|
Name |
Accession |
Description |
Interval |
E-value |
| Dzip-like_N |
pfam13815 |
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ... |
50-170 |
9.08e-50 |
|
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: 170.58 E-value: 9.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 50 FKFQPRRESIDWRRISAVDVDRVARELDVATLQENIAGVTFCNLDGEVCNHcrqPVDPVLLKVLRLAQLIIEYLLHCQDC 129
Cdd:pfam13815 1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568962132 130 LSASVAQLEARLQASLGQQQRGQQELGRQADELKGVREESR 170
Cdd:pfam13815 78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
142-505 |
5.91e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 142 QASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQllLQTSAHSYHTCHLCDKtfmNATFLRGHIQRRHAGMADV 221
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKK---KADEAKKAEEAKKADEAKK 1529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 222 GKQKQEQPLGEVLEELRAKLKWTQGelEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKERSKlygeIDKLKQLFWD 301
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR----IEEVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 302 EFKTVANQ-NSTLEEKLKALQSYSMTE--SHLGSLRDEESEERlKHAQEVQALQEKMEVQKTEWKRkmKALHEERAAERR 378
Cdd:PTZ00121 1604 EKKMKAEEaKKAEEAKIKAEELKKAEEekKKVEQLKKKEAEEK-KKAEELKKAEEENKIKAAEEAK--KAEEDKKKAEEA 1680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 379 QLQEENERlhvsLSQDQKKAAAQSQRHINALRAQLQEQARLIEsqeetiqtlSLRKVEEVQEMPKAVATEEDSSEEELEA 458
Cdd:PTZ00121 1681 KKAEEDEK----KAAEALKKEAEEAKKAEELKKKEAEEKKKAE---------ELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568962132 459 SLEERQEQRKVLAALRKN-----PTWLKQFRPILEDTLEEKLEGLGIKRDTK 505
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEeekkaEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-543 |
6.53e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 219 ADVGKQKQEQPLGEVLEELR-----AKLKWTQGELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKERSKLYGEID 293
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEekaeaAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 294 KLKQlfwDEFKTVANQNSTLEEKLKALQSYSMTEShlgSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALH-EE 372
Cdd:PTZ00121 1424 KKKA---EEKKKADEAKKKAEEAKKADEAKKKAEE---AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEaKK 1497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 373 RAAERRQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMPKAVATEEDSS 452
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 453 EEELEASLEERQEQRKVLAALRKNPTWLKQFRPILEDTLEEKL---------------EGLGIKRDTKGISAQTVRRLEP 517
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaeelkkaeeekkkvEQLKKKEAEEKKKAEELKKAEE 1657
|
330 340
....*....|....*....|....*.
gi 568962132 518 LLRTQREQIARSFREFPSLREKLNKE 543
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-496 |
7.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 230 LGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKERSKLYGEIDKLKQLFWDEF---KTV 306
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 307 ANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEERAAERRQLQEENER 386
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 387 LHVSLSQDQKKAAAQSQR-----HINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMPKAVATEEDSSEEELEASLE 461
Cdd:COG1196 378 EEELEELAEELLEALRAAaelaaQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270
....*....|....*....|....*....|....*
gi 568962132 462 ERQEQRKVLAALRKNPTWLKQFRPILEDTLEEKLE 496
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
136-418 |
1.20e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 136 QLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHSYHtchlcdktfmnatfLRGHIQRRH 215
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE--------------LLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 216 AGMADVGKQKQEqplgevLEELRAKLKWTQGELEAQRE---AERQRQVQELEMARQREMEAKKKFDEwKEKERSKLYGEI 292
Cdd:COG1196 302 QDIARLEERRRE------LEERLEELEEELAELEEELEeleEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 293 DKLKQLFWDEFKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEE 372
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568962132 373 RAAERRQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQAR 418
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-579 |
4.87e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 219 ADVGKQKQEQplGEVLEELRAKLKWTQGELEAQREAERQRQVQEL----EMARQREMEAKKKFDEWKEKERSKLYGEIDK 294
Cdd:PTZ00121 1446 ADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 295 LKQLFWDEFKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKR---KMKALHE 371
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieeVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 372 E---RAAERRQLQEENERlhvslsQDQKKAAAQSQRHINALRAQLQEQARLIEsqeetiqtlSLRKVEEVQEMPKA-VAT 447
Cdd:PTZ00121 1604 EkkmKAEEAKKAEEAKIK------AEELKKAEEEKKKVEQLKKKEAEEKKKAE---------ELKKAEEENKIKAAeEAK 1668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 448 EEDSSEEELEASLEERQEQRKVLAALRKnptwlkqfrpilEDTLEEKLEGLGIKRDTKGISAQTVRRLEPLLRTQREQIA 527
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKK------------EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568962132 528 RSFREFPSLREKLNKEVSSRVKQRWESTTQPDGQPPVKSQRVTLATREVRPK 579
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
224-570 |
1.24e-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: 55.51 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 224 QKQEQPLGEVLEELRAKlkwtQGELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKERSKLYGEIDKLKQlfwDEF 303
Cdd:pfam17380 286 ERQQQEKFEKMEQERLR----QEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQ---EER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 304 KtvaNQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKhaqevqalqekmevQKTEWKRKMKALHEERAAERRQLQEE 383
Cdd:pfam17380 359 K---RELERIRQEEIAMEISRMRELERLQMERQQKNERVR--------------QELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 384 NERLHvslsQDQKKAAAQSQRHINALRAQLQEQARLiESQEETIQTLSLRKVEEVQEMPKavATEEDSSEEELEASLEER 463
Cdd:pfam17380 422 MEQIR----AEQEEARQREVRRLEEERAREMERVRL-EEQERQQQVERLRQQEEERKRKK--LELEKEKRDRKRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 464 QEQRKVLAALRKNPTWLKQFRPILEDTLEEKLEGLGIKRDTKGISAQTVRRLEPLLRTQREQIARSFREFPSLREKLNKE 543
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
330 340 350
....*....|....*....|....*....|....*
gi 568962132 544 --------VSSRVKQRWESTTQPDGQPPVKSQRVT 570
Cdd:pfam17380 575 remmrqivESEKARAEYEATTPITTIKPIYRPRIS 609
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-444 |
1.81e-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: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 232 EVLEELRAKLKWTQG-ELEAQREAERQRQVQELEMARQREmEAKKKFDEWKEK-ERSKLY-GEIDKLKQLFWDEFKTVAN 308
Cdd:TIGR02168 217 ELKAELRELELALLVlRLEELREELEELQEELKEAEEELE-ELTAELQELEEKlEELRLEvSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 309 QNSTLEEKLKALQ---SYSMTESHLGSLRDEESEERLKHAQE-VQALQEKMEVQKTEWKRkMKALHEERAAERRQLQEEN 384
Cdd:TIGR02168 296 EISRLEQQKQILRerlANLERQLEELEAQLEELESKLDELAEeLAELEEKLEELKEELES-LEAELEELEAELEELESRL 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 385 ERLHVSLsQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMPKA 444
Cdd:TIGR02168 375 EELEEQL-ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-543 |
7.63e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 219 ADVGKQKQEQP-----LGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMARQREM-------------EAKKKFDEW 280
Cdd:PTZ00121 1304 ADEAKKKAEEAkkadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaeekaeaaekkkeEAKKKADAA 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 281 KEK-------ERSKLYGEIDKLKQlfwDEFKTVANQNSTLEE-KLKALQSYSMTESHLGSLRDEESEERLKHAQE---VQ 349
