|
Name |
Accession |
Description |
Interval |
E-value |
| Dzip-like_N |
pfam13815 |
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ... |
24-144 |
5.53e-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: 162.49 E-value: 5.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 24 FKFQPRHDSMDWRRISTLDVDRVARELDVATLQENIAGITFCNLDREVCsrcGQPVDPALLKVLRLAQLIIEYLLHCQDC 103
Cdd:pfam13815 1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEA---PHFVDPHFLKLFRLAQLTIEYLLHSQEC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 578807130 104 LSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESR 144
Cdd:pfam13815 78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
121-468 |
8.28e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 121 QQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQTGTHsyhtchlcdktfmNATFLRGHIQRRHAGVAEGGKQKK 200
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK-------------KADEAKKAEEAKKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 201 QEQPVEEVlEELRaklkwtqgELEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKlfwDEFKN 280
Cdd:PTZ00121 1547 KADELKKA-EELK--------KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA---EEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 281 VAkqnstlEEKLRALQSHSVME--SKLGSLRDEESEEwLRQARELQALREKTEIQKTEWKRKVKElhEEHMAEKKELQEE 358
Cdd:PTZ00121 1615 AE------EAKIKAEELKKAEEekKKVEQLKKKEAEE-KKKAEELKKAEEENKIKAAEEAKKAEE--DKKKAEEAKKAEE 1685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 359 NQRLQAslsqDQKKAAAQSQCQISTLRAQLQEQARiiaSQEEMIQSLSLRKVEgIHKVPKAVDTEEDSPEEEMEDsQDEQ 438
Cdd:PTZ00121 1686 DEKKAA----EALKKEAEEAKKAEELKKKEAEEKK---KAEELKKAEEENKIK-AEEAKKEAEEDKKKAEEAKKD-EEEK 1756
|
330 340 350
....*....|....*....|....*....|
gi 578807130 439 HKVLAALRRNPTLLKHFRPILEDTLEEKLE 468
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
82-408 |
4.83e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 82 ALLKVLRLAQLIIEYLLHCQDCLSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMqtg 161
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 162 thsyhtcHLCDKtfmnATFLRGHIQRRHAGVAEGGKQKKQEqpvEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELI 241
Cdd:COG1196 306 -------RLEER----RRELEERLEELEEELAELEEELEEL---EEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 242 HQREIEAKKEFDKWKEQEwtklygeidklkklfwDEFKNVAKQNSTLEEKLRALQShsvmesklgslRDEESEEWLRQAR 321
Cdd:COG1196 372 AELAEAEEELEELAEELL----------------EALRAAAELAAQLEELEEAEEA-----------LLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 322 ELQALREKTEIQKTEWKRKVKELHEEHmaekKELQEENQRLQASLSQDQKKAAAQSQcQISTLRAQLQEQARIIASQEEM 401
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEE----AELEEEEEALLELLAELLEEAALLEA-ALAELLEELAEAAARLLLLLEA 499
|
....*..
gi 578807130 402 IQSLSLR 408
Cdd:COG1196 500 EADYEGF 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
198-405 |
8.68e-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: 55.16 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 198 QKKQEQPVEEVLEELRAKLKWTQGELEAQrEAERQRQLQEAELIHQREIEAKKEFDKwKEQEWTKLYGEIDKLKKLFWDE 277
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 278 FKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELH------EEHMAE 351
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAalraelEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578807130 352 KKELQEENQRLQASLSQ---DQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSL 405
Cdd:COG4942 176 LEALLAELEEERAALEAlkaERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-476 |
1.88e-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: 55.06 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 197 KQKKQEQPVEEVLEELRAKLKWTQGeLEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWD 276
Cdd:TIGR02168 207 RQAEKAERYKELKAELRELELALLV-LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 277 ---EFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKK 353
Cdd:TIGR02168 286 lqkELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 354 ELQEENQRLQAS--LSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVEgihKVPKAVDTEEDSPEEEM 431
Cdd:TIGR02168 366 ELEELESRLEELeeQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE---LLKKLEEAELKELQAEL 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 578807130 432 EDSQDEQHKVLAALRRNPTLLKHFRPILE------DTLEEKLESMGIRKDA 476
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEeaeqalDAAERELAQLQARLDS 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
120-408 |
2.14e-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: 54.69 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 120 GQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQtgthsyhtchlcdktfmnATFLRGHIQRrhagvaEGGKQK 199
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD------------------ASRKIGEIEK------EIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 200 KQEQPVEEVLEELRAKLKWTQGELEAQRE--AERQRQLQEAEL-IHQREIEAKKEFDKWKEQEWTKLYGEIDKLKklfwd 276
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSelKELEARIEELEEdLHKLEEALNDLEARLSHSRIPEIQAELSKLE----- 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 277 efknvaKQNSTLEEKLRALqshsvmESKLGSL-RDEESEEWLRQarELQALREKTEIQKTEWKRKVKELHeehmAEKKEL 355
