|
Name |
Accession |
Description |
Interval |
E-value |
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
431-745 |
4.06e-11 |
|
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: 66.69 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 431 IVDYQTKERERIRNDELDFL---RERQTVENMQAEVDEQRAKDEAwyqkqEMLRRAEETRREMLLQEEEKMAQQRHRlaa 507
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERER--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 508 vkrelEIKEIHLQDaARRRLLKLQQDQREMELRRLEdEIERkVQMRDQEiaataKDLEMRQlELEA--RKRLYEKDltaS 585
Cdd:pfam17380 349 -----ELERIRQEE-RKRELERIRQEEIAMEISRMR-ELER-LQMERQQ-----KNERVRQ-ELEAarKVKILEEE---R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 586 QEAIAKGIREDTDAHRRKMVLEEHVFQKLLENSqmgSRRTPRVMEDNLAKAEQA-CLNADWQIQTLHK--QNREDRQRSE 662
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEER---AREMERVRLEEQERQQQVeRLRQQEEERKRKKleLEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 663 GYYEVATLLRKDRQKEIQvldAMMEEEAKkwKEAREKEFhlqsEKKASALSDASRKWFLGQETNAALEHEEVPWLQKQHM 742
Cdd:pfam17380 489 AEEQRRKILEKELEERKQ---AMIEEERK--RKLLEKEM----EERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMR 559
|
...
gi 1958788591 743 DST 745
Cdd:pfam17380 560 KAT 562
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
438-624 |
1.57e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 438 ERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIKEI 517
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 518 HLQDAARRRLLKLQQDQRemELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYE--KDLTASQEAIAKGIRE 595
Cdd:COG1196 387 ELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEaaEEEAELEEEEEALLEL 464
|
170 180
....*....|....*....|....*....
gi 1958788591 596 DTDAHRRKMVLEEHVFQKLLENSQMGSRR 624
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
435-690 |
2.58e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEML---RRAEETRREMLLQEEEKMAQQRHRLAAVKRE 511
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 512 LEIKEIHLQDAARRRLLKLQQ--DQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAI 589
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEaeEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 590 AKGIREDTDAHRRKMVLEEhvfqkllensqmgsrrtprvmEDNLAKAEQACLNADWQIQTLHKQNREDRQRSEGYYEVAT 669
Cdd:COG1196 422 ELEELEEALAELEEEEEEE---------------------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260
....*....|....*....|.
gi 1958788591 670 LLRKDRQKEIQVLDAMMEEEA 690
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
434-712 |
5.56e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 434 YQT-KERERIRNDELdFLRERQTVENMQAEVDEQRAkdeawyQKQEMLRRAEETRREMllqeEEKMAQQRHRLAAVKREL 512
Cdd:COG1196 215 YRElKEELKELEAEL-LLLKLRELEAELEELEAELE------ELEAELEELEAELAEL----EAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 513 EIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAIAKG 592
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 593 IREDTDAHRRKMVLEEHVFQKLLEnsqmgsrrtprvmEDNLAKAEQACLNADWQIQTLHKQNREDRQRSEGyyEVATLLR 672
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEE-------------LLEALRAAAELAAQLEELEEAEEALLERLERLEE--ELEELEE 428
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958788591 673 KDRQKEIQVLDAMMEEEAKKWKEAREKEFHLQSEKKASAL 712
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
435-601 |
1.09e-08 |
|
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: 58.60 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEE----KMAQQRHRLAAVKR 510
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 511 ELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAI 589
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTI 600
|
170
....*....|..
gi 1958788591 590 AKGIREDTDAHR 601
Cdd:pfam17380 601 KPIYRPRISEYQ 612
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
435-700 |
1.74e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIRNDELdflreRQTVENMQAEVDEQRAKDEAwYQKQEMLRRAEETRR--EMLLQEEEKMAQQRHRLAAVKREL 512
Cdd:PTZ00121 1476 KKKAEEAKKADEA-----KKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKKAD 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 513 EIKEI-HLQDAARRRLL---KLQQDQREMELRRLED--EIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQ 586
Cdd:PTZ00121 1550 ELKKAeELKKAEEKKKAeeaKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 587 EAIAKGIREDTDAHRRKMVLEEhvFQKLLENSQMGSRRTPRVMEDNLAKAEQAclnadwqiqtlHKQNREDRQRSEgyye 666
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEE--LKKAEEENKIKAAEEAKKAEEDKKKAEEA-----------KKAEEDEKKAAE---- 1692
|
250 260 270
....*....|....*....|....*....|....
gi 1958788591 667 vATLLRKDRQKEIQVLDAMMEEEAKKWKEAREKE 700
Cdd:PTZ00121 1693 -ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
209-352 |
1.84e-08 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 54.95 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 209 LQKKYPIKSRRLLRVLQRTLSALAHWsaiFSDMPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN-- 283
Cdd:pfam00566 20 FPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdf 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 284 PPINI-LTMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSSHPSFLLM 352
Cdd:pfam00566 94 PGLKRdLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
433-718 |
5.32e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 433 DYQTKERER---IRNDELDFLRERQTVENMQAEvdEQRAKDEAwYQKQEMLRRAEETRR--EMLLQEEEKMAQQRHRLAA 507
Cdd:PTZ00121 1080 DFDAKEDNRadeATEEAFGKAEEAKKTETGKAE--EARKAEEA-KKKAEDARKAEEARKaeDARKAEEARKAEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 508 VKReleikeihLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQE----IAATAKDLEMRQLElEARKrlYEKDLT 583
Cdd:PTZ00121 1157 ARK--------AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERKAE-EARK--AEDAKK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 584 ASQEAIAKGIREDTDAHRRKmvleEHVFQKLLENSQMGSRRTPRVMEDNLAKAEQAcLNADWQIQTLHKQNREDRQRSEG 663
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKA----EEERNNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKAEEKKKADEAKKAEE 1300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788591 664 YYEVATLLRK-DRQKEIQVLDAMMEEEAKKWKEAREKEfhlQSEKKASALSDASRK 718
Cdd:PTZ00121 1301 KKKADEAKKKaEEAKKADEAKKKAEEAKKKADAAKKKA---EEAKKAAEAAKAEAE 1353
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
474-718 |
1.62e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 474 YQKQEMLRRAEETRREM-LLQEEEKMAQQRHRLAAVKRELEIKEIHLQDAARRRLlklQQDQREME---------LRRLE 543
Cdd:COG1196 218 LKEELKELEAELLLLKLrELEAELEELEAELEELEAELEELEAELAELEAELEEL---RLELEELEleleeaqaeEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 544 DEIERKVQMRDQEiAATAKDLEMRQLELEARKRLYEKDLTASQEAIAKGIREDTDAHRRKMVLEEHVFQKLLENSQMGSR 623
Cdd:COG1196 295 AELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 624 RTPRVME-DNLAKAEQACLNADWQIQTLHKQNREDRQRSEGYYEVATLLRKDRQKEIQVLDAMMEEEAKKWKEAREKEFH 702
Cdd:COG1196 374 LAEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250
....*....|....*.
