEDEEASWL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2153 RAqaeqaalrqkQAADAEMEKHKKFAEQTLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE--ATEAARQRSQ 2229
Cdd:PRK10246 668 AT----------RQQEAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQclSLHSQLQTLQ 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2230 VEEELFSVRVQmeelsKLKARIEAENRALILRDKDNTQRFLQEEaEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2309
Cdd:PRK10246 738 QQDVLEAQRLQ-----KAQAQFDTALQASVFDDQQAFLAALLDE-ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQ 811
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 2310 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE 2375
Cdd:PRK10246 812 QHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2002-2526 |
1.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2002 EEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSV 2079
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2080 LDQLRGEAEAARRAAEEAEEARVQAEREAAQS-RRQVEEAER----LKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRA 2154
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEReierLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2155 QAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE--------------- 2219
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlaealgldeaelpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2220 ------ATEAARQRSQVEEEL----FSVRVQMEELSKLKARIEAENRALILRdkdnTQRFLQEEAEKMKQVAEE---AAR 2286
Cdd:COG4913 464 gelievRPEEERWRGAIERVLggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdslAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2287 LSVAAQEAAR-LRQL-----------AEEDLAQ-QRAL-AEKMLKEKMQAVQEATRLKAEAELL-----QQQKELAQEQA 2347
Cdd:COG4913 540 LDFKPHPFRAwLEAElgrrfdyvcvdSPEELRRhPRAItRAGQVKGNGTRHEKDDRRRIRSRYVlgfdnRAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2348 RRLQEDKEQMAQQLAEetqgfqrtLEAERQRQLEMSAEAERLklrvaemsRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2427
Cdd:COG4913 620 AELEEELAEAEERLEA--------LEAELDALQERREALQRL--------AEYSWDEIDVASAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2428 TQEkvtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLL 2507
Cdd:COG4913 684 SDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
570 580
....*....|....*....|....*....
gi 41322914 2508 QRERF----------IEQEKAKLEQLFQD 2526
Cdd:COG4913 760 GDAVErelrenleerIDALRARLNRAEEE 788
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
968-1393 |
1.51e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 968 HYQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRIAEQQKAQAEVEGL 1040
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1041 GKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLR------AHEE 1114
Cdd:COG4717 169 EAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEneleaaALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1115 QLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQA 1194
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1195 VLAQTDVRQREleqlgrQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQAL--LEEIERHGEKVEEC 1272
Cdd:COG4717 324 LLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVedEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1273 QRFAKQYINAikdyelqlvtyKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISET---LRRME 1349
Cdd:COG4717 398 QELKEELEEL-----------EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeaeLEQLE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 41322914 1350 EEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE 1393
Cdd:COG4717 467 EDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2220-2645 |
1.51e-03 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 44.60 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2220 ATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQ 2299
Cdd:COG5281 2 AALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2300 LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2379
Cdd:COG5281 82 AALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAA--AAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2380 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAEL 2459
Cdd:COG5281 160 AAAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2460 EREKEKLQQEAKLLQLKSEEmQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQ 2539
Cdd:COG5281 240 ASAAAQALAALAAAAAAAAL-ALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2540 RQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQL--QLLEEQHRAALAHSE 2617
Cdd:COG5281 319 AAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWaaGAKAALAEYADSATN 398
|
410 420
....*....|....*....|....*...
gi 41322914 2618 EVTASQVAATKTLPNGRDALDGPAAEAE 2645
Cdd:COG5281 399 VAAQVAQAATSAFSGLTDALAGAVTTGK 426
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1403-1744 |
1.54e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1403 EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR------QAEAAERSRLRIEEEIRVvrLQLEATERQRGGAE 1476
Cdd:COG3206 97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNvieisyTSPDPELAAAVANALAEA--YLEQNLELRREEAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1477 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESqrkrqaevelasrVKAEAEAAREKQRALQA-LEELRLQAEEAERR 1555
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-------------LSEEAKLLLQQLSELESqLAEARAELAEAEAR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1556 LRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAerraqqqaeaerareeaerel 1635
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI--------------------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1636 erwqlkanEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgKAEEQAVRQRElaeQELEKQRQLAEGTAQQRLAA 1715
Cdd:COG3206 301 --------AALRAQLQQEAQRILASL--------------------EAELEALQARE---ASLQAQLAQLEARLAELPEL 349
|
330 340
....*....|....*....|....*....
gi 41322914 1716 EQELIRLRAETeqgEQQRQLLEEELARLQ 1744
Cdd:COG3206 350 EAELRRLEREV---EVARELYESLLQRLE 375
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1355-1548 |
1.54e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1355 AEQQRAEERERlaEVEAALEKQRqlaeahAQAKAQAEREAKELQQrmqeevVRREEAAVDAQQQKRsiqeelqqlrqsSE 1434
Cdd:PTZ00491 667 AARHQAELLEQ--EARGRLERQK------MHDKAKAEEQRTKLLE------LQAESAAVESSGQSR------------AE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1435 AEIQAKARQAEAaersrlriEEEIRVVRLQLEAterQRGGAEGELQALRARAeEAEAQKRQAQEEAERLR-RQVQDESQR 1513
Cdd:PTZ00491 721 ALAEAEARLIEA--------EAEVEQAELRAKA---LRIEAEAELEKLRKRQ-ELELEYEQAQNELEIAKaKELADIEAT 788
|
170 180 190
....*....|....*....|....*....|....*..
gi 41322914 1514 KRQAEVELASR--VKAEAEAAREKQRALqaLEELRLQ 1548
Cdd:PTZ00491 789 KFERIVEALGRetLIAIARAGPELQAKL--LGGLGLK 823
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1733-2045 |
1.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1733 RQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1812
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1813 LAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 1892
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1893 ADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1972
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1973 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2045
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1742-1974 |
1.65e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1742 RLQREAAAATQKRQELEAELAKVRAEMEVLLA--SKARAEEESRSTSEKSKQRLEaeagRFRELAEEAARLRALAEEAKR 1819
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQ----QLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1820 QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIAlkekeaeneRLRRLAEDEAFQRRRLEEQaaqhKADIEERL 1899
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA---------ELSARYTPNHPDVIALRAQ----IAALRAQL 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1900 AQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAA 1974
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1639-1845 |
1.67e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1639 QLKANEALRLRLQAEEVAQQKSLAQAEAE-----KQKEEAEREARRRGKAEEQAvrQRELAEQELEKQRQLAegTAQQRL 1713
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRiraleQELAALEAELAELEKEIAEL--RAELEAQKEELAELLR--ALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1714 AAEQELIRLRAET-EQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1792
Cdd:COG4942 118 RQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1793 LEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1845
Cdd:COG4942 198 QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2375-2699 |
1.71e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2375 ERQRQLEMSAEA-ERLKLRVAEMSR------AQARAEEDAQRFRKQAEEI------------GEKLHRTELATQEKVTLV 2435
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERqlksleRQAEKAERYKELKAELRELelallvlrleelREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2436 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllQETQALQQSFLSEKDSLLQRERFIEQ 2515
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2516 EKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRkqeelqqleqQRRQQEELLAEEN 2595
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----------LRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2596 QrLREQLQLLEEQ-HRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSAEELQ 2674
Cdd:TIGR02168 397 S-LNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*
gi 41322914 2675 RLAQGHTTVDELARREDVRHYLQGR 2699
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQEN 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1690-2468 |
1.71e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1690 QRELAEQE-----LEKQRQLAE---GTAQQRLAAEQELIRLRAE----TEQGEQQRQLLE---EELARLQREAAAATQKR 1754
Cdd:PRK04863 313 ARELAELNeaesdLEQDYQAASdhlNLVQTALRQQEKIERYQADleelEERLEEQNEVVEeadEQQEENEARAEAAEEEV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1755 QELEAELAKVRAEMEVLlASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ-----RQLAEEDAA 1829
Cdd:PRK04863 393 DELKSQLADYQQALDVQ-QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEllsleQKLSVAQAA 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1830 RQRAEAERVLAEKLAaiGEATRlkTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASD 1907
Cdd:PRK04863 472 HSQFEQAYQLVRKIA--GEVSR--SEAWDVARELLRRLREQRHLAEQLQQLRMRLSelEQRLRQQQRAERLLAEFCKRLG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1908 SELERqkglvEDTLRQ-RRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdTLRSKEQAELEA----ARQRQLAAE 1982
Cdd:PRK04863 548 KNLDD-----EDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ-RLAARAPAWLAAqdalARLREQSGE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1983 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKakvEEARRLRERAEQESARQLQLA-----------------QE 2045
Cdd:PRK04863 622 EFEDSQDVTEYMQQLLERERELTVERDELAARKQALD---EEIERLSQPGGSEDPRLNALAerfggvllseiyddvslED 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2046 AAQKRLQAEEKAHAFAVQQKEQELQQTLQqeqsvLDQLRGEAEAARRAAEEAEEARVQA-EREAAQSRRQVEEAERLKQS 2124
Cdd:PRK04863 699 APYFSALYGPARHAIVVPDLSDAAEQLAG-----LEDCPEDLYLIEGDPDSFDDSVFSVeELEKAVVVKIADRQWRYSRF 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2125 AEEQAQARAQAQAAAEKLRKEAEQEAARRAQAE---QAALRQKQAADAEMEKHKKFAEQtlrqkAQVEQELTTLRLQLEE 2201
Cdd:PRK04863 774 PEVPLFGRAAREKRIEQLRAEREELAERYATLSfdvQKLQRLHQAFSRFIGSHLAVAFE-----ADPEAELRQLNRRRVE 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2202 TDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEElsKLKARIEaENRALILRDKDNtQRFLQEEAEKMKQVA 2281
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE--TLADRVE-EIREQLDEAEEA-KRFVQQHGNALAQLE 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2282 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQ-----AVQEATRLKAEA----ELLQQQKELAQEQARRL 2350
Cdd:PRK04863 925 PIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfaLTEVVQrrahfSYEDAAEMLAKNsdlnEKLRQRLEQAEQERTRA 1004
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2351 QEDKEQMAQQLAEETQgFQRTLEAERQRQLEMSAEAERlklrvaEMSRAQARAEEDA-QRFRKQAEEIGEKLHRTELATQ 2429
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQ-VLASLKSSYDAKRQMLQELKQ------ELQDLGVPADSGAeERARARRDELHARLSANRSRRN 1077
|
810 820 830
....*....|....*....|....*....|....*....