Cdd:TIGR02169 805 ------EEVSRIEARLREI------EQKLNRLtLEKEYLEKEIQ--ELQEQRIDLKEQIKSIEKEIENLN----GKKEEL 866
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 578807130 356 QEENQRLQASLSQDQKKAAAQSQcQISTLRAQLQEQARIIASQEEMIQSLSLR 408
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKK-ERDELEAQLRELERKIEELEAQIEKKRKR 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-409 |
2.92e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 209 LEELRAKLKWTQGELEAQREAERQRQLQEAELIHQ-REIEAKKEFDKWKEQEWTKlygEIDKLKklfwdefknvAKQNST 287
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAElAELEAELEELRLELEELEL---ELEEAQ----------AEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 288 LEEKLRALQSHSVMESKLGSLRDEEsEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEENQRLQASLS 367
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERL-EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578807130 368 QDQKKAAAQSQC--QISTLRAQLQEQARIIASQEEMIQSLSLRK 409
Cdd:COG1196 373 ELAEAEEELEELaeELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-532 |
7.74e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 193 AEGGKQKKQEQpveEVLEELRAKLKWTQGELEAQREAERQRQLQE----AELIHQREIEAKKEFDKWKEQEWTKLYGEID 268
Cdd:PTZ00121 1446 ADEAKKKAEEA---KKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 269 KLKKLFWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKR--KVKELHE 346
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 347 EHMAEKKE--LQEENQRLQAslsqDQKKAAAQSQCQISTLRAQLQEQARiiasqeemiQSLSLRKVEGIHKVPKAVDTEE 424
Cdd:PTZ00121 1603 EEKKMKAEeaKKAEEAKIKA----EELKKAEEEKKKVEQLKKKEAEEKK---------KAEELKKAEEENKIKAAEEAKK 1669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 425 DSPEEEMED----SQDEQHKVLAALRRNPTLLKHFRPILEDTLEEKLESMGIRKDAKGISIQTlrhlESLLRVQREQK-- 498
Cdd:PTZ00121 1670 AEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA----EEAKKEAEEDKkk 1745
|
330 340 350
....*....|....*....|....*....|....*...
gi 578807130 499 ---ARKFSEFLSLRGKLVKEVTSRAKE-RQENGAVVSQ 532
Cdd:PTZ00121 1746 aeeAKKDEEEKKKIAHLKKEEEKKAEEiRKEKEAVIEE 1783
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
141-393 |
1.15e-06 |
|
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: 52.05 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 141 EESRRRRKMISTLQQLLMQTGTHS--YHTCHLCDKTFMNATFlrgHIQRRHAGVAEGGKQKKQEQPVEEVLEelraklkw 218
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTMTPEYTvrYNGQTMTENEFLNQLL---HIVQHQKAVSERQQQEKFEKMEQERLR-------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 219 tQGELEAQREAERQRQLQEAELIHQREIEakKEFDKWKEQEWTKLYGEiDKLKKLFWDEFKnvaKQNSTLEEKLRALQSH 298
Cdd:pfam17380 303 -QEKEEKAREVERRRKLEEAEKARQAEMD--RQAAIYAEQERMAMERE-RELERIRQEERK---RELERIRQEEIAMEIS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 299 SVMESKLGSLRDEESEEWLRQarELQALReKTEIQKTEWKRKVKELHEEHMAEKKELQEENQRLQASLSQDQ-------K 371
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQ--ELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERaremervR 452
|
250 260
....*....|....*....|..
gi 578807130 372 KAAAQSQCQISTLRAQLQEQAR 393
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKR 474
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
190-501 |
1.36e-06 |
|
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: 52.28 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 190 AGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQR---------EAERQRQLQEAELIHQREIEAKKEFD-KWKEQE 259
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQElklkeqakkALEYYQLKEKLELEEEYLLYLDYLKLnEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 260 WTKLY----GEIDKLKKLFWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKT 335
Cdd:pfam02463 242 LQELLrdeqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 336 EWKRKVKEL-----------HEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQS 404
Cdd:pfam02463 322 EKKKAEKELkkekeeieeleKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 405 LSLRKVEGIHKVPKAVDTEEDSPEEEMEDSQDEQHKVLAALRRNPTLLKHFRpILEDTLEEKLESMGIRKDAKGISIQTL 484
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL-EKQELKLLKDELELKKSEDLLKETQLV 480
|
330
....*....|....*..
gi 578807130 485 RHLESLLRVQREQKARK 501
Cdd:pfam02463 481 KLQEQLELLLSRQKLEE 497
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-529 |
1.46e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 193 AEGGKQKKQEQpvEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREiEAKKEFDKWKEQEWTKLYGEIDKLKK 272
Cdd:PTZ00121 1331 ADAAKKKAEEA--KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 273 lfwDEFKNVAkqnstlEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTE-----IQKTEWKRKVKELHEE 347
Cdd:PTZ00121 1408 ---DELKKAA------AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeeaKKKAEEAKKADEAKKK 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 348 HMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLR-AQLQEQARIIASQEEMIQSLSLRKVEGIHK---VPKAVDTE 423
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKKadeLKKAEELK 1558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 424 EDSPEEEMEDSQDEQHKVLAALRRNPTLLKhfrpiledtLEEK--LESMGIRKDAKGISIQTLRHLES----LLRVQREQ 497
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKK---------AEEAriEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAE 1629
|
330 340 350
....*....|....*....|....*....|..