gi 1958788591 703 LQSEKKASALSDASRK 718
Cdd:COG1196 454 LEEEEEALLELLAELL 469
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
437-718 |
3.67e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRR---------EMLLQEEEKMAQQrhrLAA 507
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKkaeeakkaaEAAKAEAEAAADE---AEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 508 VKRELEIKEIHLQDAARrrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKdltASQE 587
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKK----KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK---KKAD 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 588 AIAKGIREDTDAHRRKMVLEEhvfQKLLENSQMGSRRTpRVMEDNLAKAEQAclnadwqiqtlhKQNREDRQRSEGYYEV 667
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEE---AKKAEEAKKKAEEA-KKADEAKKKAEEA------------KKADEAKKKAEEAKKK 1498
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958788591 668 ATLLRKDRQKEIQVLDAMMEEEAKKWKEAREKEfhlqSEKKASALSDASRK 718
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE----EAKKADEAKKAEEK 1545
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
438-619 |
3.99e-07 |
|
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: 53.42 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 438 ERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETR-REMLLQEEEKMAQQRHRLAAVKRELEIKE 516
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRlRKQRLEEERQRQEEEERKQRLQLQAAQER 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 517 IHLQDAA-RRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLE-LEARKRLYEKDLTASQEAIAKGIR 594
Cdd:pfam15709 421 ARQQQEEfRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEErLEYQRQKQEAEEKARLEAEERRQK 500
|
170 180
....*....|....*....|....*
gi 1958788591 595 EDTDAhrrKMVLEEHVFQKLLENSQ 619
Cdd:pfam15709 501 EEEAA---RLALEEAMKQAQEQARQ 522
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
429-586 |
1.14e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 429 KFIVDYQTKERERIRNDELdfLRERQTVENMQAEVDEQRAKDEAWYQKQE-MLRRAEET---RREMLLQEEEKMAQQRHR 504
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEkRLLQKEENldrKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 505 LAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEMrQLELEARKRL 577
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIEE-EAKEEADKKA 190
|
....*....
gi 1958788591 578 YEKDLTASQ 586
Cdd:PRK12704 191 KEILAQAIQ 199
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
437-575 |
1.15e-06 |
|
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: 51.88 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIKE 516
Cdd:pfam15709 386 FEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQ 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 517 IHLQD-AARRRLLKLQQDQREMELRRLEDEIERKvqmRDQEIAATAKDLEMRQLELEARK 575
Cdd:pfam15709 466 KRLMEmAEEERLEYQRQKQEAEEKARLEAEERRQ---KEEEAARLALEEAMKQAQEQARQ 522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
437-708 |
1.23e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELDFLRERQTVENMQaEVDEQRAKDEawyQKQEMLRRAEETRremllQEEEKMAQQRHRLAAVKRELEIKE 516
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKK-KAEEAKKAEE---DKNMALRKAEEAK-----KAEEARIEEVMKLYEEEKKMKAEE 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 517 IHLQDAARRRLLKLQQDQRE----MELRRLEDEIERKVQM--RDQEIAATAKDLEMRQLELEARK----RLYEKDLTASQ 586
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEkkkvEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKaeeaKKAEEDEKKAA 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 587 EAIAKGIREDTDAHRRKMVLEEHVFQkllensqmgSRRTPRVMEDNLAKAEQAclnadwqiqtlHKQNREDRQRSEGyye 666
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKK---------AEELKKAEEENKIKAEEA-----------KKEAEEDKKKAEE--- 1748
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958788591 667 vatlLRKDRQKEIQVLDAMMEEEAKKWKEAREKEFHLQSEKK 708
Cdd:PTZ00121 1749 ----AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
437-734 |
2.29e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELDFLRERQTVENMQAEvdEQRAKDEAWYQKQEMLRRAEETRREMllQEEEKMAQQRHRLAAVKRELEikE 516
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKE--EAKKKADAAKKKAEEKKKADEAKKKA--EEDKKKADELKKAAAAKKKAD--E 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 517 IHLQDAARRrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLElEARKRLYEKDLTASQEAIAKGIRED 596
Cdd:PTZ00121 1423 AKKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 597 TDAHRRKmvleEHVFQKLLENSQMGSRRTPrvmeDNLAKAEQAcLNADWQIQTLHKQNREDRQRSEGYY---EVATLLRK 673
Cdd:PTZ00121 1499 ADEAKKA----AEAKKKADEAKKAEEAKKA----DEAKKAEEA-KKADEAKKAEEKKKADELKKAEELKkaeEKKKAEEA 1569
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958788591 674 DRQKEIQVLDAMMEEEAKKWKEAREKEFHLQSEKKASALSDASRKwflgqETNAALEHEEV 734
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEEL 1625
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
437-669 |
3.81e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNdELDFLR-------ERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMllqeeekmaqQRHRLAAVK 509
Cdd:pfam17380 389 QKNERVRQ-ELEAARkvkileeERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM----------ERVRLEEQE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 510 RELEIKEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVqmrdqeiaaTAKDLEMRQ---LELEARKRLYEKDLTASQ 586
Cdd:pfam17380 458 RQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKI---------LEKELEERKqamIEEERKRKLLEKEMEERQ 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 587 EAIAkgiredtDAHRRKMVLEEHVFQKLLENsqmgSRRTPRVMEdnLAKAEQACLNADWQIQTLHKQNRE-DRQRSEgyY 665
Cdd:pfam17380 527 KAIY-------EEERRREAEEERRKQQEMEE----RRRIQEQMR--KATEERSRLEAMEREREMMRQIVEsEKARAE--Y 591
|
....
gi 1958788591 666 EVAT 669
Cdd:pfam17380 592 EATT 595
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
437-707 |
4.50e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREM-LLQEEEKMAQQRHRLAAVKRELEIK 515
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 516 EIHLQDAARRrllKLQQDQREMElrrledEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAIAKGIRE 595
Cdd:pfam02463 256 SKQEIEKEEE---KLAQVLKENK------EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 596 DTDAHRRKMVLEEhvFQKLLENSQmGSRRTPRVMEDNLAKAEQACLNADWQIQTLHKQNREDRQRSEGYYEVATLLRKDR 675
Cdd:pfam02463 327 EKELKKEKEEIEE--LEKELKELE-IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270
....*....|....*....|....*....|....
