|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
162-474 |
3.60e-150 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 433.58 E-value: 3.60e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 162 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRqNLEPLFEQYINNLRRQLDSIVGERGRLDSELRN 241
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 242 MQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDA-LSQMQTHISDTSVVLS 320
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEeVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 321 MDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 400
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119617035 401 CASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 474
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
17-159 |
1.91e-25 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 102.43 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 17 GFSANSARLPGVSRSGFSSISVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISI---GGGSCAISG---GYGSRAGGS 90
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISIsvaGGGSRPGSGfgfGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119617035 91 YGFGGAGSGFGFGGG-------AGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPAIQRV 159
Cdd:pfam16208 81 GGFGGGGGGGFGGGGgfgggfgGGGYGGGGFGGGGFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-456 |
2.43e-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: 66.62 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 162 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGERGRLDSELRN 241
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 242 MQDLVEDLKNKYEDEINKRTAAENEFVTLKKdvdaaymNKVELQAKADTLTDEINFLRALYDALSQM--QTHISDTSVVL 319
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEltLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 320 SMDNNRN---------LDLDSIIAEVKAQYEEIAQ----------RSRAEAESWYQtKYEELQVTAGRHGDDLRNTKQEI 380
Cdd:TIGR02168 825 RLESLERriaaterrlEDLEEQIEELSEDIESLAAeieeleelieELESELEALLN-ERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 381 AEINRMIQRLRSEIDHVKKQCASLQAAIADAEQR-----------GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQE 449
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
....*..
gi 119617035 450 LMNVKLA 456
Cdd:TIGR02168 984 LGPVNLA 990
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
179-446 |
1.75e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 179 DKVRFLEQQNKVLDTKWTLLQEQgTKTvrqnleplFEQYINNLRRQLDSIVgergrldSELRNMQDLVEDLKNKYEDEIN 258
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ-IKT--------YNKNIEEQRKKNGENI-------ARKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 259 KRTAAENEFVTLKKDVDAAY----MNKVELQAKADTLTDEINFLRALYDALSQMQThISDTsvvlsmdnnrnldlDSIIA 334
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQ-ISEG--------------PDRIT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 335 EVKAQYEEIAQRSRAEaeswyQTKYEELQVTAgrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIadaeQR 414
Cdd:PHA02562 303 KIKDKLKELQHSLEKL-----DTAIDELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI----EE 369
|
250 260 270
....*....|....*....|....*....|..
gi 119617035 415 GEMALKDAKNKLEGLEDALQKAKQDLARLLKE 446
Cdd:PHA02562 370 LQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
303-442 |
2.63e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.66 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 303 DALSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEiAQRSRAEAESWYQTKYEELQVTAGRHGD---DLRNTKQE 379
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQV 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119617035 380 IAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGemalKDAKNKLEG----LEDALQKAKQDLAR 442
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
164-450 |
3.49e-07 |
|
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: 53.53 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 164 REQIKTLNNKFASF---IDKVRF-LEQQNKVLDTKWTLLQEQGTKtvrqnLEPLFEQYINNLRRQLDSIVGERGRLDSEL 239
Cdd:TIGR02169 236 ERQKEAIERQLASLeeeLEKLTEeISELEKRLEEIEQLLEELNKK-----IKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 240 RNMQDLVEDLKN---KYEDEINKrTAAENEfvTLKKDVDaaymnkvELQAKADTLTDEINFLRALYDALSQmqthisdts 316
Cdd:TIGR02169 311 AEKERELEDAEErlaKLEAEIDK-LLAEIE--ELEREIE-------EERKRRDKLTEEYAELKEELEDLRA--------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 317 vvlsmdnnrnlDLDSIIAEVKAQYEEIAQRSRAEAEswYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDH 396
Cdd:TIGR02169 372 -----------ELEEVDKEFAETRDELKDYREKLEK--LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 119617035 397 VKKQCASLQAAIADAEQrgemalkdaknKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEW-----------KLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-450 |
6.93e-07 |
|
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: 52.38 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 204 KTVRQNLEpLFEQYINNLRRQLDSIVGERgrldSELRNMQDLVEDL-KNKYEDEINKRTAAENEFVTLKKDVDAAYMNKV 282
Cdd:TIGR02169 180 EEVEENIE-RLDLIIDEKRQQLERLRRER----EKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 283 ELQAKADTLTDEINFLRALydaLSQMQTHISDtsvvlsMDNNRNLDLDSIIAEVKAqyeEIAQRSRAEAEswYQTKYEEL 362
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQL---LEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE--KERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 363 QVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGE----------MALKDAKNKLEGLEDA 432
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdkefaetrDELKDYREKLEKLKRE 400
|
250
....*....|....*...