gi 578807130 498 KARKFSEFLSLRGKLVKEVTSRAKERQENGAV 529
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
311-418 |
3.20e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 311 EESEEWLRQ-ARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEE-NQRLQASlsqdqKKAAAQSqcqISTLRAQL 388
Cdd:PRK00409 526 EELERELEQkAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEA-----KKEADEI---IKELRQLQ 597
|
90 100 110
....*....|....*....|....*....|....
gi 578807130 389 QEQARIIASQE--EMIQSL--SLRKVEGIHKVPK 418
Cdd:PRK00409 598 KGGYASVKAHEliEARKRLnkANEKKEKKKKKQK 631
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
201-364 |
3.96e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.24 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 201 QEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEaeliHQREIEakkefdkwkeqewtKLYGEIDKLKklfwdefkn 280
Cdd:COG2433 374 RGLSIEEALEELIEKELPEEEPEAEREKEHEERELTE----EEEEIR--------------RLEEQVERLE--------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 281 vaKQNSTLEEKLRAL-QSHSVMESKLGSLRDEESEEwLRQARELQALREktEIQKTEwkrkvKELHEEHMaEKKELQEEN 359
Cdd:COG2433 427 --AEVEELEAELEEKdERIERLERELSEARSEERRE-IRKDREISRLDR--EIERLE-----RELEEERE-RIEELKRKL 495
|
....*
gi 578807130 360 QRLQA 364
Cdd:COG2433 496 ERLKE 500
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
197-372 |
9.59e-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: 49.25 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 197 KQKKQEQpVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKKEFD-KWKEQEWTKLYGEIDKLKKLFW 275
Cdd:TIGR04523 358 NSEKQRE-LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 276 D---EFKNVAKQNSTLEEKLRalqshsvmesKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELhEEHMAEK 352
Cdd:TIGR04523 437 KnnsEIKDLTNQDSVKELIIK----------NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEK 505
|
170 180
....*....|....*....|...
gi 578807130 353 KELQEENQRL---QASLSQDQKK 372
Cdd:TIGR04523 506 KELEEKVKDLtkkISSLKEKIEK 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-522 |
1.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 197 KQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELI-HQREIEAK-KEFDKWKEQEwtKLYGEIDKLKKLF 274
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkEIEELEEKvKELKELKEKA--EEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 275 WDEFKNVAKQNSTLEEKLRALQSH----SVMESKLGSLRDEESE---------EWLRQARELQALREKTEIQKTEWK--- 338
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERikelEEKEERLEELKKKLKElekrleeleERHELYEEAKAKKEELERLKKRLTglt 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 339 -RKVKELHEEHMAEKKELQEENQRLQASLSQDQKKAA-----------AQSQCQISTLRAQLQEQARIIASQEEMIQSLS 406
Cdd:PRK03918 386 pEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKelkkaieelkkAKGKCPVCGRELTEEHRKELLEEYTAELKRIE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 407 LRKVEGIHKVPKAvdteedspeeemedsQDEQHKVLAALRRNPTLLKhFRPILED--TLEEKLESMGIRKdakgisiqtl 484
Cdd:PRK03918 466 KELKEIEEKERKL---------------RKELRELEKVLKKESELIK-LKELAEQlkELEEKLKKYNLEE---------- 519
|
330 340 350
....*....|....*....|....*....|....*...
gi 578807130 485 rhlesllrvqREQKARKFSEFLSLRGKLVKEVTSRAKE 522
Cdd:PRK03918 520 ----------LEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-401 |
1.22e-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: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 181 LRGHIQRRHAGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKK---EFDKWKE 257
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 258 QeWTKLYGEIDKLKKlfwdEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEW 337
Cdd:TIGR02168 797 E-LKALREALDELRA----ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 338 KRKVKEL------HEEHMAEKK-----------ELQEENQRLQASLSQDQKKaAAQSQCQISTLRAQLQEQARIIASQEE 400
Cdd:TIGR02168 872 ESELEALlnerasLEEALALLRseleelseelrELESKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLSEEYS 950
|
.
gi 578807130 401 M 401
Cdd:TIGR02168 951 L 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-448 |
1.93e-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: 48.51 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 209 LEELRAKLKWTQGELEA--QREAERQRQLQEAEL---IHQREI-EAKKEFDKwKEQEWTKLYGEIDKL---KKLFWDEFK 279
Cdd:TIGR02168 234 LEELREELEELQEELKEaeEELEELTAELQELEEkleELRLEVsELEEEIEE-LQKELYALANEISRLeqqKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 280 NVAKQNSTLEEKLRALQSHSV--------MESKLGSLR---DEESEEWLRQARELQALREKTEIQKTEW---KRKVKELH 345
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDelaeelaeLEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 346 EEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVEGIHKVPKAVDTEED 425
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260
....*....|....*....|....*...
gi 578807130 426 SPEEEMEDSQDEQH-----KVLAALRRN 448
Cdd:TIGR02168 473 AEQALDAAERELAQlqarlDSLERLQEN 500
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
214-401 |
5.27e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 214 AKLKWTQGELEAQREAERQrqLQEAElihqREIEAKKefdKWKEQEWTKlygEIDKLKKLFWDEFKNVAKQNSTLEEKLr 293
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRI--LEEAK----KEAEAIK---KEALLEAKE---EIHKLRNEFEKELRERRNELQKLEKRL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 294 aLQSHSVMESKLGSLRDEEseewlrqaRELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEenqrlQASLSQDQKKa 373
Cdd:PRK12704 92 -LQKEENLDRKLELLEKRE--------EELEKKEKELEQKQQELEKKEEELEELIEEQLQELER-----ISGLTAEEAK- 156
|
170 180
....*....|....*....|....*...
