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Conserved domains on  [gi|2022792582|ref|XP_040409121|]
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rab-3A-interacting protein isoform X1 [Cygnus olor]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 304-496 2.09e-149

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


:

Pssm-ID: 411032  Cd Length: 193  Bit Score: 424.72  E-value: 2.09e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 304 GHARNKSTSSAMGGSHQDLTMMQPIVKDCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYREDIFPCLTFSKSELASAVL 383
Cdd:cd21068     1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 384 EAVENNTLSIEPVGLQPVRFVKASAVECGGPKKCALSGQSKSCKHRIKLGDSSSYYYISPFCRYRITSVCNFFTYIRYIQ 463
Cdd:cd21068    81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2022792582 464 QGLLKQQDVDQMFWEVMQLRREMSLAKLGYYKE 496
Cdd:cd21068   161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Sec2p super family cl05764
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 211-279 6.90e-13

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


The actual alignment was detected with superfamily member pfam06428:

Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 64.51  E-value: 6.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022792582 211 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEK-------QLKEAQGKIDVLQAEVAALKT 279
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVAAARREKHAVEIkndqlkeQLKEKETLLESLQEQLKELKQ 78
sbcc super family cl31020
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 142-264 1.86e-03

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]


The actual alignment was detected with superfamily member TIGR00618:

Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  142 HNNSRKESNNAEREFLQGATVADVAEGNEDIFGLSTDS-LSHLRSPsvLEVREKGYERLKEELA--KAQRELKLKDEE-- 216
Cdd:TIGR00618  741 LNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAeLSHLAAE--IQFFNRLREEDTHLLKtlEAEIGQEIPSDEdi 818

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2022792582  217 ----CERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAQ 264
Cdd:TIGR00618  819 lnlqCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
 
Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 304-496 2.09e-149

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411032  Cd Length: 193  Bit Score: 424.72  E-value: 2.09e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 304 GHARNKSTSSAMGGSHQDLTMMQPIVKDCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYREDIFPCLTFSKSELASAVL 383
Cdd:cd21068     1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 384 EAVENNTLSIEPVGLQPVRFVKASAVECGGPKKCALSGQSKSCKHRIKLGDSSSYYYISPFCRYRITSVCNFFTYIRYIQ 463
Cdd:cd21068    81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2022792582 464 QGLLKQQDVDQMFWEVMQLRREMSLAKLGYYKE 496
Cdd:cd21068   161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 211-279 6.90e-13

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 64.51  E-value: 6.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022792582 211 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEK-------QLKEAQGKIDVLQAEVAALKT 279
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVAAARREKHAVEIkndqlkeQLKEKETLLESLQEQLKELKQ 78
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
197-279 3.38e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAA 276
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119


                  ...
gi 2022792582 277 LKT 279
Cdd:COG4372   120 LQK 122
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
185-278 2.04e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 185 SPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVKEANVKQ----AAAEKQL 260
Cdd:PRK03918  610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAGLRAEL 682

                          90
                  ....*....|....*...
gi 2022792582 261 KEAQGKIDVLQAEVAALK 278
Cdd:PRK03918  683 EELEKRREEIKKTLEKLK 700
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 188-278 7.44e-04

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: 42.35  E-value: 7.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  188 VLEVREKGYERLKEELAKAQRELKLKDEECE---RLSKVR-DQLGQELEELTASLfeeahkmvKEANVKQAAAEKQLKEA 263
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAERYKELKAELRElelALLVLRlEELREELEELQEEL--------KEAEEELEELTAELQEL 265

                           90
                   ....*....|....*
gi 2022792582  264 QGKIDVLQAEVAALK 278
Cdd:TIGR02168  266 EEKLEELRLEVSELE 280
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 142-264 1.86e-03

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: 41.11  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  142 HNNSRKESNNAEREFLQGATVADVAEGNEDIFGLSTDS-LSHLRSPsvLEVREKGYERLKEELA--KAQRELKLKDEE-- 216
Cdd:TIGR00618  741 LNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAeLSHLAAE--IQFFNRLREEDTHLLKtlEAEIGQEIPSDEdi 818

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2022792582  217 ----CERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAQ 264
Cdd:TIGR00618  819 lnlqCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 201-287 6.58e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  201 EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMvKEANVKQAAAEKQLKEAQG----KIDVLQAEVAA 276
Cdd:smart00787 204 TELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKK-SELNTEIAEAEKKLEQCRGftfkEIEKLKEQLKL 282