gi 119617035 433 LQKAKQDLARLLKEYQEL 450
Cdd:TIGR02169 401 INELKRELDRLQEELQRL 418
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-433 |
8.24e-07 |
|
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: 51.98 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 145 LTPLNLQIDPAIQRVRAEEREqIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgTKTVRQNLEpLFEQYINNLRRQ 224
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQ-ILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 225 LDSIVGERGRLDSELRNMQDLVEDLKNKYEDeinkrtaAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDA 304
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 305 LSQMQT----HISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEI 380
Cdd:TIGR02168 391 LELQIAslnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 119617035 381 AEINRMIQRLRSEIDHVKKQCASLQAAIADAE--QRGEMALKDAKNKLEGLEDAL 433
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEgfSEGVKALLKNQSGLSGILGVL 525
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
215-489 |
1.08e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 215 EQYIN-NLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDeinkrTAAENEFVTLKKDVDAAYMNKVELQAKADTLTD 293
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 294 EINFLRALYDALSQMqthisdtsVVLSMDNNRNLDLDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQVTAGRHGDDL 373
Cdd:COG3206 234 ELAEAEARLAALRAQ--------LGSGPDALPELLQSPVIQQLRAQLAEL------------EAELAELSARYTPNHPDV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 374 RNTKQEIAEINRMIQRLRSEIDhvkkqcASLQAAIADAEQRgemalkdaKNKLEGLEDALQKAKQDLARLLKEYQELMNv 453
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQRIL------ASLEAELEALQAR--------EASLQAQLAQLEARLAELPELEAELRRLER- 358
|
250 260 270
....*....|....*....|....*....|....*....
gi 119617035 454 klalDVEIA--TYRKLLEG-EECRLNgEGVGQVNVSVVQ 489
Cdd:COG3206 359 ----EVEVAreLYESLLQRlEEARLA-EALTVGNVRVID 392
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
152-472 |
1.42e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 152 IDP-AIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQ------GTKTVRQNLEPLFEQYINNLRR- 223
Cdd:PRK01156 402 IDPdAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 224 --QLDSIVGERGRLDSELRNMQDLVEDLKNKyedEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAL 301
Cdd:PRK01156 482 eeKIREIEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 302 Y-DALSQMQTHISDTSVVLSmdnnrNLDLDSIIA---EVKAQYEEIAQRSRaEAESWYQTKYEELQVTAGRHGDD---LR 374
Cdd:PRK01156 559 KlEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 375 NTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALkDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVK 454
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
330
....*....|....*...
gi 119617035 455 LALDVEIATYRKLLEGEE 472
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-400 |
1.50e-06 |
|
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: 51.22 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 144 LLTPLNLQIDPAIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQnleplfeqyINNLRR 223
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE---------IEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 224 QLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEinfLRALYD 303
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE---LQRLSE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 304 ALSQMQTHISdtsvvlsmdnnrnlDLDSIIAEVKAQYEEIAQRSRAEaeswyQTKYEELQVTAGRHGDDLRNTKQEIAEI 383
Cdd:TIGR02169 421 ELADLNAAIA--------------GIEAKINELEEEKEDKALEIKKQ-----EWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
250
....*....|....*..
gi 119617035 384 NRMIQRLRSEIDHVKKQ 400
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQ 498
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
199-443 |
1.98e-06 |
|
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: 50.94 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 199 QEQGTKTVRQNLE-----PLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKD 273
Cdd:pfam01576 474 QELLQEETRQKLNlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 274 VDAAYMNKVELQAKADTLTDEINFLRALYDALSQMQTHisDTSVVLSMDnNRNLDLDSIIAEVK---AQYEEiaQRSRAE 350
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDH--QRQLVSNLE-KKQKKFDQMLAEEKaisARYAE--ERDRAE 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 351 AESwyqTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQ----RLRSEIDHVKKQCASLQAAIADAEQrgemALKDAKNKL 426
Cdd:pfam01576 629 AEA---REKETRALSLARALEEALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQL 701
|
250
....*....|....*..