gi 578807130 374 aaqsQCQISTLRAQLQEQARIIASQEEM 401
Cdd:PRK12704 157 ----EILLEKVEEEARHEAAVLIKEIEE 180
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
198-393 |
5.91e-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: 46.48 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 198 QKKQEQPVEEVLEELRAKLKWTQGElEAQREAERQRQLQEAELihQREIEAKKEFdkwkEQEWTKLYGEIDKLKKLFWDE 277
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVE-RKRREQEEQRRLQQEQL--ERAEKMREEL----ELEQQRRFEEIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 278 fknvaKQNSTLEEKLRALQSHSVMESKlgslrDEESEEWLRQARELQALREKTEIQKTEW-KRKVKELHEEHMAEKKEL- 355
Cdd:pfam15709 400 -----RQRQEEEERKQRLQLQAAQERA-----RQQQEEFRRKLQELQRKKQQEEAERAEAeKQRQKELEMQLAEEQKRLm 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578807130 356 --------------QEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQAR 393
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 ... |
199-532 |
6.51e-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: 46.50 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 199 KKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKKEFD-KWKEQEWTKLYG----EIDKLKKL 273
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRdeqeEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 274 FWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEwlrqarelqalREKTEIQKTEWKRKVKelHEEHMAEKK 353
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-----------LLKLERRKVDDEEKLK--ESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 354 ELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVEGIhkvpKAVDTEEDSPEEEMED 433
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL----SSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 434 SQDEQHKVLAALRRNPTLLKHFRPILEDTLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKARKFSEFLSLRGKLV 513
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330
....*....|....*....
gi 578807130 514 KEVTSRAKERQENGAVVSQ 532
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQK 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-411 |
8.25e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 193 AEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQL--------QEAELIHQREIEAK-KEFDKWKEqEWTKL 263
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeqlkeleEKLKKYNLEELEKKaEEYEKLKE-KLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 264 YGEIDKLKK-------------LFWDEFKNVAKQNSTLEEKLRALQSHSV--MESKLGSLRdEESEEWLR---QARELQA 325
Cdd:PRK03918 538 KGEIKSLKKelekleelkkklaELEKKLDELEEELAELLKELEELGFESVeeLEERLKELE-PFYNEYLElkdAEKELER 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 326 LREKTEIQKTEWKRKVKELhEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSl 405
Cdd:PRK03918 617 EEKELKKLEEELDKAFEEL-AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK- 694
|
....*.
gi 578807130 406 SLRKVE 411
Cdd:PRK03918 695 TLEKLK 700
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-411 |
8.62e-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: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 201 QEQPVEEVLEELRAKLKWTQGELEAQREaerqrQLQEAElihqreieakKEFDKWKEQewtklYGEIDklkklFWDEFKN 280
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRK-----ELEEAE----------AALEEFRQK-----NGLVD-----LSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 281 VAKQNSTLEEKLRALQS-HSVMESKLGSLRDEESEEW-----LRQARELQALREK---TEIQKTEWKRKVKELHEEHmae 351
Cdd:COG3206 217 LLQQLSELESQLAEARAeLAEAEARLAALRAQLGSGPdalpeLLQSPVIQQLRAQlaeLEAELAELSARYTPNHPDV--- 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 352 kKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVE 411
Cdd:COG3206 294 -IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-516 |
8.96e-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: 46.21 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 205 VEEVLEELRAKLKWTQGELEAqREAERQRQLQEAELIhQREIEAKKEFDKWKEQEWTKLYGEIDKLkklfwdefknvAKQ 284
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGE-IEKEIEQLEQEEEKL-KERLEELEEDLSSLEQEIENVKSELKEL-----------EAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 285 NSTLEEKLRALQshsvmeSKLGSLRDEESEEWLRQ----ARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEENQ 360
Cdd:TIGR02169 767 IEELEEDLHKLE------EALNDLEARLSHSRIPEiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 361 RLQAslSQDQKKAAAQsqcQISTLRAQLQEQARIIASQEEMIQSLslrkvegihkvpkavdteedspeeemedsqDEQHK 440
Cdd:TIGR02169 841 QRID--LKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDL------------------------------ESRLG 885
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578807130 441 VLAALRRNptllkhfrpiledtLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKARKFSEFLSLRGKLVKEV 516
Cdd:TIGR02169 886 DLKKERDE--------------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
220-577 |
9.61e-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: 46.12 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 220 QGELEA---QREAERQRQLQEAELIHQREIEAKKEFDKWKEqewtkLYGEIDKLKKLFWDEFKNVAKQNSTLEEKLRalq 296
Cdd:TIGR00618 151 QGEFAQflkAKSKEKKELLMNLFPLDQYTQLALMEFAKKKS-----LHGKAELLTLRSQLLTLCTPCMPDTYHERKQ--- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 297 shsVMESKLGSLRDE-----ESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEENQRLQASLSQDQK 371
Cdd:TIGR00618 223 ---VLEKELKHLREAlqqtqQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 372 KAAAQSQCQISTLRAQLQEQARIIASqeEMIQSLSLRKVEGIHKVPKAVDTEEDSPEEEMEDSQDEQHKVLAALRRNPTL 451
