|
Name |
Accession |
Description |
Interval |
E-value |
| Cnn_1N |
pfam07989 |
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ... |
6-73 |
2.48e-17 |
|
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.
Pssm-ID: 462333 [Multi-domain] Cd Length: 69 Bit Score: 78.33 E-value: 2.48e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313637 6 RTLSQHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTW 73
Cdd:pfam07989 1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAE 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
31-679 |
5.22e-17 |
|
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: 88.19 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 31 ERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQ 110
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 111 LLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVpgdqvkpdqyTEALAQRDKRIEELNQSLAAQERLVE 190
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL----------QEELERLEEALEELREELEEAEQALD 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 191 QLSREKQQLLHLLEEPTSMEVQPMTE-ELLKQQKLNSHETTITQQSVSDshLAELQEKIQQteATNKILQEKLNemsyel 269
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFsEGVKALLKNQSGLSGILGVLSE--LISVDEGYEA--AIEAALGGRLQ------ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 270 KCAQESSQKQDGTIQNLKEtlKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALF 349
Cdd:TIGR02168 549 AVVVENLNAAKKAIAFLKQ--NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 350 CSQ-----LEIQKLQR----------------------------VVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKH 396
Cdd:TIGR02168 627 VVDdldnaLELAKKLRpgyrivtldgdlvrpggvitggsaktnsSILERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 397 NQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEK 476
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 477 LRQRIHDkavaLERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQ 556
Cdd:TIGR02168 787 LEAQIEQ----LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 557 NLQWLKEEMETKFSRWQKEQESIIQQlqtsLHDRNKEVEDLSATLLcklgpgqsEIAEELcQRLQRKERMLQDLLSDRNK 636
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEA----LALLRSELEELSEELR--------ELESKR-SELRRELEELREKLAQLEL 929
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 525313637 637 QVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQA 679
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
240-1038 |
3.02e-16 |
|
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: 85.88 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 240 HLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLH 319
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 320 QSQlgqlhssegTSPAQQQVALLDLQSALFCSQLEIQKLqrvvrqkERQLADAKQCVQFVEAAAHESEQQKEASWKHNQE 399
Cdd:TIGR02168 313 NLE---------RQLEELEAQLEELESKLDELAEELAEL-------EEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 400 LRKALQQLQEELQNKSQQLRAWEaekyNEIRTQEQNIQHLNHSLshkEQLLQEFRELLQYRDNSDktLEANEMLLEKLRQ 479
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLN----NEIERLEARLERLEDRR---ERLQQEIEELLKKLEEAE--LKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 480 RIHDKAVALERAIdekfSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQ 559
Cdd:TIGR02168 448 ELEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 560 WLKEEMETKfSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLLCKLGPGQSEIAEElcqrlqrkermlqDLLSDRNKQVL 639
Cdd:TIGR02168 524 VLSELISVD-EGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL-------------DSIKGTEIQGN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 640 EHEM--EIQGLLQSVSTREqESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAE-VTPTGRLGKQTDQG 716
Cdd:TIGR02168 590 DREIlkNIEGFLGVAKDLV-KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDlVRPGGVITGGSAKT 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 717 SMQIPSRDdSTSLTAKEDVSIPRSTLGDLDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAA 795
Cdd:TIGR02168 669 NSSILERR-REIEELEEKIEELEEKIAELEKaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 796 DMESLTRNIQIKEDLIKDLQMQLvdpedipamERLTQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDERSRLNE 875
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERL---------EEAEEELAEAEAEIEELEAQIEQLK-EELKALREALDELRAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 876 ALQAERQLYSSLVKFHAHPESSERDRT------------LQVELEGAQVLRSRLEEVLGRSLERLNRLET---LAAIGGA 940
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEeqieelsediesLAAEIEELEELIEELESELEALLNERASLEEalaLLRSELE 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 941 AAGDDTEDTSTEFTDSieEEAAHHSHQQLVKVALEKSLATVETQNpsfsppspmggdsnrcLQE---EMLHLRAEFHQHL 1017
Cdd:TIGR02168 898 ELSEELRELESKRSEL--RRELEELREKLAQLELRLEGLEVRIDN----------------LQErlsEEYSLTLEEAEAL 959
|
810 820
....*....|....*....|....*.
gi 525313637 1018 EEKR-----KAEEELKELKAQIEEAG 1038
Cdd:TIGR02168 960 ENKIeddeeEARRRLKRLENKIKELG 985
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-587 |
8.03e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 5 YRTLSQHLNDLKKEnfSLKLRIYFLEERMQ------QKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVEN 78
Cdd:COG1196 215 YRELKEELKELEAE--LLLLKLRELEAELEeleaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 79 LNS---QNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKEcNLELSEKLKGVTKnwedvp 155
Cdd:COG1196 293 LLAelaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-LEEAEAELAEAEE------ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 156 gdqvkpdQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEvqpmTEELLKQQKLNSHETTITQQS 235
Cdd:COG1196 366 -------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 236 VSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLR 315
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 316 EMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALfcsqleiqkLQRVVRqkeRQLADAKQCVQFV--EAAAHESEQQKEAS 393
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA---------LQNIVV---EDDEVAAAAIEYLkaAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 394 WKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEML 473
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 474 LEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKG--LEVEQL 551
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEReeLLEELL 742
|
570 580 590
....*....|....*....|....*....|....*.