gi 119617035 427 EGLEDALQKAKQDLARL 443
Cdd:pfam01576 702 EELEDELQATEDAKLRL 718
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-478 |
3.06e-06 |
|
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: 50.44 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 279 MNKVELQAKADTLtdeinfLRALYDALSQMQTHISDTSVVlsmDNNRNLD-LDSIIAEVKAQYEEIAQRSRAEAESWYQT 357
Cdd:TIGR02168 202 LKSLERQAEKAER------YKELKAELRELELALLVLRLE---ELREELEeLQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 358 KYE--ELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMA---LKDAKNKLEGLEDA 432
Cdd:TIGR02168 273 RLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEE 352
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 119617035 433 LQKAKQDLARLLKEYQELMNVKLALDVEIATYRK---LLEGEECRLNGE 478
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-472 |
3.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 165 EQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgtktvRQNLEPLFEQyINNLRRQLDSIVGERGRLDSELRNMQD 244
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 245 LVEDLKNKYED------EINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDALSQMqthisdtsvv 318
Cdd:PRK03918 267 RIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK---------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 319 lsmdNNRNLDLDSIIAEVKAQYEEIAQRSRAeaeswyqtkYEELQVTAGRhgddLRNTKQEIA-----EINRMIQRLRSE 393
Cdd:PRK03918 337 ----EERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE----LERLKKRLTgltpeKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 394 IDHVKKQCASLQAAIADAEQRGE------MALKDAKNKL---------EGLEDALQKAKQDLARLLKEYQELMNVKLALD 458
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLR 479
|
330
....*....|....
gi 119617035 459 VEIATYRKLLEGEE 472
Cdd:PRK03918 480 KELRELEKVLKKES 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
215-471 |
3.34e-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: 50.12 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 215 EQYINNLRRQLDS---IVGERGRLDSELrnmqdLVEdlKNKYEDEINKRTAAENEFVTLKKDVDAAYMnkvELQAK-ADT 290
Cdd:pfam15921 561 DKVIEILRQQIENmtqLVGQHGRTAGAM-----QVE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARvSDL 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 291 LTDEINFLRALYDALSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVkaqyeEIAQRSraeaeswYQTKYEELQVTAGRHG 370
Cdd:pfam15921 631 ELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY-----EVLKRN-------FRNKSEEMETTTNKLK 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 371 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIadAEQRGEMalkDA-KNKLEGLEDALQKAKQDlARLLKEYQE 449
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI--TAKRGQI---DAlQSKIQFLEEAMTNANKE-KHFLKEEKN 772
|
250 260
....*....|....*....|..
gi 119617035 450 LMNVKLAldvEIATYRKLLEGE 471
Cdd:pfam15921 773 KLSQELS---TVATEKNKMAGE 791
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-469 |
4.01e-06 |
|
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: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 221 LRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRA 300
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 301 LYDAL----SQMQTHISdtSVVLSMDNNRNLDLDSIIAEVKAQYEEI-AQRSRAEAeswyqtKYEELQVTAGRHGDDLRN 375
Cdd:TIGR02169 759 ELKELeariEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 376 TKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKL 455
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....
gi 119617035 456 ALDVEIATYRKLLE 469
Cdd:TIGR02169 907 ELEAQIEKKRKRLS 920
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-450 |
4.73e-06 |
|
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: 49.67 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 191 LDTKWTLLQEQGTKTVRqnleplFEQYINNLRR-QLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVT 269
Cdd:TIGR02168 198 LERQLKSLERQAEKAER------YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 270 LKKDVDAAYMNKVELQAKADTLTDEIN----FLRALYDALSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQ 345
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISrleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 346 RSRA------EAESWYQ---TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQR-G 415
Cdd:TIGR02168 352 ELESleaeleELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlE 431
|
250 260 270
....*....|....*....|....*....|....*
gi 119617035 416 EMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
218-436 |
1.48e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 218 INNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEI-N 296
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 297 FLRALYDALSQmqthISDTSVVLSMDN-----NRNLDLDSIIAEVKAQYEEI--AQRSRAEAESWYQTKYEELQVTAGRH 369
Cdd:COG3883 91 RARALYRSGGS----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119617035 370 GDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKA 436
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-452 |
3.00e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 283 ELQAKADTLTDEINFLRALYDALSQMQTHISDTSVVLSMDnnrnLDLDSI---IAEVKAQYEEI---------AQRSRAE 350
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE----IDVASAereIAELEAELERLdassddlaaLEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 351 AESWYQTKYEELQVTAGRHGDdlrnTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLE 430
Cdd:COG4913 697 LEAELEELEEELDELKGEIGR----LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
170 180
....*....|....*....|..
