|
Name |
Accession |
Description |
Interval |
E-value |
| Dzip-like_N |
pfam13815 |
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ... |
52-172 |
3.77e-47 |
|
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.
Pssm-ID: 433498 [Multi-domain] Cd Length: 118 Bit Score: 163.26 E-value: 3.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 52 FKFQPRHDSMDWRRISTLDVDRVARELDVATLQENIAGITFCNLDREVCsrcGQPVDPALLKVLRLAQLIIEYLLHCQDC 131
Cdd:pfam13815 1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEA---PHFVDPHFLKLFRLAQLTIEYLLHSQEC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767925954 132 LSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESR 172
Cdd:pfam13815 78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
149-496 |
4.10e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 149 QQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQTGTHsyhtchlcdktfmNATFLRGHIQRRHAGVAEGGKQKK 228
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK-------------KADEAKKAEEAKKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 229 QEQPVEEVlEELRaklkwtqgELEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKlfwDEFKN 308
Cdd:PTZ00121 1547 KADELKKA-EELK--------KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA---EEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 309 VAkqnstlEEKLRALQSHSVME--SKLGSLRDEESEEwLRQARELQALREKTEIQKTEWKRKVKElhEEHMAEKKELQEE 386
Cdd:PTZ00121 1615 AE------EAKIKAEELKKAEEekKKVEQLKKKEAEE-KKKAEELKKAEEENKIKAAEEAKKAEE--DKKKAEEAKKAEE 1685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 387 NQRLQAslsqDQKKAAAQSQCQISTLRAQLQEQARiiaSQEEMIQSLSLRKVEgIHKVPKAVDTEEDSPEEEMEDsQDEQ 466
Cdd:PTZ00121 1686 DEKKAA----EALKKEAEEAKKAEELKKKEAEEKK---KAEELKKAEEENKIK-AEEAKKEAEEDKKKAEEAKKD-EEEK 1756
|
330 340 350
....*....|....*....|....*....|
gi 767925954 467 HKVLAALRRNPTLLKHFRPILEDTLEEKLE 496
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-436 |
3.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 110 ALLKVLRLAQLIIEYLLHCQDCLSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMqtg 189
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 190 thsyhtcHLCDKtfmnATFLRGHIQRRHAGVAEGGKQKKQEqpvEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELI 269
Cdd:COG1196 306 -------RLEER----RRELEERLEELEEELAELEEELEEL---EEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 270 HQREIEAKKEFDKWKEQEwtklygeidklkklfwDEFKNVAKQNSTLEEKLRALQShsvmesklgslRDEESEEWLRQAR 349
Cdd:COG1196 372 AELAEAEEELEELAEELL----------------EALRAAAELAAQLEELEEAEEA-----------LLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 350 ELQALREKTEIQKTEWKRKVKELHEEHmaekKELQEENQRLQASLSQDQKKAAAQSQcQISTLRAQLQEQARIIASQEEM 429
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEE----AELEEEEEALLELLAELLEEAALLEA-ALAELLEELAEAAARLLLLLEA 499
|
....*..
gi 767925954 430 IQSLSLR 436
Cdd:COG1196 500 EADYEGF 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
226-433 |
6.28e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 226 QKKQEQPVEEVLEELRAKLKWTQGELEAQrEAERQRQLQEAELIHQREIEAKKEFDKwKEQEWTKLYGEIDKLKKLFWDE 305
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 306 FKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELH------EEHMAE 379
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAalraelEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767925954 380 KKELQEENQRLQASLSQ---DQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSL 433
Cdd:COG4942 176 LEALLAELEEERAALEAlkaERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
148-436 |
1.20e-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: 55.46 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 148 GQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQtgthsyhtchlcdktfmnATFLRGHIQRrhagvaEGGKQK 227
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD------------------ASRKIGEIEK------EIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 228 KQEQPVEEVLEELRAKLKWTQGELEAQRE--AERQRQLQEAEL-IHQREIEAKKEFDKWKEQEWTKLYGEIDKLKklfwd 304
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSelKELEARIEELEEdLHKLEEALNDLEARLSHSRIPEIQAELSKLE----- 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 305 efknvaKQNSTLEEKLRALqshsvmESKLGSL-RDEESEEWLRQarELQALREKTEIQKTEWKRKVKELHeehmAEKKEL 383
Cdd:TIGR02169 805 ------EEVSRIEARLREI------EQKLNRLtLEKEYLEKEIQ--ELQEQRIDLKEQIKSIEKEIENLN----GKKEEL 866
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767925954 384 QEENQRLQASLSQDQKKAAAQSQcQISTLRAQLQEQARIIASQEEMIQSLSLR 436
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKK-ERDELEAQLRELERKIEELEAQIEKKRKR 918
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-504 |
1.47e-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: 55.45 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 225 KQKKQEQPVEEVLEELRAKLKWTQGeLEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWD 304
Cdd:TIGR02168 207 RQAEKAERYKELKAELRELELALLV-LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 305 ---EFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKK 381
Cdd:TIGR02168 286 lqkELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 382 ELQEENQRLQAS--LSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVEgihKVPKAVDTEEDSPEEEM 459