                           90
                   ....*....|....*
gi 2022792582  277 LKTL----VLSTSPT 287
Cdd:smart00787 283 LQSLtgwkITKLSGN 297
 
Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 304-496 2.09e-149

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411032  Cd Length: 193  Bit Score: 424.72  E-value: 2.09e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 304 GHARNKSTSSAMGGSHQDLTMMQPIVKDCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYREDIFPCLTFSKSELASAVL 383
Cdd:cd21068     1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 384 EAVENNTLSIEPVGLQPVRFVKASAVECGGPKKCALSGQSKSCKHRIKLGDSSSYYYISPFCRYRITSVCNFFTYIRYIQ 463
Cdd:cd21068    81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2022792582 464 QGLLKQQDVDQMFWEVMQLRREMSLAKLGYYKE 496
Cdd:cd21068   161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Rab11BD_RAB3IL1 cd21069
Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called ...
 331-494 5.12e-95

Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IL1 lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411033  Cd Length: 163  Bit Score: 284.83  E-value: 5.12e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 331 DCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYREDIFPCLTFSKSELASAVLEAVENNTLSIEPVGLQPVRFVKASAVE 410
Cdd:cd21069     1 EGKEVDTVLFAEFQAWKESPTLDRSCPFLSRIYREDIGPCLDFTKRELSDLVQSAVENNTLTIEPVASQALPVVKASAVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 411 CGGPKKCALSGQSKSCKHRIKLGDSSSYYYISPFCRYRITSVCNFFTYIRYIQQGLLKqQDVDQMFWEVMQLRREMSLAK 490
Cdd:cd21069    81 CGGPKKCALSGLSRTCRHRIKLGDSGNYYYISPSCRARITAVCNFFTYIRYIQQGLVR-QDAEQMFWEVMRLRREMSLAK 159


                  ....
gi 2022792582 491 LGYY 494
Cdd:cd21069   160 LGFY 163
Rab11BD_RAB3IP_like cd21044
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 ...
 333-492 1.42e-57

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 (RAB3IL1) and similar proteins; The family includes RAB3IP and RAB3IL1, as well as Rab guanine nucleotide exchange factor SEC2 from yeast. RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. SEC2 is a guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. SEC2 binds the Rab GTPase YPT32 but does not have exchange activity on YPT32. The model corresponds to the Rab11a/Rab11b-binding region of family members which lies within the carboxy-terminus, a region distinct from their GEF domain and Rab3a-binding region.


Pssm-ID: 411031  Cd Length: 178  Bit Score: 188.73  E-value: 1.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 333 KEADLSLYNEFRSWKDEP-----TMDRTCPFLDKIYREDIFPCLTFSKS----ELASAVLEAVENNTLSIEPV------G 397
Cdd:cd21044     1 FEVDLVLFEEFQEFLKAPsslslSLLKSSPFLKRILAEDIEPCLRFDPAllnwLLKKRLLAAILENTLEIEPIsgstetS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 398 LQPVRFVKASAVECGGPKKCALSGQSK--SCKHRIKLGDSSS-YYYISPFCRYRITSVCNFFTYIRYIQQGLLKQQDVDQ 474
Cdd:cd21044    81 SSSNNTAPVSSPPPASPKKCALCGESRldACLYRLRLSDSDSeWYPICSYCRNRLRAVCDFFAYLRYIRQGLVKSRSIEK 160

                         170
                  ....*....|....*...
gi 2022792582 475 MFWEVMQLRREMSLAKLG 492
Cdd:cd21044   161 LYLEILRLRLRMFLARLG 178
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 211-279 6.90e-13

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 64.51  E-value: 6.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022792582 211 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEK-------QLKEAQGKIDVLQAEVAALKT 279
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVAAARREKHAVEIkndqlkeQLKEKETLLESLQEQLKELKQ 78
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
197-279 3.38e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAA 276
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119


                  ...
gi 2022792582 277 LKT 279
Cdd:COG4372   120 LQK 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
183-278 2.88e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 2.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  183 LRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKE 262
Cdd:COG4913    277 LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE 356

                           90
                   ....*....|....*.
gi 2022792582  263 AQGKIDVLQAEVAALK 278
Cdd:COG4913    357 RERRRARLEALLAALG 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 197-281 3.67e-07