gi 119617035 431 DALQKAKQDLARLLKEYQELMN 452
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-466 |
4.72e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 272 KDVDAAYMNKVELQAKADTLTDeinfLRALYDALSQMQTHISDTSVVLSM-----DNNRNLDLDSIIAEVKAQYEEI-AQ 345
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP----IRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLeAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 346 RSRAEAE-SWYQTKYEELQVT-AGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAK 423
Cdd:COG4913 311 LERLEARlDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 119617035 424 NKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 466
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-453 |
5.05e-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: 45.91 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 372 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQ 448
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 119617035 449 ELMNV 453
Cdd:COG4942 108 ELLRA 112
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-449 |
5.13e-05 |
|
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: 46.17 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 165 EQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgTKTVRQNLEPLfEQYINNLRRQLDSIVGERGRLDSELRNMQD 244
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE-IKNDKEQKNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 245 LVEDLKNKYEDEINKRTAAENEFVTLKKdvdaaymnkvELQAKADTLTDEINFLRALYDALSQMQTHISdtsvvlsmdnn 324
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEK----------EKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 325 RNLDLDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQcasL 404
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQL------------KDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQ---L 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 119617035 405 QAAIADAEQrgemalkdAKNKLEGLEDALQKAKQDLARLLKEYQE 449
Cdd:TIGR04523 270 SEKQKELEQ--------NNKKIKELEKQLNQLKSEISDLNNQKEQ 306
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-475 |
6.37e-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: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 283 ELQAKADTLTDEINFLRALYDALSQMQTHISDTSVVLS-MDNNRNLDLDsiIAEVKAQYEEI-AQRSRAEAESwyqtkye 360
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQrLAEYSWDEID--VASAEREIAELeAELERLDASS------- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 361 elqvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRgemaLKDAKNKLEGLEDAlqKAKQDL 440
Cdd:COG4913 685 ----------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDL--ARLELR 748
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 119617035 441 ARLLKEYQELM------NVKLALDVEIATYRKLLEGEECRL 475
Cdd:COG4913 749 ALLEERFAAALgdaverELRENLEERIDALRARLNRAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-450 |
6.40e-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: 45.53 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 371 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
231-450 |
9.41e-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: 44.75 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 231 ERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAlydALSQMQT 310
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 311 HISDTSVVLSMDNNRNldldsiIAEVKAQYEEIAQRSRAEAesWYQTKYEELQvtagRHGDDLRNTKQEIAEINRMIQRL 390
Cdd:COG4942 105 ELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 391 RSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
371-477 |
1.09e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 371 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQC----------------ASLQAAIADAEQRGEmALKDAKNKLEGLEDALQ 434
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAELE-RLDASSDDLAALEEQLE 695
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 119617035 435 KAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNG 477
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
328-469 |
1.19e-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: 43.76 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 328 DLDSIIAEVKAQYEEI-AQRSRAEAE-SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVK--KQCAS 403
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617035 404 LQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELmnvKLALDVEIATYRKLLE 469
Cdd:COG1579 94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
218-473 |
1.52e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 218 INNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTaaenEFVTLKKDVDAAYMNKVELQAKADTLTDEINF 297
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 298 LRALYDALSQMQTHISDTSVVLSMDNN----RNLDLDSIIAEVKAQYEEI---AQRSRAEAESW------YQTKYEELQV 364
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 365 TAGRHGDDLRNTKQEIAEINRMIQRLRSEIDhvkkqcaSLQAAIADAeqrgEMALKDAKNKLEGLEDALQKAKQDLARLL 444
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIE-------ELRERFGDA----PVDLGNAEDFLEELREERDELREREAELE 432
|
250 260
....*....|....*....|....*....