Cdd:TIGR02168 366 ELEELESRLEELeeQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE---LLKKLEEAELKELQAEL 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767925954 460 EDSQDEQHKVLAALRRNPTLLKHFRPILE------DTLEEKLESMGIRKDA 504
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEeaeqalDAAERELAQLQARLDS 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-437 |
2.13e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 237 LEELRAKLKWTQGELEAQREAERQRQLQEAELIHQ-REIEAKKEFDKWKEQEWTKlygEIDKLKklfwdefknvAKQNST 315
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAElAELEAELEELRLELEELEL---ELEEAQ----------AEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 316 LEEKLRALQSHSVMESKLGSLRDEEsEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEENQRLQASLS 395
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERL-EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767925954 396 QDQKKAAAQSQC--QISTLRAQLQEQARIIASQEEMIQSLSLRK 437
Cdd:COG1196 373 ELAEAEEELEELaeELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-560 |
3.85e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 221 AEGGKQKKQEQpveEVLEELRAKLKWTQGELEAQREAERQRQLQE----AELIHQREIEAKKEFDKWKEQEWTKLYGEID 296
Cdd:PTZ00121 1446 ADEAKKKAEEA---KKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 297 KLKKLFWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKR--KVKELHE 374
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 375 EHMAEKKE--LQEENQRLQAslsqDQKKAAAQSQCQISTLRAQLQEQARiiasqeemiQSLSLRKVEGIHKVPKAVDTEE 452
Cdd:PTZ00121 1603 EEKKMKAEeaKKAEEAKIKA----EELKKAEEEKKKVEQLKKKEAEEKK---------KAEELKKAEEENKIKAAEEAKK 1669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 453 DSPEEEMED----SQDEQHKVLAALRRNPTLLKHFRPILEDTLEEKLESMGIRKDAKGISIQTlrhlESLLRVQREQK-- 526
Cdd:PTZ00121 1670 AEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA----EEAKKEAEEDKkk 1745
|
330 340 350
....*....|....*....|....*....|....*...
gi 767925954 527 ---ARKFSEFLSLRGKLVKEVTSRAKE-RQENGAVVSQ 560
Cdd:PTZ00121 1746 aeeAKKDEEEKKKIAHLKKEEEKKAEEiRKEKEAVIEE 1783
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
169-421 |
4.92e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 169 EESRRRRKMISTLQQLLMQTGTHS--YHTCHLCDKTFMNATFlrgHIQRRHAGVAEGGKQKKQEQPVEEVLEelraklkw 246
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTMTPEYTvrYNGQTMTENEFLNQLL---HIVQHQKAVSERQQQEKFEKMEQERLR-------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 247 tQGELEAQREAERQRQLQEAELIHQREIEakKEFDKWKEQEWTKLYGEiDKLKKLFWDEFKnvaKQNSTLEEKLRALQSH 326
Cdd:pfam17380 303 -QEKEEKAREVERRRKLEEAEKARQAEMD--RQAAIYAEQERMAMERE-RELERIRQEERK---RELERIRQEEIAMEIS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 327 SVMESKLGSLRDEESEEWLRQarELQALReKTEIQKTEWKRKVKELHEEHMAEKKELQEENQRLQASLSQDQ-------K 399
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQ--ELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERaremervR 452
|
250 260
....*....|....*....|..
gi 767925954 400 KAAAQSQCQISTLRAQLQEQAR 421
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKR 474
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-557 |
6.80e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 221 AEGGKQKKQEQpvEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREiEAKKEFDKWKEQEWTKLYGEIDKLKK 300
Cdd:PTZ00121 1331 ADAAKKKAEEA--KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 301 lfwDEFKNVAkqnstlEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTE-----IQKTEWKRKVKELHEE 375
Cdd:PTZ00121 1408 ---DELKKAA------AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeeaKKKAEEAKKADEAKKK 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 376 HMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLR-AQLQEQARIIASQEEMIQSLSLRKVEGIHK---VPKAVDTE 451
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKKadeLKKAEELK 1558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 452 EDSPEEEMEDSQDEQHKVLAALRRNPTLLKhfrpiledtLEEK--LESMGIRKDAKGISIQTLRHLES----LLRVQREQ 525
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKK---------AEEAriEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAE 1629
|
330 340 350
....*....|....*....|....*....|..
gi 767925954 526 KARKFSEFLSLRGKLVKEVTSRAKERQENGAV 557
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
218-529 |
8.55e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 218 AGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQR---------EAERQRQLQEAELIHQREIEAKKEFD-KWKEQE 287
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQElklkeqakkALEYYQLKEKLELEEEYLLYLDYLKLnEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 288 WTKLY----GEIDKLKKLFWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKT 363
Cdd:pfam02463 242 LQELLrdeqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 364 EWKRKVKEL-----------HEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQS 432
Cdd:pfam02463 322 EKKKAEKELkkekeeieeleKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 433 LSLRKVEGIHKVPKAVDTEEDSPEEEMEDSQDEQHKVLAALRRNPTLLKHFRpILEDTLEEKLESMGIRKDAKGISIQTL 512
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL-EKQELKLLKDELELKKSEDLLKETQLV 480
|
330
....*....|....*..