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: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAA 276
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRAELEA 101


                  ....*
gi 2022792582 277 LKTLV 281
Cdd:COG4942   102 QKEEL 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
189-295 6.51e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 6.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKID 268
Cdd:COG4372    82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR-KQLEAQIAELQSEIAEREEELKELEEQLE 160

                          90       100
                  ....*....|....*....|....*..
gi 2022792582 269 VLQAEVAALKTLVLSTSPTSPTKELQS 295
Cdd:COG4372   161 SLQEELAALEQELQALSEAEAEQALDE 187
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 189-279 4.12e-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: 48.00  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELKLKDEECE----RLSKVRDQLGQ------------ELEELTASLfEEAHKMVKEANVK 252
Cdd:COG1579    40 LAALEARLEAAKTELEDLEKEIKRLELEIEeveaRIKKYEEQLGNvrnnkeyealqkEIESLKRRI-SDLEDEILELMER 118

                          90       100
                  ....*....|....*....|....*..
gi 2022792582 253 QAAAEKQLKEAQGKIDVLQAEVAALKT 279
Cdd:COG1579   119 IEELEEELAELEAELAELEAELEEKKA 145
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 190-278 4.22e-06

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 46.00  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 190 EVRE------KGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQEL-------EELTASLFEEAHKMVKEANVKqaaA 256
Cdd:COG3599    24 EVDEfldevaEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLvvaqetaEEVKENAEKEAELIIKEAELE---A 100

                          90       100
                  ....*....|....*....|..
gi 2022792582 257 EKQLKEAQGKIDVLQAEVAALK 278
Cdd:COG3599   101 EKIIEEAQEKARKIVREIEELK 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
197-278 5.38e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  197 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEElTASLFEEAHKMVKE-----------ANVKQAAAEKQLKEAQG 265
Cdd:COG4913    341 EQLEREIERLERELEERERRRARLEALLAALGLPLPA-SAEEFAALRAEAAAllealeeeleaLEEALAEAEAALRDLRR 419

                           90
                   ....*....|...
gi 2022792582  266 KIDVLQAEVAALK 278
Cdd:COG4913    420 ELRELEAEIASLE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 189-277 7.39e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKID 268
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELA 361


                  ....*....
gi 2022792582 269 VLQAEVAAL 277
Cdd:COG1196   362 EAEEALLEA 370
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 193-278 7.99e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 193 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQA 272
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                  ....*.
gi 2022792582 273 EVAALK 278
Cdd:COG1196   380 ELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 196-277 8.48e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 196 YERLKEELAKAQRELKL-----KDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVL 270
Cdd:COG1196   215 YRELKEELKELEAELLLlklreLEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYEL 293


                  ....*..
gi 2022792582 271 QAEVAAL 277
Cdd:COG1196   294 LAELARL 300
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
192-279 1.18e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 192 REKGYERLKEELAKAQRELKLKDEECERLS---KVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAQGKID 268
Cdd:COG4717   123 KLLQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                          90
                  ....*....|.
gi 2022792582 269 VLQAEVAALKT 279
Cdd:COG4717   203 ELQQRLAELEE 213
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 189-279 1.37e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQ------AAAEKQLKE 262
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleerrRELEERLEE 320

                          90
                  ....*....|....*..
gi 2022792582 263 AQGKIDVLQAEVAALKT 279
Cdd:COG1196   321 LEEELAELEEELEELEE 337
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 196-278 1.50e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 196 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKmVKEANVKQAAAEKQLKEAQGKIDVLQAEVA 275
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRR 312


                  ...
gi 2022792582 276 ALK 278
Cdd:COG1196   313 ELE 315
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
189-294 1.57e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAQG 265
Cdd:COG4717   141 LAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                          90       100
                  ....*....|....*....|....*....
gi 2022792582 266 KIDVLQAEVAALKTLVLSTSPTSPTKELQ 294
Cdd:COG4717   221 ELEELEEELEQLENELEAAALEERLKEAR 249
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 166-276 1.70e-04

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: 44.40  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  166 AEGNEDIFGLSTDSLSHLRSPSVLEVREKGYERLKEELAKAQRELK-----LKDEECE---RLSKVRDQLGQELEELTAS 237
Cdd:pfam01576  169 AEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEgestdLQEQIAElqaQIAELRAQLAKKEEELQAA 248