gi 41322914 2430 EkvtLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ 2468
Cdd:PRK04863 1078 Q---LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2259-2466 |
1.72e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2259 ILRDKDNTQRFLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2332
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2333 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQR 2409
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 2410 FRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKL 2466
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1322-1657 |
1.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1322 DLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAKELQQRM 1401
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1402 QEEVVRREEAAvDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQA 1481
Cdd:COG4372 94 AELAQAQEELE-SLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1482 LRARAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEV 1561
Cdd:COG4372 169 LEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1562 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1641
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330
....*....|....*.
gi 41322914 1642 ANEALRLRLQAEEVAQ 1657
Cdd:COG4372 327 KLELALAILLAELADL 342
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1475-1584 |
1.76e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1475 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEElRLQA 1549
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE-ELEK 114
|
90 100 110
....*....|....*....|....*....|....*
gi 41322914 1550 EEAERRLRQAEVERARQVqvaLETAQRSAEAELQS 1584
Cdd:PRK12704 115 KEKELEQKQQELEKKEEE---LEELIEEQLQELER 146
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2161-2382 |
1.81e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2161 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQ-VEEELFSVRV 2239
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2240 QMEELSKLKARIEAENRALILRDKdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--- 2316
Cdd:pfam13868 199 EKAERDELRAKLYQEEQERKERQK---EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEdee 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 2317 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEM 2382
Cdd:pfam13868 276 IEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1692-1866 |
1.86e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1692 ELAEQELEKQRQLAEGTAqqrLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE-LAKVRAEMEV 1770
Cdd:PHA03247 1552 ERVDQSPVKDTAYAEYVA---FVARRDLAEAKDALVRAKQQRAEATDRVTAALREALAAHERRAQSEAEsLANLKTLLRV 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1771 --LLASKARAEEESRSTSEKSKQrLEAeagrFRELAEEAARLRALA----EEAKRQRQLAEEDAARQRAEAERV-LAEKL 1843
Cdd:PHA03247 1629 aaIPATAAKTLDQARSVAEIVDQ-IEL----LLEQTEKAAELDVAAvdwlEHARRVFEAHPLTAARGGGPDPLArLHARL 1703
|
170 180
....*....|....*....|...
gi 41322914 1844 AAIGEATRLKTEAEIALKEKEAE 1866
Cdd:PHA03247 1704 DALGETRRRTEALRRSLEAAEAE 1726
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2242-2370 |
1.93e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2242 EELSKLKARIEAENRALILRDKDNTQrfLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2321
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322914 2322 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAEETQGFQR 2370
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1194-1453 |
1.96e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1194 AVLAQTDVR---QRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVE 1270
Cdd:COG4942 14 AAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1271 ECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESVIQEYVDLRthyseLTTLTSQYIKFISETLRRMEE 1350
Cdd:COG4942 94 ELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1351 EERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAKELQQRMQEEvvrrEEAAVDAQQQKRSIQEELQQLR 1430
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|...
gi 41322914 1431 QSSEAEIQAKARQAEAAERSRLR 1453
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKLP 256
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2184-2526 |
1.98e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2184 QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENralilrDK 2263
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI------DK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2264 DNTQRFLQEEaekmkqvaeeaaRLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ-K 2340
Cdd:TIGR04523 192 IKNKLLKLEL------------LLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQlN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2341 ELAQEQarrlQEDKEQMAQQLAEETQGFQRTLEAERQRQlEMSAEAERLKlrvaemsraqaraeedaqrfrKQAEEIGEK 2420
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN---------------------NQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2421 LHRTELATQEKVtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTvqqeqllqetqaLQQSFL 2500
Cdd:TIGR04523 311 ELKSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN------------EIEKLK 376
|
330 340
....*....|....*....|....*.
gi 41322914 2501 SEKDSLLQRERFIEQEKAKLEQLFQD 2526
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN 402
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1514-1748 |
2.01e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1514 KRQAEVELASRVKAEaeaaREKQRALQAleELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEkt 1593
Cdd:pfam15709 327 KREQEKASRDRLRAE----RAEMRRLEV--ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1594 aqlERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeea 1673
Cdd:pfam15709 399 ---ERQRQEEEERKQRLQLQAAQ-------------------ERARQQQEEFRRKLQELQRKKQQEEAE----------- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 1674 erearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1748
Cdd:pfam15709 446 --------RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1795-2305 |
2.02e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.46 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1795 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLa 1874
Cdd:COG3899 752 AEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEA- 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1875 edeafQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGR 1954
Cdd:COG3899 831 -----RALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1955 IRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2034
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2035 ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQ 2114
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2115 VEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfaeqtLRQKAQVEQELTT 2194
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAAL------------AALALAAAARAAA 1133
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2195 LRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEA 2274
Cdd:COG3899 1134 ALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALA 1213
|
490 500 510
....*....|....*....|....*....|.
gi 41322914 2275 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2305
Cdd:COG3899 1214 LLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1340-1556 |
2.14e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.74 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1340 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAKELQQRMQEEVVRREEAAVDAQQQ- 1418
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRLEQQTEQAKKLEEKAQAALTKGNEEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1419 KRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1498
Cdd:pfam04012 85 AREALAEKKSLEKQAEALETQLAQQRSAVEQ-----------LRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 1499 EAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQaLEELRLQAEEAERRL 1556
Cdd:pfam04012 154 LGSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1349-1602 |
2.18e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 44.28 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1349 EEEERLAEQQRAEERERLAEVEA--ALEKQRQLAEAHAQAKAQAEREAKelQQRMQEEVVRREEAAVDAqqqkrsiqeEL 1426
Cdd:pfam04747 72 KSEKKKAQKQIAKDHEAEQKVNAkkAAEKEARRAEAEAKKRAAQEEEHK--QWKAEQERIQKEQEKKEA---------DL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1427 QQLRQSSEAEIQAKARQAEAAERSR-----LRIEEEIRVVRLqleATERQRGGAEGELQALRARAEEAEaqkrQAQEEAE 1501
Cdd:pfam04747 141 KKLQAEKKKEKAVKAEKAEKAEKTKkastpAPVEEEIVVKKV---ANDRSAAPAPEPKTPTNTPAEPAE----QVQEITG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1502 RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAE 1581
Cdd:pfam04747 214 KKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPASENQ 293
|
250 260
....*....|....*....|.