gi 525313637 552 STTCQNLQWLKEEMETKFSRwqKEQESIIQQLQTSL 587
Cdd:COG1196 743 EEEELLEEEALEELPEPPDL--EELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-1111 |
1.09e-14 |
|
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: 80.49 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 388 QQKEASWKHNQELRKALQQLQEELQNKSQ-------QLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYR 460
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQeleekleELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 461 DNSDKTLEANEMLLEKLRQRIHDKAVALERAIDE---KFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSM 537
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 538 ESLLRAK----GLEVEQLSTTCQNLQWLKEEMETKFSRWQ-KEQESIIQQLQTSLHDRNKEVEDLSATLlcKLGPGQSEI 612
Cdd:TIGR02168 395 IASLNNEierlEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEAL--EELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 613 AEEL-------CQRLQRKERMLQDLL------SDRNKQVLEHEMEIQGLLQSVSTR-------EQESQAAAEKLVQALME 672
Cdd:TIGR02168 473 AEQAldaaereLAQLQARLDSLERLQenlegfSEGVKALLKNQSGLSGILGVLSELisvdegyEAAIEAALGGRLQAVVV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 673 RNSE-----LQALRQYLGGRDSLMsqAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSiprSTLGDLDT 747
Cdd:TIGR02168 553 ENLNaakkaIAFLKQNELGRVTFL--PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 748 VAGLEKELSNAKEELE----------------LMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLI 811
Cdd:TIGR02168 628 VDDLDNALELAKKLRPgyrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 812 KDLQMQLVDPEDIPamERLTQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKfh 891
Cdd:TIGR02168 708 EELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-- 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 892 ahpESSERDRTLQVELEGAQVLRSRLEEVLGRsLERLNRLETLAAIGGAAAGDDTEDTSTEFTDsIEEEAAHHSHQQLvk 971
Cdd:TIGR02168 783 ---EIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLED-LEEQIEELSEDIE-- 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 972 vALEKSLATVETQNPSFSPPSPMGGDSNRCLQEEMLHLRAEFHQHLEEKRKAEEELKELKAQIEEAGfSSVSHIRNTMLS 1051
Cdd:TIGR02168 856 -SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR-EKLAQLELRLEG 933
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1052 LCLENAELKEQmgeaMSDGWEIEEDkekgevMVETVVTKEGLSESSLQAEFRKLQGKLKN 1111
Cdd:TIGR02168 934 LEVRIDNLQER----LSEEYSLTLE------EAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-879 |
1.09e-13 |
|
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: 77.40 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 170 QRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEpTSMEVQPMTEELLKQQK-LNSH-------ETTITQQSVSDSHL 241
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKeLYALaneisrlEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 242 ----AELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREM 317
Cdd:TIGR02168 315 erqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 318 L--HQSQLGQLhSSEGTSPAQQQVALLDLQSALFCSQLE--IQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEAS 393
Cdd:TIGR02168 395 IasLNNEIERL-EARLERLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 394 WKHNQELR----------KALQQLQEELQNKSQQLRAWEAEKyneiRTQEQNIQHLNHSLSHKEQLLQE----FRELLQY 459
Cdd:TIGR02168 474 EQALDAAErelaqlqarlDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAieaaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 460 --RDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDlERLRDVLSS-------- 529
Cdd:TIGR02168 550 vvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD-PKLRKALSYllggvlvv 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 530 ---NEATMQSMES------------LLRAKGLEVEQLSTTCQNLQWLKEEMEtkfsrwqkEQESIIQQLQTSLHDRNKEV 594
Cdd:TIGR02168 629 ddlDNALELAKKLrpgyrivtldgdLVRPGGVITGGSAKTNSSILERRREIE--------ELEEKIEELEEKIAELEKAL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 595 EDLSATLlcklgpgqSEIAEELCQRLQRKERMLQDlLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERN 674
Cdd:TIGR02168 701 AELRKEL--------EELEEELEQLRKELEELSRQ-ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 675 SELQALRQYLGGRDSLMSQAP------------ISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTL 742
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 743 GDLdtvAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPE 822
Cdd:TIGR02168 852 EDI---ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 525313637 823 DipAMERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQA 879
Cdd:TIGR02168 929 L--RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-681 |
1.49e-13 |
|
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: 77.02 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 50 ELKVEVESLKR---------ELQDKKQHLDKtWADVENLNSQNEAelRRQFEERQQETEHVYELLENKIQLLQEEsrlak 120
Cdd:TIGR02168 197 ELERQLKSLERqaekaerykELKAELRELEL-ALLVLRLEELREE--LEELQEELKEAEEELEELTAELQELEEK----- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 121 neaarmaaLVEAEKEcNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRdkrieeLNQSLAAQERLVEQLSREKQQLL 200
Cdd:TIGR02168 269 --------LEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRER------LANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 201 HLLEEPTSMEVQpmTEELLKQQKLNSHEttitqqsvsdshLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQD 280
Cdd:TIGR02168 334 ELAEELAELEEK--LEELKEELESLEAE------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 281 GTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEgtspAQQQVALLDLQSALFCSQLEIQKLQR 360
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL----EELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 361 VVRQKERQLADAKQCVQFVEA--AAHESEQQKEASWKHNQELRKALQQ-------------------LQEELQ-----NK 414
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERlqENLEGFSEGVKALLKNQSGLSGILGvlselisvdegyeaaieaaLGGRLQavvveNL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 415 SQQLRAWEAEKYNEI--------------------RTQEQNIQHLNHSLSHKEQLLQEFRELLQYR-------DNSD--- 464
Cdd:TIGR02168 556 NAAKKAIAFLKQNELgrvtflpldsikgteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvDDLDnal 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 465 ---KTLEANEML-------------------------------LEKLRQRI---HDKAVALERAIDEKFSALEEKEKELR 507
Cdd:TIGR02168 636 elaKKLRPGYRIvtldgdlvrpggvitggsaktnssilerrreIEELEEKIeelEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 508 QLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSL 587
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 588 HDRNKEVEDLSA-----TLLCKLGPGQSEIAEELCQRLQRKERMLQDlLSDRNKQVLEHEMEIQGLLQSVSTREQESQAA 662
Cdd:TIGR02168 796 EELKALREALDElraelTLLNEEAANLRERLESLERRIAATERRLED-LEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
730
....*....|....*....