Cdd:PTZ00121 1384 KKKaeekkkaDEAKKKAEEDKKKA---DELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakkAE 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 350 ALQEKMEVQKTEWKRKMKALHEERAAERRQLQEENERlhvsLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQT 429
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK----KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 430 LSLRKVEEVQEMPKAVATEEDSSEEELEASLEERQEQRKVLAALRKnptwLKQFRPILEDTLEEKLEGLGIKRDTKG--- 506
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK----AEEAKKAEEARIEEVMKLYEEEKKMKAeea 1612
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568962132 507 -------ISAQTVRRLEPlLRTQREQIARSFREFPSLREKLNKE 543
Cdd:PTZ00121 1613 kkaeeakIKAEELKKAEE-EKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
224-431 |
9.41e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 224 QKQEQPLGEVLEELRAKLKWTQGELEAQRE---------AERQRQVQELEMARQrEMEAKKKFDEWKEKERsklygEIDK 294
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSelkeleariEELEEDLHKLEEALN-DLEARLSHSRIPEIQA-----ELSK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 295 LKqlfwdefKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEwKRKMKALHEERA 374
Cdd:TIGR02169 803 LE-------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEELEEELEELE 874
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 375 AERRQLQEEnerlHVSLSQDQKKAAAQ---SQRHINALRAQLQEQARLIESQEETIQTLS 431
Cdd:TIGR02169 875 AALRDLESR----LGDLKKERDELEAQlreLERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
223-444 |
2.26e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 223 KQKQEQPLGEVLEELRAKlkwtqgelEAQREAERQRQVQELemarqREMEAKKKFDEWKEKERSKLYGEIDKLKQLFWDE 302
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAE--------EAKKKAEDARKAEEA-----RKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 303 FKTVANQNSTLEEKLKALQSYSMTEshlgsLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKAL---HEERAAERRQ 379
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEE-----LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVkkaEEAKKDAEEA 1242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568962132 380 LQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMPKA 444
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-441 |
4.07e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 145 LGQQQRGQQELGRQA-DELKGVREESRRRRKMISTLQQLLLQTSahsyhtchlcdktfmnatflrghiQRRHAGMADVGK 223
Cdd:TIGR02168 682 LEEKIEELEEKIAELeKALAELRKELEELEEELEQLRKELEELS------------------------RQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 224 QKQEQplgEVLEELRAKLKWTQGELEAQREAERQRqvqeLEMARQREMEAKKKFDEWKEK------ERSKLYGEIDKLKQ 297
Cdd:TIGR02168 738 LEAEV---EQLEERIAQLSKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQieqlkeELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 298 LFWDEFKTVANQNSTLEEKLKALqsySMTESHLGSLrDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEERAAER 377
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRI---AATERRLEDL-EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568962132 378 RQLQEENERLHvSLSQDQKKAAaqsqRHINALRAQLQEQARLIESQEETIQTLSLRkVEEVQEM 441
Cdd:TIGR02168 887 EALALLRSELE-ELSEELRELE----SKRSELRRELEELREKLAQLELRLEGLEVR-IDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
135-375 |
8.88e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 135 AQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHSYHtcHLCDKTFMNATFLRGHIQRR 214
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 215 HAGMADV-GKQKQEQPLGEVLEELRAKLKWTQGELEAQREAERQRqvQELEMARQREMEA----KKKFDEWKEKERSKLY 289
Cdd:TIGR02169 811 EARLREIeQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE--IENLNGKKEELEEeleeLEAALRDLESRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 290 GEIDKLK-----------QLFWDEFK-------------TVANQNSTLEEKLKALQSYSMTESHLGSL--RDEESEERLK 343
Cdd:TIGR02169 889 KERDELEaqlrelerkieELEAQIEKkrkrlselkakleALEEELSEIEDPKGEDEEIPEEELSLEDVqaELQRVEEEIR 968
|
250 260 270
....*....|....*....|....*....|....*.
gi 568962132 344 HAQEVQ--ALQEKMEVQKT--EWKRKMKALHEERAA 375
Cdd:TIGR02169 969 ALEPVNmlAIQEYEEVLKRldELKEKRAKLEEERKA 1004
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
250-552 |
1.02e-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: 48.61 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 250 AQREAERQRQvQELEMARQREMEAKKKFDEwKEKERSKLYGEIDKLKQlfwdefktvanQNSTLEEKLKALQSysmtesh 329
Cdd:COG4942 17 AQADAAAEAE-AELEQLQQEIAELEKELAA-LKKEEKALLKQLAALER-----------RIAALARRIRALEQ------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 330 lgslRDEESEERLK-HAQEVQALQEKMEVQKTEWKRKMKALheeraaerrQLQEENERLHVSLSQDQkkaAAQSQRHINA 408
Cdd:COG4942 77 ----ELAALEAELAeLEKEIAELRAELEAQKEELAELLRAL---------YRLGRQPPLALLLSPED---FLDAVRRLQY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 409 LRAQLQEQARLIESQEETIQTLSlRKVEEVQEMPKAVATEEDSSEEELEASLEERQEQRKVLAALRKNptwlkqfrpilE 488
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELA-ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE-----------L 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568962132 489 DTLEEKLEGLgikrdtkgisAQTVRRLEPLLRTQREQIARSFRE-----FPSLREKLNKEVSSRVKQRW 552
Cdd:COG4942 209 AELAAELAEL----------QQEAEELEALIARLEAEAAAAAERtpaagFAALKGKLPWPVSGRVVRRF 267
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
219-433 |
1.59e-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: 47.84 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 219 ADVGKQKQEQplgevLEELRAKLKWTQGELEAQrEAERQRQVQELEMARQREMEAKKKFDEwKEKERSKLYGEIDKLKQL 298
Cdd:COG4942 19 ADAAAEAEAE-----LEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 299 FWDEFKTVANQNSTLEEKLKALQSYSMT---------ESHLGSLRDEE-----SEERLKHAQEVQALQEKMEVQKTEW-- 362
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQpplalllspEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELea 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568962132 363 -KRKMKALHEERAAERRQLQEENERLHVSLSQDQKKAAAQSQRhINALRAQLQEQARLIESQEETIQTLSLR 433
Cdd:COG4942 172 eRAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-LAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
250-543 |
2.10e-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: 48.14 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 250 AQREAERQRQVQELEMARQREMEAKKKFDEwKEKERSKLygEIDKLKQLFWDEFKTV---ANQNSTLEEKLKALQSYSMT 326
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDE-KRQQLERL--RREREKAERYQALLKEkreYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 327 ESHLGSLRdEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEEraaERRQLQEENERLHVSLSQ---------DQKK 397
Cdd:TIGR02169 243 ERQLASLE-EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE---EQLRVKEKIGELEAEIASlersiaekeRELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 398 AAAQSQRHINALRAQLQEQarlIESQEETIQTLSLRK---VEEVQEMPKAVATEEDSSEEELEASLEERQEQRKVLAAL- 473
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAE---IEELEREIEEERKRRdklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLe 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568962132 474 ----RKNPtwLKQFRPILEDTLEEKLEGLG-IKRDTKGISAQtVRRLEPLLRTQREQIARSFREFPSLREKLNKE 543
Cdd:TIGR02169 396 klkrEINE--LKRELDRLQEELQRLSEELAdLNAAIAGIEAK-INELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-472 |
2.52e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 233 VLEELRAKLKwtqgELEAQRE-AERQRQVQELEmaRQREMEAKKKFDEWKEKERSKLYGEIDKLKQlfwdEFKTVANQNS 311
Cdd:COG1196 194 ILGELERQLE----PLERQAEkAERYRELKEEL--KELEAELLLLKLRELEAELEELEAELEELEA----ELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 312 TLEEKLKALQSysmteshlgSLRDEESEERLKHAQEVQALQEKMEVQKTEwkrkmkalhEERAAERRQLQEENERLHVSL 391
Cdd:COG1196 264 ELEAELEELRL---------ELEELELELEEAQAEEYELLAELARLEQDI---------ARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 392 SQDQKKAAAQSQRhINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMpkavateedsseeeleaslEERQEQRKVLA 471
Cdd:COG1196 326 AELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-------------------AEAEEELEELA 385
|
.