gi 41322914 1582 LQSKRasfAEKTAQLERSLQE 1602
Cdd:pfam04747 294 KKNKK---DKKKSESEKVVEE 311
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1376-1538 |
2.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1376 QRQLAEAHAQAK---AQAEREAKELQQRM----QEEVVR-REEAAVDAQQQKRSIQEELQQLRQSSEAEiqakARQAEAA 1447
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAEAIKKEAlleaKEEIHKlRNEFEKELRERRNELQKLEKRLLQKEENL----DRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1448 ERSrlriEEEIRVVRLQLEATERqrggaegELQALRARAEEAEAQKRQA--------QEEA-ERLRRQVQDESQRkrqae 1518
Cdd:PRK12704 106 EKR----EEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKVEEEARH----- 169
|
170 180
....*....|....*....|..
gi 41322914 1519 vELASRVKAEAEAARE--KQRA 1538
Cdd:PRK12704 170 -EAAVLIKEIEEEAKEeaDKKA 190
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2210-2362 |
2.26e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2210 DEELQRLKAEATEAARQRSQVEEELfSVRVQMEELSKLKARIEAENRALILR---DKDNTQRFLQEEAEKMKQVAEEAAR 2286
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEAEL-AKKKAEERREAETARAEAEAAYEIAEanaEREVQRQLEIAEREREIELQEKEAE 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 2287 LSVAAQEAA-RLRQLAEEDLAQQRALAE-KMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLA 2362
Cdd:COG2268 301 REEAELEADvRKPAEAEKQAAEAEAEAEaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLE 378
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2337-2618 |
2.28e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2337 QQQKELAQEQARRLQEDKEQMAQQLAEEtqgfQRTLEAERQRQlemsAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2416
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERR----RKLEEAEKARQ----AEMDRQAAIYAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2417 I-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDhdaERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQA 2494
Cdd:pfam17380 360 ReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2495 LQQsflsekdslLQRERFIEQEKAKLEQLFQDEvakaqqlREEQQRQQQQMEQERQRlvaSMEEARRRQHEAEEgVRRKQ 2574
Cdd:pfam17380 437 VRR---------LEEERAREMERVRLEEQERQQ-------QVERLRQQEEERKRKKL---ELEKEKRDRKRAEE-QRRKI 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 41322914 2575 EELQQLEQQRRQQeellaeENQRLREQLQLLEEQHRAALAHSEE 2618
Cdd:pfam17380 497 LEKELEERKQAMI------EEERKRKLLEKEMEERQKAIYEEER 534
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
43-151 |
2.36e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.13 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 43 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 113
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322914 114 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 151
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1691-2124 |
2.38e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.13 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1691 RELAEQELEKQRQLAEGTAQQRlaaeQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEV 1770
Cdd:COG5278 85 RAEIDELLAELRSLTADNPEQQ----ARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1771 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1850
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1851 RLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEE 1930
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1931 ILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2010
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2011 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAA 2090
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430
....*....|....*....|....*....|....
gi 41322914 2091 RRAAEEAEEARVQAEREAAQSRRQVEEAERLKQS 2124
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAE 514
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
54-144 |
2.58e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 40.75 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 54 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 126
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 41322914 127 DDIADGNPKLTLGLIWTI 144
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1548-1945 |
2.66e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1548 QAEEAERRLRQAEVERARQVQvALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEA 1624
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQ-AQEAANRQREKEKErykRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1625 ERAREeaerelerwQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE--EQAVRQRELAEQELEKQR 1702
Cdd:pfam07888 107 SASSE---------ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKEraKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1703 QLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1782
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1783 RSTSEKSKQR--LEAEAGRFR-ELAEEAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLkteaE 1857
Cdd:pfam07888 258 EELSSMAAQRdrTQAELHQARlQAAQLTLQLAdaSLALREGRARWAQERETLQQSAEADKDRIEKLSA--ELQRL----E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1858 IALKEKEAENERLR-RLAEDEAFQRRRLEEQaaqhkadieERLAQLRKASDSELERQKglvEDTLRQRRQVEEEILALKA 1936
Cdd:pfam07888 332 ERLQEERMEREKLEvELGREKDCNRVQLSES---------RRELQELKASLRVAQKEK---EQLQAEKQELLEYIRQLEQ 399
|
....*....
gi 41322914 1937 SFEKAAAGK 1945
Cdd:pfam07888 400 RLETVADAK 408
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1475-1558 |
2.70e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1475 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVElasrvKAEAEAAREKQralQALEELRLQAEEAER 1554
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-----EAKEEAERILE---QAKAEIEQEKEKALA 113
|
....
gi 41322914 1555 RLRQ 1558
Cdd:cd06503 114 ELRK 117
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1373-1551 |
2.86e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1373 LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrl 1452
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1453 rieeeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEVELASRVKAEAEaa 1532
Cdd:PRK12705 100 ------------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180
....*....|....*....|
gi 41322914 1533 REK-QRALQALEELRLQAEE 1551
Cdd:PRK12705 157 EEKaQRVKKIEEEADLEAER 176
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2161-2425 |
2.86e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2161 LRQKQAADAEMEKHKK-----FAE-QTLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE 2233
Cdd:COG1340 14 EEKIEELREEIEELKEkrdelNEElKELAEKrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2234 LFSVRVQMEEL-------SKLKARIEA-------------ENRALILRDKDntqrfLQEEAEKMKQVAEEAARLSVAAQE 2293
Cdd:COG1340 94 LDELRKELAELnkaggsiDKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2294 AARLRQLAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaeetqgfqr 2370
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL--------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 2371 tleaerqRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2425
Cdd:COG1340 240 -------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1868-2049 |
2.90e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1868 ERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEIlalkasfEKAAAGKAE 1947
Cdd:COG1579 7 RALLDLQELDS-ELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEI-------EEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1948 LELELGRIRSNAE-DTLrskeQAELEAARQRQlaaeeerrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2026
Cdd:COG1579 78 YEEQLGNVRNNKEyEAL----QKEIESLKRRI---------SDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
170 180
....*....|....*....|...