gi 525313637 663 AEKLVQALMERNSELQALR 681
Cdd:TIGR02168 875 LEALLNERASLEEALALLR 893
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
288-857 |
1.25e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 288 ETLKsRERETEELYQVIEgqndtmAKLREMLHQSQLGQLHSsegtspAQQQVALLDLQSALfcSQLEIQKLQRVVRQKER 367
Cdd:COG1196 203 EPLE-RQAEKAERYRELK------EELKELEAELLLLKLRE------LEAELEELEAELEE--LEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 368 QLADAKQcvqfveaAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKE 447
Cdd:COG1196 268 ELEELRL-------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 448 QLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSAL---EEKEKELRQLRLAVRERDHDLERLR 524
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALraaAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 525 DVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLLCK 604
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 605 ---LGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTR-EQESQAAAEKLVQALMER------- 673
Cdd:COG1196 501 adyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEdDEVAAAAIEYLKAAKAGRatflpld 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 674 ----------NSELQALRQYLGGRDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLG 743
Cdd:COG1196 581 kiraraalaaALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 744 DLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAA-DMESLTRNIQIKEDLIKDLQMQLVDPE 822
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAeEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590
....*....|....*....|....*....|....*
gi 525313637 823 DIPAMERLTQEVLLLREKVASVESQGQEISGNRRQ 857
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
356-1038 |
3.50e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 356 QKLQRV---VRQKERQLA----DAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEkyne 428
Cdd:COG1196 186 ENLERLediLGELERQLEplerQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE---- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 429 IRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQ 508
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 509 LRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTtcQNLQWLKEEMETkfsrwQKEQESIIQQLQTSLH 588
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--ELLEALRAAAEL-----AAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 589 DRNKEVEDLSATLLcklgpgQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQ 668
Cdd:COG1196 415 RLERLEEELEELEE------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 669 ALMERNSELQALRQYLGGRDSLMSQAPISnQQAEVTPTGRLGKQTDQGsmqiPSRDDSTSLTAKEDVSIPRSTLGDLDTV 748
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLA-GLRGLAGAVAVLIGVEAA----YEAALEAALAAALQNIVVEDDEVAAAAI 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 749 AGLEKELSNAKEELELMAKKERESQMELSALQSMMA--VQEEELQVQAADMESLTRNIQIKEDLIKDlqmqlvDPEDIPA 826
Cdd:COG1196 564 EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAavDLVASDLREADARYYVLGDTLLGRTLVAA------RLEAALR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 827 MERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQAERQLYSslvkfhahpESSERDRTLQVE 906
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE---------EALLAEEEEERE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 907 LEGAQVLRSRLEEVLGRSLERLNRLETLAAIGGAAAGDDTEDTSTEFTDSIEEEAAhhshqqlvkvalekslatvetqnp 986
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE------------------------ 764
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 525313637 987 sfsppspmggdsnrclqeemlhlraefhqhleekrkAEEELKELKAQIEEAG 1038
Cdd:COG1196 765 ------------------------------------LERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-669 |
4.27e-11 |
|
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: 68.94 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 399 ELRKALQQLQEE---------LQNKSQQLRAWEaeKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDnsdKTLEA 469
Cdd:TIGR02169 195 EKRQQLERLRRErekaeryqaLLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE---KRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 470 NEMLLEKLRQRIHDKAVALERAIDEKfsaLEEKEKELRQLRLAVRERDHDLERLrdvlssnEATMQSMESLLRAKGLEVE 549
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIAEKERELEDA-------EERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 550 QLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQtSLHDRNKEVEDLSATLLCKLGPGQSEIAEelcqrLQRKERMLQD 629
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELE-EVDKEFAETRDELKDYREKLEKLKREINE-----LKRELDRLQE 413
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 525313637 630 LLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQA 669
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
12-510 |
1.24e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.97 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 12 LNDLKKENFSLKLRIYFLEERMQQ--KYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEaELRR 89
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKnkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN-KIKK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 90 QFEERQQETEHVYELLENKIQLLQEesrlAKNEaarmaaLVEAEKECNLELSEKLKGVTKNWEDvpgdqvKPDQYTEALA 169
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQ----LKSE------ISDLNNQKEQDWNKELKSELKNQEK------KLEEIQNQIS 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 170 QRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSmEVQPMTEEllKQQKLNSHETTITQQSvsdshlaELQEKIQ 249
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN-EIEKLKKE--NQSYKQEIKNLESQIN-------DLESKIQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 250 QTEATNKILQEKlnemsyelkcaqessqkqdgtIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSS 329
Cdd:TIGR04523 402 NQEKLNQQKDEQ---------------------IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 330 EGTSPAQQQVALLdlqsalfcsQLEIQKLQRVVRQKERQLAdakqcvqfveaaahESEQQKEASWKHNQELR---KALQQ 406
Cdd:TIGR04523 461 NTRESLETQLKVL---------SRSINKIKQNLEQKQKELK--------------SKEKELKKLNEEKKELEekvKDLTK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 407 LQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSH---KEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRiHD 483
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK-EK 596
|
490 500
....*....|....*....|....*..
gi 525313637 484 KAVALERAIDEKFSALEEKEKELRQLR 510
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-527 |
3.25e-10 |
|
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: 65.85 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 120 KNEAARMAALVEAEKECNLELSEKLKGVtknwedvpgdQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQL 199
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAEL----------RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 200 LHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQsvsDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQ 279
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 280 DGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREmlhqsqlgqlhssegtspaqqqvALLDLQSALFCSQLEIQKLQ 359
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAA-----------------------EIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 360 RVVRQKERQLADAKqcvqfvEAAAHESEQQKEASwKHNQELRKALQQLQEELqnksqqlraweAEKYNEIRTQEQNIQHL 439
Cdd:TIGR02168 880 NERASLEEALALLR------SELEELSEELRELE-SKRSELRRELEELREKL-----------AQLELRLEGLEVRIDNL 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 440 NHSLSHKEQLLQEFrellqyrdnsdktLEANEMLLEKLRQRIHDKAVALERAIDE----KFSALEEKEkELRQLRLAVRE 515
Cdd:TIGR02168 942 QERLSEEYSLTLEE-------------AEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYE-ELKERYDFLTA 1007
|
410
....*....|..