gi 568962132 472 A 472
Cdd:COG1196 386 E 386
|
|
| PTZ00249 |
PTZ00249 |
variable surface protein Vir28; Provisional |
537-689 |
3.49e-05 |
|
variable surface protein Vir28; Provisional
Pssm-ID: 140276 [Multi-domain] Cd Length: 516 Bit Score: 47.33 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 537 REKlNKEVSSRVKQRWESTTQPdgqPPVKSQRVTLATREVRPKTRtltvalPSKPAEPSTPtlQGHSSHgPGLTQvsTP- 615
Cdd:PTZ00249 219 REE-QKAVTAHAHRRISGEARP---PKHISFSSPHAHGRPPVETR------PPNPVSVSSP--QAHGRH-PGETH--TPp 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 616 ---IPRPRVHG------PSSTPVS----PGSGLSTPPfSSEEEPEGDVVQRVSLQP-PKVLPRSAAKPEDNwgwSDSETS 681
Cdd:PTZ00249 284 lvtVPSSKAHDrnpvqtPTPTSVSgyssQAKGLEKQA-GGESERTSSVPSEQFPLPlPVLLPLGQSGPLES---SESEET 359
|
....*...
gi 568962132 682 EESAQPPG 689
Cdd:PTZ00249 360 DEYAGPKG 367
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-420 |
3.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 234 LEELRAKLKwtqgELEAQrEAERQRQVQELEMARQREMEAKKKFDEWKEKERsklygEIDKLKQLF--WDEFKTVANQNS 311
Cdd:COG4717 73 LKELEEELK----EAEEK-EEEYAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLplYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 312 TLEEKLKAL----QSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEERAAERRQLQEENERL 387
Cdd:COG4717 143 ELPERLEELeerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190
....*....|....*....|....*....|...
gi 568962132 388 HvslSQDQKKAAAQSQRHINALRAQLQEQARLI 420
Cdd:COG4717 223 E---ELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
111-441 |
4.05e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 111 KVLRLAQLIIEYL----LHCQDCLSASVAQLEARLQASLGQQQ-RGQQELGRQADELKGVREESRRRRKMISTLQQLL-- 183
Cdd:pfam15921 224 KILRELDTEISYLkgriFPVEDQLEALKSESQNKIELLLQQHQdRIEQLISEHEVEITGLTEKASSARSQANSIQSQLei 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 184 LQTSAHSYHTCHLCDKTFMNATflrghiqrrhagmadvgkqkqeqplgevLEELRAKLKwtqgelEAQREAERQrqVQEL 263
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLEST----------------------------VSQLRSELR------EAKRMYEDK--IEEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 264 E----MARQREMEAKKKFDEWKEKErsklyGEID-KLKQLFWDEFKTvANQNSTLEEKLKALQSYSMTESHLGSLRDEES 338
Cdd:pfam15921 348 EkqlvLANSELTEARTERDQFSQES-----GNLDdQLQKLLADLHKR-EKELSLEKEQNKRLWDRDTGNSITIDHLRREL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 339 EERLKHAQEVQALQEKMEVQ-KTEWKRKMKALH------EERAAERRQLQEENERLHVSLSQ--DQKKAAAQSQRHINAL 409
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEEltAKKMTLESSERTVSDL 501
|
330 340 350
....*....|....*....|....*....|....*
gi 568962132 410 RAQLQEQARLIESQEETIQTLSLR---KVEEVQEM 441
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRvdlKLQELQHL 536
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
223-492 |
4.40e-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: 47.36 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 223 KQKQEQPLGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMARQREmEAKKKFDEWKEK--ERSKLYGEIDKLKQLFW 300
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE-ELESKLDELAEElaELEEKLEELKEELESLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 301 DEFKTVANQNSTLEEKLKALQsysmteshlgslrdeesEERLKHAQEVQALQEKMEVQKTEWKRkMKALHEERAAERRQL 380
Cdd:TIGR02168 358 AELEELEAELEELESRLEELE-----------------EQLETLRSKVAQLELQIASLNNEIER-LEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 381 QEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMPKAVATEEDSSEEELEASL 460
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
250 260 270
....*....|....*....|....*....|..
gi 568962132 461 EERQEQRKVlAALRKNPTWLKQFRPILEDTLE 492
Cdd:TIGR02168 500 NLEGFSEGV-KALLKNQSGLSGILGVLSELIS 530
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
223-418 |
4.56e-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: 46.87 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 223 KQKQEQPLGEVLEELRAKLKWTQGELEAQREAERQRQVQElemarqrEMEAKKKFDEWKEKERSKLYGEIDKLKQLFWDE 302
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQE-------QLERAEKMREELELEQQRRFEEIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 303 fktvaNQNSTLEEKLKALQSYSMTE----------SHLGSLRDEESEERLKHAQEVQALQEKMEVQ-KTEWKRKMKALHE 371
Cdd:pfam15709 400 -----RQRQEEEERKQRLQLQAAQErarqqqeefrRKLQELQRKKQQEEAERAEAEKQRQKELEMQlAEEQKRLMEMAEE 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568962132 372 ERAAERRQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQAR 418
Cdd:pfam15709 475 ERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
135-445 |
4.78e-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: 47.27 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 135 AQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMistlqqllLQTSAHSYHTCHlcdktfmnatfLRGHIQRR 214
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKA--------APLAAHIKAVTQ-----------IEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 215 HAGMadvgkQKQEQPLGEVLEELRAKLKwTQGELEAQREAERQRQVQELEMARQREMEakKKFDEWKEKERSKLygeidk 294
Cdd:TIGR00618 313 HTEL-----QSKMRSRAKLLMKRAAHVK-QQSSIEEQRRLLQTLHSQEIHIRDAHEVA--TSIREISCQQHTLT------ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 295 lkqlfwDEFKTVANQNSTLEEKLKALQSYSMTEshlgslrDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEERA 374
Cdd:TIGR00618 379 ------QHIHTLQQQKTTLTQKLQSLCKELDIL-------QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568962132 375 AERRQLQEENERlhvslsqdqKKAAAQSQRHINALRAQLQeQARLIESQEETIQTLSLRKVEEVQEMPKAV 445
Cdd:TIGR00618 446 AITCTAQCEKLE---------KIHLQESAQSLKEREQQLQ-TKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
284-475 |
5.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 284 ERSKLYGEIDKLKQLFwDEFKTVANQNSTLEEKLKAL-------QSYSMTESHLGSLRDEESEERLKHAQ-EVQALQEKM 355
Cdd:COG4913 219 EEPDTFEAADALVEHF-DDLERAHEALEDAREQIELLepirelaERYAAARERLAELEYLRAALRLWFAQrRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 356 EVQKTEWKRKMKALhEERAAERRQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKV 435
Cdd:COG4913 298 EELRAELARLEAEL-ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568962132 436 EEVQEMPKAVATEEDSSEEELEASLEERQEQRKVLAALRK 475
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
147-440 |
9.33e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 147 QQQ----RGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHSYHTchlcdktfmnatflrghiQRRHAgmadvg 222
Cdd:pfam17380 288 QQQekfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE------------------QERMA------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 223 kQKQEQPLGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMARQR-------EMEAKKKFdEWKEKERSKlygeidKL 295
Cdd:pfam17380 344 -MERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQknervrqELEAARKV-KILEEERQR------KI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 296 KQLFWDEFKTVANQNSTLEEKLKALQsysmteshlgslrDEESEERLKHAQEVQALQEKME-VQKTEWKRKMKALHEERA 374
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQREVRRLE-------------EERAREMERVRLEEQERQQQVErLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568962132 375 AERRQLQEENERLHVSLS-QDQKKAAAQSQRHINALRAQLQEQARLI-ESQEETIQTLSLRKVEEVQE 440
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKEMEERQKAIyEEERRREAEEERRKQQEMEE 550
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
553-795 |
9.88e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.32 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 553 ESTTQPDGQPPVKSQRVTLATREVRPKTRTLTVALPSKPAEPSTPtlQGHSSHGPGLTQVStPIPRPRVHGPSSTPVSPG 632
Cdd:PHA03307 118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAV--ASDAASSRQAALPL-SSPEETARAPSSPPAEPP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 633 SGLSTPPFSSEEEPEGDVVQRVSLQPPKVLPRSAA--KPEDNWGWSDSETSEESAQPPGKGSGGLASSGTLVQSIVKNLE 710
Cdd:PHA03307 195 PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAAddAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 711 KQLETPAKKPSGGVNMFLRPNAALQR-------ASTPARKSQLSEDESDVEISSLEDLSQDLGQKGKPKPLSHSKLPEKF 783
Cdd:PHA03307 275 WNGPSSRPGPASSSSSPRERSPSPSPsspgsgpAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS 354
|
250
....*....|..