gi 767925954 513 RHLESLLRVQREQKARK 529
Cdd:pfam02463 481 KLQEQLELLLSRQKLEE 497
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
229-392 |
2.92e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 229 QEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEaeliHQREIEakkefdkwkeqewtKLYGEIDKLKklfwdefkn 308
Cdd:COG2433 374 RGLSIEEALEELIEKELPEEEPEAEREKEHEERELTE----EEEEIR--------------RLEEQVERLE--------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 309 vaKQNSTLEEKLRAL-QSHSVMESKLGSLRDEESEEwLRQARELQALREktEIQKTEwkrkvKELHEEHMaEKKELQEEN 387
Cdd:COG2433 427 --AEVEELEAELEEKdERIERLERELSEARSEERRE-IRKDREISRLDR--EIERLE-----RELEEERE-RIEELKRKL 495
|
....*
gi 767925954 388 QRLQA 392
Cdd:COG2433 496 ERLKE 500
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
339-446 |
2.93e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.98 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 339 EESEEWLRQ-ARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEE-NQRLQASlsqdqKKAAAQSqcqISTLRAQL 416
Cdd:PRK00409 526 EELERELEQkAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEA-----KKEADEI---IKELRQLQ 597
|
90 100 110
....*....|....*....|....*....|....
gi 767925954 417 QEQARIIASQE--EMIQSL--SLRKVEGIHKVPK 446
Cdd:PRK00409 598 KGGYASVKAHEliEARKRLnkANEKKEKKKKKQK 631
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
225-400 |
4.62e-06 |
|
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: 50.40 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 225 KQKKQEQpVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKKEFD-KWKEQEWTKLYGEIDKLKKLFW 303
Cdd:TIGR04523 358 NSEKQRE-LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 304 D---EFKNVAKQNSTLEEKLRalqshsvmesKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELhEEHMAEK 380
Cdd:TIGR04523 437 KnnsEIKDLTNQDSVKELIIK----------NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEK 505
|
170 180
....*....|....*....|...
gi 767925954 381 KELQEENQRL---QASLSQDQKK 400
Cdd:TIGR04523 506 KELEEKVKDLtkkISSLKEKIEK 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
225-550 |
5.15e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 225 KQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELI-HQREIEAK-KEFDKWKEQEwtKLYGEIDKLKKLF 302
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkEIEELEEKvKELKELKEKA--EEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 303 WDEFKNVAKQNSTLEEKLRALQSH----SVMESKLGSLRDEESE---------EWLRQARELQALREKTEIQKTEWK--- 366
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERikelEEKEERLEELKKKLKElekrleeleERHELYEEAKAKKEELERLKKRLTglt 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 367 -RKVKELHEEHMAEKKELQEENQRLQASLSQDQKKAA-----------AQSQCQISTLRAQLQEQARIIASQEEMIQSLS 434
Cdd:PRK03918 386 pEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKelkkaieelkkAKGKCPVCGRELTEEHRKELLEEYTAELKRIE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 435 LRKVEGIHKVPKAvdteedspeeemedsQDEQHKVLAALRRNPTLLKhFRPILED--TLEEKLESMGIRKdakgisiqtl 512
Cdd:PRK03918 466 KELKEIEEKERKL---------------RKELRELEKVLKKESELIK-LKELAEQlkELEEKLKKYNLEE---------- 519
|
330 340 350
....*....|....*....|....*....|....*...
gi 767925954 513 rhlesllrvqREQKARKFSEFLSLRGKLVKEVTSRAKE 550
Cdd:PRK03918 520 ----------LEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-429 |
8.55e-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: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 209 LRGHIQRRHAGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKK---EFDKWKE 285
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 286 QeWTKLYGEIDKLKKlfwdEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEW 365
Cdd:TIGR02168 797 E-LKALREALDELRA----ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 366 KRKVKEL------HEEHMAEKK-----------ELQEENQRLQASLSQDQKKaAAQSQCQISTLRAQLQEQARIIASQEE 428
Cdd:TIGR02168 872 ESELEALlnerasLEEALALLRseleelseelrELESKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLSEEYS 950
|
.
gi 767925954 429 M 429
Cdd:TIGR02168 951 L 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
237-476 |
1.38e-05 |
|
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: 48.90 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 237 LEELRAKLKWTQGELEA--QREAERQRQLQEAEL---IHQREI-EAKKEFDKwKEQEWTKLYGEIDKL---KKLFWDEFK 307
Cdd:TIGR02168 234 LEELREELEELQEELKEaeEELEELTAELQELEEkleELRLEVsELEEEIEE-LQKELYALANEISRLeqqKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 308 NVAKQNSTLEEKLRALQSHSV--------MESKLGSLR---DEESEEWLRQARELQALREKTEIQKTEW---KRKVKELH 373
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDelaeelaeLEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 374 EEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVEGIHKVPKAVDTEED 453
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260
....*....|....*....|....*...