gi 119617035 445 KEYQELMNVklaldveIATYRKLLEGEEC 473
Cdd:PRK02224 433 ATLRTARER-------VEEAEALLEAGKC 454
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-463 |
2.77e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 333 IAEVKAQYEEIAQRSRAEAEswyqtKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAE 412
Cdd:COG1196 262 LAELEAELEELRLELEELEL-----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 119617035 413 QR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIAT 463
Cdd:COG1196 337 EEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
156-454 |
3.16e-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: 43.56 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 156 IQRVRAEEREQIKTLNNKFASfidkvrfLEQQNKVLDTKWTLLQE-----------QGTKTVRQNLEPLFEQYINNLRRQ 224
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEkkqfekiaeelKGKEQELIFLLQAREKEIHDLEIQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 225 LDSIVGERGRLDSElrnmqdlVEDLKNKYEDEINKRTAaenefvtLKKDVDAAYMNKVELQAKADTLTDEI-NFLRALYD 303
Cdd:pfam05483 459 LTAIKTSEEHYLKE-------VEDLKTELEKEKLKNIE-------LTAHCDKLLLENKELTQEASDMTLELkKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 304 ALSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLR--NTKQEIA 381
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIE 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119617035 382 EINRMIQRLRSEIDHVKKQcaslqaaiADAEQRGEMALKDAKNKLEgLEdaLQKAKQDLARLLKEYQELMNVK 454
Cdd:pfam05483 605 NKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKLE-LE--LASAKQKFEEIIDNYQKEIEDK 666
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
205-450 |
5.78e-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: 41.83 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 205 TVRQNLEPLFEqyINNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvEL 284
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 285 QAKADTLTDEINFLRalydalsqmqthisdtsvvlsmdNNRnlDLDSIIAEVkaqyeEIAQRSRAEAEswyqtkyeelqv 364
Cdd:COG1579 72 EARIKKYEEQLGNVR-----------------------NNK--EYEALQKEI-----ESLKRRISDLE------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 365 tagrhgddlrntkQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDL-ARL 443
Cdd:COG1579 110 -------------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPEL 176
|
....*..
gi 119617035 444 LKEYQEL 450
Cdd:COG1579 177 LALYERI 183
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
282-466 |
6.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 282 VELQAKADTLTDEINFLRALYDALSQMQTHISDTSVVLSMDNNRNLdLDSIIAEVKAQYEEIAQRSRAEAEswYQTKYEE 361
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQE--LKEELEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 362 LQ---------VTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEmalkdaknkLEGLEDA 432
Cdd:COG4717 407 LEeqleellgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQE 477
|
170 180 190
....*....|....*....|....*....|....
gi 119617035 433 LQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 466
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-472 |
7.17e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 335 EVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQR 414
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 119617035 415 gemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEE 472
Cdd:COG1196 297 ----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
263-466 |
9.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 263 AENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDA----LSQMQTHISDTsvvlsmdnnrNLDLDSIIAEVKA 338
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaeLEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 339 QYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNtkqeIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEmA 418
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLA-E 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 119617035 419 LKDAKNKLEGLEDALQKAKQD----LARLLKEYQELMNVKLALDVEIATYRK 466
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| DUF1351 |
pfam07083 |
Protein of unknown function (DUF1351); This family consists of several bacterial and phage ... |
326-461 |
1.25e-03 |
|
Protein of unknown function (DUF1351); This family consists of several bacterial and phage proteins of around 230 residues in length. The function of this family is unknown.