gi 41322914 2027 RLRERAEQESARQLQLAQEAAQK 2049
Cdd:COG1579 145 AELDEELAELEAELEELEAEREE 167
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1100-1771 |
2.90e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1100 RGTQGAEEVLRAHEEQLKEAQAVPATLPEleatkaslkklrAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVE 1179
Cdd:NF041483 569 RQAEAAEELTRLHTEAEERLTAAEEALAD------------ARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQEAE 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1180 RWRERVAQLLERWQAVLAQTDVRQR-----ELEQLGRQLRyyrESADPLGAWLQDARRR--QEQIQAMPLADSQAVREQL 1252
Cdd:NF041483 637 RLRTEAAADASAARAEGENVAVRLRseaaaEAERLKSEAQ---ESADRVRAEAAAAAERvgTEAAEALAAAQEEAARRRR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1253 RQEQALL-------EEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESV--IQEYVDl 1323
Cdd:NF041483 714 EAEETLGsaraeadQERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVagLQEQAE- 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1324 rthySELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEvEAALEKQRQLAEAHAqAKAQAER----------- 1392
Cdd:NF041483 793 ----EEIAGLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASE-DANRLRREAQEETEA-AKALAERtvseaiaeaer 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1393 ---EAKELQQRMQEEVV-RREEAAVDAQQQKRSIQEELQQLRqsSEAEIQAKARQAEAAErsrlrieEEIRVVRLQLEAT 1468
Cdd:NF041483 867 lrsDASEYAQRVRTEASdTLASAEQDAARTRADAREDANRIR--SDAAAQADRLIGEATS-------EAERLTAEARAEA 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1469 ERQRGGAEGELQALRARA-EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL---ASRVKAEAEAAREKQRALQALEE 1544
Cdd:NF041483 938 ERLRDEARAEAERVRADAaAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIrteAERVKAEAAAEAERLRTEAREEA 1017
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1545 LRL----QAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASfAEKTAQLERSLQEEHVAVAQLREEAERRAQQ 1620
Cdd:NF041483 1018 DRTldeaRKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT-TEAEAQADTMVGAARKEAERIVAEATVEGNS 1096
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1621 QAEAERAREEAERELERWQLKAN----EALRLRLQAE-----EVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1691
Cdd:NF041483 1097 LVEKARTDADELLVGARRDATAIreraEELRDRITGEieelhERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKE 1176
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1692 ELAEQELE----------KQRQLAEGTAQQRLAAEQELIRLRAETEQgeQQRQLLEEElarlQREAAAATQKRQELEAEL 1761
Cdd:NF041483 1177 LVSDANSEaskvriaavkKAEGLLKEAEQKKAELVREAEKIKAEAEA--EAKRTVEEG----KRELDVLVRRREDINAEI 1250
|
730
....*....|
gi 41322914 1762 AKVRAEMEVL 1771
Cdd:NF041483 1251 SRVQDVLEAL 1260
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1479-1603 |
2.98e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1479 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELasrvKAEAEaarekQRALQALEELRLQAEEAERRLRQ 1558
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 41322914 1559 AEVERARQVqvaletaqrsAEAELQSKRASFAEKTAQLERSLQEE 1603
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1730-1940 |
3.00e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1730 EQQRQLLEeeLARLQREAAAATQKRQELEAELAKVRAEMEvllaskaraeeesrstsekskqrleaeagrfrELAEEAAR 1809
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELA--------------------------------ALEARLEA 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1810 LRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIgeatrlKTEAEI-ALKEKEAENERLRRLAEDEAFQRRRLEEQA 1888
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNV------RNNKEYeALQKEIESLKRRISDLEDEILELMERIEEL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 41322914 1889 AQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEK 1940
Cdd:COG1579 123 EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1807-1951 |
3.01e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1807 AARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIAlkEKEAENERLRRLAEDEAFQRRRLEE 1886
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1887 QAAQ------HKADIEERLAQLRKASDSELERQKGLVEDTLRQR--RQVEEEILALKASFEKAAAGKAELELE 1951
Cdd:PRK12705 103 LENQleerekALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1888-2064 |
3.03e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1888 AAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE 1967
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1968 QAELEAARQRQLAAEEERRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2033
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 41322914 2034 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2064
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1364-1535 |
3.16e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.87 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1364 ERLAEVEAALEK-QRQLAEAHAQAKAQAEREAKELQQRMQ---EEVVRREEAAVDAQQQKrsIQEELQQLRQsseaeiQA 1439
Cdd:pfam01442 4 DSLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQkdlEEVRAKLEPYLEELQAK--LGQNVEELRQ------RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1440 KARQAEAAERSRLRIEEEIRVVRlqlEATERQRGGAEGELQALRARAEEAEAQKRQ-----AQEEAERLRRQVQDESQRK 1514
Cdd:pfam01442 76 EPYTEELRKRLNADAEELQEKLA---PYGEELRERLEQNVDALRARLAPYAEELRQklaerLEELKESLAPYAEEVQAQL 152
|
170 180
....*....|....*....|.
gi 41322914 1515 RQAEVELASRVKAEAEAAREK 1535
Cdd:pfam01442 153 SQRLQELREKLEPQAEDLREK 173
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1413-1559 |
3.23e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1413 VDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvvrlqleaterqrggAEGELQALRARAEEAEAQ 1492
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1493 KRQAQEEAERLRRQVQDESQRKRQaevelasrvkaeaeaaREKQRALQALEELRLqaEEAERR------LRQA 1559
Cdd:PRK11448 193 QQELEAQLEQLQEKAAETSQERKQ----------------KRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1685-1850 |
3.31e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1764
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1765 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1844
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
....*.
gi 41322914 1845 AIGEAT 1850
Cdd:COG3883 275 GAAAAS 280
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1690-1783 |
3.35e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.29 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1690 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEME 1769
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 41322914 1770 VLLASKARAEEESR 1783
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2693-2730 |
3.37e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.37e-03
10 20 30
....*....|....*....|....*....|....*...
gi 41322914 2693 RHYLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTA 2730
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1346-1435 |
3.39e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.76 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1346 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAH-------AQAKAQAEREAKE-LQQRMQEEVVRREEAAVDAQ 1416
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARkqaqaviAEAEAEADKLAAEaLAEAQAEAQASKEKARREIE 111
|
90
....*....|....*....
gi 41322914 1417 QQKrsiQEELQQLRQSSEA 1435
Cdd:PRK07353 112 QQK---QAALAQLEQQVDA 127
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1393-1531 |
3.50e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1393 EAKELQQRMQEevVRREEAAVDAQQQKRSiQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1472
Cdd:COG0542 412 ELDELERRLEQ--LEIEKEALKKEQDEAS-FERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 1473 GGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEVELASRVKAEAEA 1531
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2163-2531 |
3.57e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.59 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2163 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKnlldEELQRLKAEATEAARQrsQVEEELFSVRVQME 2242
Cdd:pfam09731 98 SSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKA----ESATAVAKEAKDDAIQ--AVKAHTDSLKEASD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2243 --ELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA------LAEK 2314
Cdd:pfam09731 172 taEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLaklvdqYKEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2315 MLKEKMQAVQEATRLkaEAELLQQQKELAQEQARRL-------QEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEA 2386
Cdd:pfam09731 252 VASERIVFQQELVSI--FPDIIPVLKEDNLLSNDDLnsliahaHREIDQLSKKLAElKKREEKHIERALEKQKEELDKLA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2387 ERLKLR---VAEMSRAQARAEEDAQRFRkQAEEIGEKLhRTELATQEKV---TLVQTLEIQRQQSDHDAERLREAIAELE 2460
Cdd:pfam09731 330 EELSARleeVRAADEAQLRLEFEREREE-IRESYEEKL-RTELERQAEAheeHLKDVLVEQEIELQREFLQDIKEKVEEE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2461 REKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQ---------SFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 2531
Cdd:pfam09731 408 RAGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQlwlavealrSTLEDGSADSRPRPLVRELKALKELASDDEVVKA 487
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1361-1591 |
3.58e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1361 EERERLAEVEAAL-------EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSS 1433
Cdd:pfam13868 3 ENSDELRELNSKLlaakcnkERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1434 EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL---------- 1503
Cdd:pfam13868 83 EEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREederileylk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1504 -----RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQaEEAERRLRQAEVERARQVQVALETAQRSA 1578
Cdd:pfam13868 163 ekaerEEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQ-EEQERKERQKEREEAEKKARQRQELQQAR 241
|
250
....*....|...