gi 767925954 454 SPEEEMEDSQDEQH-----KVLAALRRN 476
Cdd:TIGR02168 473 AEQALDAAERELAQlqarlDSLERLQEN 500
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
226-421 |
2.71e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 226 QKKQEQPVEEVLEELRAKLKWTQGElEAQREAERQRQLQEAELihQREIEAKKEFdkwkEQEWTKLYGEIDKLKKLFWDE 305
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVE-RKRREQEEQRRLQQEQL--ERAEKMREEL----ELEQQRRFEEIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 306 fknvaKQNSTLEEKLRALQSHSVMESKlgslrDEESEEWLRQARELQALREKTEIQKTEW-KRKVKELHEEHMAEKKEL- 383
Cdd:pfam15709 400 -----RQRQEEEERKQRLQLQAAQERA-----RQQQEEFRRKLQELQRKKQQEEAERAEAeKQRQKELEMQLAEEQKRLm 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767925954 384 --------------QEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQAR 421
Cdd:pfam15709 470 emaeeerleyqrqkQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
227-556 |
3.95e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 227 KKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKKEFD-KWKEQEWTKLYG----EIDKLKKL 301
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRdeqeEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 302 FWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEwlrqarelqalREKTEIQKTEWKRKVKelHEEHMAEKK 381
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-----------LLKLERRKVDDEEKLK--ESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 382 ELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVEGIhkvpKAVDTEEDSPEEEMED 461
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL----SSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 462 SQDEQHKVLAALRRNPTLLKhfrpILEDTLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKARKFSEFLSLRGKLV 541
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLK----EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330
....*....|....*
gi 767925954 542 KEVTSRAKERQENGA 556
Cdd:pfam02463 479 LVKLQEQLELLLSRQ 493
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
242-429 |
4.19e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 242 AKLKWTQGELEAQREAERQrqLQEAElihqREIEAKKefdKWKEQEWTKlygEIDKLKKLFWDEFKNVAKQNSTLEEKLr 321
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRI--LEEAK----KEAEAIK---KEALLEAKE---EIHKLRNEFEKELRERRNELQKLEKRL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 322 aLQSHSVMESKLGSLRDEEseewlrqaRELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEenqrlQASLSQDQKKa 401
Cdd:PRK12704 92 -LQKEENLDRKLELLEKRE--------EELEKKEKELEQKQQELEKKEEELEELIEEQLQELER-----ISGLTAEEAK- 156
|
170 180
....*....|....*....|....*...
gi 767925954 402 aaqsQCQISTLRAQLQEQARIIASQEEM 429
Cdd:PRK12704 157 ----EILLEKVEEEARHEAAVLIKEIEE 180
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-439 |
4.68e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 221 AEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQL--------QEAELIHQREIEAK-KEFDKWKEqEWTKL 291
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeqlkeleEKLKKYNLEELEKKaEEYEKLKE-KLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 292 YGEIDKLKK-------------LFWDEFKNVAKQNSTLEEKLRALQSHSV--MESKLGSLRdEESEEWLR---QARELQA 353
Cdd:PRK03918 538 KGEIKSLKKelekleelkkklaELEKKLDELEEELAELLKELEELGFESVeeLEERLKELE-PFYNEYLElkdAEKELER 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 354 LREKTEIQKTEWKRKVKELhEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSl 433
Cdd:PRK03918 617 EEKELKKLEEELDKAFEEL-AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK- 694
|
....*.
gi 767925954 434 SLRKVE 439
Cdd:PRK03918 695 TLEKLK 700
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-544 |
5.31e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 233 VEEVLEELRAKLKWTQGELEAqREAERQRQLQEAELIhQREIEAKKEFDKWKEQEWTKLYGEIDKLkklfwdefknvAKQ 312
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGE-IEKEIEQLEQEEEKL-KERLEELEEDLSSLEQEIENVKSELKEL-----------EAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 313 NSTLEEKLRALQshsvmeSKLGSLRDEESEEWLRQ----ARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEENQ 388
Cdd:TIGR02169 767 IEELEEDLHKLE------EALNDLEARLSHSRIPEiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 389 RLQAslSQDQKKAAAQsqcQISTLRAQLQEQARIIASQEEMIQSLslrkvegihkvpkavdteedspeeemedsqDEQHK 468
Cdd:TIGR02169 841 QRID--LKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDL------------------------------ESRLG 885
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925954 469 VLAALRRNptllkhfrpiledtLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKARKFSEFLSLRGKLVKEV 544
Cdd:TIGR02169 886 DLKKERDE--------------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
248-605 |
6.57e-05 |
|
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: 46.50 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 248 QGELEA---QREAERQRQLQEAELIHQREIEAKKEFDKWKEqewtkLYGEIDKLKKLFWDEFKNVAKQNSTLEEKLRalq 324
Cdd:TIGR00618 151 QGEFAQflkAKSKEKKELLMNLFPLDQYTQLALMEFAKKKS-----LHGKAELLTLRSQLLTLCTPCMPDTYHERKQ--- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 325 shsVMESKLGSLRDE-----ESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEENQRLQASLSQDQK 399
Cdd:TIGR00618 223 ---VLEKELKHLREAlqqtqQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 400 KAAAQSQCQISTLRAQLQEQARIIASqeEMIQSLSLRKVEGIHKVPKAVDTEEDSPEEEMEDSQDEQHKVLAALRRNPTL 479
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAK--LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 480 LKHFRPILED--TLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKAR-KFSEFLSLRGKLVKEVTSRAKERQENGA 556
Cdd:TIGR00618 378 TQHIHTLQQQktTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767925954 557 VVSQPDGQPSVKS------QQSTLVTREAQPKTRTLQVALPSTPAEPPPPTRQSH 605