gi 568962132 784 DVSPWSSGSRPR 795
Cdd:PHA03307 355 RPPPPADPSSPR 366
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
139-494 |
1.15e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 139 ARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHSYHTCHLCDKTFMnatflrghIQRRHAGM 218
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK--------EQREKEEL 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 219 ADVGKQKQEQPLGEVLEELRAklkwtQGELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKERSKLYGEIDKLKQL 298
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDK-----INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 299 FWDEFKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEERAAERR 378
Cdd:pfam02463 788 VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEE 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 379 QLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMpkavaTEEDSSEEELEA 458
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEIL-----LKYEEEPEELLL 942
|
330 340 350
....*....|....*....|....*....|....*.
gi 568962132 459 sleerqEQRKVLAALRKNPTWLKQFRPILEDTLEEK 494
Cdd:pfam02463 943 ------EEADEKEKEENNKEEEEERNKRLLLAKEEL 972
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
160-422 |
1.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 160 DELKGVREESRRRRKMISTLQQLLLQTSAHsyhtchlcdktfmNATFLRGHIQRRHAGMADVGKQKQEQPLGE-VLEELR 238
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERY-------------AAARERLAELEYLRAALRLWFAQRRLELLEaELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 239 AKLKWTQGELEAQrEAERQRQVQELEMARQREMEAKkkfdewkekersklYGEIDKLKQLfwdefktVANQNSTLEEKLK 318
Cdd:COG4913 302 AELARLEAELERL-EARLDALREELDELEAQIRGNG--------------GDRLEQLERE-------IERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 319 ALQSYSMTESHLGsLRDEESEErlkhaqEVQALQEKMEVQKTEWKRKMKALHEERAAERRQLQEENERLHvslSQDQKKA 398
Cdd:COG4913 360 RRARLEALLAALG-LPLPASAE------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR---ELEAEIA 429
|
250 260
....*....|....*....|....*....
gi 568962132 399 AAQSQR-----HINALRAQLQEQARLIES 422
Cdd:COG4913 430 SLERRKsnipaRLLALRDALAEALGLDEA 458
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-475 |
1.73e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 247 ELEAQREAERQRQVQELEMARQ-REMEAKKKFDEWKEKERSKLYGEIDKLkqlfwDEFKTVANQNSTLEEKLKALQSYSM 325
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEDaRKAEAARKAEEERKAEEARKAEDAKKA-----EAVKKAEEAKKDAEEAKKAEEERNN 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 326 TESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALheERAAERRQLQEENERLHVSLSQDQ-KKAAAQSQR 404
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA--KKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKK 1329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568962132 405 HINALRAQLQEQARLIESqeetiqtlslRKVEEvqempKAVATEEDSSEEELEASLEERQEQRKVLAALRK 475
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEA----------AKAEA-----EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
224-432 |
2.52e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 224 QKQEQPLGEVLEELRAKLKWT------QGELEAQREAE------------RQRQVQELEMaRQREMEAKKKFDEWKEK-E 284
Cdd:pfam01576 291 EKQRRDLGEELEALKTELEDTldttaaQQELRSKREQEvtelkkaleeetRSHEAQLQEM-RQKHTQALEELTEQLEQaK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 285 RSKlyGEIDKLKQlfwdefkTVANQNSTLEEKLKALQSysmteshlgslRDEESEERLKHA-QEVQALQEKmeVQKTEWK 363
Cdd:pfam01576 370 RNK--ANLEKAKQ-------ALESENAELQAELRTLQQ-----------AKQDSEHKRKKLeGQLQELQAR--LSESERQ 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568962132 364 RkmkalhEERAAERRQLQEENERLHVSLSQDQKKaAAQSQRHINALRAQLQEQARLIesQEETIQTLSL 432
Cdd:pfam01576 428 R------AELAEKLSKLQSELESVSSLLNEAEGK-NIKLSKDVSSLESQLQDTQELL--QEETRQKLNL 487
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
128-439 |
2.95e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.90 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 128 DCLSASVAQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMIST----LQQLLLQTSAHSYHTCHL------- 196
Cdd:pfam19220 65 GKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDktaqAEALERQLAAETEQNRALeeenkal 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 197 ------CDKTFMNATFLRGHIQRRHAgMADVGKQKQEQPLGEVLEELrAKLKWTQGELEAQREAERQRqVQELEMARQRE 270
Cdd:pfam19220 145 reeaqaAEKALQRAEGELATARERLA-LLEQENRRLQALSEEQAAEL-AELTRRLAELETQLDATRAR-LRALEGQLAAE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 271 MEAKKKFDEWKEKERSKLYGEIdklkqlfwdefktvanqnSTLEEKLKALQSYSM-TESHLGSLRDE---------ESEE 340
Cdd:pfam19220 222 QAERERAEAQLEEAVEAHRAER------------------ASLRMKLEALTARAAaTEQLLAEARNQlrdrdeairAAER 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 341 RLKHAQ-EVQALQEKMEVQKTEWKRKMKALHE-ERAaeRRQLQEENERLHVSLSqDQKKAAAQSQRHINALRAQLQEQAR 418
Cdd:pfam19220 284 RLKEASiERDTLERRLAGLEADLERRTQQFQEmQRA--RAELEERAEMLTKALA-AKDAALERAEERIASLSDRIAELTK 360
|
330 340
....*....|....*....|.