gi 525313637 516 RDHDLERLRDVL 527
Cdd:TIGR02168 1008 QKEDLTEAKETL 1019
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
29-693 |
6.15e-10 |
|
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: 64.99 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 29 LEERMQQKYEAsrEDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEA-ELRRQFEERQQETEHVYELLEN 107
Cdd:TIGR00618 231 LREALQQTQQS--HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 108 KIQLLQE-ESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVkpDQYTEALAQRDKRIEELNQSLAAQE 186
Cdd:TIGR00618 309 AQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH--EVATSIREISCQQHTLTQHIHTLQQ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 187 R---LVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQE--- 260
Cdd:TIGR00618 387 QkttLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaq 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 261 KLNEMSYELKCAQESSQKQDGT----------IQNLKETLKSRERETE-ELYQVIEGQNDTMAKLREMLHQSQLGQlhsS 329
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKkavvlarlleLQEEPCPLCGSCIHPNpARQDIDNPGPLTRRMQRGEQTYAQLET---S 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 330 EGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQE 409
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 410 ELQNksQQLRAweaekyneirTQEQNIQHLNHSLSHKEQLLQEfrelLQYRDNSDKTLEANEMLLEKL--RQRIHDKAVA 487
Cdd:TIGR00618 624 EQDL--QDVRL----------HLQQCSQELALKLTALHALQLT----LTQERVREHALSIRVLPKELLasRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 488 LERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTcqNLQWLKEEMET 567
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART--VLKARTEAHFN 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 568 KFSRWQKEQESI--IQQLQTSLHDRNKEVEDLSATLLCKLgpgqSEIAEELCQRLQrkERMLQDLLSDRNKQVLEHEMEI 645
Cdd:TIGR00618 766 NNEEVTAALQTGaeLSHLAAEIQFFNRLREEDTHLLKTLE----AEIGQEIPSDED--ILNLQCETLVQEEEQFLSRLEE 839
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 525313637 646 QGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQ 693
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQ 887
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
395-1131 |
7.16e-10 |
|
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: 64.61 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 395 KHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQ---------------------HLNHSLSHKEQLLQEF 453
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeeyllylDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 454 RELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEAT 533
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 534 MQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHD----RNKEVEDLSATLLCKLGPGQ 609
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLeserLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 610 SEiaeelcQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQ---ALRQYLGG 686
Cdd:pfam02463 406 EA------QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKkseDLLKETQL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 687 RDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEdvsiPRSTLGDLDTVAGLEKELSNAKEELELMA 766
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIS----AHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 767 KK------ERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQmQLVDPEDIPAMERLTQEVLLLREK 840
Cdd:pfam02463 556 TAdeveerQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK-ATLEADEDDKRAKVVEGILKDTEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 841 VASVESQGQEISGNRRQQlllMLEGLVDERSRLNEALQAERQLYSSLVKFHAHPESSERDRTLQVELEGAQVLRSRLEEV 920
Cdd:pfam02463 635 TKLKESAKAKESGLRKGV---SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 921 LGRSLERLNRLETLAAIGGAAAGDDTEDTSTEFTDSIEEEAAHHSHQQLVKVALEKSLATVETQNpsfsppSPMGGDSNR 1000
Cdd:pfam02463 712 LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL------AEEREKTEK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1001 CLQEEMLHLRAEFHQHLEEKRKAEEELKELKAQIEEAGFSSVSHIRNTMLSlcLENAELKEQMGEAMSDGWEIEEDKEKG 1080
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE--ELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 525313637 1081 EVMVETVVTKEGLSESSLQAEFRKLQGKLKNAHNIinlLKEQLVLSSKEGN 1131
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEE---KKELEEESQKLNL 911
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-838 |
2.75e-09 |
|
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: 62.83 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 17 KENFSLKLRIYFLEER-MQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTwADVENLNSQNEAELRRQFEERQ 95
Cdd:pfam15921 73 KEHIERVLEEYSHQVKdLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAM-ADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 96 QETEHVYELLENKI-----QLLQEESRLAKNEAARM---AALVEAEKECNLELSEKLKGVTKNWEDVpGDQVkpdqyTEA 167
Cdd:pfam15921 152 HELEAAKCLKEDMLedsntQIEQLRKMMLSHEGVLQeirSILVDFEEASGKKIYEHDSMSTMHFRSL-GSAI-----SKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 168 LAQRDKRIEELNQSLAAQERLVEQLSREKQQLLhlleeptsmevqpmteELLKQQKLNSHETTITQQSVsdsHLAELQEK 247
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKI----------------ELLLQQHQDRIEQLISEHEV---EITGLTEK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 248 IQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQviegqndtmAKLREMLHQSQLGQLH 327
Cdd:pfam15921 287 ASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE---------DKIEELEKQLVLANSE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 328 SSEGTSPAQQqvalLDLQSALFCSQLeiQKLQRVVRQKERQLAdakqcvqfveaaaHESEQQKEAsWKHN-------QEL 400
Cdd:pfam15921 358 LTEARTERDQ----FSQESGNLDDQL--QKLLADLHKREKELS-------------LEKEQNKRL-WDRDtgnsitiDHL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 401 RKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQR 480
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 481 IHDKAVALEraidEKFSALEEKEKELRQLRLAVRERDHDLERLR---DVLSSNEATMQSMESLLRAKGLEVEQLSTTCQN 557
Cdd:pfam15921 498 VSDLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 558 LQWLKEEMETKFSRWQKEQesiiQQLQTSLHDRNKEVEDLSatLLCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQ 637
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEK----AQLEKEINDRRLELQEFK--ILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRA 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 638 VLEHEMEIQGLLQSVSTREQESQAAAEKLvqALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTPTGRLGKQTDQGS 717
Cdd:pfam15921 648 VKDIKQERDQLLNEVKTSRNELNSLSEDY--EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 718 MQIpsrddstSLTAKEDVSIPRSTLGDLDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAAD 796
Cdd:pfam15921 726 MKV-------AMGMQKQITAKRGQIDALQSkIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ 798
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 525313637 797 MESLTRNIQIKEDLIKDLQMQLVDPEDIpaMERLTQEVLLLR 838
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASLQFAECQDI--IQRQEQESVRLK 838
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1-579 |
3.70e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.05 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1 MSNGYRTLSQHLNDLKKENFSLKLRIYFLEERMQQK---YEASREDIYKRNIELKVEVESLKRELQD-----KKQHLDKT 72
Cdd:pfam05483 76 LSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENrkiIEAQRKAIQELQFENEKVSLKLEEEIQEnkdliKENNATRH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 73 WADVENLNSQNEAELRRQFEERQQETEHVYELLENKIqllqeESRLAKNEAARMAAlveaeKECNLELSEKLKgvtknwE 152