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAK--LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 452 LKHFRPILED--TLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKAR-KFSEFLSLRGKLVKEVTSRAKERQENGA 528
Cdd:TIGR00618 378 TQHIHTLQQQktTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578807130 529 VVSQPDGQPSVKS------QQSTLVTREAQPKTRTLQVALPSTPAEPPPPTRQSH 577
Cdd:TIGR00618 458 KIHLQESAQSLKEreqqlqTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-272 |
1.09e-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: 45.14 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 104 LSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQTGTHSYHTCHL----CDKTFMNAT 179
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLspedFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 180 FLRGHIQRRHAGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELI--HQREIEAKKEFDKWKE 257
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLarLEKELAELAAELAELQ 219
|
170
....*....|....*
gi 578807130 258 QEWTKLYGEIDKLKK 272
Cdd:COG4942 220 QEAEELEALIARLEA 234
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
283-403 |
2.11e-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: 44.20 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 283 KQNSTLEEKLRALQSHSVMESKLGSLRDEES--EEWLRQA-RELQALRekteiqktewkRKVKELHEEHMAEKKELQEEN 359
Cdd:pfam17060 134 KPQESPETPRRINRKYKSLELRVESMKDELEfkDETIMEKdRELTELT-----------STISKLKDKYDFLSREFEFYK 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578807130 360 QRlQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQ 403
Cdd:pfam17060 203 QH-HEHGGNNSIKTATKHEFIISELKRKLQEQNRLIRILQEQIQ 245
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
245-396 |
2.37e-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: 43.85 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 245 EIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWDEFKNVAKQNSTLEEKLRALQ-SHSVMESKLGSLRDEESEEWLRQAREL 323
Cdd:smart00787 127 RLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRdRKDALEEELRQLKQLEDELEDCDPTEL 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578807130 324 QALREKteiqktewkrkVKELHEEHMAEKKELQEENQRLQASLSQDQKKAAaqsqcQISTLRAQLQEQARIIA 396
Cdd:smart00787 207 DRAKEK-----------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-----KKSELNTEIAEAEKKLE 263
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-400 |
2.85e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 201 QEQPVEEVLEELRAKLKWTQGELEA-QREAER-QRQLQEAelihQREIEAKKEfdkwkeqEWTKLYGEIDKLKKlfwdef 278
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDAlQAELEElNEEYNEL----QAELEALQA-------EIDKLQAEIAEAEA------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 279 kNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEES-EEWLRQA--------------RELQALREKTEIQKTEWKRKVKE 343
Cdd:COG3883 80 -EIEERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLsalskiadadadllEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578807130 344 LH------EEHMAEKKELQEENQRLQASLSQDQKKAAAqsqcQISTLRAQLQEQARIIASQEE 400
Cdd:COG3883 159 LEalkaelEAAKAELEAQQAEQEALLAQLSAEEAAAEA----QLAELEAELAAAEAAAAAAAA 217
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
200-526 |
3.99e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 200 KQEQPVEEVLEELRAKLKWTQGELEAQREA-----ERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKlf 274
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDaddleERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 275 wdEFKNVAKQNSTLEEKLRALQS-HSVMESKLGSLRD--EESEEWLRQAREL----------QALREKTEIQKTEWKRKV 341
Cdd:PRK02224 399 --RFGDAPVDLGNAEDFLEELREeRDELREREAELEAtlRTARERVEEAEALleagkcpecgQPVEGSPHVETIEEDRER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 342 KELHEEHMAEKKELQEE-NQRLqaslsqDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRkVEGIHKVPKAV 420
Cdd:PRK02224 477 VEELEAELEDLEEEVEEvEERL------ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAEL 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 421 DTEEDSPEEEMEDSQDEQHKVLAALRRnptlLKHFRPILEDTLE--EKLESMGIRKDAKGISIQTLR----HLESLLRVQ 494
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAE----LNSKLAELKERIEslERIRTLLAAIADAEDEIERLRekreALAELNDER 625
|
330 340 350
....*....|....*....|....*....|..
gi 578807130 495 REQKARKFSEFLSLRGKLVKEVTSRAKERQEN 526
Cdd:PRK02224 626 RERLAEKRERKRELEAEFDEARIEEAREDKER 657
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
207-521 |
3.99e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 207 EVLEELRAKLKWTQGELEAQREAERQRQLQEAELIH-QREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFwDEFKNVAKQN 285
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvLREINEISSELPELREELEKLEKEVKELEELK-EEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 286 STLEEKLRALqshsvmESKLGSLRD--EESEEwlrqarELQALREKT-EIQKTEWK----RKVKELHEEHMAEKKELQEE 358
Cdd:PRK03918 248 ESLEGSKRKL------EEKIRELEEriEELKK------EIEELEEKVkELKELKEKaeeyIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 359 NQRLQAslsqdqkkaaaqsqcQISTLRAQLQEqariIASQEEMIQSLSLRKVEgihkvpkavdteedspeeemedsqdeq 438
Cdd:PRK03918 316 LSRLEE---------------EINGIEERIKE----LEEKEERLEELKKKLKE--------------------------- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 439 hkvlaaLRRNPTLLKHFRPILEDTLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKARKFSEFLSLRGKLVKEVTS 518
Cdd:PRK03918 350 ------LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
...