gi 568962132 419 LIESQEETIQTLSLRKVEEVQ 439
Cdd:pfam19220 361 RFEVERAALEQANRRLKEELQ 381
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
235-437 |
3.46e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 235 EELRAKLKWTQGE----LEAQREAERQRQVQELEMAR--------QREMEAKKKFDEWKEKERSKLYGEIDKLKQLFWDE 302
Cdd:PTZ00121 1185 EEVRKAEELRKAEdarkAEAARKAEEERKAEEARKAEdakkaeavKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 303 FKTVANQNSTlEEKLKAlqsysmteSHLGSLRDEESEERLKHAQEVQALQEKMevQKTEWKRKMKALhEERAAERRQLQE 382
Cdd:PTZ00121 1265 FARRQAAIKA-EEARKA--------DELKKAEEKKKADEAKKAEEKKKADEAK--KKAEEAKKADEA-KKKAEEAKKKAD 1332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568962132 383 EnerlhvslsqdQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKVEE 437
Cdd:PTZ00121 1333 A-----------AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
336-425 |
3.48e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 336 EESEERLK-HAQEVQALQEKMEVQKTEWKRKMKALHEERAAERRQLQEE-NERLHVSlsqdqKKAAAQSQRHINALRAQL 413
Cdd:PRK00409 526 EELERELEqKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEA-----KKEADEIIKELRQLQKGG 600
|
90
....*....|..
gi 568962132 414 QEQARLIESQEE 425
Cdd:PRK00409 601 YASVKAHELIEA 612
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
130-297 |
3.68e-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: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 130 LSASVAQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHSYHTCHL----CDKTFMNAT 205
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLspedFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 206 FLRGHIQRRHAGMADVGKQKQE-QPLGEVLEELRAKLKWTQGELEAQR---EAERQRQVQELEMARQREMEAKKKFDEwK 281
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAElAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAELAAELAE-L 218
|
170
....*....|....*.
gi 568962132 282 EKERSKLYGEIDKLKQ 297
Cdd:COG4942 219 QQEAEELEALIARLEA 234
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
237-440 |
3.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 237 LRAKLKWTQGELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKERsklygEIDKLKQlfwdEFKTVANQNSTLEEK 316
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE-----ELEELEE----ELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 317 LKALqsysmteshlgslrdEESEERLKHAQEVQALQEKMEVQKTEWKRkmkalHEERAAERRQLQEENERLHVSLSQDQK 396
Cdd:COG4717 118 LEKL---------------EKLLQLLPLYQELEALEAELAELPERLEE-----LEERLEELRELEEELEELEAELAELQE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568962132 397 KAAAQSQRHINALRAQLQEQARLIESQEETIQTLSlRKVEEVQE 440
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELE-EELEEAQE 220
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-440 |
5.76e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 130 LSASVAQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQ---QLLLQTSAhsyhtchlcdKTFMNATF 206
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEE----------KLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 207 LRGHIQRRHAGMADVGKQKQE-----QPLGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMARQR----------EM 271
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKEleariEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRiearlreieqKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 272 EAKKKFDEWKEKERSKLYGEIDKLKQLFWDEFKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQAL 351
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 352 QEKMEVQKTEWKRKMKALhEERAAERRQLQEENERLHVSLSQDQKKAAAQSQrhINALRAQLQEQARLIESQEEtIQTLS 431
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRL-SELKAKLEALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRALEP-VNMLA 977
|
....*....
gi 568962132 432 LRKVEEVQE 440
Cdd:TIGR02169 978 IQEYEEVLK 986
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
224-433 |
6.11e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 224 QKQEQPLGEVLEELRAKLKWTQGELEaqrEAERQRqvqelEMARQREMEAKKKFDEWKEK--ERSKLYGEIDKL------ 295
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIE---RYEEQR-----EQARETRDEADEVLEEHEERreELETLEAEIEDLretiae 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 296 ----KQLFWDEFKTVANQNSTLEEKLKALQSysmtESHLGSLRDEESEERLKH-AQEVQALQEKMEVQKTEWKRKMKALh 370
Cdd:PRK02224 270 tereREELAEEVRDLRERLEELEEERDDLLA----EAGLDDADAEAVEARREElEDRDEELRDRLEECRVAAQAHNEEA- 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568962132 371 eERAAER-RQLQEENERLHvslsqdqkKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLR 433
Cdd:PRK02224 345 -ESLREDaDDLEERAEELR--------EEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
234-429 |
6.50e-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: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 234 LEELRAKLKWTQGELEAQREAERQRQVQELEMARQREmeakkkfdewkekersklygEIDKLKQLFWDE--FKTVANQNS 311
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERRE--------------------ALQRLAEYSWDEidVASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 312 TLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALheERAAERRQLQEENERLHVSL 391
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL--DELQDRLEAAEDLARLELRA 749
|
170 180 190
....*....|....*....|....*....|....*...
gi 568962132 392 SQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQT 429
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
342-441 |
9.92e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.59 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 342 LKHAQEVQALQEKMEVQKTEWKRKMKALHEERAAERRQLQEENerlhVSLSQDQKKAAaqsQRHINALRAQLQEQARliE 421
Cdd:COG2825 35 LQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEA----ATLSEEERQKK---ERELQKKQQELQRKQQ--E 105
|
90 100
....*....|....*....|
gi 568962132 422 SQEEtiqtLSLRKVEEVQEM 441
Cdd:COG2825 106 AQQD----LQKRQQELLQPI 121
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-549 |
1.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 230 LGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMAR-QREMEAKKKFDEWKEKERSKLYGEIDKLKQLFwDEFKTVAN 308
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvLREINEISSELPELREELEKLEKEVKELEELK-EEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 309 QNSTLEEKLKALqsysmtESHLGSLRD--EESEERLKHAQEVQALQEKMEVQKTEWkRKMKALHEERAAERRQLQEENER 386
Cdd:PRK03918 246 ELESLEGSKRKL------EEKIRELEEriEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 387 LhvslsqdqkkaaaqsQRHINALRAQLQEqarlIESQEETIQTLSLRKVEevqempkavateedsseeeleasleerqeq 466
Cdd:PRK03918 319 L---------------EEEINGIEERIKE----LEEKEERLEELKKKLKE------------------------------ 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 467 rkvlaaLRKNPTWLKQFRPILEDTLEEKLEGLGIKRDTKGISAQTVRRLEPLLRTQREQIARSFREFPSLREKLNKEVSS 546
Cdd:PRK03918 350 ------LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
...