Cdd:TIGR00618 458 KIHLQESAQSLKEreqqlqTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
132-300 |
9.23e-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: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 132 LSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQTGTHSYHTCHL----CDKTFMNAT 207
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLspedFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 208 FLRGHIQRRHAGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELI--HQREIEAKKEFDKWKE 285
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLarLEKELAELAAELAELQ 219
|
170
....*....|....*
gi 767925954 286 QEWTKLYGEIDKLKK 300
Cdd:COG4942 220 QEAEELEALIARLEA 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
229-439 |
9.41e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 229 QEQPVEEVLEELRAKLKWTQGELEAQREaerqrQLQEAElihqreieakKEFDKWKEQewtklYGEIDklkklFWDEFKN 308
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRK-----ELEEAE----------AALEEFRQK-----NGLVD-----LSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 309 VAKQNSTLEEKLRALQS-HSVMESKLGSLRDEESEEW-----LRQARELQALREK---TEIQKTEWKRKVKELHEEHmae 379
Cdd:COG3206 217 LLQQLSELESQLAEARAeLAEAEARLAALRAQLGSGPdalpeLLQSPVIQQLRAQlaeLEAELAELSARYTPNHPDV--- 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 380 kKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVE 439
Cdd:COG3206 294 -IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
311-431 |
1.72e-04 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 44.58 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 311 KQNSTLEEKLRALQSHSVMESKLGSLRDEES--EEWLRQA-RELQALRekteiqktewkRKVKELHEEHMAEKKELQEEN 387
Cdd:pfam17060 134 KPQESPETPRRINRKYKSLELRVESMKDELEfkDETIMEKdRELTELT-----------STISKLKDKYDFLSREFEFYK 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767925954 388 QRlQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQ 431
Cdd:pfam17060 203 QH-HEHGGNNSIKTATKHEFIISELKRKLQEQNRLIRILQEQIQ 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
235-549 |
1.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 235 EVLEELRAKLKWTQGELEAQREAERQRQLQEAELIH-QREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFwDEFKNVAKQN 313
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvLREINEISSELPELREELEKLEKEVKELEELK-EEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 314 STLEEKLRALqshsvmESKLGSLRD--EESEEwlrqarELQALREKT-EIQKTEWK----RKVKELHEEHMAEKKELQEE 386
Cdd:PRK03918 248 ESLEGSKRKL------EEKIRELEEriEELKK------EIEELEEKVkELKELKEKaeeyIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 387 NQRLQAslsqdqkkaaaqsqcQISTLRAQLQEqariIASQEEMIQSLSLRKVEgihkvpkavdteedspeeemedsqdeq 466
Cdd:PRK03918 316 LSRLEE---------------EINGIEERIKE----LEEKEERLEELKKKLKE--------------------------- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 467 hkvlaaLRRNPTLLKHFRPILEDTLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKARKFSEFLSLRGKLVKEVTS 546
Cdd:PRK03918 350 ------LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
...
gi 767925954 547 RAK 549
Cdd:PRK03918 424 LKK 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
229-428 |
1.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 229 QEQPVEEVLEELRAKLKWTQGELEA-QREAER-QRQLQEAelihQREIEAKKEfdkwkeqEWTKLYGEIDKLKKlfwdef 306
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDAlQAELEElNEEYNEL----QAELEALQA-------EIDKLQAEIAEAEA------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 307 kNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEES-EEWLRQA--------------RELQALREKTEIQKTEWKRKVKE 371
Cdd:COG3883 80 -EIEERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLsalskiadadadllEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925954 372 LH------EEHMAEKKELQEENQRLQASLSQDQKKAAAqsqcQISTLRAQLQEQARIIASQEE 428
Cdd:COG3883 159 LEalkaelEAAKAELEAQQAEQEALLAQLSAEEAAAEA----QLAELEAELAAAEAAAAAAAA 217
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
273-424 |
2.02e-04 |
|
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: 44.24 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 273 EIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWDEFKNVAKQNSTLEEKLRALQ-SHSVMESKLGSLRDEESEEWLRQAREL 351
Cdd:smart00787 127 RLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRdRKDALEEELRQLKQLEDELEDCDPTEL 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925954 352 QALREKteiqktewkrkVKELHEEHMAEKKELQEENQRLQASLSQDQKKAAaqsqcQISTLRAQLQEQARIIA 424
Cdd:smart00787 207 DRAKEK-----------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-----KKSELNTEIAEAEKKLE 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
228-554 |
2.20e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 228 KQEQPVEEVLEELRAKLKWTQGELEAQREA-----ERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKlf 302
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDaddleERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 303 wdEFKNVAKQNSTLEEKLRALQS-HSVMESKLGSLRD--EESEEWLRQAREL----------QALREKTEIQKTEWKRKV 369
Cdd:PRK02224 399 --RFGDAPVDLGNAEDFLEELREeRDELREREAELEAtlRTARERVEEAEALleagkcpecgQPVEGSPHVETIEEDRER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 370 KELHEEHMAEKKELQEE-NQRLqaslsqDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRkVEGIHKVPKAV 448
Cdd:PRK02224 477 VEELEAELEDLEEEVEEvEERL------ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAEL 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 449 DTEEDSPEEEMEDSQDEQHKVLAALRRnptlLKHFRPILEDTLE--EKLESMGIRKDAKGISIQTLR----HLESLLRVQ 522
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAE----LNSKLAELKERIEslERIRTLLAAIADAEDEIERLRekreALAELNDER 625
|
330 340 350
....*....|....*....|....*....|..