Cdd:pfam05483 156 LCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNI-----EKMILAFEELRVQA-----ENARLEMHFKLK------E 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 153 DVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLS---REKQQLLHLLEEPTSMEVQPMTEELLKQQKLNshet 229
Cdd:pfam05483 220 DHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTfllEESRDKANQLEEKTKLQDENLKELIEKKDHLT---- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 230 titqqsvsdSHLAELQEKIQQTEATNKILQEKLN-------EMSYELKCAQESSQKQDGT----IQNLKETLKSRERETE 298
Cdd:pfam05483 296 ---------KELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 299 ELYQVIEGQNDTMAKLREMLhqsqlgQLHSSEgtspaqqqvaLLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQcvqf 378
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMEL------QKKSSE----------LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ---- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 379 VEAAAHESEQQKeaswkhnQELRKALQQLQEELQNKSQQLRA------WEAEKYNEIRTQEQNIQHLNHSL-SHKEQLLQ 451
Cdd:pfam05483 427 FEKIAEELKGKE-------QELIFLLQAREKEIHDLEIQLTAiktseeHYLKEVEDLKTELEKEKLKNIELtAHCDKLLL 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 452 EFRELLQyrDNSDKTLEanemlLEKLRQRIHDKAVALERAIdEKFSALEEKEKELRQLRLAVRER-DHDLERLRDVLSSN 530
Cdd:pfam05483 500 ENKELTQ--EASDMTLE-----LKKHQEDIINCKKQEERML-KQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKS 571
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 525313637 531 EATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESI 579
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
50-602 |
4.32e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 50 ELKVEVESLKRELQDKKQHLDKTWADVENLNSQ----------NEAELRRQFEERQQETEHVYELLeNKIQLLQEESRLA 119
Cdd:TIGR04523 79 ILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEikndkeqknkLEVELNKLEKQKKENKKNIDKFL-TEIKKKEKELEKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 120 KNEAARMAALVEA-EKECNLELSEKLKgVTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQ 198
Cdd:TIGR04523 158 NNKYNDLKKQKEElENELNLLEKEKLN-IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 199 LLHLLEEptsmevqpmteellKQQKLNSHETTITQQSVSDSH-LAELQEKIQQTEATNKILQEKLNEMS-YELKCAQESS 276
Cdd:TIGR04523 237 KQQEINE--------------KTTEISNTQTQLNQLKDEQNKiKKQLSEKQKELEQNNKKIKELEKQLNqLKSEISDLNN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 277 QKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREmlhqsQLGQLHSSegtspaqqqvaLLDLQSALFCSQLEIQ 356
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE-----QISQLKKE-----------LTNSESENSEKQRELE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 357 KLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQ---LRAWEAEKYNEIRTQE 433
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEierLKETIIKNNSEIKDLT 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 434 QNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANemlLEKLRQRIHDKAVALERAIDEKfSALEEKEKELRQLRLAV 513
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISSL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 514 RERDHDLE----RLRDVLSSNEATMQSMESLLRAKGLEvEQLSTTCQNLQWLKEEmETKFSRWQKEQESIIQQLQTSLHD 589
Cdd:TIGR04523 523 KEKIEKLEsekkEKESKISDLEDELNKDDFELKKENLE-KEIDEKNKEIEELKQT-QKSLKKKQEEKQELIDQKEKEKKD 600
|
570
....*....|...
gi 525313637 590 RNKEVEDLSATLL 602
Cdd:TIGR04523 601 LIKEIEEKEKKIS 613
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-524 |
9.29e-09 |
|
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: 61.24 E-value: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 210 EVQPMTEELLKQQKLnsHETTITQQSVSDSHLAELQEKIQQteatnkiLQEKLNEMSYELKCAQESSQKQDGTIQNLKET 289
Cdd:TIGR02169 675 ELQRLRERLEGLKRE--LSSLQSELRRIENRLDELSQELSD-------ASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 290 LKSRERETEELYQVIEGQNDTMAKLREMLH--QSQLGQLHSSEGTSPAQQQVALL---------------DLQSALFCSQ 352
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHklEEALNDLEARLSHSRIPEIQAELskleeevsriearlrEIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 353 LEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAekynEIRTQ 432
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA----QLREL 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 433 EQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLE----------ANEMLLEKLRQRIHDKAVALE-------RAIDE- 494
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipEEELSLEDVQAELQRVEEEIRalepvnmLAIQEy 981
|
330 340 350
....*....|....*....|....*....|....*
gi 525313637 495 -----KFSALEEKEKELRQLRLAVRERDHDLERLR 524
Cdd:TIGR02169 982 eevlkRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-1036 |
1.86e-08 |
|
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: 60.08 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 92 EERQQETEHVYELLENKIQLLQEEsrlaKNEAARMAALVEAEKEcnLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQR 171
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKRE--YEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 172 DKRIEELNQSLAAQERLVEQLSREkqqllhlleeptsmeVQPMTEELLKQQKLNSHETTITQQSVSDShLAELQEKIQQT 251
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKK---------------IKDLGEEEQLRVKEKIGELEAEIASLERS-IAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 252 EATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLhqsqlgqlhsseg 331
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL------------- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 332 tspAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEaswkhnqELRKALQQLQEEL 411
Cdd:TIGR02169 388 ---KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE-------DKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 412 QNKSQQLRAWEAEKYNeirtQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERa 491
Cdd:TIGR02169 458 EQLAADLSKYEQELYD----LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 492 IDEKFSALEEKEKELRqLRLAVRERDHDLERLRDVLSSNEATMQSMESL--LRAKGLEVEQLSTT-----CQNLQWLKEE 564
Cdd:TIGR02169 533 VGERYATAIEVAAGNR-LNNVVVEDDAVAKEAIELLKRRKAGRATFLPLnkMRDERRDLSILSEDgvigfAVDLVEFDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 565 METKFsrWQKEQESIIqqlqtslhdrnkeVEDLsatllcklgpgqseiaeELCQRLQRKERMLQ---DLLSDRNKQVLEH 641
Cdd:TIGR02169 612 YEPAF--KYVFGDTLV-------------VEDI-----------------EAARRLMGKYRMVTlegELFEKSGAMTGGS 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 642 EMEIQGLLQSVSTREQESQAAAEklvqaLMERNSELQALRQYLGGRDSLMSQAPISNQQAEvtptgrlgkqtdqgsmqip 721
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRER-----LEGLKRELSSLQSELRRIENRLDELSQELSDAS------------------- 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 722 srddstsltakedvsiprstlgdldtvagleKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLT 801
Cdd:TIGR02169 716 -------------------------------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 802 RNIQIKEDLIKDLQMQLVDPEDIPAMER---LTQEVLLLREKVASVESQGQEISG--NRRQQLLLMLEGLVDERSRLNEA 876
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSHSRipeIQAELSKLEEEVSRIEARLREIEQklNRLTLEKEYLEKEIQELQEQRID 844
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 877 LQAERqlysslVKFHAHPESSE-RDRTLQVELEGAQV----LRSRLEEVLGRSLERLNRLETLaaiggaaagddtEDTST 951
Cdd:TIGR02169 845 LKEQI------KSIEKEIENLNgKKEELEEELEELEAalrdLESRLGDLKKERDELEAQLREL------------ERKIE 906