gi 568962132 547 RVK 549
Cdd:PRK03918 424 LKK 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
130-475 |
1.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 130 LSASVAQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHSYhtchlcdktfmnatfLRG 209
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---------------LLL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 210 HIQRRHAGMADVGKQKQEQPLGEVLEELRAKLKWTQGELEAQREAE-----RQRQVQELEMARQREMEAKKKFDE----- 279
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalQNIVVEDDEVAAAAIEYLKAAKAGratfl 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 280 --WKEKERSKLYGEIDKLKQLFwdEFKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEV 357
Cdd:COG1196 578 plDKIRARAALAAALARGAIGA--AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 358 -----QKTEWKRKMKALHEERAAERRQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSL 432
Cdd:COG1196 656 gsaggSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568962132 433 RKVEEVQEMPKAvateEDSSEEELEASLEERQEQRKVLAALRK 475
Cdd:COG1196 736 ELLEELLEEEEL----LEEEALEELPEPPDLEELERELERLER 774
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
235-441 |
1.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 235 EELRAKLKWTQGELEAQREaerqrQVQELEMARQREMEAKKKFDewKEKERSKLYGEIDKLKQlfwdEFKTVANQNSTLE 314
Cdd:COG3206 171 EEARKALEFLEEQLPELRK-----ELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELES----QLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 315 EKLKALQSY-SMTESHLGSLRDEESEERLKhaQEVQALQEKMEVQKTEWKRK---MKALHEERAAERRQLQEENERLHVS 390
Cdd:COG3206 240 ARLAALRAQlGSGPDALPELLQSPVIQQLR--AQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568962132 391 LSQDQKKAAAQSQRhINALRAQLQEQARLIESQEETIQTLSlRKVEEVQEM 441
Cdd:COG3206 318 LEAELEALQAREAS-LQAQLAQLEARLAELPELEAELRRLE-REVEVAREL 366
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
130-418 |
1.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 130 LSASVAQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKM-----ISTLQQLLLQTSAHSYHTCHLCDKTFMNA 204
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 205 TFLRGHIQRRHAGMADVGKQKQEQPLGEVLEELRAKlKWTqgELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKE 284
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEE-ELE--ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 285 RSKLYGEIDKLKQLFWDEFKtvANQNSTLEEKLKALQSYSMTESHLGSLRDE-ESEERLKHAQEVQALQEKMEVQKTEWK 363
Cdd:COG4717 361 EELQLEELEQEIAALLAEAG--VEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568962132 364 RKMKALHEERAAERRQLQEENERLHvSLSQDQKKAAAQSQRHInaLRAQLQEQAR 418
Cdd:COG4717 439 EELEELEEELEELREELAELEAELE-QLEEDGELAELLQELEE--LKAELRELAE 490
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
336-428 |
1.48e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 336 EESEERLKHAQEVQaLQEKMEVQKTEWKRKMKALHEERAAERRQLQEENERLHVSLSQDQKKaaaqsqrhinALRAQLQE 415
Cdd:cd16269 210 AEQERKLLEEQQRE-LEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA----------LLEEGFKE 278
|
90
....*....|...
gi 568962132 416 QARLIESQEETIQ 428
Cdd:cd16269 279 QAELLQEEIRSLK 291
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
232-542 |
1.60e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 232 EVLEELRAKLKWTQGELEAQRE--AERQRQVQELEmARQREMEAKKKFD---EWKEKERSKLYGEIDKLKQLFWDEFKTV 306
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEkiRELEERIEELK-KEIEELEEKVKELkelKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 307 ANQNSTLEEKLKALQSYSMTESHLGSLRDEESE---------ERLKHAQEVQALQEKMEVQKTEWK----RKMKALHEER 373
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKElekrleeleERHELYEEAKAKKEELERLKKRLTgltpEKLEKELEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 374 AAERRQLQEENERLHVSLSQdQKKAAAQSQRHINALRAQLQE----QARLIESQEETIQTLSLRKVEEVQEMPKAVAtee 449
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGE-LKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIE--- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 450 dsseeelEASLEERQEQRKVLAALRKNPTWLKQfRPILED--TLEEKLEGLGIkrdtkgisaqtvrrlepllrtqrEQIA 527
Cdd:PRK03918 473 -------EKERKLRKELRELEKVLKKESELIKL-KELAEQlkELEEKLKKYNL-----------------------EELE 521
|
330
....*....|....*
gi 568962132 528 RSFREFPSLREKLNK 542
Cdd:PRK03918 522 KKAEEYEKLKEKLIK 536
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-437 |
1.62e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 137 LEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHsyhtchlcdktfmnatflrghiqrrha 216
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK--------------------------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 217 gMADVGKQKQEQpLGEVLEELRAKLKWTQG-----ELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKERSKLYGE 291
Cdd:TIGR02169 281 -IKDLGEEEQLR-VKEKIGELEAEIASLERsiaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 292 IDKLKQLFWDEFKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKmKALHE 371
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI-EAKIN 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568962132 372 ERAAERRQLQEENERLHVSLSQDQKKAAAQSQRHINaLRAQLQE-QARLIESQEETIQTLSLRKVEE 437
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD-LKEEYDRvEKELSKLQRELAEAEAQARASE 503
|
|
| Treacle |
pfam03546 |
Treacher Collins syndrome protein Treacle; |
617-754 |
1.75e-03 |
|
Treacher Collins syndrome protein Treacle;
Pssm-ID: 460967 [Multi-domain] Cd Length: 531 Bit Score: 41.60 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 617 PRPRVHGPSSTPVSPGSGLSTPPFSSEEEP--EGDVVQRVSLQPPKVlPRSAAKPEDNWGWSDSETSEESAQPpgkgsgg 694
Cdd:pfam03546 261 PQTKASPRKGTPITPTSAKVPPVRVGTPAPwkAGTVTSPACASSPAV-ARGAQRPEEDSSSSEESESEEETAP------- 332
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568962132 695 lASSGTLVQSIVKNLE-KQLETPAKKPSGGVNMFLRPN----AALQRASTPARKSQLSEDESDVE 754
Cdd:pfam03546 333 -AAAVGQAKSVGKGLQgKAASAPTKGPSGQGTAPVPPGktgpAVAQVKAEAQEDSESSEEESDSE 396
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
122-433 |
2.43e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 122 YLLHCQDcLSASVAQLEARLQASLGQQQRGQQELGRQA----DELKGVREE----SRRRRKMISTLQQLLL-------QT 186
Cdd:pfam15921 315 YMRQLSD-LESTVSQLRSELREAKRMYEDKIEELEKQLvlanSELTEARTErdqfSQESGNLDDQLQKLLAdlhkrekEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 187 SAHSYHTCHLCDKTFMNATFLrGHIQRRhagMADvgKQKQEQPLGEVLEELRAKlkwTQGELEAQREAerqrqVQELEMA 266
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGNSITI-DHLRRE---LDD--RNMEVQRLEALLKAMKSE---CQGQMERQMAA-----IQGKNES 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 267 RQREMEAKKKFDEWKEKERsKLYGEIDKLKQLFWDEFKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEE--RLK- 343
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLR-KVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQElqHLKn 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 344 ---HAQEVQALQEKMEVQKTEwKRKMKALHEERAAERRQLQEENERLHVSLSQDQkkaaAQSQRHINALRAQLQEQARLI 420
Cdd:pfam15921 539 egdHLRNVQTECEALKLQMAE-KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEK----AQLEKEINDRRLELQEFKILK 613
|
330
....*....|...
gi 568962132 421 ESQEETIQTLSLR 433
Cdd:pfam15921 614 DKKDAKIRELEAR 626
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
330-547 |
2.55e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 330 LGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEERAAERRQLQEENERL------HVSLSQDQKKAAAQSQ 403
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsrekHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 404 ---RHINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMPKAVATEEDSSEEELEASLEERQEQRKVLAALRKNPTWL 480
Cdd:pfam07888 112 elsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568962132 481 KQFRpILEDTLEEKLEGLGIKRDT-------KGISAQTVRRLEPL---LRTQREQIARSFREFPSLREKLNKEVSSR 547
Cdd:pfam07888 192 KEFQ-ELRNSLAQRDTQVLQLQDTittltqkLTTAHRKEAENEALleeLRSLQERLNASERKVEGLGEELSSMAAQR 267
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
544-799 |
2.86e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 544 VSSRVKQRWESTTQPDGQPPVKSQRVTLATREVRPKTRTLTVALPSKPA--EPSTPT--LQGHSSHGPGLTQVSTPIPRP 619
Cdd:PHA03247 2752 GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSpwDPADPPaaVLAPAAALPPAASPAGPLPPP 2831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 620 RVHGPSSTPVSPGSGLSTPPFSSEEEPEGDVVQRVSLQPPKVLP--------RSAAKPednwgwSDSETSEESAQPP-GK 690
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPaaparppvRRLARP------AVSRSTESFALPPdQP 2905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 691 GSGGLASSGTLVQSIVKNLEKQLETPAKKPSGgvnmflRPNAALQRASTPARKSQLSEDESDVEISSLEDLSQDLGQKGK 770
Cdd:PHA03247 2906 ERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP------RPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979
|
250 260
....*....|....*....|....*....