gi 1958788591 676 QKEIQVLD--AMMEEEAKKWKEAREKEFHLQSEK 707
Cdd:pfam02463 404 EKEAQLLLelARQLEDLLKEEKKEELEILEEEEE 437
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
468-608 |
4.52e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 468 AKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLaavKRELEIKEIHLQDAARRRLlklqqdQREMELRRLEDEIE 547
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKRLL------QKEENLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958788591 548 RkvqmRDQEIAATAKDLEMRQLELEARKRLYEKdLTASQ----EAIAKGIREDTdahrRKMVLEE 608
Cdd:PRK12704 107 K----REEELEKKEKELEQKQQELEKKEEELEE-LIEEQlqelERISGLTAEEA----KEILLEK 162
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
435-620 |
5.71e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEEtrremLLQEEEKMAQQRHRLAAVKRELEi 514
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 515 kEIHLQDAARRRLLKlQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAIAKgIR 594
Cdd:COG4717 150 -ELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE-LE 226
|
170 180
....*....|....*....|....*.
gi 1958788591 595 EDTDAHRRKMVLEEHvFQKLLENSQM 620
Cdd:COG4717 227 EELEQLENELEAAAL-EERLKEARLL 251
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
435-701 |
6.72e-06 |
|
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: 49.15 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEI 514
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 515 KEIHLQDAARRRLLKLQQDQRE-----MELRRLEDEIERKVQMRDQE----IAATAKDLEMRQLELEARKRLYEKDLTAS 585
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEfneeqAEWKELEKEEEREEDERILEylkeKAEREEEREAEREEIEEEKEREIARLRAQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 586 QEAIaKGIREDTDAHRRKMVLEEHVF-----------QKLLENSQMGSRRTPRVMEDNLAKAEQACLNADWQIQTLHKQN 654
Cdd:pfam13868 193 QEKA-QDEKAERDELRAKLYQEEQERkerqkereeaeKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958788591 655 REDRQrsegYYEVATLLRKDRQKEIQVLDAMMEEEAKKWKEAREKEF 701
Cdd:pfam13868 272 EDEEI----EQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEEL 314
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
173-356 |
8.78e-06 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 47.69 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 173 PTKYRMFIWRSLLQLPENHTA-----FSSLMDKG-------THAAYLDLQKKYP------IKSRRLLRVLQRTLSALA-H 233
Cdd:smart00164 6 PPSLRGVVWKLLLNAQPMDTSadkdlYSRLLKETapddksiVHQIEKDLRRTFPehsffqDKEGPGQESLRRVLKAYAlY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 234 WSAI--FSDMPYL--PLL--------AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppiniltmienvLAFHD 300
Cdd:smart00164 86 NPEVgyCQGMNFLaaPLLlvmedeedAFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788591 301 KELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSSHPSFLLMTVVA 356
Cdd:smart00164 151 PDLYKHLKDLGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
433-608 |
1.50e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 433 DYQTKERERIRNDELDFLRERQTVENMQaevdeqrakdeawyQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKREL 512
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 513 EIKEIHLQDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQ----------EIAATAKDLEMRQLELEARKRLYEKDL 582
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLER-----EIERLERELEERERRRARleallaalglPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*.
gi 1958788591 583 TASQEAIAKGIREDTDAHRRKMVLEE 608
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEA 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
440-744 |
1.84e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 440 ERIRNDEldflRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRremllQEEEKMAQQRHRLAAVKRELEIKEIHL 519
Cdd:PTZ00121 1610 EEAKKAE----EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 520 QDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAiakgireDTDA 599
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA-------KKDE 1753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 600 HRRKMVleEHVFQKLLENSQMGSRRTPRVMEDNLAKA-EQACLNADWQIQTLhKQNREDRQrsEGYYEVATLLRKDRQ-- 676
Cdd:PTZ00121 1754 EEKKKI--AHLKKEEEKKAEEIRKEKEAVIEEELDEEdEKRRMEVDKKIKDI-FDNFANII--EGGKEGNLVINDSKEme 1828
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788591 677 ----KEIQVLDAMMEEEAKKWKEAREKEFHLQSEKKASALSDASRKWFLGQETNAALEHEEVPWLQKQHMDS 744
Cdd:PTZ00121 1829 dsaiKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER 1900
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
439-730 |
1.86e-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: 48.58 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 439 RERIRNDELDFLRE----RQTVENMQAEVDEQRAKDE---AWYQKQEMLRRAE----ETRREMLLQEEEKMAQQRHRLAA 507
Cdd:pfam15921 305 QEQARNQNSMYMRQlsdlESTVSQLRSELREAKRMYEdkiEELEKQLVLANSElteaRTERDQFSQESGNLDDQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 508 V--KREleiKEIHLQDAARRRL-------------LKLQQDQREMELRRLEDEI-----ERKVQMRDQEIAATAKDLEMR 567
Cdd:pfam15921 385 DlhKRE---KELSLEKEQNKRLwdrdtgnsitidhLRRELDDRNMEVQRLEALLkamksECQGQMERQMAAIQGKNESLE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 568 QL-ELEARkrlyekdLTASQEAIAKGIREDTdahRRKMVLEEHvfQKLLENSQMGSRRTPRVMEDNLAKAEQACLNADWQ 646
Cdd:pfam15921 462 KVsSLTAQ-------LESTKEMLRKVVEELT---AKKMTLESS--ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 647 IQTL-HKQNREDRQRS-EGYYEVATLLRKDRQKEIQVL------------------DAMMEEEAKKWKEAREKEFHLQSE 706
Cdd:pfam15921 530 LQELqHLKNEGDHLRNvQTECEALKLQMAEKDKVIEILrqqienmtqlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEF 609
|
330 340
....*....|....*....|....
gi 1958788591 707 KKASALSDASRKWFLGQETNAALE 730
Cdd:pfam15921 610 KILKDKKDAKIRELEARVSDLELE 633
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
476-707 |
3.11e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 476 KQEMLRRAEETR----REMLLQEE--------EKMAQQRHRLAAVKRELEIKEIHLQdAARRRLLKLQQDQREMELRRLE 543
Cdd:COG1196 174 KEEAERKLEATEenleRLEDILGElerqleplERQAEKAERYRELKEELKELEAELL-LLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 544 DEIER-KVQMRDQEIAATAKDLEMRQLELE---ARKRLYEkdLTASQEAIAKGIREDTDAHRRkmvleehvfqkllensq 619
Cdd:COG1196 253 AELEElEAELAELEAELEELRLELEELELEleeAQAEEYE--LLAELARLEQDIARLEERRRE----------------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 620 mgsrrtprvMEDNLAKAEQACLNADWQIQTLHKQ---NREDRQRSEGYYEVATLLRKDRQKEIQVLDAMMEEEAKKWKEA 696
Cdd:COG1196 314 ---------LEERLEELEEELAELEEELEELEEEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250
....*....|.