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 952 EFTDSIEEEAAHHSHQQLVKVALEKSLATVETQNPSFSPPSPMGGDSnRCLQEEMLHLRAEFH----------QHLEEKR 1021
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRalepvnmlaiQEYEEVL 985
|
970
....*....|....*
gi 525313637 1022 KAEEELKELKAQIEE 1036
Cdd:TIGR02169 986 KRLDELKEKRAKLEE 1000
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-554 |
2.10e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 31 ERMQQKYEASREDIyKRNIELKVEVESLKReLQDKKQHLDKTWADVENLNSQNE-AELRRQ--------FEERQQETEHv 101
Cdd:PRK02224 179 ERVLSDQRGSLDQL-KAQIEEKEEKDLHER-LNGLESELAELDEEIERYEEQREqARETRDeadevleeHEERREELET- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 102 yelLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEE-LNQ 180
Cdd:PRK02224 256 ---LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 181 SLAAQERLVEQLSREKQQLLHLLEEPTsmEVQPMTEELlkQQKLNSHETTITQQSvsdSHLAELQEKIQQTEATNKILQE 260
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAE--ELREEAAEL--ESELEEAREAVEDRR---EEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 261 KLNEMSYELKCAQESSQKQDGTIQNLKETLKS---RERETEELYQ------------------VIEGQNDTMAKLREMLH 319
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTareRVEEAEALLEagkcpecgqpvegsphveTIEEDRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 320 QSQLGQ------LHSSEGTSPAQQQVALLDLQSALFCSQLEIQKlqRVVRQKERQLADAKQCVQFVEAAAHESEQQKEAS 393
Cdd:PRK02224 486 DLEEEVeeveerLERAEDLVEAEDRIERLEERREDLEELIAERR--ETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 394 WKHNQELRKALQQLQEELQNKSQQLRAWE--AEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEA-- 469
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAef 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 470 NEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRakglEVE 549
Cdd:PRK02224 644 DEARIEEARED-KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYD----EAE 718
|
....*
gi 525313637 550 QLSTT 554
Cdd:PRK02224 719 ELESM 723
|
|
| Olduvai |
pfam06758 |
Olduvai domain; This domain formerly known as DUF1220 or NBPF domain has been renamed as the ... |
1552-1621 |
4.98e-08 |
|
Olduvai domain; This domain formerly known as DUF1220 or NBPF domain has been renamed as the Olduvai domain. It is found highly duplicated in the human lineage.
Pssm-ID: 429104 [Multi-domain] Cd Length: 68 Bit Score: 51.65 E-value: 4.98e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1552 DHKSEKDQaglEPLALRLSRELQEKEKViEVLQAKLDARSLTPSSSHALSDSHRSPSSTSFLSDELEACS 1621
Cdd:pfam06758 1 DEEEEEDQ---EPLAPRLSRELPEVEEQ-EVPQDSLDECYLTPSVLPDLSDSYQPYRSTIFSFEEQQVSS 66
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
30-516 |
1.19e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 30 EERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLE-NK 108
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKK 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 109 IQLLQEESRLAKNEAARMAALVEAEKECNlELSEKLKGVTKNWE-DVPGDQVKPDQYTEALAQRDKRIEELNQSlAAQER 187
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEAKKAEEAKKK-AEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 188 LVEQLSREKQQLLHLLE-EPTSMEVQPMTEELLK--QQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNE 264
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEaKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 265 M--SYELKCAQESSQKQDGtiQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALL 342
Cdd:PTZ00121 1551 LkkAEELKKAEEKKKAEEA--KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 343 DlQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEA--SWKHNQELRKALQQL--QEELQNKSQQL 418
Cdd:PTZ00121 1629 E-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALkkEAEEAKKAEEL 1707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 419 RAWEAEkynEIRTQEQNIQHLNHSLSHKEQLLQEFREllqyRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSA 498
Cdd:PTZ00121 1708 KKKEAE---EKKKAEELKKAEEENKIKAEEAKKEAEE----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
490
....*....|....*...
gi 525313637 499 LEEKEKELRQLRLAVRER 516
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDK 1798
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
10-582 |
1.54e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 10 QHLNDLKKENFSLKLRIYFLEERMQQK---YEASREDIYKRNIELKVEVESLKrELQDKKQHLDKTWADVEnLNSQNEAE 86
Cdd:pfam05483 233 KEINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIK-MSLQRSMS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 87 LRRQFEERQQ-ETEHVYELLENKIQLLQEesrlaKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKpdQYT 165
Cdd:pfam05483 311 TQKALEEDLQiATKTICQLTEEKEAQMEE-----LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLK--IIT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 166 EALAQRDKRIEELNQSLAAQERLVEQLSR---EKQQLLHLLE--EPTSMEVQPMTEELL-----KQQKLNSHETTITQQS 235
Cdd:pfam05483 384 MELQKKSSELEEMTKFKNNKEVELEELKKilaEDEKLLDEKKqfEKIAEELKGKEQELIfllqaREKEIHDLEIQLTAIK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 236 VSDSH----LAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTM 311
Cdd:pfam05483 464 TSEEHylkeVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKE 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 312 AKLREMLHQSQLGQLHSSEGTspaqqqvalldlqsalfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKE 391
Cdd:pfam05483 544 MNLRDELESVREEFIQKGDEV-------------------KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 392 ASWKHNQELRKALQQLQEELQNKSQQLRAWEAeKYNEIRTQEQNIQhlnhslshkeqllQEFRELLqyrDNSDKTLEANE 471
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSAENKQLNAYEI-KVNKLELELASAK-------------QKFEEII---DNYQKEIEDKK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 472 MLLEKLRQRIH------DKAVALERAIDEK-------FSALEEKEKElrQLRLAVRERDHDLERLRDVLSSNEATMQSME 538
Cdd:pfam05483 668 ISEEKLLEEVEkakaiaDEAVKLQKEIDKRcqhkiaeMVALMEKHKH--QYDKIIEERDSELGLYKNKEQEQSSAKAALE 745
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 525313637 539 SLLraKGLEVEQLSTTCQnLQWLKEEMEtKFSRWQKEQESIIQQ 582
Cdd:pfam05483 746 IEL--SNIKAELLSLKKQ-LEIEKEEKE-KLKMEAKENTAILKD 785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
58-559 |
1.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 58 LKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECN 137
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 138 L-ELSEKLKGVTKNWEDVpgdqvkPDQYtEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTE 216
Cdd:COG4717 127 LlPLYQELEALEAELAEL------PERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 217 ELLKQQKLnshettitqqsvsdshLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKET----LKS 292
Cdd:COG4717 200 ELEELQQR----------------LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallaLLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 293 RERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSS-EGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVrQKERQLAD 371
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLgKEAEELQALPALEELEEEELEELLAALGLPPDL-SPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 372 AKQCVQFVEAAAHESEQQKEASWKHNQELRKALqqLQEELQNKSQQLRAWeAEKYNEIRTQEQNIQHLNHSLshkEQLLQ 451
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAA-LEQAEEYQELKEELEELEEQL---EELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 452 EFRELLQYRDnsdktleanemlLEKLRQRIHDKAVALErAIDEKFSALEEKEKELRQlRLAVRERDHDLERLRDVLSSNE 531
Cdd:COG4717 417 ELEELLEALD------------EEELEEELEELEEELE-ELEEELEELREELAELEA-ELEQLEEDGELAELLQELEELK 482
|
490 500
....*....|....*....|....*...