gi 578807130 519 RAK 521
Cdd:PRK03918 424 LKK 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-412 |
4.39e-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: 43.21 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 197 KQKKQEQPVEEVLEELRAKLKWTQGELeaqREAERQRQLQEAEL--IHQREIEAKKEFDKWKEQEWTKLY-----GEIDK 269
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRI---RALEQELAALEAELaeLEKEIAELRAELEAQKEELAELLRalyrlGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 270 LKKLF-WDEFKNVAKQNSTLEEKLRALQShsvmesKLGSLRdEESEEWLRQARELQALREKTEIQKTEWKRKVKELheeh 348
Cdd:COG4942 122 LALLLsPEDFLDAVRRLQYLKYLAPARRE------QAEELR-ADLAELAALRAELEAERAELEALLAELEEERAAL---- 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807130 349 MAEKKELQEENQRLQASLSQDQKKAAAQSQcQISTLRAQLQEQARIIASQEEMIQSLSLRKVEG 412
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
197-361 |
5.52e-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: 43.57 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 197 KQKKQEQPVEEVLEELRAKlkwtqgELEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKlygEIDKLKKLFWD 276
Cdd:pfam17380 428 EQEEARQREVRRLEEERAR------EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK---RAEEQRRKILE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 277 EFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQK-----TEWKRKVKELHEEHMAE 351
Cdd:pfam17380 499 KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEqmrkaTEERSRLEAMEREREMM 578
|
170
....*....|
gi 578807130 352 KKELQEENQR 361
Cdd:pfam17380 579 RQIVESEKAR 588
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
134-364 |
6.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 134 DELKGVREESRRRRKMISTLQQLLMQTGTHsyhtchlcDKTFMNATFLRghiQRRHAGVAEGGKQKKQEqpVEEVLEELR 213
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERY--------AAARERLAELE---YLRAALRLWFAQRRLEL--LEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 214 AKLKWTQGELEAQREAERQRQLQEAELIHQREiEAKkefdkwkeqewtklYGEIDKLKKLfwdefknVAKQNSTLEEKLR 293
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIR-GNG--------------GDRLEQLERE-------IERLERELEERER 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578807130 294 ALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEiqktEWKRKVKELHEEHMAEKKELQEENQRLQA 364
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE----EELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-390 |
6.22e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 198 QKKQEQPVEEVLEELRAKLKWTQGEL---EAQREAERQRqLQEAELIhqreIEAKKEfdkwKEQEWTKLYGEIDKLKKLF 274
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIeryEEQREQARET-RDEADEV----LEEHEE----RREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 275 W------DEFKN-VAKQNSTLEEkLRALQSHSVMESKLGSL--------------RDEESEEWLRQAReLQALREKTEIq 333
Cdd:PRK02224 268 AetererEELAEeVRDLRERLEE-LEEERDDLLAEAGLDDAdaeavearreeledRDEELRDRLEECR-VAAQAHNEEA- 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578807130 334 ktEWKRKVKELHEEhmaEKKELQEENQRLQASLsQDQKKAAAQSQCQISTLRAQLQE 390
Cdd:PRK02224 345 --ESLREDADDLEE---RAEELREEAAELESEL-EEAREAVEDRREEIEELEEEIEE 395
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-369 |
6.96e-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: 43.12 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 104 LSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQllmqtgthsyhtchlcdkTFMNATFLRG 183
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE------------------EAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 184 HIQRRHAgvaeggKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQrqlqeaeliHQREIEAKKEFDKWKEQEWTKL 263
Cdd:TIGR02168 828 SLERRIA------ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE---------LESELEALLNERASLEEALALL 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 264 YGEIDKLKklfwDEFKNVAKQNSTLEEKLRALQSH--------SVMESKLGSLRDEESEEWLRQARELQALREKTEIQKT 335
Cdd:TIGR02168 893 RSELEELS----EELRELESKRSELRRELEELREKlaqlelrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578807130 336 EWKRKVKELHEE-------HMAEKKELQEENQRLQASLSQD 369
Cdd:TIGR02168 969 EARRRLKRLENKikelgpvNLAAIEEYEELKERYDFLTAQK 1009
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-364 |
6.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 197 KQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFwD 276
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL-E 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 277 EFKNVAKQNSTLEEKLRALQSHsvMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELhEEHMAEKKELQ 356
Cdd:COG4717 157 ELRELEEELEELEAELAELQEE--LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL-EELEEELEQLE 233
|
....*...