gi 1958788591 697 REKEFHLQSEK 707
Cdd:COG1196 385 AEELLEALRAA 395
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-709 |
4.20e-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: 47.37 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 439 RERIR--NDELDFLRERQtvENMQAEVDEQRAKDEAWYQK-------QEMLRRAEETRREMLLQEEEKMAQQRHRLAAVK 509
Cdd:TIGR02169 680 RERLEglKRELSSLQSEL--RRIENRLDELSQELSDASRKigeiekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 510 RELE--IKEIhlqDAARRRLLKLQQDQREMElRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEAR--KRLYEK----- 580
Cdd:TIGR02169 758 SELKelEARI---EELEEDLHKLEEALNDLE-ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKlnRLTLEKeylek 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 581 ----------DLTASQEAIAKGIrEDTDAHRRKM--VLEEH-VFQKLLENSQMGSRRTPRVMEDNLAKAEQACLNADWQI 647
Cdd:TIGR02169 834 eiqelqeqriDLKEQIKSIEKEI-ENLNGKKEELeeELEELeAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 648 QTL-HKQNREDRQRSEGYYEVATLLRKDR---------------QKEIQVLDAMM--------------EEEAKKWKEAR 697
Cdd:TIGR02169 913 EKKrKRLSELKAKLEALEEELSEIEDPKGedeeipeeelsledvQAELQRVEEEIralepvnmlaiqeyEEVLKRLDELK 992
|
330
....*....|..
gi 1958788591 698 EKEFHLQSEKKA 709
Cdd:TIGR02169 993 EKRAKLEEERKA 1004
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
464-789 |
5.99e-05 |
|
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: 46.76 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 464 DEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIKEIHLQDAarRRLLKlqqdQREMELRRLE 543
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA--RTALK----NARLDLRRLF 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 544 DEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAIAKGIREDTDA--HRRKMVLEEHVFQKLLENSQMG 621
Cdd:pfam12128 660 DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqAYWQVVEGALDAQLALLKAAIA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 622 SRRTPR-------------------VMEDNLAKAEQaclnadwQIQTLHK------QNREDRQRSEGYYEVATLLRKDR- 675
Cdd:pfam12128 740 ARRSGAkaelkaletwykrdlaslgVDPDVIAKLKR-------EIRTLERkieriaVRRQEVLRYFDWYQETWLQRRPRl 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 676 ----------QKEIQVLDAMMEEEAKKWKEAREKEFHlQSEKKASALSDASRKWFLGQETNAALeHEEVPWLQKQHMDST 745
Cdd:pfam12128 813 atqlsnieraISELQQQLARLIADTKLRRAKLEMERK-ASEKQQVRLSENLRGLRCEMSKLATL-KEDANSEQAQGSIGE 890
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958788591 746 CLPQ--TLRLNDVSDMDSSTQIFSRDKPTEWNHTESDLLKNVRDLR 789
Cdd:pfam12128 891 RLAQleDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLR 936
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
492-708 |
8.86e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 492 LQEEEKMAQQRHRLAAVKRELEI---------KEIH-----LQDAARR-RLLKLQQDQREMELRRLEDEIE---RKVQMR 553
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSlqselrrieNRLDelsqeLSDASRKiGEIEKEIEQLEQEEEKLKERLEeleEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 554 DQEIAATAKDLEmrqlELEARKRLYEKDLTASQEAIAKgiredtdahrrkmvLEEHVFQKLLENSQMGSRRTPRVMEDNL 633
Cdd:TIGR02169 750 EQEIENVKSELK----ELEARIEELEEDLHKLEEALND--------------LEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788591 634 AKAEQacLNADWQIQTLHKQNRED-RQRSEGYYEVATLLRKDRQKEIQVLDAMMEEEAKKWKEAREKEFHLQSEKK 708
Cdd:TIGR02169 812 ARLRE--IEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
437-614 |
9.71e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 9.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRH-RLAAVKRELEIK 515
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAeREELLEELLEEE 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 516 EIHLQDAARRRLLKLQQDQREMELRRLEDEIER--KVQMR-DQEIAATAKDLEmrqlELEARKrlyeKDLTASQEAIAKG 592
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLEREIEAlgPVNLLaIEEYEELEERYD----FLSEQR----EDLEEARETLEEA 817
|
170 180 190
....*....|....*....|....*....|.
gi 1958788591 593 IREdTDAHRRKMVLE---------EHVFQKL 614
Cdd:COG1196 818 IEE-IDRETRERFLEtfdavnenfQELFPRL 847
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
450-730 |
1.42e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 450 LRERQTVENMQA--EVDEQRAKDEAwyQKQEMLRRAEETRRemlLQEEEKMAQQRHRLAAVKRELEIKEIhlqDAARRRL 527
Cdd:PTZ00121 1193 LRKAEDARKAEAarKAEEERKAEEA--RKAEDAKKAEAVKK---AEEAKKDAEEAKKAEEERNNEEIRKF---EEARMAH 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 528 LKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdlEMRQLElEARKRLYEKDLTASQEAIAKGIREDTDAHRRKM--- 604
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeea 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 605 -------VLEEHVFQKLLENSQMGSRRTPRVMEDNLAKAEQACLNAD--WQIQTLHKQNREDRQRSEGYYEVATLLRKDR 675
Cdd:PTZ00121 1342 kkaaeaaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958788591 676 QKEIQVLDAMMEEEAKkwKEAREKEFHLQSEKKASALSDASRKWFLGQETNAALE 730
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
435-692 |
1.46e-04 |
|
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: 44.91 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIR-NDELDFLRERQTVENMQAEVDEQRAKdeawyQKQEMLRRAEETRREMLLQEEEKMAQ-QRHRLAAVKREL 512
Cdd:pfam13868 81 QIEEREQKRqEEYEEKLQEREQMDEIVERIQEEDQA-----EAEEKLEKQRQLREEIDEFNEEQAEWkELEKEEEREEDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 513 EIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLE-LEARKRLYEKDLTASQEAIAK 591
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEeQERKERQKEREEAEKKARQRQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 592 GIREdtdAHRRKMVLEEHVFQKLLENSQMGSRRtprVMEDNLAKAEQACLNADWQIQTLHKQNREDRQRSEgyyEVATLL 671
Cdd:pfam13868 236 ELQQ---AREEQIELKERRLAEEAEREEEEFER---MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIE---EREEQR 306
|
250 260
....*....|....*....|.