Pssm-ID: 429283 [Multi-domain] Cd Length: 210 Bit Score: 40.44 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 326 NLDLDSIIAEVKAQYEEIAQRSRAEAEswyqtKYEELQVTAgrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCAslq 405
Cdd:pfam07083 1 ELSVTQKPAAISFNFEELETYVDGIVA-----KYEGLVVTE----DTVKEAKKERAELNKIAKALDDKRKEVKKQYS--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119617035 406 AAIADAEQRG---EMALKDAKNKL----EGLEDALQKAKQDLARLLK-EYQELMNVKLAlDVEI 461
Cdd:pfam07083 69 EPYDEFEAKIkelVAKIKEAIDPIdeqiKAFEEKEKDAKRQLVKALIsELAEEYGVPLE-EIEI 131
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-474 |
1.81e-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: 41.49 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 128 PVCPP--GGIQEVTVNQSLLTPLNLQIDpaiqrvraEEREQIKTLNNKFASFIDKVRFLEQQnkvldtkWTLLQEQGTKT 205
Cdd:TIGR00618 525 PLTRRmqRGEQTYAQLETSEEDVYHQLT--------SERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNL 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 206 vrQNLEPLFEQYINNLRRQLDSIVGERGRLDSELR---NMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDvdaaymnKV 282
Cdd:TIGR00618 590 --QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-------RV 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 283 ELQAKADTlTDEINFLRALYDALSQMQTHISDTSVVLSMDNNRNLDLDSI---IAEVKAQYEEIAQRSRA---------E 350
Cdd:TIGR00618 661 REHALSIR-VLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELethIEEYDREFNEIENASSSlgsdlaareD 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 351 AESWYQTKYEELQVTAGRHG--DDLRNTKQEIAEINRM--IQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKL 426
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARteAHFNNNEEVTAALQTGaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 119617035 427 EGLEDALQKAKQDLARLLKEyqelmnvKLALDVEIAtyRKLLEGEECR 474
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEE-------KSATLGEIT--HQLLKYEECS 858
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
244-475 |
2.14e-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: 40.39 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 244 DLVEDLKNKyedeiNKRTAAENEFVTLKK----DVDAAYMNKVEL----QAKADTLTDEINFLRALYDALSQmQTHISDT 315
Cdd:smart00787 25 ELLTTKRRH-----TPAPAISLNRISEEDcsldQYVVAGYCTVPLlelyQFSCKELKKYISEGRDLFKEIEE-ETLINNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 316 SVV---LSMDNNRNLDLDSIIAEVKaqyeeiaQRSRAEA-ESWY-------QTKYEELQVTAGRHGDDLRNTKQEIAEIN 384
Cdd:smart00787 99 PLFkeyFSASPDVKLLMDKQFQLVK-------TFARLEAkKMWYewrmkllEGLKEGLDENLEGLKEDYKLLMKELELLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 385 RMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL-------MNVKLAL 457
Cdd:smart00787 172 SIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELeskiedlTNKKSEL 251
|
250
....*....|....*...
gi 119617035 458 DVEIATYRKLLegEECRL 475
Cdd:smart00787 252 NTEIAEAEKKL--EQCRG 267
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
162-435 |
2.28e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 162 EEREQIKTLNNKFASFIDKVRFLE-------------QQNKVLDTkWTLLQEQGTKTVRQNLEPLFEQYiNNLRRQLDSI 228
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMEtatvelhlsnienKKNELLDI-IVEIKKHIHGEINKDLNKILEDF-KNKEKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 229 VGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEfvtLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDALsqm 308
Cdd:TIGR01612 771 INDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDF--- 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 309 qthISDTSVVLSMDNNRNLDLDSiiaeVKAQYEEIAQRSRAEAESWYQTKYEelqvtagrhgDDLRNTKQEIAEINRMIQ 388
Cdd:TIGR01612 845 ---LNKVDKFINFENNCKEKIDS----EHEQFAELTNKIKAEISDDKLNDYE----------KKFNDSKSLINEINKSIE 907
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 119617035 389 RLRSEIDHVKKQCASLQAAIADAEqrgemALKDAKNKLEGLEDALQK 435
Cdd:TIGR01612 908 EEYQNINTLKKVDEYIKICENTKE-----SIEKFHNKQNILKEILNK 949
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
371-484 |
2.56e-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: 40.82 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 371 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQ-------RGEMALKDA---KNKLEGLEDALQKAKQDL 440
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiekEIEQLEQEEeklKERLEELEEDLSSLEQEI 753
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 119617035 441 ARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVN 484
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-455 |
5.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 153 DPAIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGER 232
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED--RREEIEELEEEIEELRERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 233 GRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYM-----------NKVELQAKADTLTDEINFLRAL 301
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQPVEGSPHVETIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 302 YDALSQMQTHISDTSVVL--------------SMDNNRNlDLDSIIAEVKAQYEE---IAQRSRAEAESwYQTKYEELQV 364
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLeraedlveaedrieRLEERRE-DLEELIAERRETIEEkreRAEELRERAAE-LEAEAEEKRE 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 365 TAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKqCASLQAAIADAEQR-----------GEM---------ALKDAKN 424
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEierlrekrealAELnderrerlaEKRERKR 637
|
330 340 350
....*....|....*....|....*....|...