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2022792582  238 LfeeaHKMVKEANVKqAAAEKQLKEAQGKIDVLQAEVAA 276
Cdd:pfam01576  249 L----ARLEEETAQK-NNALKKIRELEAQISELQEDLES 282
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 197-277 1.91e-04

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: 41.70  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQREL--KLKDEECER---LSKVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAqgkidvLQ 271
Cdd:COG0711    44 ERAKEEAEAALAEYeeKLAEARAEAaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAE------LR 117


                  ....*.
gi 2022792582 272 AEVAAL 277
Cdd:COG0711   118 AEVADL 123
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
185-278 2.04e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 185 SPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVKEANVKQ----AAAEKQL 260
Cdd:PRK03918  610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAGLRAEL 682

                          90
                  ....*....|....*...
gi 2022792582 261 KEAQGKIDVLQAEVAALK 278
Cdd:PRK03918  683 EELEKRREEIKKTLEKLK 700
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 204-281 3.10e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 3.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022792582 204 AKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALKTLV 281
Cdd:COG3883    12 AFADPQIQAKQKELSELQAELEAAQAELDALQAEL-EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 186-286 3.31e-04

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: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 186 PSVLEVREKGYERLKEELAKAQRELKLKDEEceRLSKVRDQLGQELEELTAslFEEAHKMVKEANVKQAAAEKQLKEAQG 265
Cdd:COG0542   410 PEELDELERRLEQLEIEKEALKKEQDEASFE--RLAELRDELAELEEELEA--LKARWEAEKELIEEIQELKEELEQRYG 485

                          90       100
                  ....*....|....*....|.
gi 2022792582 266 KIDVLQAEVAALKTLVLSTSP 286
Cdd:COG0542   486 KIPELEKELAELEEELAELAP 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 188-278 7.44e-04

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: 42.35  E-value: 7.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  188 VLEVREKGYERLKEELAKAQRELKLKDEECE---RLSKVR-DQLGQELEELTASLfeeahkmvKEANVKQAAAEKQLKEA 263
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAERYKELKAELRElelALLVLRlEELREELEELQEEL--------KEAEEELEELTAELQEL 265

                           90
                   ....*....|....*
gi 2022792582  264 QGKIDVLQAEVAALK 278
Cdd:TIGR02168  266 EEKLEELRLEVSELE 280
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
197-281 8.84e-04

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: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  197 ERLKEELAKAQREL--------KLKDEE---------CERLSKVR-------------DQLGQELEELTAS--LFEEAHK 244
Cdd:COG4913    613 AALEAELAELEEELaeaeerleALEAELdalqerreaLQRLAEYSwdeidvasaereiAELEAELERLDASsdDLAALEE 692

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2022792582  245 MVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALKTLV 281
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 189-276 8.92e-04

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: 39.13  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYErlkEELAKAQREL--------------KLKDEECERLSKVRdqlgQELEELTASLFEEAHKMVKEanvkQA 254
Cdd:pfam20492  11 LEERLKQYE---EETKKAQEELeeseetaeeleeerRQAEEEAERLEQKR----QEAEEEKERLEESAEMEAEE----KE 79

                          90       100
                  ....*....|....*....|..
gi 2022792582 255 AAEKQLKEAQGKIDVLQAEVAA 276
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEEVER 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 197-279 1.05e-03

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: 41.98  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  197 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAA 276
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755


                   ...
gi 2022792582  277 LKT 279
Cdd:TIGR02169  756 VKS 758
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
189-280 1.13e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVKEANVKQAAAEKQLKEAQGKID 268
Cdd:COG4717    76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLE 149

                          90
                  ....*....|..
gi 2022792582 269 VLQAEVAALKTL 280
Cdd:COG4717   150 ELEERLEELREL 161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 197-278 1.35e-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: 41.58  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  197 ERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAE 273
Cdd:TIGR02168  189 DRLEdilNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK 268


                   ....*
gi 2022792582  274 VAALK 278
Cdd:TIGR02168  269 LEELR 273
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
201-279 1.39e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 201 EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL----FEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAA 276
Cdd:COG4717   385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464


                  ...
gi 2022792582 277 LKT 279
Cdd:COG4717   465 LEE 467
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 142-264 1.86e-03