gi 1958788591 672 RKDRQKEIQVLDAMMEEEAKK 692
Cdd:pfam13868 307 AAEREEELEEGERLREEEAER 327
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
491-706 |
4.60e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 491 LLQEEEKMAQQRHRLAAVKRELEIKEIHLQDAARRRLLKLQQ----DQREMELRRLEDEIERKVQMRDQEIAATAKDLEM 566
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 567 RQLELEARKRLYEKDLTASQ-------EAIAKGIREDTDAHRRKMVLEEhvfqklLENSQMGSRRTPRVMEDNLAKAEQA 639
Cdd:COG4942 95 LRAELEAQKEELAELLRALYrlgrqppLALLLSPEDFLDAVRRLQYLKY------LAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788591 640 CLNADWQIQTLHKQNREDRQRSEgyyevatLLRKDRQKEIQVLDAMMEEEAKKWKEAREKEFHLQSE 706
Cdd:COG4942 169 LEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-619 |
5.33e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 439 RERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLrraeETRREMLLQEEEKMAQQRHrlAAVKRELEIKEIH 518
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL----KEELESLEAELEELEAELE--ELESRLEELEEQL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 519 LQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQeiaatakdLEMRQLELEARKRLYEKDLTASQEAIAKGIREDTD 598
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER--------LQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
170 180
....*....|....*....|.
gi 1958788591 599 AHRRKMVLEEHVFQKLLENSQ 619
Cdd:TIGR02168 454 EELERLEEALEELREELEEAE 474
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
526-712 |
6.14e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 526 RLLKLQQDQREMELRRLEDEIERKVQMRDQEiaatakDLEMRQLELEARKRLYEKDlTASQEAIAKGIREDTDAHRRKMV 605
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQ------EKEEKAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 606 LEEHVFQKLLENSQmgsRRTPRVMEDNLAkAEQACLNADWQIQtLHKQNREDRQRSEgyYEVA---TLLRKDRQKEIQVL 682
Cdd:pfam17380 346 RERELERIRQEERK---RELERIRQEEIA-MEISRMRELERLQ-MERQQKNERVRQE--LEAArkvKILEEERQRKIQQQ 418
|
170 180 190
....*....|....*....|....*....|
gi 1958788591 683 DAMMEEEAKKWKEAREKEFHLQSEKKASAL 712
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
451-718 |
7.30e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 451 RERQTVENMQAEVDEQRAKdEAWYQKQEMLRRAEEtrREMLLQEEEKMAQQRHRLAAVKRELEIKEIHLQDAARRRLLKL 530
Cdd:TIGR02168 207 RQAEKAERYKELKAELREL-ELALLVLRLEELREE--LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 531 QQDQREM-----ELRRLEDEIERKVQmRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAIA--KGIREDTDAHRRK 603
Cdd:TIGR02168 284 EELQKELyalanEISRLEQQKQILRE-RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 604 MVLEEHVFQKLLENSQMGSRRTPRvmEDNLAKAEQACLNAdwQIQTL--------HKQNREDRQRSEGYYEVATLLRKDR 675
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRS--KVAQLELQIASLNN--EIERLearlerleDRRERLQQEIEELLKKLEEAELKEL 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958788591 676 QKEIQVLDAMMEE--EAKKWKEAREKEFHLQSEKKASALSDASRK 718
Cdd:TIGR02168 439 QAELEELEEELEElqEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
435-607 |
7.71e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIRNDElDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEetrREMLLQEEEKMAQQrhrlaAVKRELEI 514
Cdd:COG2268 215 AIAQANREAEEA-ELEQEREIETARIAEAEAELAKKKAEERREAETARAE---AEAAYEIAEANAER-----EVQRQLEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 515 keihlqdAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAkdlemrQLELEARKRLYEKDLTAsQEAIAKGIR 594
Cdd:COG2268 286 -------AEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA------EAEAEAIRAKGLAEAEG-KRALAEAWN 351
|
170
....*....|...
gi 1958788591 595 EDTDAHRRKMVLE 607
Cdd:COG2268 352 KLGDAAILLMLIE 364
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
289-405 |
9.58e-04 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 42.48 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 289 LTMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSSHPSFLLMTVVAYNTCSRAPLLNC 368
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958788591 369 TLKDDFEYFFHHRNNLDLNVVIREVYHLMETTPADIH 405
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
461-595 |
9.66e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 461 AEVDEQRAKDEAWYQKQEMLRRAEETRremllQEEEKMAQQRHRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREMELR 540
Cdd:COG2268 195 AEIIRDARIAEAEAERETEIAIAQANR-----EAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYE 269
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 541 RLEDEIERKVQM------RDQEIAATAKDLEMRQLEL--------EARKRLYEKDLTASQEAI-AKGIRE 595
Cdd:COG2268 270 IAEANAEREVQRqleiaeREREIELQEKEAEREEAELeadvrkpaEAEKQAAEAEAEAEAEAIrAKGLAE 339
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
451-579 |
1.12e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 451 RERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIKEIHLQDAARRRLLKL 530
Cdd:pfam05672 19 KRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQER 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958788591 531 QQDQREMELRRLEDEIERKVQMRDQEIaatakdLEMRQLELEARKRLYE 579
Cdd:pfam05672 99 LQKQKEEAEAKAREEAERQRQEREKIM------QQEEQERLERKKRIEE 141
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
526-711 |
1.13e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 526 RLLKLQQD--QREMELRRLEDEIERKVQMRDQEIAATAKdlemRQLELEARKRLYEKDLTASQEAIakgiREDTDAHRRK 603
Cdd:pfam05557 10 RLSQLQNEkkQMELEHKRARIELEKKASALKRQLDRESD----RNQELQKRIRLLEKREAEAEEAL----REQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 604 MVLEEHVFQKLLENSQM--GSRRTPRVMEDNLAKAEQACLNADWQIQTLHKQNREDRQRsegyyevatllrkdrqkeiqv 681
Cdd:pfam05557 82 KKYLEALNKKLNEKESQlaDAREVISCLKNELSELRRQIQRAELELQSTNSELEELQER--------------------- 140
|
170 180 190
....*....|....*....|....*....|
gi 1958788591 682 ldamMEEEAKKWKEAREKEFHLQSEKKASA 711
Cdd:pfam05557 141 ----LDLLKAKASEAEQLRQNLEKQQSSLA 166
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
433-557 |
1.20e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 433 DYQTKERERIRNDEL--DFLRERQTVEN-----------MQAEVDEQRAKDEAWYQKQEMLRraeetrrEMLLQEEEKMA 499
Cdd:pfam02841 163 KYNQVPRKGVKAEEVlqEFLQSKEAVEEailqtdqaltaKEKAIEAERAKAEAAEAEQELLR-------EKQKEEEQMME 235
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788591 500 QQRHR----LAAVKRELEIKEIHLQDAARRRLLKLQQDQREMelrrLEDEIERKVQMRDQEI 557
Cdd:pfam02841 236 AQERSyqehVKQLIEKMEAEREQLLAEQERMLEHKLQEQEEL----LKEGFKTEAESLQKEI 293
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
439-575 |
1.25e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 439 RERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIKEIH 518
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQ 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788591 519 LqdAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEiaatAKDLEMRQLELEARK 575
Cdd:PRK12705 107 L--EEREKALSARELELEELEKQLDNELYRVAGLTPEQ----ARKLLLKLLDAELEE 157
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
432-591 |
1.43e-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: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 432 VDYQTKERERIRNDELDFLRERqtVENMQAEVDEQRAKDEAwYQKQEMLRRAEETR----------REMLLQEEEKMAQQ 501
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQ--LPELRKELEEAEAALEE-FRQKNGLVDLSEEAklllqqlselESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 502 RHRLAAVKRELEIKEIHLQDAA--------RRRLLKLQQDQREM---------ELRRLEDEIERKVQMRDQEIAATAKDL 564
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLqspviqqlRAQLAELEAELAELsarytpnhpDVIALRAQIAALRAQLQQEAQRILASL 318
|
170 180
....*....|....*....|....*..