gi 578807130 357 EENQRLQA 364
Cdd:COG4717 234 NELEAAAL 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-396 |
1.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 199 KKQEQPVEEVLEELRaklkwtqgELEAQREAERQRQLQEAELIHQREiEAKKEFDKwKEQEWTKLYGEIDKLKKL----- 273
Cdd:COG4717 60 KPQGRKPELNLKELK--------ELEEELKEAEEKEEEYAELQEELE-ELEEELEE-LEAELEELREELEKLEKLlqllp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 274 FWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKK 353
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578807130 354 ELQEENQRLQASLSQ-DQKKAAAQSQCQISTLRAQLQEQARIIA 396
Cdd:COG4717 210 ELEEELEEAQEELEElEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
89-411 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 89 LAQLIIEYLLHCQDCLSASvaqleaRLQTSLGQQQRGQQELGRQADELKGVREESRRR---RKMISTLQQLLMQTGTHSY 165
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIE------EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQhtlTQHIHTLQQQKTTLTQKLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 166 HTCHLCDK--------TFMNATF--LRGHIQRRHAG-VAEGGKQKKQEQPVEEVLEELRAKlKWTQGELeAQREAERQRQ 234
Cdd:TIGR00618 397 SLCKELDIlqreqatiDTRTSAFrdLQGQLAHAKKQqELQQRYAELCAAAITCTAQCEKLE-KIHLQES-AQSLKEREQQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 235 LQEAELIHQREIEAKKEFDKWKE-----------------QEWTKLY----------GEIDKLKKLfWDEFKNVAKQNST 287
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLelqeepcplcgscihpnPARQDIDnpgpltrrmqRGEQTYAQL-ETSEEDVYHQLTS 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 288 LEEKLRAL----QSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEehmaEKKELQEENQRLQ 363
Cdd:TIGR00618 554 ERKQRASLkeqmQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA----LLRKLQPEQDLQD 629
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 578807130 364 ASLSQDQKkaaAQSQCQISTLRAQLQEQariIASQEEMIQSLSLRKVE 411
Cdd:TIGR00618 630 VRLHLQQC---SQELALKLTALHALQLT---LTQERVREHALSIRVLP 671
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
109-364 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 109 AQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQTGTHSYHtcHLCDKTFMNATFLRGHIQRR 188
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 189 HAGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQR----QLQEAELihQREIEAKKEFDKWKEQEWTKLY 264
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNGKKEEL--EEELEELEAALRDLESRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 265 GEIDKLKKlfwdEFKNVAKQNSTLEEKLRALQSH-SVMESKLGSLRDEESE------------EWLRQARELQALREKTE 331
Cdd:TIGR02169 889 KERDELEA----QLRELERKIEELEAQIEKKRKRlSELKAKLEALEEELSEiedpkgedeeipEEELSLEDVQAELQRVE 964
|
250 260 270
....*....|....*....|....*....|....*.
gi 578807130 332 --IQKTE-WKRKVKELHEEHMAEKKELQEENQRLQA 364
Cdd:TIGR02169 965 eeIRALEpVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
109-405 |
3.95e-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: 40.72 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 109 AQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQqllmqtgtHSYHTCHLCDKTFMNATFLRGHIQRR 188
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAA--------HIKAVTQIEQQAQRIHTELQSKMRSR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 189 HAGVAEGGKQKKQEQPVEEVLEELRaklKWTQGELEAQREAERQRQLQE------AELIHQREIEAKKEFDKWKEQEWTK 262
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQ---TLHSQEIHIRDAHEVATSIREiscqqhTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 263 LYGEIDKL--KKLFWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRD--EESEEWLRQARELQALREKTEI--QKTE 336
Cdd:TIGR00618 401 ELDILQREqaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaqCEKLEKIHLQESAQSLKEREQQlqTKEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 337 WKRKVKELHEEHMAEKKELQEENQRLQASLSQDQKKA-------------------AAQSQCQISTLRAQLQEQARIIAS 397
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpgpltrrmqrgeqtYAQLETSEEDVYHQLTSERKQRAS 560
|
....*...
gi 578807130 398 QEEMIQSL 405
Cdd:TIGR00618 561 LKEQMQEI 568
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-447 |
4.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 262 KLYGEIDKLKKLFwDEFKNVAKQNSTLEEKLRAL-------QSHSVMESKLGSLRDEESE-EWLRQARELQALREKTEIQ 333
Cdd:COG4913 222 DTFEAADALVEHF-DDLERAHEALEDAREQIELLepirelaERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 334 KTEWKRKVKELhEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKV--- 410
Cdd:COG4913 301 RAELARLEAEL-ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPasa 379
|
170 180 190
....*....|....*....|....*....|....*..