gi 525313637 532 ATMQSMESLLRAKGLEVEQLSTTCQNLQ 559
Cdd:COG4717 483 AELRELAEEWAALKLALELLEEAREEYR 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
290-791 |
2.53e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 290 LKSRERETEELYQVIEGQND-----TMAKLREMLHQS---QLGQLHSSEGTSPAQQQVALLDLQSAL---FCSQLEIQKL 358
Cdd:COG4717 14 FRDRTIEFSPGLNVIYGPNEagkstLLAFIRAMLLERlekEADELFKPQGRKPELNLKELKELEEELkeaEEKEEEYAEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 359 QRVVRQKERQLADAKQcvqfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEaEKYNEIRTQEQNIQH 438
Cdd:COG4717 94 QEELEELEEELEELEA-----ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE-ERLEELRELEEELEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 439 LNHSLSHKEQLLQEfrellQYRDNSDKTLEANEMLLEKLrQRIHDKAVALERAIDEKFSALEEKEKELRQLRlAVRERDH 518
Cdd:COG4717 168 LEAELAELQEELEE-----LLEQLSLATEEELQDLAEEL-EELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 519 DLERLRDVLSSNEATmqSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEvEDLS 598
Cdd:COG4717 241 LEERLKEARLLLLIA--AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL-EELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 599 ATLLCKL-------GPGQSEIAEELCQRLQRKERMLQDLLSDRNK-QVLEHEMEIQGLLQSVSTREQESQAAAEKLVQAL 670
Cdd:COG4717 318 EEELEELlaalglpPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 671 MERNSELQALRQYLGgrdslmSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTS--LTAKEDVSIPRSTLGDLDTV 748
Cdd:COG4717 398 QELKEELEELEEQLE------ELLGELEELLEALDEEELEEELEELEEELEELEEELEelREELAELEAELEQLEEDGEL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 525313637 749 AGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQ 791
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5-579 |
2.66e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 5 YRTLSQHLNDLKKEnfsLKLRIYFLEermqqKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLnsqne 84
Cdd:PRK03918 160 YENAYKNLGEVIKE---IKRRIERLE-----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKL----- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 85 aelrrqfEERQQETEHVYELLEN-KIQLLQEESRLAKNEaarmAALVEAEKECNlELSEKLKGVTKNWEDVPGDQVKPDQ 163
Cdd:PRK03918 227 -------EKEVKELEELKEEIEElEKELESLEGSKRKLE----EKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 164 YTEALAQRDKRIEELNQSlaaqERLVEQLSREKQQLLHLLEEPTSMEVQpmTEELLKQQKLNSHETTITQQSVSDSHLA- 242
Cdd:PRK03918 295 YIKLSEFYEEYLDELREI----EKRLSRLEEEINGIEERIKELEEKEER--LEELKKKLKELEKRLEELEERHELYEEAk 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 243 ELQEKIQQTEATNKILQ-EKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREML--- 318
Cdd:PRK03918 369 AKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELtee 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 319 HQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKlqrvVRQKERQLADAKQCVQFVEAAAHESE----QQKEASW 394
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK----VLKKESELIKLKELAEQLKELEEKLKkynlEELEKKA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 395 KHNQELRKALQQLQEELQN------KSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHK-----EQLLQEFRELLQYRD-- 461
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSlkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELgfesvEELEERLKELEPFYNey 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 462 ----NSDKTLEANEMLLEKLRqrihDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHdlERLRDVLSSNEATMQSM 537
Cdd:PRK03918 605 lelkDAEKELEREEKELKKLE----EELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGL 678
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 525313637 538 ESllRAKGLEvEQLSTTCQNLQWLKEEMEtKFSRWQKEQESI 579
Cdd:PRK03918 679 RA--ELEELE-KRREEIKKTLEKLKEELE-EREKAKKELEKL 716
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-1037 |
3.21e-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: 56.23 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 268 ELKCAQESSQKQDGTIQNLKETLK--SRERETEELYQviegqnDTMAKLREMlhqsqlgqlhssEGTSPAQQQVALLDLQ 345
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQ------ALLKEKREY------------EGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 346 SALfcsQLEIQKLQRVVRQKERQLAD-AKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAE 424
Cdd:TIGR02169 240 EAI---ERQLASLEEELEKLTEEISElEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 425 KYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEK 504
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 505 ----------ELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSttcQNLQWLKEEMETKFSRWQK 574
Cdd:TIGR02169 397 lkreinelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE---WKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 575 EQESiIQQLQTSLHDRNKEVEDLSATL--LCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSV 652
Cdd:TIGR02169 474 LKEE-YDRVEKELSKLQRELAEAEAQAraSEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 653 STreqESQAAAEKLVQALMERNselqalrqylGGRdslMSQAPISNQQAEVTPTGRLGKQTDQG-SMQIPSRDD------ 725
Cdd:TIGR02169 553 VV---EDDAVAKEAIELLKRRK----------AGR---ATFLPLNKMRDERRDLSILSEDGVIGfAVDLVEFDPkyepaf 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 726 -----STSLTakEDVSIPRSTLGDLDTVAgLEKEL----------SNAKEELELMAKKERESQMELSA-LQSMmavqEEE 789
Cdd:TIGR02169 617 kyvfgDTLVV--EDIEAARRLMGKYRMVT-LEGELfeksgamtggSRAPRGGILFSRSEPAELQRLRErLEGL----KRE 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 790 LQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDipAMERLTQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDE 869
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEK--EIEQLEQEEEKLKERLEELEEDLSSLE-QEIENVKSELKELEAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 870 RSRLNEALQAERQlysSLVKFHAHPeSSERDRTLQVELEGAQVLRSRLEEVLgRSLERLNRLETLAAIGGAAAGDDTEDT 949
Cdd:TIGR02169 767 IEELEEDLHKLEE---ALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARL-REIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 950 STEFTDSIEEEAAHHSHQQLVKVALEKSLATVETQnpsfsppspmggdsNRCLQEEMLHLRAEFHQHLEEKRKAEEELKE 1029
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA--------------LRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
....*...