gi 1958788591 565 EMRQLELEARKRLYEKDLTASQEAIAK 591
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAE 345
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
436-709 |
1.55e-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: 42.35 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 436 TKERERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIK 515
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 516 EIHLQD----------AARRRLLKLQQDQR----------------EMELRRLEDEI---ERKVQMRDQEIAATAKDLEM 566
Cdd:TIGR02168 763 IEELEErleeaeeelaEAEAEIEELEAQIEqlkeelkalrealdelRAELTLLNEEAanlRERLESLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 567 RQLELEaRKRLYEKDLTASQEAIAKGIREDTDAH----RRKMVLEEHVFQKLLENSQMgsRRTPRVMEDNLAKAEQACLN 642
Cdd:TIGR02168 843 LEEQIE-ELSEDIESLAAEIEELEELIEELESELeallNERASLEEALALLRSELEEL--SEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 643 AdwqiQTLHKQNREDRQRSEGyyEVATL---LRKDRQKEIQVLDAMMEEEAKKWKEAREKEFHLQSEKKA 709
Cdd:TIGR02168 920 L----REKLAQLELRLEGLEV--RIDNLqerLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
436-591 |
1.66e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 436 TKERERIRNDELDFLR---ERQTVENMQAEvdEQRAKDEAwyqKQEMLRRAEETRreMLLQEEEKMAQQRHRLAAVKREL 512
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRaeeQRKKKEQQQAE--ELQQKQAA---EQERLKQLEKER--LAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 513 EIKEIHLQDAARrrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMR-QLELEARKRlyekdltASQEAIAK 591
Cdd:PRK09510 134 AEEAAAKAAAAA----KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKkKAEAEAAAK-------AAAEAKKK 202
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
444-549 |
1.70e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 444 NDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAavKRELEIKEIHLQDAA 523
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQ--EAELELEELKKKREE 288
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958788591 524 RRRLLKLQQDQR-----------EMELRRLEDEIERK 549
Cdd:pfam02029 289 RRKLLEEEEQRRkqeeaerklreEEEKRRMKEEIERR 325
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
482-698 |
2.00e-03 |
|
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: 41.48 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 482 RAEETRREMLL--QEEEKMAQQRHRLA-AVKRELEIKEIHLQDAARRRLlklQQDQREMElRRLEDEIERKVQMRDQEIA 558
Cdd:pfam15709 315 RSEEDPSKALLekREQEKASRDRLRAErAEMRRLEVERKRREQEEQRRL---QQEQLERA-EKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 559 ATAKDLE---MRQLELEARKRLYEKdltASQEaiaKGIREDTDAHRRKMVLEEHVFQKLLENSQMGSRRTpRVMEDNLAk 635
Cdd:pfam15709 391 LRKQRLEeerQRQEEEERKQRLQLQ---AAQE---RARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQ-KELEMQLA- 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958788591 636 AEQACLNADWQIQTL----HKQNREDRQRSEgyyevatlLRKDRQKEIQVLDAMMEEEAKKWKE-ARE 698
Cdd:pfam15709 463 EEQKRLMEMAEEERLeyqrQKQEAEEKARLE--------AEERRQKEEEAARLALEEAMKQAQEqARQ 522
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
429-537 |
2.22e-03 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 40.67 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 429 KFIVdyqtKERERIRNDEldflrerqtvenmQAEVDEQRAKDEawyqkQEMLRRA-----EETrREMLLQEEEKMA---Q 500
Cdd:pfam15991 16 RHIM----RERERKKQEQ-------------EAKMEEERLRRE-----REEREKEdrmtlEET-KEQILKLEKKLAdlkE 72
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958788591 501 QRHRLAavkreLEIKEIHLQDAARRRLLKLQQDQREM 537
Cdd:pfam15991 73 EKHQLF-----LQLKKVLHEDETRKRQLKEQSELFAL 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
474-701 |
2.24e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 474 YQKQEmLRRAEETRREMllqeEEKMAQQRHRLAAVKRELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQM 552
Cdd:TIGR02168 674 ERRRE-IEELEEKIEEL----EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 553 RDQeiaatakdLEMRQLELEARKRLYEKDLTASQEAIAkgiredtdAHRRKMVLEEHVFQKLLENSQMGSRRTPRV---- 628
Cdd:TIGR02168 749 IAQ--------LSKELTELEAEIEELEERLEEAEEELA--------EAEAEIEELEAQIEQLKEELKALREALDELrael 812
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958788591 629 --MEDNLAKAEQACLNADWQIQTLHKQNREDRQRSEGYYEVATLLRKdRQKEIQVLDAMMEEEAKKWKEAREKEF 701
Cdd:TIGR02168 813 tlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA-EIEELEELIEELESELEALLNERASLE 886
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
438-591 |
2.26e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 438 ERERIRNDELDFLRERQTVENmQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIKEI 517
Cdd:COG4717 312 ALEELEEEELEELLAALGLPP-DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958788591 518 HLQDAARRRLLKlQQDQREMELRRLEDEIERKVQMRDQEiaatakDLEMRQLELEARKRLYEKDLTASQEAIAK 591
Cdd:COG4717 391 LEQAEEYQELKE-ELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
495-714 |
2.37e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 495 EEKMAQQRHRLAAVKRELEIKEIHLqDAARRRLLKLQQDQREME-----LRRLED----EIERKVQMRDQEIAATAKDLE 565
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLII-DEKRQQLERLRREREKAEryqalLKEKREyegyELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 566 MRQLELEARKRLYEkDLTASQEAIAKGIREDTDAHRRKMVLEEHVFQKLLEN---SQMGSRRTPRVMEDNLAKAEQACLN 642
Cdd:TIGR02169 248 SLEEELEKLTEEIS-ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958788591 643 ADWQIqtlHKQNREDRQRSEGYYEVATLLRK------DRQKEIQVLDAMMEEEAKKWKEAREKefHLQSEKKASALSD 714
Cdd:TIGR02169 327 LEAEI---DKLLAEIEELEREIEEERKRRDKlteeyaELKEELEDLRAELEEVDKEFAETRDE--LKDYREKLEKLKR 399
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
460-700 |
2.92e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.18 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 460 QAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELE--IKEIHLQDAARRRLLKLQQDQREM 537
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 538 ELRRLEDEIERKVQMRDQEIAATA-KDLEMRQLELEARK-RLYEKDLTASQEAIAKGIREDTDAHRRKMVLEE-HVFQKL 614
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAeAAAAAEKAAAAAEKeKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEaEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 615 LENSQMGSRRTPRVMEDNLAKAEQACLNADWQIQTLHKQNREDRQRSEGYYEVATLLRKDRQKEIQVLDAMMEEEAKKWK 694
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
....*.