gi 568962132 771 PKPLSHSKLPEKfDVSPWSSGSRPRIPGW 799
Cdd:PHA03247 2980 PQPAPSREAPAS-STPPLTGHSLSRVSSW 3007
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
226-434 |
3.26e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 226 QEQPLGEVLEELRAKLKWTQGELEAQR----EAERQRQVQELEMARQrEMEAKKkfdEWKEKERSKLYGEIDKLKQLFWD 301
Cdd:pfam10174 149 QKQTLGARDESIKKLLEMLQSKGLPKKsgeeDWERTRRIAEAEMQLG-HLEVLL---DQKEKENIHLREELHRRNQLQPD 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 302 EFKTVANQN---------STLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQA----LQEKMEVQKTEWKRK--- 365
Cdd:pfam10174 225 PAKTKALQTviemkdtkiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKShskfMKNKIDQLKQELSKKese 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568962132 366 MKALHEERAAERRQLQEENERLHV---SLS-QDQKKAAAQSQrhINALRAQLQEQARLIESQEETIQTLSLRK 434
Cdd:pfam10174 305 LLALQTKLETLTNQNSDCKQHIEVlkeSLTaKEQRAAILQTE--VDALRLRLEEKESFLNKKTKQLQDLTEEK 375
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
239-425 |
3.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 239 AKLKWTQGELEAQREAERQRQvqelemarqremEAKKKFDEWKEKERSKLYGEIDKLKQLFWDEFKTVANQNSTLEEKLK 318
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE------------EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 319 alQSYSMTESHLGSLRDEEsEERLKHAQEVQALQEKMEVQKTEWKRKmkalheeraaerrqLQEENERL-HVS-LSQDQK 396
Cdd:PRK12704 93 --QKEENLDRKLELLEKRE-EELEKKEKELEQKQQELEKKEEELEEL--------------IEEQLQELeRISgLTAEEA 155
|
170 180 190
....*....|....*....|....*....|
gi 568962132 397 KaaaqsQRHINALRAQLQEQ-ARLIESQEE 425
Cdd:PRK12704 156 K-----EILLEKVEEEARHEaAVLIKEIEE 180
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-551 |
4.10e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 341 RLKHAQEVQALQEKMEVQK---TEWKRKMKAL---HEERAAERRQLQEENERLHVSLSQdQKKAAAQSQRHINALRAQLQ 414
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEekiAELEKALAELrkeLEELEEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 415 EQARLIESQEETIQTLsLRKVEEVQEMPKAVATEEDSSEEELEASLEERQEQRKVLAALRKNPTWLKQFRpileDTLEEK 494
Cdd:TIGR02168 751 QLSKELTELEAEIEEL-EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRER 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568962132 495 LEGLGIKRDTKGISAQTVRRLEPLLRTQREQIARSFREFPSLREKLNKEVSSRVKQR 551
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
578-790 |
4.48e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 578 PKTRTLTVALPSKPAEPSTPTLQGHSSHGPGLTQVSTPIPRPRVHGPSSTPVSPGSGLSTPPFSSEEEPegdVVQRVSLQ 657
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTES---FALPPDQP 2905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 658 PPKVLPRSAAKPEDNWGWSDSETSEESAQPPGKGSGGLASSGTlvqsivknlekqlETPAKKPSGGVNMflRPNAALQRA 737
Cdd:PHA03247 2906 ERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTD-------------PAGAGEPSGAVPQ--PWLGALVPG 2970
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568962132 738 STPARKSQLSEDESDVEISSledlsqdlgqkGKPKPLSHSKLPEkfdVSPWSS 790
Cdd:PHA03247 2971 RVAVPRFRVPQPAPSREAPA-----------SSTPPLTGHSLSR---VSSWAS 3009
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
234-536 |
4.79e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 234 LEELRAKL--KWTQGELEAQREAERQRQVQELEMArqremEAKKKFDEwKEKERSKLYGEIDKLKQLFwDEFKTvanqns 311
Cdd:pfam00038 23 LEQQNKLLetKISELRQKKGAEPSRLYSLYEKEIE-----DLRRQLDT-LTVERARLQLELDNLRLAA-EDFRQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 312 TLEEKLKALQSysmTESHLGSLR---DEESEERLKHAQEVQALQEKMEVQKTewkrkmkaLHEEraaERRQLQEENERLH 388
Cdd:pfam00038 90 KYEDELNLRTS---AENDLVGLRkdlDEATLARVDLEAKIESLKEELAFLKK--------NHEE---EVRELQAQVSDTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 389 VSLSQDqkkaAAQSQ---RHINALRAQLQEQARL-IESQEETIQTlslrKVEEVQEmpkAVATEEDSSEEELEASleerQ 464
Cdd:pfam00038 156 VNVEMD----AARKLdltSALAEIRAQYEEIAAKnREEAEEWYQS----KLEELQQ---AAARNGDALRSAKEEI----T 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568962132 465 EQRKVLAALRKNPTWLKQFRPILEDTLEEkLEGLGiKRDTKGISAQtVRRLEPLLRTQREQIARSFREFPSL 536
Cdd:pfam00038 221 ELRRTIQSLEIELQSLKKQKASLERQLAE-TEERY-ELQLADYQEL-ISELEAELQETRQEMARQLREYQEL 289
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
232-422 |
5.23e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 232 EVLEELRAKLKWTQGELEAQ--REAERQRQVQELEMARQREMEAKKkfDEWKEKeRSKLYGEIDKLKQlfwdEFKTVANQ 309
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDetLIASRQEERQETSAELNQLLRTLD--DQWKEK-RDELNGELSAADA----AVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 310 NSTLEEKLKA-----LQSYSMTESHLGSLRD--EESEERLK----HAQEVQALQEKMEVQ-KTEWKRKMKALHEERAAER 377
Cdd:pfam12128 324 LEALEDQHGAfldadIETAAADQEQLPSWQSelENLEERLKaltgKHQDVTAKYNRRRSKiKEQNNRDIAGIKDKLAKIR 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568962132 378 rqlqEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIES 422
Cdd:pfam12128 404 ----EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKS 444
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
223-446 |
6.01e-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: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 223 KQKQEQPLGEVLEELRAKLKWTQGELEAQREAER-----QRQVQELEMARQREMEAKKkfdEWKEKERSKLYGEIDKLKQ 297
Cdd:pfam13868 122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDErileyLKEKAEREEEREAEREEIE---EEKEREIARLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 298 lfwdefktvanqnsTLEEKLKALQSYSMtESHLGSLRDEESEERLKHAQEVQALQEKMEVQktewkrkMKALHEERAAER 377
Cdd:pfam13868 199 --------------EKAERDELRAKLYQ-EEQERKERQKEREEAEKKARQRQELQQAREEQ-------IELKERRLAEEA 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568962132 378 RQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMPKAVA 446
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
558-669 |
6.20e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.14 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 558 PDGQPPVKSQRVTLATREVRPKTRTLTVALPSKPAEPSTPTLQGHSSH--GPGLTQVSTPIPRPRVHGPSSTPVSPGSGL 635
Cdd:pfam03154 427 PPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPitPPSGPPTSTSSAMPGIQPPSSASVSSSGPV 506
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568962132 636 ------STPPFSSEEEPEGDVVQRVSLQPPkvlPRSAAKP 669
Cdd:pfam03154 507 paavscPLPPVQIKEEALDEAEEPESPPPP---PRSPSPE 543
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-415 |
6.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 135 AQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMIStLQQLLLQTSAHSYHTCHLCDKtfmnATFLRGHIQRR 214