gi 41322914 1579 EAELQSKRASFAE 1591
Cdd:pfam13868 242 EEQIELKERRLAE 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1106-1602 |
3.61e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1106 EEVLRAHEEQLKEAQAVPATL-PELEATKASL-------KKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVE 1177
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLtKELEDIKMSLqrsmstqKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1178 VERWRERVAQLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQA 1257
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKN---EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKI-LAEDEKLLDEKKQFEK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1258 LLEEIErhgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqEYVDLRTHYSELTTLTSQY 1337
Cdd:pfam05483 430 IAEELK---GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL--KNIELTAHCDKLLLENKEL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1338 IKFISE-TLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRM---QEEVVRREEAAV 1413
Cdd:pfam05483 505 TQEASDmTLELKKHQEDIINCKKQEER-MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLdksEENARSIEYEVL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1414 DAQQQKRSIQEELQQLRQS--------SEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE-ATERQRGG-------AEG 1477
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQienknkniEELHQENKALKKKGSAENKQLNAYEIKVNKLELElASAKQKFEeiidnyqKEI 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1478 ELQALRARAEEAEAQKRQA-QEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERrl 1556
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAiADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAK-- 741
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 41322914 1557 rqaeverarqvqVALETAQRSAEAELQSKRASFA---EKTAQLERSLQE 1602
Cdd:pfam05483 742 ------------AALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKE 778
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1550-1886 |
3.70e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1550 EEAERRLRQAEVERARqvqvaLETAQRSAEAELQSKRASFAE----KTAQLERS---LQEEHVAVAQLREEAERRAQQQA 1622
Cdd:pfam03528 4 EDLQQRVAELEKENAE-----FYRLKQQLEAEFNQKRAKFKElylaKEEDLKRQnavLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1623 EAERAREEAerelERWQLKANEALRLRLQaEEVAqqkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL-EKQ 1701
Cdd:pfam03528 79 NIKAVATVS----ENTKQEAIDEVKSQWQ-EEVA---SLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIaDLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1702 RQLAEGTAQQRLaaEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAelAKVRAEMEVLLASKA-RAEE 1780
Cdd:pfam03528 151 RRLSEGQEEENL--EDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEA--SKMKELNHYLEAEKScRTDL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1781 ESR-STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL---AEKLAAIGEATRLKTEA 1856
Cdd:pfam03528 227 EMYvAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLmrdMQRMESVLTSEQLRQVE 306
|
330 340 350
....*....|....*....|....*....|
gi 41322914 1857 EIALKEKEaENERLRRLAEDEAFQRRRLEE 1886
Cdd:pfam03528 307 EIKKKDQE-EHKRARTHKEKETLKSDREHT 335
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1636-2119 |
3.76e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1636 ERWQLKANEALRLRLQAEEVAQQKSLAQ--AEAEKQKEEAER---------------EARRRGKAEEQAVRQRELAEQEL 1698
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKriRLLEKREAEAEEalreqaelnrlkkkyLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1699 EKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLE----------EELARLQREAAAATQKRQELEAELAKVRAEM 1768
Cdd:pfam05557 108 CLKNELSE-LRRQIQRAELELQSTNSELEELQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1769 EVLLASKarAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLAEKLA- 1844
Cdd:pfam05557 187 EIVKNSK--SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSw 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1845 -AIGEATRLKTEAEIALKEK--EAENERLRRLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASDSE---LERQKGLVE 1918
Cdd:pfam05557 265 vKLAQDTGLNLRSPEDLSRRieQLQQREIVLKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1919 DTLRQRRQVEEEILALKA---SFEKAAAGKAELELELGRIRSNAEDTLRSKEQ-AELEAARQRQLAAEEERRRREAEERV 1994
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAEDMTQKMQAHnEEMEAQLSVAEEELGGYKQQAQTLER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1995 QKSLAAEEEAARQRKAALEEVERLKAKVEEAR----RLRERAEQESAR--QLQLAQEAAQKR---LQAEEKAHAFAVQQK 2065
Cdd:pfam05557 423 ELQALRQQESLADPSYSKEEVDSLRRKLETLElerqRLREQKNELEMEleRRCLQGDYDPKKtkvLHLSMNPAAEAYQQR 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 41322914 2066 EQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAE 2119
Cdd:pfam05557 503 KNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAE 556
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2259-2474 |
3.85e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.40 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2259 ILRDKDNTQRFLQEeaeKMKQVAEEAARLSVAAQEAARLRQLAE---EDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2335
Cdd:pfam06008 17 INYNLENLTKQLQE---YLSPENAHKIQIEILEKELSSLAQETEelqKKATQTLAKAQQVNAESERTLGHAKELAEAIKN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2336 LQQQKELAQEQARRLQEDKEQMA-QQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAE--MSRAQARAEEDAQRFRK 2412
Cdd:pfam06008 94 LIDNIKEINEKVATLGENDFALPsSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQdlLSRIQTWFQSPQEENKA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322914 2413 QAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2474
Cdd:pfam06008 174 LANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLE 235
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1348-1428 |
3.88e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.50 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1348 MEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAH-------AQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQ 1418
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEyEEKLAEARaeaqeiiEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQE 107
|
90
....*....|
gi 41322914 1419 KRSIQEELQQ 1428
Cdd:cd06503 108 KEKALAELRK 117
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1230-1566 |
3.92e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1230 ARRRQEQIQAMpLADSQAVREQLRQE-QALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVaspakkpk 1308
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELK---DKYRELRKTLLANRFSYGPAIDEL-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1309 vqsgsESVIQEYVDLRTHYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAK 1387
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1388 AQ--------AEREAKELQQRMQEEVVRREEAAVD-AQQQKRSIQEELQQLRQSSEAEIQAKArqaeaaersrlRIEEEI 1458
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKK-----------YVEKNL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1459 RVVRLQLEATERQRGGAEGELQALRAR---AEEAEAQKRQAQEEAERLRRQVQDESQR---KRQAEVELASRVKaeaeaa 1532
Cdd:pfam06160 294 PEIEDYLEHAEEQNKELKEELERVQQSytlNENELERVRGLEKQLEELEKRYDEIVERleeKEVAYSELQEELE------ 367
|
330 340 350
....*....|....*....|....*....|....
gi 41322914 1533 rEKQRALQALEELRLQAEEAERRLRQAEvERARQ 1566
Cdd:pfam06160 368 -EILEQLEEIEEEQEEFKESLQSLRKDE-LEARE 399
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2172-2380 |
3.94e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2172 EKHKKFAEQTLrqkAQVEQELTTLRLQLE-----ETDHQKNLLDEELQRLKAEATEAAR-QRSQVEEElfsVRVQMEELS 2245
Cdd:COG2268 147 EDREKFAEKVQ---EVAGTDLAKNGLELEsvaitDLEDENNYLDALGRRKIAEIIRDARiAEAEAERE---TEIAIAQAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2246 KLKARIEAENRALIL--------RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlK 2317
Cdd:COG2268 221 REAEEAELEQEREIEtariaeaeAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-A 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322914 2318 EKMQAVQEAT-RLKAEAELLQQQKElAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQL 2380
Cdd:COG2268 300 EREEAELEADvRKPAEAEKQAAEAE-AEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLML 362
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1368-1757 |
3.97e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1368 EVEAALEKqrqlaeahaqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeaeiqAKARQAEAA 1447
Cdd:pfam02029 4 EEEAARER---------------RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1448 ERSRLRIEEEIRVVRLQlEATERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKA 1527
Cdd:pfam02029 64 FLDRTAKREERRQKRLQ-EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1528 EAEAAREKqralqalEELRLQAEEAERRLRQAEVERA-RQVQVALETAQRSAEAELQSKRASfaEKTAQLERSLQEEHVA 1606
Cdd:pfam02029 140 YQENKWST-------EVRQAEEEGEEEEDKSEEAEEVpTENFAKEEVKDEKIKKEKKVKYES--KVFLDQKRGHPEVKSQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1607 VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrlrlqaeevaqqkslaqaeaekqkeeaerearrrgkaEEQ 1686
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKL-------------------------------------EEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1687 AVRQRELAEQELEKQRQlaegtAQQRLAAEQELI--------RLRAETEQG----EQQRQLLEEELAR-----LQREAAA 1749
Cdd:pfam02029 254 RRRRQEKESEEFEKLRQ-----KQQEAELELEELkkkreerrKLLEEEEQRrkqeEAERKLREEEEKRrmkeeIERRRAE 328
|
....*...
gi 41322914 1750 ATQKRQEL 1757
Cdd:pfam02029 329 AAEKRQKL 336
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2212-2473 |
4.02e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.36 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2212 ELQRLKAEATEAARQRSQVEEElfsvrvqmEELSKLKARIEAEN-RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVA 2290
Cdd:pfam15964 325 EAQQRESSAYEQVKQAVQMTEE--------ANFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2291 AQEAARLRQLA-EEDLAQQRALAEKMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQgf 2368
Cdd:pfam15964 397 EREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH-- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2369 qRTLEAERQRQLEMS-AEAERLKL-------RVAEMSRAQARAEEDAQRFrkqAEEIGEKLHRTELATQEKVTLVQTL-- 2438
Cdd:pfam15964 473 -REYRTKTGRQLEIKdQEIEKLGLelseskqRLEQAQQDAARAREECLKL---TELLGESEHQLHLTRLEKESIQQSFsn 548
|
250 260 270
....*....|....*....|....*....|....*..
gi 41322914 2439 --EIQRQQSDHDAERLREAIAELEREKEKLQQEAKLL 2473
Cdd:pfam15964 549 eaKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSL 585
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1349-1532 |
4.25e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1349 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAV-DAQQQKRSIQEELQ 1427
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIaRAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1428 QLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALRARAEEAEAQKRQAQEEAErlrrqv 1507
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*.
gi 41322914 1508 QDESQRKrqAEVELA-SRVKAEAEAA 1532
Cdd:PRK05035 671 EAEDPKK--AAVAAAiARAKAKKAAQ 694
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2275-2369 |
4.34e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2275 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2348
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 41322914 2349 RLQEDKEQMAQQLAEETQGFQ 2369
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2182-2479 |
4.37e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2182 LRQKAQVEQ-ELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFsvrvQMEELSKLKARIEAEnraliL 2260
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2261 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2340
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2341 ELAQEQARRLQEDKEQMAQQLAEET--QGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIG 2418
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2419 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLREAIAELEREKEKL 2466
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 41322914 2467 QQEAKllQLKSEE 2479
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1376-1541 |
4.44e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1376 QRQLAEAHAQAKAQAeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAER-SRLRI 1454
Cdd:pfam00529 53 PTDYQAALDSAEAQL-AKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDlARRRV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1455 EEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqAEVElASRVKAEAEAAR 1533
Cdd:pfam00529 132 LAPIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQI-AEAE-AELKLAKLDLER 209
|
....*...