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: 41.11  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  142 HNNSRKESNNAEREFLQGATVADVAEGNEDIFGLSTDS-LSHLRSPsvLEVREKGYERLKEELA--KAQRELKLKDEE-- 216
Cdd:TIGR00618  741 LNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAeLSHLAAE--IQFFNRLREEDTHLLKtlEAEIGQEIPSDEdi 818

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2022792582  217 ----CERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAQ 264
Cdd:TIGR00618  819 lnlqCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 189-305 1.89e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELKlkdeecERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQ-----AAAEKQLKEA 263
Cdd:PRK00409  539 AEALLKEAEKLKEELEEKKEKLQ------EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQkggyaSVKAHELIEA 612

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2022792582 264 QGKIDvlqaevAALKTLVLSTSPT-SPTKELQSG----VKTPFKKGH 305
Cdd:PRK00409  613 RKRLN------KANEKKEKKKKKQkEKQEELKVGdevkYLSLGQKGE 653
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
193-281 2.11e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 193 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEAnvkqaaaeKQLKEAQGKIDVLQA 272
Cdd:PRK03918  658 EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKEL--------EKLEKALERVEELRE 728


                  ....*....
gi 2022792582 273 EVAALKTLV 281
Cdd:PRK03918  729 KVKKYKALL 737
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
157-279 2.32e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 157 LQGATVADVAEGNEDIFGLSTDSLSHLRSPsvLEVREKGYERLkEELAKAQRELKLKDEECERLSKVRDQLGQELEELT- 235
Cdd:PRK02224  461 VEGSPHVETIEEDRERVEELEAELEDLEEE--VEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRe 537

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2022792582 236 --ASLFEEAHKMVKEANVKQAAAEKQLKEAQ---GKIDVLQAEVAALKT 279
Cdd:PRK02224  538 raEELRERAAELEAEAEEKREAAAEAEEEAEearEEVAELNSKLAELKE 586
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 196-300 2.64e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 196 YERLKEELAKAQRELklkDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVA 275
Cdd:COG3883   138 LKADKAELEAKKAEL---EAKLAELEALKAELEAAKAELEAQQ-AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213

                          90       100
                  ....*....|....*....|....*
gi 2022792582 276 ALKTLVLSTSPTSPTKELQSGVKTP 300
Cdd:COG3883   214 AAAAAAAAAAAAAAAAAAAAAAAAA 238
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 197-280 2.70e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAA 276
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398


                  ....
gi 2022792582 277 LKTL 280
Cdd:COG1196   399 AAQL 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 197-277 2.72e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQRELKLKDE----ECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQA 272
Cdd:COG1196   203 EPLERQAEKAERYRELKEElkelEAELLLLKLRELEAELEELEAEL-EELEAELEELEAELAELEAELEELRLELEELEL 281


                  ....*
gi 2022792582 273 EVAAL 277
Cdd:COG1196   282 ELEEA 286
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 193-279 3.01e-03

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: 40.44  E-value: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  193 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLG---------------QELEELTASLfEEAHKMVKEANVKQAAAE 257
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeeeqlrvkEKIGELEAEI-ASLERSIAEKERELEDAE 321

                           90       100
                   ....*....|....*....|..
gi 2022792582  258 KQLKEAQGKIDVLQAEVAALKT 279
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELER 343
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 197-278 3.74e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQRelKLKDEECERLskvRDQLGQELEELTASLFEEAHKMVKEANVKQAAAEKQLKEAQGKidvlQAEVAA 276
Cdd:PRK09510   90 EELQQKQAAEQE--RLKQLEKERL---AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK----RAAAAA 160


                  ..
gi 2022792582 277 LK 278
Cdd:PRK09510  161 KK 162
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 189-275 3.88e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELklkdeecerlskvrDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKID 268
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAEL--------------DALQAELEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIE 82


                  ....*..
gi 2022792582 269 VLQAEVA 275
Cdd:COG3883    83 ERREELG 89
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
189-276 5.34e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQGKID 268
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA-EELQEELEELQKERQDLEQQRKQLEAQIA 139


                  ....*...
gi 2022792582 269 VLQAEVAA 276
Cdd:COG4372   140 ELQSEIAE 147
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 190-278 6.41e-03

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 36.78  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 190 EVRE------KGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQEL-------EELTASLFEEAHKMVKEANVKqaaA 256
Cdd:pfam05103  22 EVDEfldqvaEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLilaqetaEEVKANAQKEAELIIKEAEAK---A 98