gi 578807130 411 EGIHKVPKAVDTEEDSPEEEMEDSQDEQHKVLAALRR 447
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
201-409 |
4.99e-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: 40.33 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 201 QEQPVEEVLEELRAKLKwtqGELEAQREAERQRQLQEAELIHQREIEA-KKEFDKWKEQEWTKLYGEiDKLKKLFwdefK 279
Cdd:COG5185 272 ENAESSKRLNENANNLI---KQFENTKEKIAEYTKSIDIKKATESLEEqLAAAEAEQELEESKRETE-TGIQNLT----A 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 280 NVAKQNSTLEEKLRALQSHsvMESKLGSLRDEESEEWLRQAR-ELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEE 358
Cdd:COG5185 344 EIEQGQESLTENLEAIKEE--IENIVGEVELSKSSEELDSFKdTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQ 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578807130 359 NQRLQ-------ASLSQDQKKA-AAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRK 409
Cdd:COG5185 422 IEELQrqieqatSSNEEVSKLLnELISELNKVMREADEESQSRLEEAYDEINRSVRSKK 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-401 |
5.20e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 199 KKQEQPVEEVLEELRAKLKWTQGE-LEAQREAERQRQLQEAEL-IHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWD 276
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRRErEKAERYQALLKEKREYEGyELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 277 EFKNVAKQNSTLEE---KLRALQS----------HSVmESKLGSLRD--EESEEWLRQA----RELQALREKTEIQK--- 334
Cdd:TIGR02169 263 LEKRLEEIEQLLEElnkKIKDLGEeeqlrvkekiGEL-EAEIASLERsiAEKERELEDAeerlAKLEAEIDKLLAEIeel 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578807130 335 ----TEWKRKVKELheehMAEKKELQEENQRLQASLSQDQKKAAAqsqcqisTLRAQLQEQARIIASQEEM 401
Cdd:TIGR02169 342 ereiEEERKRRDKL----TEEYAELKEELEDLRAELEEVDKEFAE-------TRDELKDYREKLEKLKREI 401
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
223-403 |
5.77e-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: 39.52 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 223 LEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWDEFKNVA---------KQNSTLEEKLR 293
Cdd:pfam13868 16 LAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRqeleeqieeREQKRQEEYEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 294 ALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEwKRKVKELheehmaEKKELQEENQRLQASLSQDQKKA 373
Cdd:pfam13868 96 KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEE-QAEWKEL------EKEEEREEDERILEYLKEKAERE 168
|
170 180 190
....*....|....*....|....*....|
gi 578807130 374 AAQSQCQISTLRAQLQEQARIIASQEEMIQ 403
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQD 198
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
205-403 |
6.77e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 39.83 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 205 VEEVLEELRAKLKwtQGELEAQREAER--QRQLQEAELIHQREIEAKKEFDKWKEQ----------EWTKLYGEIDKLK- 271
Cdd:COG4477 260 LEEQLKEALELLE--ELDLDEAEEELEeiEEEIDELYDLLEKEVEAKKYVDKNQEEleeylehlkeQNRELKEEIDRVQq 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 272 ------------KLFWDEFKNVAKQN--------------STLEEKLRALQ--------SHSVMESKLGSLRDEESEewl 317
Cdd:COG4477 338 syrlnenelekvRNLEKQIEELEKRYdeiderieeekvaySELQEELEEIEeqleeieeEQEEFSEKLKSLRKDELE--- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 318 rqARElQALREKTEIQKTewKRKVKELH-----EEHMAEKKELQEENQRLQASLSQ------DQKKAAAQSQCQISTLRA 386
Cdd:COG4477 415 --ARE-KLDELKKKLREI--KRRLEKSNlpglpEEYLEMFEEASDEIEELSEELNEvplnmdEVNRLLEEAEEDIETLEE 489
|
250 260
....*....|....*....|
gi 578807130 387 QLQE---QARIIasqEEMIQ 403
Cdd:COG4477 490 KTEElveNATLT---ERLIQ 506
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
314-401 |
7.11e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 314 EEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQE-ENQRLQASLSQDQK----KAAAQSQCQISTLRAQL 388
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQlEKERLAAQEQKKQAeeaaKQAALKQKQAEEAAAKA 141
|
90
....*....|...
gi 578807130 389 QEQARIIASQEEM 401
Cdd:PRK09510 142 AAAAKAKAEAEAK 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
280-525 |
8.63e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 280 NVAKQNSTLEEKLRALqshsvmESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEEN 359
Cdd:COG1196 210 EKAERYRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 360 QRLQASLSQDQKKAAAQSQcQISTLRAQLQEQARIIASQEEMIQSLsLRKVEGIHKVPKAVDTEEDSPEEEMEDSQDEQH 439
Cdd:COG1196 284 EEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 440 KVLAALRRnptLLKHFRPILEDTLEEKLESMGIRKDAKGIsIQTLRHLESLLRVQREQKARKFSEFLSLRGKLVKEVTSR 519
Cdd:COG1196 362 EAEEALLE---AEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
....*.
gi 578807130 520 AKERQE 525
Cdd:COG1196 438 EEEEEA 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-391 |
9.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 225 AQREAERQRQLQEAELIHQREIEAKKEFDKWKEQeWTKLYGEIDKLKKLFWDE--FKNVAKQNSTLEEKLRALQSHSvme 302
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYSWDEidVASAEREIAELEAELERLDASS--- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 303 SKLGSLRdeeseewlRQARELQALREKTEIQKTEWKRKVKELHEEHmAEKKELQEENQRLQASLSQ----------DQKK 372
Cdd:COG4913 685 DDLAALE--------EQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDlarlelrallEERF 755
|
170
....*....|....*....
gi 578807130 373 AAAQSQCQISTLRAQLQEQ 391
Cdd:COG4913 756 AAALGDAVERELRENLEER 774
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
254-405 |
9.77e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807130 254 KWKEQEWTKLYGEIDKLKKLFWDEFKNVAKQNSTLEEKLRALQShsvMESKLGSLRDEeseewlrQARELQALREKT-EI 332
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN---TQTQLNQLKDE-------QNKIKKQLSEKQkEL 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578807130 333 QKTewKRKVKELHEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSL 405
Cdd:TIGR04523 277 EQN--NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
|
| |