gi 767925954 523 REQKARKFSEFLSLRGKLVKEVTSRAKERQEN 554
Cdd:PRK02224 626 RERLAEKRERKRELEAEFDEARIEEAREDKER 657
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
226-418 |
3.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 226 QKKQEQPVEEVLEELRAKLKWTQGEL---EAQREAERQRqLQEAELIhqreIEAKKEfdkwKEQEWTKLYGEIDKLKKLF 302
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIeryEEQREQARET-RDEADEV----LEEHEE----RREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 303 W------DEFKN-VAKQNSTLEEkLRALQSHSVMESKLGSL--------------RDEESEEWLRQAReLQALREKTEIq 361
Cdd:PRK02224 268 AetererEELAEeVRDLRERLEE-LEEERDDLLAEAGLDDAdaeavearreeledRDEELRDRLEECR-VAAQAHNEEA- 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767925954 362 ktEWKRKVKELHEEhmaEKKELQEENQRLQASLsQDQKKAAAQSQCQISTLRAQLQE 418
Cdd:PRK02224 345 --ESLREDADDLEE---RAEELREEAAELESEL-EEAREAVEDRREEIEELEEEIEE 395
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
225-440 |
3.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 225 KQKKQEQPVEEVLEELRAKLKWTQGELeaqREAERQRQLQEAEL--IHQREIEAKKEFDKWKEQEWTKLY-----GEIDK 297
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRI---RALEQELAALEAELaeLEKEIAELRAELEAQKEELAELLRalyrlGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 298 LKKLF-WDEFKNVAKQNSTLEEKLRALQShsvmesKLGSLRdEESEEWLRQARELQALREKTEIQKTEWKRKVKELheeh 376
Cdd:COG4942 122 LALLLsPEDFLDAVRRLQYLKYLAPARRE------QAEELR-ADLAELAALRAELEAERAELEALLAELEEERAAL---- 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925954 377 MAEKKELQEENQRLQASLSQDQKKAAAQSQcQISTLRAQLQEQARIIASQEEMIQSLSLRKVEG 440
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
226-389 |
3.43e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 226 QKKQEQPVEE---VLEELRAKlkwtqgELEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKlygEIDKLKKLF 302
Cdd:pfam17380 426 RAEQEEARQRevrRLEEERAR------EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK---RAEEQRRKI 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 303 WDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQK-----TEWKRKVKELHEEHM 377
Cdd:pfam17380 497 LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEqmrkaTEERSRLEAMERERE 576
|
170
....*....|..
gi 767925954 378 AEKKELQEENQR 389
Cdd:pfam17380 577 MMRQIVESEKAR 588
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-392 |
4.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 162 DELKGVREESRRRRKMISTLQQLLMQTGTHsyhtchlcDKTFMNATFLRghiQRRHAGVAEGGKQKKQEqpVEEVLEELR 241
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERY--------AAARERLAELE---YLRAALRLWFAQRRLEL--LEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 242 AKLKWTQGELEAQREAERQRQLQEAELIHQREiEAKkefdkwkeqewtklYGEIDKLKKLfwdefknVAKQNSTLEEKLR 321
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIR-GNG--------------GDRLEQLERE-------IERLERELEERER 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925954 322 ALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEiqktEWKRKVKELHEEHMAEKKELQEENQRLQA 392
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE----EELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-397 |
5.05e-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: 43.89 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 132 LSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQllmqtgthsyhtchlcdkTFMNATFLRG 211
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE------------------EAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 212 HIQRRHAgvaeggKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQrqlqeaeliHQREIEAKKEFDKWKEQEWTKL 291
Cdd:TIGR02168 828 SLERRIA------ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE---------LESELEALLNERASLEEALALL 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 292 YGEIDKLKklfwDEFKNVAKQNSTLEEKLRALQSH--------SVMESKLGSLRDEESEEWLRQARELQALREKTEIQKT 363
Cdd:TIGR02168 893 RSELEELS----EELRELESKRSELRRELEELREKlaqlelrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767925954 364 EWKRKVKELHEE-------HMAEKKELQEENQRLQASLSQD 397
Cdd:TIGR02168 969 EARRRLKRLENKikelgpvNLAAIEEYEELKERYDFLTAQK 1009
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-392 |
5.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 225 KQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFwD 304
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL-E 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 305 EFKNVAKQNSTLEEKLRALQSHsvMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELhEEHMAEKKELQ 384
Cdd:COG4717 157 ELRELEEELEELEAELAELQEE--LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL-EELEEELEQLE 233
|
....*...