                          90       100
                  ....*....|....*....|..
gi 2022792582 257 EKQLKEAQGKIDVLQAEVAALK 278
Cdd:pfam05103  99 ERIVDDANNEVKKINDEIEELK 120
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 201-287 6.58e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  201 EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMvKEANVKQAAAEKQLKEAQG----KIDVLQAEVAA 276
Cdd:smart00787 204 TELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKK-SELNTEIAEAEKKLEQCRGftfkEIEKLKEQLKL 282

                           90
                   ....*....|....*
gi 2022792582  277 LKTL----VLSTSPT 287
Cdd:smart00787 283 LQSLtgwkITKLSGN 297
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 189-279 6.70e-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: 39.23  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 189 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTaslfeeahKMVKEANVKQAAAEKQLKEAQGKID 268
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT--------KKISSLKEKIEKLESEKKEKESKIS 541

                          90
                  ....*....|.
gi 2022792582 269 VLQAEVAALKT 279
Cdd:TIGR04523 542 DLEDELNKDDF 552
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 187-238 6.79e-03

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: 39.39  E-value: 6.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2022792582  187 SVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL 238
Cdd:pfam01576  538 GTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL 589
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 187-280 7.01e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 36.91  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 187 SVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTAS------------LFEEAHKMVKEANVKQA 254
Cdd:TIGR02473   6 KLLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAgtsalelsnyqrFIRQLDQRIQQQQQELA 85

                          90       100
                  ....*....|....*....|....*.
gi 2022792582 255 AAEKQLKEAQGKIDVLQAEVAALKTL 280
Cdd:TIGR02473  86 LLQQEVEAKRERLLEARRELKALEKL 111
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
197-278 7.37e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQRELKLKDE------ECERLSKVRDQLGQELEELT----------ASLFEEAHKMVKEANvkqaAAEKQL 260
Cdd:COG1340   143 KELEKELEKAKKALEKNEKlkelraELKELRKEAEEIHKKIKELAeeaqelheemIELYKEADELRKEAD----ELHKEI 218

                          90
                  ....*....|....*...
gi 2022792582 261 KEAQGKIDVLQAEVAALK 278
Cdd:COG1340   219 VEAQEKADELHEEIIELQ 236
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
197-303 7.62e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 197 ERLKEELAKAQRELKLKDEECER----LSKVRDQLGQELEELtaslfEEAHKMVKEAnvkqAAAEKQLKEAQGKIDVLQA 272
Cdd:COG2433   423 ERLEAEVEELEAELEEKDERIERlereLSEARSEERREIRKD-----REISRLDREI----ERLERELEEERERIEELKR 493

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2022792582 273 EVAALKTLVlstsptsptKELQSGVKTPFKK 303
Cdd:COG2433   494 KLERLKELW---------KLEHSGELVPVKV 515
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
190-278 7.80e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 7.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582  190 EVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeeahkmvKEANVKQAAAEKQLKEAQG-KID 268
Cdd:COG4913    270 RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL--------DALREELDELEAQIRGNGGdRLE 341

                           90
                   ....*....|
gi 2022792582  269 VLQAEVAALK 278
Cdd:COG4913    342 QLEREIERLE 351
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 192-291 8.78e-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: 38.59  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 192 REKGYERLKEELAKAQRELKlkdEECERLSKVRDQLGQELEELtASLFEEAHKMVKEANVKQAAAEKQLKEAQGKIDVLQ 271
Cdd:COG4942   151 QAEELRADLAELAALRAELE---AERAELEALLAELEEERAAL-EALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                          90       100
                  ....*....|....*....|
gi 2022792582 272 AEVAALKTLVLSTSPTSPTK 291
Cdd:COG4942   227 ALIARLEAEAAAAAERTPAA 246
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 193-281 9.34e-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: 37.60  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 193 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAhkmvKEANVKQAAAEKQLKEAQGKIDVLQA 272
Cdd:COG1579    88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE----AELEEKKAELDEELAELEAELEELEA 163


                  ....*....
gi 2022792582 273 EVAALKTLV 281
Cdd:COG1579   164 EREELAAKI 172
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 198-278 9.85e-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: 37.60  E-value: 9.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022792582 198 RLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVKEANVKQAAAEKQLKEAQG--KIDVLQAEVA 275
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-KRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIE 99


                  ...
gi 2022792582 276 ALK 278
Cdd:COG1579   100 SLK 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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