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPER----LEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 215 HAgmadvgKQKQEQPLGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEK----------- 283
Cdd:COG4717 159 RE------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEleeleeeleql 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 284 ----ERSKLYGEIDKLKQLFWDE------FKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQE 353
Cdd:COG4717 233 enelEAAALEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568962132 354 KMEVQKTEWKRKMKALHEERAAERRQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQE 415
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
223-386 |
6.55e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 39.55 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 223 KQKQEQPLGEVLEELRAKLKWTQGELEA-QREAERQ-RQVQELEMARQREMEAKKKfdEWKEKERSKLYgEIDKLKQLFW 300
Cdd:pfam09728 47 KQDQLQKEKDQLQSELSKAILAKSKLEKlCRELQKQnKKLKEESKKLAKEEEEKRK--ELSEKFQSTLK-DIQDKMEEKS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 301 DEFKTVANQNSTLEEKLKAL-QSYSMTESHLGSL---RDEE---SEERLKHAQEVQ--ALQEKMEVQKTEWKRKMKALHE 371
Cdd:pfam09728 124 EKNNKLREENEELREKLKSLiEQYELRELHFEKLlktKELEvqlAEAKLQQATEEEekKAQEKEVAKARELKAQVQTLSE 203
|
170
....*....|....*
gi 568962132 372 ERAAERRQLQEENER 386
Cdd:pfam09728 204 TEKELREQLNLYVEK 218
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
253-443 |
7.49e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 39.84 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 253 EAERQRQVQELEMARQREMEAKKKFDEWKEKERSkLYGEIDKLKQlfwdefktvanQNSTLEEKL-KALQSYSMTESHLG 331
Cdd:pfam09726 401 EQDIKKLKAELQASRQTEQELRSQISSLTSLERS-LKSELGQLRQ-----------ENDLLQTKLhNAVSAKQKDKQTVQ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 332 SLrdeesEERLKHAQEVQALQEKMevqktewkrkmkaLHEERaaERRQLQEENERLHVSLSQDQKKAAAQS-QRHINALR 410
Cdd:pfam09726 469 QL-----EKRLKAEQEARASAEKQ-------------LAEEK--KRKKEEEATAARAVALAAASRGECTESlKQRKRELE 528
|
170 180 190
....*....|....*....|....*....|...
gi 568962132 411 AQLQEQARLIESQEETIQTLSLrkveEVQEMPK 443
Cdd:pfam09726 529 SEIKKLTHDIKLKEEQIRELEI----KVQELRK 557
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
71-473 |
7.66e-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: 39.95 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 71 RVARELDVATLQENIAGVTFCNLDGEVCNHCRQPvdpvllKVLRLAQLIIEYLLHCQDCLSASvaqleaRLQASLGQQQR 150
Cdd:TIGR00618 285 RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS------KMRSRAKLLMKRAAHVKQQSSIE------EQRRLLQTLHS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 151 GQQELGRQADELKGVREESRRR---RKMISTLQQLLLQTSAHSYHTCHLCDK-TFMNATFLRGHIQRRHAGMADVGKQKQ 226
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQhtlTQHIHTLQQQKTTLTQKLQSLCKELDIlQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 227 EQPLGEVLEELRA---------KLKWTQGELEAQREAERQRQVQELEMARQREMEAKK----KFDEWKEKER-------- 285
Cdd:TIGR00618 433 QELQQRYAELCAAaitctaqceKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAvvlaRLLELQEEPCplcgscih 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 286 ---------------SKLYGEIDKLKQLfWDEFKTVANQNSTLEEKLKAL----QSYSMTESHLGSLRDEESEERLKHAQ 346
Cdd:TIGR00618 513 pnparqdidnpgpltRRMQRGEQTYAQL-ETSEEDVYHQLTSERKQRASLkeqmQEIQQSFSILTQCDNRSKEDIPNLQN 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 347 EVQALQEKMEVQKTEWKRKMKALHEER------------AAERRQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQ 414
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLrklqpeqdlqdvRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP 671
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568962132 415 EQARLIESQEETIQTLSLRKVEEVQEMPKAVATEEDSSEEELEASLEERQEQRKVLAAL 473
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
138-443 |
8.36e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 39.25 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 138 EARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHSYHTCH-LCDKTFMNATFLRGHIQRRHA 216
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGReERRRADRREKQVIEKESRWRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 217 GMADVGKQKQEQPLGEVLEELRAK------LKWTQGELEAQREAERQRQVQELEMARQ----REMEAKKKFDEWKEKERS 286
Cdd:pfam15558 99 QAEDQENQRQEKLERARQEAEQRKqcqeqrLKEKEEELQALREQNSLQLQERLEEACHkrqlKEREEQKKVQENNLSELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 287 KLygeiDKLKQLFwdEFKTVANQ---NSTLEEKLKALQS--YSMTESHLGSLRDEESEERlKHAQEVQALQEKMEVQKTE 361
Cdd:pfam15558 179 NH----QARKVLV--DCQAKAEEllrRLSLEQSLQRSQEnyEQLVEERHRELREKAQKEE-EQFQRAKWRAEEKEEERQE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 362 WKRKMKALHEERAAERRQLQEENERLHVSLSQdQKKAAAQSQRHINALRAQLQEQARL------IESQEETIQTLSLRKV 435
Cdd:pfam15558 252 HKEALAELADRKIQQARQVAHKTVQDKAQRAR-ELNLEREKNHHILKLKVEKEEKCHRegikeaIKKKEQRSEQISREKE 330
|
....*...
gi 568962132 436 EEVQEMPK 443
Cdd:pfam15558 331 ATLEEARK 338
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
226-388 |
8.70e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 226 QEQPLGEVLEELRAKLKWTQGELEAQREAERQRqvQELEMARQREMEAKKKFdewkEKERSKLYGEIDKLKqlfwDEFKT 305
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSELEQRLRQQQRAERLL--AEFCKRLGKNLDDEDEL----EQLQEELEARLESLS----ESVSE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 306 VANQNSTLEEKLKALQS-YSMTESH----------LGSLRdEESEERLKHAQEV-QALQEKMEvqktewkrKMKALHEER 373
Cdd:PRK04863 577 ARERRMALRQQLEQLQArIQRLAARapawlaaqdaLARLR-EQSGEEFEDSQDVtEYMQQLLE--------RERELTVER 647
|
170
....*....|....*...
gi 568962132 374 ---AAERRQLQEENERLH 388
Cdd:PRK04863 648 delAARKQALDEEIERLS 665
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
209-401 |
9.12e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 209 GHIQRRHAGMADVGKQ--KQEQPLGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMARQREMEAKKKFDE-WKEKER 285
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQrkKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAaAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962132 286 SKLYGEidklkqlfwDEFKTVANQNSTLEEKLKALqsysmteshlgslrdEESEERLKHAQEVQALQEKMEVQKT--EWK 363
Cdd:PRK09510 145 AKAKAE---------AEAKRAAAAAKKAAAEAKKK---------------AEAEAAKKAAAEAKKKAEAEAAAKAaaEAK 200
|
170 180 190
....*....|....*....|....*....|....*....
gi 568962132 364 RKMKALHEERAAERRQLQEENE-RLHVSLSQDQKKAAAQ 401
Cdd:PRK09510 201 KKAEAEAKKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAE 239
|
|
| |