gi 119617035 425 KLEGL--EDALQKAKQDLARlLKEYQELMNVKL 455
Cdd:PRK02224 638 ELEAEfdEARIEEAREDKER-AEEYLEQVEEKL 669
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
223-450 |
5.66e-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: 39.67 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 223 RQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEI------- 295
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripe 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 296 --NFLRALYDALSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQR--SRAEAESWYQTKYEELQvtagrhgD 371
Cdd:TIGR02169 796 iqAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQikSIEKEIENLNGKKEELE-------E 868
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617035 372 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAeqrgEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 450
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL----EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
380-475 |
6.06e-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: 39.67 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 380 IAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEmALKDAKNKLEGLeDALQKAKQDLA--RLLKEYQELMNVKLAL 457
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE-RLRREREKAERY-QALLKEKREYEgyELLKEKEALERQKEAI 242
|
90
....*....|....*...
gi 119617035 458 DVEIATYRKLLEGEECRL 475
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI 260
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
333-444 |
6.30e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.09 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 333 IAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQ-EIAEINRMIQRLRSEIDHVKKQCASLQAAIADA 411
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
90 100 110
....*....|....*....|....*....|....*.
gi 119617035 412 EQRGEMALKDAKNKLEGLE---DALQKAKQDLARLL 444
Cdd:COG2268 326 EAEAEAIRAKGLAEAEGKRalaEAWNKLGDAAILLM 361
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
325-472 |
7.23e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 325 RNLDLDSIIAEVKAQYEEIAQRSRAEAESwyQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASL 404
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEEL--EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119617035 405 QAAIADAEQRG---EMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEE 472
Cdd:COG1196 301 EQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-300 |
7.65e-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: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 136 QEVTVNQSLLTPLNLQIDpaiQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLfE 215
Cdd:COG4913 269 ERLAELEYLRAALRLWFA---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL-E 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 216 QYINNLRRQLDSIVGERGRLDSELRNMQ----DLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTL 291
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
....*....
gi 119617035 292 TDEINFLRA 300
Cdd:COG4913 425 EAEIASLER 433
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
334-449 |
8.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 334 AEVKAQYEEIAQRSRAEAE-----SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAI 408
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKElrerrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 119617035 409 ADAEQRGE----MALKDAKNKLegLEDALQKAKQDLARLLKEYQE 449
Cdd:PRK12704 138 EEQLQELErisgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-466 |
9.53e-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: 37.98 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 329 LDSIIAEVKAQYEEIAQRSRAEAEswYQTKYEELQVTAGRHGDDLRNTKQEIAEI---------NRMIQRLRSEIDHVKK 399
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEA--AKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnNKEYEALQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119617035 400 QCASLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNvklALDVEIATYRK 466
Cdd:COG1579 104 RISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
233-445 |
9.95e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.12 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 233 GRLDSELRNMQDLVEDLKNKYEDE--INKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEIN-FLRALYDALSQMQ 309
Cdd:cd22656 87 GTIDSYYAEILELIDDLADATDDEelEEAKKTIKALLDDLLKEAK-------KYQDKAAKVVDKLTdFENQTEKDQTALE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617035 310 THISDTSVVLSMDNNRNL--DLDSIIAEVKAQYEEIAQRsraeaeswYQTKYEELQvtagrhgDDLRNTKQEIAeinrMI 387
Cdd:cd22656 160 TLEKALKDLLTDEGGAIArkEIKDLQKELEKLNEEYAAK--------LKAKIDELK-------ALIADDEAKLA----AA 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 119617035 388 QRLRSEIDHVKKQCASLQAAIAdaeqrgemalkDAKNKLEGLEDALQKAKQDLARLLK 445
Cdd:cd22656 221 LRLIADLTAADTDLDNLLALIG-----------PAIPALEKLQGAWQAIATDLDSLKD 267
|
|
| |