gi 41322914 1534 EKQRALQA 1541
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1112-1610 |
4.52e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1112 HEEQLKEAQAVPATLPELEatkaslkklrAQAEAQQPTFDAlRDElrGAQEVGERLQQRHGERDVEVERWrERVAQLLEr 1191
Cdd:pfam10174 125 HERQAKELFLLRKTLEEME----------LRIETQKQTLGA-RDE--SIKKLLEMLQSKGLPKKSGEEDW-ERTRRIAE- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1192 WQAVLAQTDVrqrELEQLGRQLRYYRESAdplgawlqdarRRQEQIQAMPlADSQAVREQLRQEQALLEEIERHGEKVEE 1271
Cdd:pfam10174 190 AEMQLGHLEV---LLDQKEKENIHLREEL-----------HRRNQLQPDP-AKTKALQTVIEMKDTKISSLERNIRDLED 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1272 CQRFAKQyiNAIKDYELQLVTYKaQLEPVASPAK--KPKVQSGSESVIQEYVDLRTHYSELTTLTS------QYIKFISE 1343
Cdd:pfam10174 255 EVQMLKT--NGLLHTEDREEEIK-QMEVYKSHSKfmKNKIDQLKQELSKKESELLALQTKLETLTNqnsdckQHIEVLKE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1344 TLRRMEEEERLAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQA-------------EREAKELQQRMQ--EEVVR 1407
Cdd:pfam10174 332 SLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEKSTLAgeirdlkdmldvkERKINVLQKKIEnlQEQLR 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1408 reeaavDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEA-------AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ 1480
Cdd:pfam10174 412 ------DKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAlsekeriIERLKEQREREDRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1481 ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAER-RLRQA 1559
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQ 565
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 1560 EV----ERARQVQVALE---TAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1610
Cdd:pfam10174 566 EVarykEESGKAQAEVErllGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI 623
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1427-1907 |
5.02e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1427 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1505
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1506 QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK 1585
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1586 RASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAE 1665
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1666 AEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELiRLRAETEQGEQQRQLLEEELARLQR 1745
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGL-VLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1746 EAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE 1825
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1826 EDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 1905
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
..
gi 41322914 1906 SD 1907
Cdd:COG3064 481 LL 482
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2178-2351 |
5.08e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2178 AEQTLRQKAQVEQELTTLRLQL-------EETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKlkar 2250
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA---- 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2251 ieaenRALILRDkdntqrflqeeaekmkqvaeeaarlsvAAQEAARLRQLAEEDLAQQRALAEKMlkekMQAVQEATRLK 2330
Cdd:COG3096 600 -----RAPAWLA---------------------------AQDALERLREQSGEALADSQEVTAAM----QQLLEREREAT 643
|
170 180
....*....|....*....|.
gi 41322914 2331 AEAELLQQQKELAQEQARRLQ 2351
Cdd:COG3096 644 VERDELAARKQALESQIERLS 664
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1721-1829 |
5.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1721 RLRAETEQGEQQRQLLEEELARLQREAAAAT--------QKRQELEAELAKVRAEMEVLLAsKARAEEESRSTSEKSKQR 1792
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKkeqdeasfERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322914 1793 LEAEAGRFRELAEEAARLRALAEEAKRQRQLA--EEDAA 1829
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLLREEvtEEDIA 518
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1316-1583 |
5.19e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.72 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1316 VIQEYVDLRThYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEererLAEVEAALEKQRQLAEAHAQAKAQAEREAK 1395
Cdd:COG1538 78 VAQAYFDLLA-AQEQLALAEENLALAEELLELARARYEAGLASRLD----VLQAEAQLAQARAQLAQAEAQLAQARNALA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1396 ELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeAEIQAKARQAEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1475
Cdd:COG1538 153 LLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERR-PDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1476 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1536
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41322914 1537 RALQALEEL-------RLQAEEAERRLRQAEVERarqvqVALETAQRSAEAELQ 1583
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1693-1978 |
5.21e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1693 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL 1772
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1773 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedaarqraeAERVLAeKLAAIGEAtRL 1852
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1853 KTEAEialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVedtlrqrrqveeeil 1932
Cdd:PRK11637 170 ETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT--------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41322914 1933 ALKASFEKAAAGKAELELELGRIRSN-AEDTLRSKEQAELEA-------ARQRQ 1978
Cdd:PRK11637 223 GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2259-2421 |
5.21e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2259 ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQ---EATRLKAEAEL 2335
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2336 LQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtleaerqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2415
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEA--------------ELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*.
gi 41322914 2416 EIGEKL 2421
Cdd:COG1579 167 ELAAKI 172
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1488-1587 |
5.34e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.08 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1488 EAEAQKRQAQEEAERLR--RQVQDESQRK-------RQAEVELASRVKAEAEA-AREKQRALQA-LEELRLQAeEAERRL 1556
Cdd:PTZ00491 671 QAELLEQEARGRLERQKmhDKAKAEEQRTkllelqaESAAVESSGQSRAEALAeAEARLIEAEAeVEQAELRA-KALRIE 749
|
90 100 110
....*....|....*....|....*....|..
gi 41322914 1557 RQAEVERARQVQVA-LETAQRSAEAELQSKRA 1587
Cdd:PTZ00491 750 AEAELEKLRKRQELeLEYEQAQNELEIAKAKE 781
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1712-2058 |
5.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1712 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQ 1791
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1792 RLEAEAgRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 1871
Cdd:COG4372 96 LAQAQE-ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1872 RLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRR--QVEEEILALKASFEKAAAGKAELE 1949
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEakLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1950 LELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2029
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
330 340
....*....|....*....|....*....
gi 41322914 2030 ERAEQESARQLQLAQEAAQKRLQAEEKAH 2058
Cdd:COG4372 335 LLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1350-1610 |
5.95e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1350 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmQEEVVRR-----------EEAAVDAQQQ 1418
Cdd:PRK10811 514 SEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAAAPKAAAATPPA-QPGLLSRffgalkalfsgGEETKPQEQP 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1419 KRSIQE--ELQQLRQSSeaeiqakaRQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1496
Cdd:PRK10811 593 APKAEAkpERQQDRRKP--------RQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEK 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1497 QEEAERLRRQVQDESQRKRQAEVELASrvkAEAEAarekqralQALEELRLQAEEAERRLRQAEVERA-RQV--QVALET 1573
Cdd:PRK10811 665 ARTQDEQQQAPRRERQRRRNDEKRQAQ---QEAKA--------LNVEEQSVQETEQEERVQQVQPRRKqRQLnqKVRIEQ 733
|
250 260 270
....*....|....*....|....*....|....*..
gi 41322914 1574 AQrSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1610
Cdd:PRK10811 734 SV-AEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPL 769
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1683-1783 |
5.97e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1683 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1762
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 41322914 1763 KvRAEMEVLLaskarAEEESR 1783
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1730-1845 |
6.06e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.54 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1730 EQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLaskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAAR 1809
Cdd:COG0711 30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEII---AEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIE 106
|
90 100 110
....*....|....*....|....*....|....*.