gi 767925954 385 EENQRLQA 392
Cdd:COG4717 234 NELEAAAL 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
227-424 |
7.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 227 KKQEQPVEEVLEELRaklkwtqgELEAQREAERQRQLQEAELIHQREiEAKKEFDKwKEQEWTKLYGEIDKLKKL----- 301
Cdd:COG4717 60 KPQGRKPELNLKELK--------ELEEELKEAEEKEEEYAELQEELE-ELEEELEE-LEAELEELREELEKLEKLlqllp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 302 FWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKK 381
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767925954 382 ELQEENQRLQASLSQ-DQKKAAAQSQCQISTLRAQLQEQARIIA 424
Cdd:COG4717 210 ELEEELEEAQEELEElEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
117-439 |
1.01e-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: 42.65 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 117 LAQLIIEYLLHCQDCLSASvaqleaRLQTSLGQQQRGQQELGRQADELKGVREESRRR---RKMISTLQQLLMQTGTHSY 193
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIE------EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQhtlTQHIHTLQQQKTTLTQKLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 194 HTCHLCDK--------TFMNATF--LRGHIQRRHAG-VAEGGKQKKQEQPVEEVLEELRAKlKWTQGELeAQREAERQRQ 262
Cdd:TIGR00618 397 SLCKELDIlqreqatiDTRTSAFrdLQGQLAHAKKQqELQQRYAELCAAAITCTAQCEKLE-KIHLQES-AQSLKEREQQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 263 LQEAELIHQREIEAKKEFDKWKE-----------------QEWTKLY----------GEIDKLKKLfWDEFKNVAKQNST 315
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLelqeepcplcgscihpnPARQDIDnpgpltrrmqRGEQTYAQL-ETSEEDVYHQLTS 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 316 LEEKLRAL----QSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEehmaEKKELQEENQRLQ 391
Cdd:TIGR00618 554 ERKQRASLkeqmQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA----LLRKLQPEQDLQD 629
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767925954 392 ASLSQDQKkaaAQSQCQISTLRAQLQEQariIASQEEMIQSLSLRKVE 439
Cdd:TIGR00618 630 VRLHLQQC---SQELALKLTALHALQLT---LTQERVREHALSIRVLP 671
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-392 |
2.12e-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: 41.59 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 137 AQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQTGTHSYHtcHLCDKTFMNATFLRGHIQRR 216
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 217 HAGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQR----QLQEAELihQREIEAKKEFDKWKEQEWTKLY 292
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNGKKEEL--EEELEELEAALRDLESRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 293 GEIDKLKKlfwdEFKNVAKQNSTLEEKLRALQSH-SVMESKLGSLRDEESE------------EWLRQARELQALREKTE 359
Cdd:TIGR02169 889 KERDELEA----QLRELERKIEELEAQIEKKRKRlSELKAKLEALEEELSEiedpkgedeeipEEELSLEDVQAELQRVE 964
|
250 260 270
....*....|....*....|....*....|....*.
gi 767925954 360 --IQKTE-WKRKVKELHEEHMAEKKELQEENQRLQA 392
Cdd:TIGR02169 965 eeIRALEpVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
251-431 |
2.19e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 251 LEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWDEFKNVA---------KQNSTLEEKLR 321
Cdd:pfam13868 16 LAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRqeleeqieeREQKRQEEYEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 322 ALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEwKRKVKELheehmaEKKELQEENQRLQASLSQDQKKA 401
Cdd:pfam13868 96 KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEE-QAEWKEL------EKEEEREEDERILEYLKEKAERE 168
|
170 180 190
....*....|....*....|....*....|
gi 767925954 402 AAQSQCQISTLRAQLQEQARIIASQEEMIQ 431
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQD 198
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
137-433 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 137 AQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQqllmqtgtHSYHTCHLCDKTFMNATFLRGHIQRR 216
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAA--------HIKAVTQIEQQAQRIHTELQSKMRSR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 217 HAGVAEGGKQKKQEQPVEEVLEELRaklKWTQGELEAQREAERQRQLQE------AELIHQREIEAKKEFDKWKEQEWTK 290
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQ---TLHSQEIHIRDAHEVATSIREiscqqhTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 291 LYGEIDKL--KKLFWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRD--EESEEWLRQARELQALREKTEI--QKTE 364
Cdd:TIGR00618 401 ELDILQREqaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaqCEKLEKIHLQESAQSLKEREQQlqTKEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 365 WKRKVKELHEEHMAEKKELQEENQRLQASLSQDQKKA-------------------AAQSQCQISTLRAQLQEQARIIAS 425
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpgpltrrmqrgeqtYAQLETSEEDVYHQLTSERKQRAS 560
|
....*...
gi 767925954 426 QEEMIQSL 433
Cdd:TIGR00618 561 LKEQMQEI 568
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
229-437 |
2.91e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 229 QEQPVEEVLEELRAKLKwtqGELEAQREAERQRQLQEAELIHQREIEA-KKEFDKWKEQEWTKLYGEiDKLKKLFwdefK 307
Cdd:COG5185 272 ENAESSKRLNENANNLI---KQFENTKEKIAEYTKSIDIKKATESLEEqLAAAEAEQELEESKRETE-TGIQNLT----A 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 308 NVAKQNSTLEEKLRALQSHsvMESKLGSLRDEESEEWLRQAR-ELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEE 386
Cdd:COG5185 344 EIEQGQESLTENLEAIKEE--IENIVGEVELSKSSEELDSFKdTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQ 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925954 387 NQRLQ-------ASLSQDQKKA-AAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRK 437