gi 1958788591 695 EAREKE 700
Cdd:COG3064 241 EEAALG 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-705 |
3.28e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 439 RERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIKEIH 518
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 519 LQDA-ARRRLLKLQQDQREMELRRLEDEIErKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEA-------IA 590
Cdd:TIGR02168 756 LTELeAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERleslerrIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 591 KGIREDTDAHRRKMVLEEHVfqKLLENSQMGSRRTPRVMEDNLAKAEQAclnadwqiqtLHKQNREDRQRSEGYYEVATL 670
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELEALLNE----------RASLEEALALLRSELEELSEE 902
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958788591 671 LRKDRQK------EIQVLDAMMEEEAKKWKEAREKEFHLQS 705
Cdd:TIGR02168 903 LRELESKrselrrELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
437-592 |
3.86e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELDFLRE-----RQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEkmaQQRHRLAavkre 511
Cdd:PRK02224 229 REQARETRDEADEVLEeheerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE---ERDDLLA----- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 512 leikEIHLQDAARRRLLKLQQD--QREMELRRLEDEIERKVQMRDQEI---AATAKDLEMRQLELEARKRLYEKDLTASQ 586
Cdd:PRK02224 301 ----EAGLDDADAEAVEARREEleDRDEELRDRLEECRVAAQAHNEEAeslREDADDLEERAEELREEAAELESELEEAR 376
|
....*.
gi 1958788591 587 EAIAKG 592
Cdd:PRK02224 377 EAVEDR 382
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
436-718 |
4.12e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 436 TKERERIRNdeLDFLRERQtvENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLlqeEEKMAQQRHRLAAVKRELEIK 515
Cdd:pfam01576 169 AEEEEKAKS--LSKLKNKH--EAMISDLEERLKKEEKGRQELEKAKRKLEGESTDL---QEQIAELQAQIAELRAQLAKK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 516 EIHLQDAARR------RLLKLQQDQREME--LRRLEDEIERKVQMRDQeIAATAKDLEMrqlELEARKRLYEK--DLTAS 585
Cdd:pfam01576 242 EEELQAALARleeetaQKNNALKKIRELEaqISELQEDLESERAARNK-AEKQRRDLGE---ELEALKTELEDtlDTTAA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 586 QEAIaKGIREDTDAHRRKmVLEEHVFQKLLENSQMGSRRTPRVME--DNLAKAEQACLNADWQIQTLHKQNR----EDRQ 659
Cdd:pfam01576 318 QQEL-RSKREQEVTELKK-ALEEETRSHEAQLQEMRQKHTQALEEltEQLEQAKRNKANLEKAKQALESENAelqaELRT 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958788591 660 RSEGYYEVATlLRKDRQKEIQVLDAMMEEEAKKWKEAREKEFHLQSEKKA--SALSDASRK 718
Cdd:pfam01576 396 LQQAKQDSEH-KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESvsSLLNEAEGK 455
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
435-540 |
4.53e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.48 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIRNDELdflRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREMLLQEEEKMA-QQRHRLAAVKRELE 513
Cdd:pfam05672 36 EKEEEERLRKEEL---RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQErLQKQKEEAEAKARE 112
|
90 100
....*....|....*....|....*..