gi 41322914 1810 lralAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1845
Cdd:COG0711 107 ----QERAKALAELRAEVADLAVAIAEKILGKELDA 138
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1357-1560 |
6.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1357 QQRAEERERLAEVEAALEKQRQLAEAHAQAK---AQAEREAKELQQRMQEEVVRRE------------EAAVDAQQQKRS 1421
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEeekelvekikelEKELEKAKKALE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1422 IQEELQQLRqsseAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAE 1501
Cdd:COG1340 158 KNEKLKELR----AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEA-------DELRKEADELHKEIVEAQEKAD 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 1502 RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRalqalEELRLQAEEAERRLRQAE 1560
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-----EELEEKAEEIFEKLKKGE 280
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
1705-1848 |
6.27e-03 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.48 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1705 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS 1784
Cdd:COG4191 1 ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322914 1785 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGE 1848
Cdd:COG4191 81 LLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGE 144
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1234-1516 |
6.50e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1234 QEQIQAM-----PLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAspakkpk 1308
Cdd:PRK11281 42 QAQLDALnkqklLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1309 vqsgsesviqeyvdlRTHYSELttltsqyikfiseTLRRMEE--EERLAEQQRAeererlaeveaalekQRQLAEAHAQ- 1385
Cdd:PRK11281 115 ---------------RETLSTL-------------SLRQLESrlAQTLDQLQNA---------------QNDLAEYNSQl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1386 --AKAQAEREAKEL---QQRMQEevVRREEAAVDAQQqkRSIQEELQQLRQSSEAEIQAKA--RQAEAAERSRLrieeeI 1458
Cdd:PRK11281 152 vsLQTQPERAQAALyanSQRLQQ--IRNLLKGGKVGG--KALRPSQRVLLQAEQALLNAQNdlQRKSLEGNTQL-----Q 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1459 RVVRLQLEATERQRGGAEGELQALRA-----RAEEAEAQKRQAQEEAERLRRQ----VQDESQRKRQ 1516
Cdd:PRK11281 223 DLLQKQRDYLTARIQRLEHQLQLLQEainskRLTLSEKTVQEAQSQDEAARIQanplVAQELEINLQ 289
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1343-1510 |
6.60e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEERLAEQQRA---EERERLAEVEAALEKQRQLAEAHAQ----AKAQAEREAKELqqrmqeevvrreeaavda 1415
Cdd:PRK00409 492 EIAKRLGLPENIIEEAKKligEDKEKLNELIASLEELERELEQKAEeaeaLLKEAEKLKEEL------------------ 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1416 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAersrlrIEEEIRVVRL--QLEATERQRGGAEGELQALRARAEEAEAQK 1493
Cdd:PRK00409 554 EEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE------ADEIIKELRQlqKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
170
....*....|....*..
gi 41322914 1494 RQAQEEAERLrrQVQDE 1510
Cdd:PRK00409 628 KKQKEKQEEL--KVGDE 642
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
47-149 |
6.72e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 39.98 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 47 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 122
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 41322914 123 NIRNDDIADGNPKLTLGLIWTIILHFQ 149
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2291-2473 |
6.83e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2291 AQEAARLRQLAEED--LAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETqgf 2368
Cdd:COG1579 3 PEDLRALLDLQELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2369 qrtleaERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTElatqekvtlvQTLEIQRQQSDHD 2448
Cdd:COG1579 80 ------EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE----------AELAELEAELEEK 143
|
170 180
....*....|....*....|....*
gi 41322914 2449 AERLREAIAELEREKEKLQQEAKLL 2473
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREEL 168
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1685-1945 |
6.95e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1685 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQreaaaatQKRQELEAELAKV 1764
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK-------EERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1765 RAEMEVLLASKARAEEESRSTSEKSKqRLEAEAGRF----------RELAEEAARLRALAEEAKRQRQLAEE-DAARQRA 1833
Cdd:COG1340 91 REELDELRKELAELNKAGGSIDKLRK-EIERLEWRQqtevlspeeeKELVEKIKELEKELEKAKKALEKNEKlKELRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1834 EAERVLAEKL-----AAIGEATRLKTEAeIALKEKEaenERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDS 1908
Cdd:COG1340 170 KELRKEAEEIhkkikELAEEAQELHEEM-IELYKEA---DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 41322914 1909 ElerqKGLVEDTLRQRRQVEEEILALKAS--FEKAAAGK 1945
Cdd:COG1340 246 L----KKLRKKQRALKREKEKEELEEKAEeiFEKLKKGE 280
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1464-1589 |
6.98e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1464 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQAL 1542
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 1543 EELR---------LQAEEAERRLRQAEVER-ARQVQVALetAQRSaeAELQSKRASF 1589
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKIADlGRRLNVAL--AQRV--QELNRYRSEF 199
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1451-1568 |
6.98e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1451 RLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDESQR-KRQAEVELASRVK 1526
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLeqkRQEAEEEKERlEESAEMEAEEKEQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 41322914 1527 AEAEaAREKQRALQALEELRLQAEEAERRLrQAEVERARQVQ 1568
Cdd:pfam20492 81 LEAE-LAEAQEEIARLEEEVERKEEEARRL-QEELEEAREEE 120
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1682-1822 |
7.34e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 41.51 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1682 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEA-- 1759
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322914 1760 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1822
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1124-1567 |
7.40e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1124 ATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQ 1203
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1204 RELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAI 1283
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1284 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEER 1363
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1364 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQ 1443
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1444 AEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS 1523
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 41322914 1524 RVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1567
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1343-1444 |
7.49e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1343 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAKELQQrmqeevvRREEAAVDAQQQKRSI 1422
Cdd:PRK11448 152 LTLKQQLELQAREKAQSQALAEAQQQELVALEG---LAAELEEKQQELEAQLEQLQE-------KAAETSQERKQKRKEI 221
|
90 100
....*....|....*....|....*.
gi 41322914 1423 QEELQQLRQSSEAE----IQAKARQA 1444
Cdd:PRK11448 222 TDQAAKRLELSEEEtrilIDQQLRKA 247
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1788-1935 |
7.49e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1788 KSKQRLEAEAGRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LAEKLAAigEATRLKTE 1855
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1856 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALK 1935
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2324-2402 |
7.63e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 42.01 E-value: 7.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322914 2324 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAEETQgfqrTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2402
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQAK----ALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1532-1586 |
7.70e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 7.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 1532 AREKQRALQaleelRLQAEEAERRlRQAEVERARQVQVALETAQRS-AEAELQSKR 1586
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1691-1858 |
7.75e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1691 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtqkRQELEAELAKVRAEmev 1770
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKE--- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1771 llaskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1850
Cdd:PRK00409 582 -----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNK-ANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL 655
|
....*...
gi 41322914 1851 RLKTEAEI 1858
Cdd:PRK00409 656 SIPDDKEA 663
|
|
| PRK01294 |
PRK01294 |
lipase secretion chaperone; |
1397-1570 |
8.17e-03 |
|
lipase secretion chaperone;
Pssm-ID: 234937 [Multi-domain] Cd Length: 336 Bit Score: 41.97 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1397 LQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaersrlrieeeirvvrLQLEATERQRGGAE 1476
Cdd:PRK01294 187 YQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRAALQESQRQQAL----------------LQQLAQLQASGASP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1477 GELQALRARAEEAEAqkrqaqeeAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1556
Cdd:PRK01294 251 QELRLMRAQLVGPEA--------AQRLEQLDQQRAAWQQRYDDYLAQRAQILNAAGLSPQDRQAQIAQLRQQRFSPQEAL 322
|
170
....*....|....
gi 41322914 1557 RQAEVERARQVQVA 1570
Cdd:PRK01294 323 RLAALERIHDAGQT 336
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1999-2502 |
8.37e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1999 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQS 2078
Cdd:COG3899 738 DPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2079 VLDQLRGEAEAARRAAEEAEEARVQAER-EAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAE 2157
Cdd:COG3899 818 ALAERLGDRRLEARALFNLGFILHWLGPlREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLL 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2158 QAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSV 2237
Cdd:COG3899 898 AAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2238 RVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2317
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2318 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMS 2397
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2398 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKS 2477
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*
gi 41322914 2478 EEMQTVQQEQLLQETQALQQSFLSE 2502
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRL 1242
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1435-1602 |
8.40e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.20 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1435 AEIQAKARQAEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1514
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA-AAATPAAPAAAARRAARAAAAARQAEQPAAEAAAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1515 RQAEVELASRVKAEAEAAREKQRALQALEelRLQAEEAERRLRQAEVERARQVQVALE---TAQRSAEAELQSKRASFAE 1591
Cdd:PRK12678 101 KAEAAPAARAAAAAAAEAASAPEAAQARE--RRERGEAARRGAARKAGEGGEQPATEAradAAERTEEEERDERRRRGDR 178
|
170
....*....|.