Cdd:COG5185 422 IEELQrqieqatSSNEEVSKLLnELISELNKVMREADEESQSRLEEAYDEINRSVRSKK 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
227-429 |
3.18e-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: 41.21 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 227 KKQEQPVEEVLEELRAKLKWTQGE-LEAQREAERQRQLQEAEL--------IHQREIEA-KKEFDKwKEQEWTKLYGEID 296
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRRErEKAERYQALLKEKREYEGyellkekeALERQKEAiERQLAS-LEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 297 KLKKlfwdEFKNVAKQNSTLEEKLRALQS----------HSVmESKLGSLRD--EESEEWLRQA----RELQALREKTEI 360
Cdd:TIGR02169 262 ELEK----RLEEIEQLLEELNKKIKDLGEeeqlrvkekiGEL-EAEIASLERsiAEKERELEDAeerlAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925954 361 QK-------TEWKRKVKELheehMAEKKELQEENQRLQASLSQDQKKAAAqsqcqisTLRAQLQEQARIIASQEEM 429
Cdd:TIGR02169 337 EIeelereiEEERKRRDKL----TEEYAELKEELEDLRAELEEVDKEFAE-------TRDELKDYREKLEKLKREI 401
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
233-431 |
3.72e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 40.60 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 233 VEEVLEELRAKLKwtQGELEAQREAER--QRQLQEAELIHQREIEAKKEFDKWKEQ----------EWTKLYGEIDKLK- 299
Cdd:COG4477 260 LEEQLKEALELLE--ELDLDEAEEELEeiEEEIDELYDLLEKEVEAKKYVDKNQEEleeylehlkeQNRELKEEIDRVQq 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 300 ------------KLFWDEFKNVAKQN--------------STLEEKLRALQ--------SHSVMESKLGSLRDEESEewl 345
Cdd:COG4477 338 syrlnenelekvRNLEKQIEELEKRYdeiderieeekvaySELQEELEEIEeqleeieeEQEEFSEKLKSLRKDELE--- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 346 rqARElQALREKTEIQKTewKRKVKELH-----EEHMAEKKELQEENQRLQASLSQ------DQKKAAAQSQCQISTLRA 414
Cdd:COG4477 415 --ARE-KLDELKKKLREI--KRRLEKSNlpglpEEYLEMFEEASDEIEELSEELNEvplnmdEVNRLLEEAEEDIETLEE 489
|
250 260
....*....|....*....|
gi 767925954 415 QLQE---QARIIasqEEMIQ 431
Cdd:COG4477 490 KTEElveNATLT---ERLIQ 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
290-475 |
3.88e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 290 KLYGEIDKLKKLFwDEFKNVAKQNSTLEEKLRAL-------QSHSVMESKLGSLRDEESE-EWLRQARELQALREKTEIQ 361
Cdd:COG4913 222 DTFEAADALVEHF-DDLERAHEALEDAREQIELLepirelaERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 362 KTEWKRKVKELhEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKV--- 438
Cdd:COG4913 301 RAELARLEAEL-ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPasa 379
|
170 180 190
....*....|....*....|....*....|....*..
gi 767925954 439 EGIHKVPKAVDTEEDSPEEEMEDSQDEQHKVLAALRR 475
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
342-429 |
5.97e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.79 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 342 EEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQE-ENQRLQASLSQDQK----KAAAQSQCQISTLRAQL 416
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQlEKERLAAQEQKKQAeeaaKQAALKQKQAEEAAAKA 141
|
90
....*....|...
gi 767925954 417 QEQARIIASQEEM 429
Cdd:PRK09510 142 AAAAKAKAEAEAK 154
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
282-433 |
6.83e-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: 40.00 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 282 KWKEQEWTKLYGEIDKLKKLFWDEFKNVAKQNSTLEEKLRALQShsvMESKLGSLRDEeseewlrQARELQALREKT-EI 360
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN---TQTQLNQLKDE-------QNKIKKQLSEKQkEL 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925954 361 QKTewKRKVKELHEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSL 433
Cdd:TIGR04523 277 EQN--NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-419 |
7.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 253 AQREAERQRQLQEAELIHQREIEAKKEFDKWKEQeWTKLYGEIDKLKKLFWDE--FKNVAKQNSTLEEKLRALQSHSvme 330
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYSWDEidVASAEREIAELEAELERLDASS--- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 331 SKLGSLRdeeseewlRQARELQALREKTEIQKTEWKRKVKELHEEHmAEKKELQEENQRLQASLSQ----------DQKK 400
Cdd:COG4913 685 DDLAALE--------EQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDlarlelrallEERF 755
|
170
....*....|....*....
gi 767925954 401 AAAQSQCQISTLRAQLQEQ 419
Cdd:COG4913 756 AAALGDAVERELRENLEER 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
308-553 |
7.47e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 308 NVAKQNSTLEEKLRALqshsvmESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEEN 387
Cdd:COG1196 210 EKAERYRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 388 QRLQASLSQDQKKAAAQSQcQISTLRAQLQEQARIIASQEEMIQSLsLRKVEGIHKVPKAVDTEEDSPEEEMEDSQDEQH 467
Cdd:COG1196 284 EEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 468 KVLAALRRnptLLKHFRPILEDTLEEKLESMGIRKDAKGIsIQTLRHLESLLRVQREQKARKFSEFLSLRGKLVKEVTSR 547
Cdd:COG1196 362 EAEEALLE---AEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
....*.
gi 767925954 548 AKERQE 553
Cdd:COG1196 438 EEEEEA 443
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-403 |
8.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 221 AEGGKQKKQEQPVEEV--LEELRaKLKWTQGELEAQREAERQRQLQEaelihQREIEAKKEFDKWKEQEWTKLYGEIDKL 298
Cdd:PTZ00121 1202 AEAARKAEEERKAEEArkAEDAK-KAEAVKKAEEAKKDAEEAKKAEE-----ERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925954 299 KKLFWDEFKNvAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMA 378
Cdd:PTZ00121 1276 EARKADELKK-AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180
....*....|....*....|....*...
gi 767925954 379 EKKELQEENQRLQAS---LSQDQKKAAA 403
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAekkKEEAKKKADA 1382
|
|
| |