gi 1958788591 514 ikeihlqDAARRRLLKLQQDQREMELR 540
Cdd:pfam05672 113 -------EAERQRQEREKIMQQEEQER 132
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
437-576 |
5.05e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.40 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELDFLRER-----QTVENMQAEVDE-----QRAKDEAWYQKQEMLRRAEETRR-----EMLLQEEEKMAQ- 500
Cdd:pfam05667 327 EELQQQREEELEELQEQledleSSIQELEKEIKKlessiKQVEEELEELKEQNEELEKQYKVkkktlDLLPDAEENIAKl 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 501 QR------HRLAAVKRELEIKEIHLQDAARRrlLKLQQDQREMELRRLEDEIER-KVQMRDQEIAATAKDLEMRQL--EL 571
Cdd:pfam05667 407 QAlvdasaQRLVELAGQWEKHRVPLIEEYRA--LKEAKSNKEDESQRKLEEIKElREKIKEVAEEAKQKEELYKQLvaEY 484
|
....*
gi 1958788591 572 EARKR 576
Cdd:pfam05667 485 ERLPK 489
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
526-709 |
5.29e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 526 RLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAIAKGIrEDTDAHRRKmv 605
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKE-EQLDARAEK-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 606 leehvfqklLENsqmgsrrtprvMEDNLAKAEQAClnadwqIQTLHKQNREDRQRSEGYYEVATLLRKDRQKEI-QVLDA 684
Cdd:PRK12705 100 ---------LDN-----------LENQLEEREKAL------SARELELEELEKQLDNELYRVAGLTPEQARKLLlKLLDA 153
|
170 180
....*....|....*....|....*
gi 1958788591 685 MMEEEAKKWKEAREKEFHLQSEKKA 709
Cdd:PRK12705 154 ELEEEKAQRVKKIEEEADLEAERKA 178
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
6-83 |
5.46e-03 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 39.89 E-value: 5.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958788591 6 RAVRHLEFLPDSfdagsnQVLGVLSQDGIMRFVNIQTCKLLFQIGTVEEGVSSSVISPHGRYITAIMENGSLNVYSVQ 83
Cdd:COG2319 205 GAVRSVAFSPDG------KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
437-706 |
5.48e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 437 KERERIRNDELdflRERQTVENMQAEVDEQRAKDEAWYQKQEMLRRAEE---TRREML------------LQEEEKMAQQ 501
Cdd:TIGR00618 317 QSKMRSRAKLL---MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatSIREIScqqhtltqhihtLQQQKTTLTQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 502 RHRLAAVKRELEIKEIHLQDAARRRLLKLQQDqremeLRRLEDEIE---RKVQMRDQEIAATAKDLEMRQLEL-EARKRL 577
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQ-----LAHAKKQQElqqRYAELCAAAITCTAQCEKLEKIHLqESAQSL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 578 YEKDltaSQEAIAKGIredTDAHRRKMVLEEHVFQKLLENSQM--GSRRTPRV-----------------MEDNLAKAEQ 638
Cdd:TIGR00618 469 KERE---QQLQTKEQI---HLQETRKKAVVLARLLELQEEPCPlcGSCIHPNParqdidnpgpltrrmqrGEQTYAQLET 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 639 ACLNADWQIQTLHKQNREDRQRSE--------------GYYEVATLLRKDRQKEIQVLDAMMEEEAKKWKEAREKEFHLQ 704
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQeiqqsfsiltqcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
..
gi 1958788591 705 SE 706
Cdd:TIGR00618 623 PE 624
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
435-604 |
5.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 435 QTKERERIRNDELDFLRERQTVENMQAEVDEQ----RAKDEAWYQKQEMLRRAEETRREmllqeeekMAQQRHRLAAVKR 510
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEYSWDeidvASAEREIAELEAELERLDASSDD--------LAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 511 ELeikeihlqDAARRRLLKLQQDQR--EMELRRLEDEIERKvqmrdQEIAATAKDLEMRQLELEARKRLYEKDLTASQEA 588
Cdd:COG4913 700 EL--------EELEEELDELKGEIGrlEKELEQAEEELDEL-----QDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170
....*....|....*.
gi 1958788591 589 IAKGIREDTDAHRRKM 604
Cdd:COG4913 767 LRENLEERIDALRARL 782
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
457-717 |
5.87e-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: 40.21 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 457 ENMQAEVDEQRAKDEAWYQKQEMLRRAEETRREML-LQEEEKMAQQRH-RLAAVKREleIKEIHLQDAARRRLLKLQQDQ 534
Cdd:pfam12128 210 GVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTkLQQEFNTLESAElRLSHLHFG--YKSDETLIASRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 535 REMELRRLEDEIERKVQMRDQEIAATAKDLEMRQLELEA---RKRLYEKDLTAS-----------------QEAIAKG-- 592
Cdd:pfam12128 288 LNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAledQHGAFLDADIETaaadqeqlpswqselenLEERLKAlt 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 593 -----IREDTDAHRRKMVLEEH----VFQKLLENSQMGSRRTPRVMEDNLAKAEQAclnadWQIQtLHKQNREDRQRSEG 663
Cdd:pfam12128 368 gkhqdVTAKYNRRRSKIKEQNNrdiaGIKDKLAKIREARDRQLAVAEDDLQALESE-----LREQ-LEAGKLEFNEEEYR 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958788591 664 YYEVATLLRkdrqkeIQVLDAMMEEEAKKWKEAREKEFHLQSEKKASALSDASR 717
Cdd:pfam12128 442 LKSRLGELK------LRLNQATATPELLLQLENFDERIERAREEQEAANAEVER 489
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
495-608 |
8.37e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 38.05 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 495 EEKMAQQRHRLAAVKRELEIKEIHLQDAARRRllklQQDQREMELRRLEDEIErkvQMRDQEIAaTAKdLEMRQLELEAR 574
Cdd:PRK02292 8 EDIRDEARARASEIRAEADEEAEEIIAEAEAD----AEEILEDREAEAEREIE---QLREQELS-SAK-LEAKRERLNAR 78
|
90 100 110
....*....|....*....|....*....|....
gi 1958788591 575 KRLYEKDLTASQEAIAkgireDTDAHRRKMVLEE 608
Cdd:PRK02292 79 KEVLEDVRNQVEDEIA-----SLDGDKREELTKS 107
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
454-599 |
8.74e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 39.06 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 454 QTVENMQAE-VDEQRAKDEAWYQKQEM-------------LRRAEETRREMLLQEEEKMAQQRHRLAAVKRELEIKEIHL 519
Cdd:TIGR02794 33 GGAEIIQAVlVDPGAVAQQANRIQQQKkpaakkeqerqkkLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 520 QDAARRRLLKLQQDQREME-LRRLEDEIERKVQM---RDQEIAATAKDLEMRQLELEARKRLYEKDLTASQEAIAKGIRE 595
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAEaKAKAEAEAERKAKEeaaKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
|
....
gi 1958788591 596 DTDA 599
Cdd:TIGR02794 193 EAKA 196
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
454-651 |
9.28e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 454 QTVENMQAEVDEQRAKDEAwyqkQEMLRRAEETR--------REMLLQEEEKMAQQRHRLAAVKRELEIK-EIHLQDAAr 524
Cdd:PRK04863 480 QLVRKIAGEVSRSEAWDVA----RELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRlGKNLDDED- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788591 525 rrLLKLQQDQREMELRRLEDE----IERKVQMRDQEiaataKDLEMRQLELEARkrlyEKDLTASQEAIAKgIRE---DT 597
Cdd:PRK04863 555 --ELEQLQEELEARLESLSESvseaRERRMALRQQL-----EQLQARIQRLAAR----APAWLAAQDALAR-LREqsgEE 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958788591 598 DAHRRKMvleEHVFQKLLENsqmgsRRTPRVMEDNLAKAEQAClnaDWQIQTLH 651
Cdd:PRK04863 623 FEDSQDV---TEYMQQLLER-----ERELTVERDELAARKQAL---DEEIERLS 665
|
|
| |