gi 41322914 1592 KTAQLERSLQE 1602
Cdd:PRK12678 179 EDRQAEAERGE 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2307-2507 |
8.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2307 QQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaeETQGFQRTLEAERQRQLEMSAEA 2386
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2387 ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvqtleiqrqqsdhdaERLREAIAELEREKEKL 2466
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL-----------------QDLAEELEELQQRLAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41322914 2467 QQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLL 2507
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2337-2471 |
8.88e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2337 QQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSR------AQARAEEDAQRF 2410
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322914 2411 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDHDAERLREAIAelereKEKLQQEAK 2471
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1634-1931 |
8.93e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1634 ELERWQLKANEALRLRLQAEEVAQQkslaqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQ--- 1710
Cdd:pfam15558 59 SQEQWQAEKEQRKARLGREERRRAD------------RREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQcqe 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1711 QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAeMEVLLASKARAEEESRSTS-EKS 1789
Cdd:pfam15558 127 QRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQA-RKVLVDCQAKAEELLRRLSlEQS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1790 KQRLEAE-----AGRFRELAEEAA-------RLRALAEEAKRQRQ--------LAEEDAARQRAEAERVLAEKLAAIGEA 1849
Cdd:pfam15558 206 LQRSQENyeqlvEERHRELREKAQkeeeqfqRAKWRAEEKEEERQehkealaeLADRKIQQARQVAHKTVQDKAQRAREL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1850 TRLKTEAEIALKEKeaenerlrrlAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASDSELERQKGLVEDTLRQRRQVEE 1929
Cdd:pfam15558 286 NLEREKNHHILKLK----------VEKEEKCHREGIKEAIKKK---EQRSEQISREKEATLEEARKTARASFHMREKVRE 352
|
..
gi 41322914 1930 EI 1931
Cdd:pfam15558 353 ET 354
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
1341-1444 |
9.08e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 40.69 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1341 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKA----QAEREAKELQQRMQEEVVRREEAA---- 1412
Cdd:pfam06391 63 VEETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRkeekQEEEEEKEKKEKAKQELIDELMTSnkda 142
|
90 100 110
....*....|....*....|....*....|....
gi 41322914 1413 --VDAQQQKRSIQEELQQLRQSSEAEIQAKARQA 1444
Cdd:pfam06391 143 eeIIAQHKKTAKKRKSERRRKLEELNRVLEQKPT 176
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1349-1536 |
9.11e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.29 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1349 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER----------EAKELQQRMQEEVVRRE-----EAAV 1413
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegeiEAKEADHKGETEAEEVEhegetEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1414 DAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1490
Cdd:TIGR00927 726 TEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 41322914 1491 AQKRQAQEEAERlRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1536
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2198-2474 |
9.12e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2198 QLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEEL-SKLKARIEAENRALILRDKDNTQrfLQEEAEK 2276
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELnAQVKELREEAQELREKRDELNEK--VKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2277 MKQVAEEAARLSvaaQEAARLRQLAEEDLAQQRALAEkmLKEKMQAVQ-----EATRLKAEAELLQQQKELAQE-QARRL 2350
Cdd:COG1340 80 RDELNEKLNELR---EELDELRKELAELNKAGGSIDK--LRKEIERLEwrqqtEVLSPEEEKELVEKIKELEKElEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2351 QEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA--QARAEEDA-----QRFRKQAEEIGEKLHR 2423
Cdd:COG1340 155 ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEadELRKEADElhkeiVEAQEKADELHEEIIE 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322914 2424 T-----ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQ-QEAKLLQ 2474
Cdd:COG1340 235 LqkelrELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTtEELKLLQ 291
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2189-2416 |
9.43e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2189 EQELTTLRLQLEETDHQKNLLD-------EELQRLKAEATEAARQRSQVEEELFSVRVQMEELSklKARIEAENRAlilr 2261
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQleldnlrLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEAT--LARVDLEAKI---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2262 dkdntqRFLQEEAEKMKQVAEEaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK- 2340
Cdd:pfam00038 127 ------ESLKEELAFLKKNHEE--EVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKl 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322914 2341 ELAQEQARRLQEDKEQMAQQLAEETQGFQRtLEAERQRQLEMSAEAERlklRVAEMSRAQARAEEDAQRFRKQAEE 2416
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTIQS-LEIELQSLKKQKASLER---QLAETEERYELQLADYQELISELEA 270
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1681-1841 |
9.62e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1681 GKAEEQAVRQRELAEQELEKQRQLA---EGTAQQRL-AAEQELIR-LRAETEQGEQQRQLLEEELARLQREAAAATQKRQ 1755
Cdd:pfam04012 42 RQALAQTIARQKQLERRLEQQTEQAkklEEKAQAALtKGNEELAReALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1756 ELEAELAKVRAEMEVLLA--SKARAEEESRSTSEKSK-QRLEAEAGRFRE-LAEEAARLRALAEEAKRQRQLAE-EDAAR 1830
Cdd:pfam04012 122 ALETKIQQLKAKKNLLKArlKAAKAQEAVQTSLGSLStSSATDSFERIEEkIEEREARADAAAELASAVDLDAKlEQAGI 201
|
170
....*....|.
gi 41322914 1831 QRAEAERVLAE 1841
Cdd:pfam04012 202 QMEVSEDVLAR 212
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
50-262 |
9.68e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 42.24 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 50 KTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFHKLQNVQIALDYLRHRQV 119
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 120 KLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMVEGY---QGLRCDNFTS 189
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGLKGdkeEGIRSFGDPA 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 190 SWRDGRLFNAIIHRHKPLLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdEKSIITYVSSL 262
Cdd:COG5069 532 GSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-RLDVLTFIESL 609
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4285-4315 |
9.70e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.70e-03
10 20 30
....*....|....*....|....*....|.
gi 41322914 4285 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4315
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
49-107 |
9.71e-03 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 38.79 E-value: 9.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 49 KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK----GRMRFHKLQNV 107
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVV 65
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1102-1266 |
9.76e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1102 TQGAEEVLRAHEEQLKEAQAvpaTLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERW 1181
Cdd:COG4913 663 VASAEREIAELEAELERLDA---SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1182 ----RERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQA 1257
Cdd:COG4913 740 edlaRLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA 819
|
....*....
gi 41322914 1258 LLEEIERHG 1266
Cdd:COG4913 820 LLDRLEEDG 828
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2008-2573 |
9.76e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2008 RKAALEEVERLKAKVEEARRLRERAE--QESARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqSVLDQLRG 2085
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEdaREQIELLEPIRELAERYAAARERL--------------------AELEYLRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2086 EAEAARRAAEEAEEARVQAEREAAQSRRQvEEAERLKQsaeeqaqaraqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQ 2165
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLE-AELERLEA-----------------RLDALREELDELEAQIRGNGGDRLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2166 AADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQknlLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELS 2245
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2246 KLKARIEAENRALILRDKDNTQRFLQeeaekMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML-------- 2316
Cdd:COG4913 419 RELRELEAEIASLERRKSNIPARLLA-----LRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfaltll 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2317 --KEKMQAVQEAT-RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE------------------ 2375
Cdd:COG4913 493 vpPEHYAAALRWVnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspeelrr 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2376 ------RQRQLEMSAEAERLKLRVAEMSRAQ--ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQ--- 2444
Cdd:COG4913 573 hpraitRAGQVKGNGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqr 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 2445 ------SDHDAERLREAIAELEREKEKLQQ--------EAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRE 2510
Cdd:COG4913 653 laeyswDEIDVASAEREIAELEAELERLDAssddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322914 2511 RFIEQEKAKLEQLFQDEVAKAqqlREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRK 2573
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEE---RFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1426-1601 |
9.93e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1426 LQQLRQSSEAEIQAKaRQAEAAERSRLR--IEEEIRVVRLQLEATERQRGGAEGELQALRARAE------EAEAQKRQAQ 1497
Cdd:pfam00038 23 LEQQNKLLETKISEL-RQKKGAEPSRLYslYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEdfrqkyEDELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322914 1498 E-EAERLRRQVQDESQRKRQAEV-------ELASRVKAEAEAAREKQRALQ------------------ALEELRLQAEE 1551
Cdd:pfam00038 102 EnDLVGLRKDLDEATLARVDLEAkieslkeELAFLKKNHEEEVRELQAQVSdtqvnvemdaarkldltsALAEIRAQYEE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 41322914 1552 -AERRLRQAEVERARQVQVALETAQRSAEAELQSKrasfaEKTAQLERSLQ 1601
Cdd:pfam00038 182 iAAKNREEAEEWYQSKLEELQQAAARNGDALRSAK-----EEITELRRTIQ 227
|
|
| |