gi 525313637 1030 LKAQIEEA 1037
Cdd:TIGR02169 908 LEAQIEKK 915
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
29-829 |
4.11e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.82 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 29 LEERmQQKYEASREDIYKRNIELKvEVESLKRELQDKKQHLDKTWADV-----ENLNS--QNEAELRRQFEERQQETEHV 101
Cdd:TIGR00606 250 LKNR-LKEIEHNLSKIMKLDNEIK-ALKSRKKQMEKDNSELELKMEKVfqgtdEQLNDlyHNHQRTVREKERELVDCQRE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 102 YELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLE-----LSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIE 176
Cdd:TIGR00606 328 LEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdsliQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 177 ELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDS-HLAELQEKIQQTEATN 255
Cdd:TIGR00606 408 KTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSdRILELDQELRKAEREL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 256 KILQEKLNE--MSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLG--QLHSSEG 331
Cdd:TIGR00606 488 SKAEKNSLTetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHsdELTSLLG 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 332 TSPAQQQValldlqsalfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAH------ESEQQKEASWKHN-------Q 398
Cdd:TIGR00606 568 YFPNKKQL------------EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNhinnelESKEEQLSSYEDKlfdvcgsQ 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 399 ELRKALQQLQEELQNKSQQLRAWEAEK------YNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKT-LEANE 471
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSKQRAMLAGATavysqfITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 472 MLLEKLRQRIHDKAVALERaideKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQS-MESLLRAKGLEVEq 550
Cdd:TIGR00606 716 SELKKKEKRRDEMLGLAPG----RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTiMPEEESAKVCLTD- 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 551 lSTTCQNLQWLKEEMETKFSRWQKEQESIiqQLQTSLHDRNKEVEDlsatllcklgpgqseiAEELCQRLQRKERMLQDL 630
Cdd:TIGR00606 791 -VTIMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQE----------------KQHELDTVVSKIELNRKL 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 631 LSDRNKQVLEHEMEIQGLLQ---SVSTREQESQAAAEKLVqalmERNSELQALRQylggrdslmsqaPISNQQAEVTPTG 707
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLV----ELSTEVQSLIR------------EIKDAKEQDSPLE 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 708 RLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRStlgDLDTVAGLEKELSNAKEELELMAKKERESqmELSALQSMMAVQE 787
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKE---KVKNIHGYMKDIENKIQDGKDDYLKQKET--ELNTVNAQLEECE 990
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 525313637 788 EELQVQAADMESLTRNI---QIKEDLIKDLQMQLVDPEDIPAMER 829
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdtqKIQERWLQDNLTLRKRENELKEVEE 1035
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-455 |
6.95e-07 |
|
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: 54.00 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 241 LAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLhQ 320
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-A 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 321 SQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLeIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL 400
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313637 401 RKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRE 455
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
223-693 |
1.04e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 223 KLNSHETTITQqsvSDSHLAELQEKIQQTEATNKILQEKLNEmsYELKcaQESSQKQDGTIQNLKETLKSRERETEELYQ 302
Cdd:PRK02224 207 RLNGLESELAE---LDEEIERYEEQREQARETRDEADEVLEE--HEER--REELETLEAEIEDLRETIAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 303 VIEGQNDTMAKLREMLHqsqlGQLHSSEGTSPAQQqvALLDLQSALfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAA 382
Cdd:PRK02224 280 EVRDLRERLEELEEERD----DLLAEAGLDDADAE--AVEARREEL---EDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 383 AHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAE------KYNEIRTQEQNIQHLNHSL-SHKEQLLQEFRE 455
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelreRFGDAPVDLGNAEDFLEELrEERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 456 LLQYRDNSDKTLEANEMLLEKLR-----QRIHDKAVAleRAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDV---- 526
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAGKcpecgQPVEGSPHV--ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLveae 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 527 --LSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQK---EQESIIQQLQTSLHDRNKEVEDLSATL 601
Cdd:PRK02224 509 drIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERI 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 602 --LCKLGPGQSEIAE--ELCQRLQRKERMLQDL-------LSDRNKQVLEHEMEIQGllqsvsTREQESQAAAEKLVQAL 670
Cdd:PRK02224 589 esLERIRTLLAAIADaeDEIERLREKREALAELnderrerLAEKRERKRELEAEFDE------ARIEEAREDKERAEEYL 662
|
490 500
....*....|....*....|...
gi 525313637 671 MERNSELQALRQylgGRDSLMSQ 693
Cdd:PRK02224 663 EQVEEKLDELRE---ERDDLQAE 682
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-684 |
1.50e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 2 SNGYRTLSQHLNDLKKENFSLKLRIYFLEERMQQ-------------KYEASREDIYKRNIELKVEVESLKRELQDKKQH 68
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDaeerlakleaeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 69 LDKTWADVENLnsqnEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEkecnlelseklkgvt 148
Cdd:TIGR02169 366 LEDLRAELEEV----DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN--------------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 149 knwEDVPGDQVKPDQYTEALAQRDKRIEELNQSLaaqERLVEQLSREKQQLLHLLEEptsmevqpmteellkQQKLNshe 228
Cdd:TIGR02169 427 ---AAIAGIEAKINELEEEKEDKALEIKKQEWKL---EQLAADLSKYEQELYDLKEE---------------YDRVE--- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 229 ttitqqsvsdSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETE-----ELYQV 303
Cdd:TIGR02169 483 ----------KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnRLNNV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 304 IEGQNDTMAKLREMLHQSQLGQL----------HSSEGTSPAQQQVA--LLDL---------------QSALFCSQLEIQ 356
Cdd:TIGR02169 553 VVEDDAVAKEAIELLKRRKAGRAtflplnkmrdERRDLSILSEDGVIgfAVDLvefdpkyepafkyvfGDTLVVEDIEAA 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 357 KLQ----RVVRQKERQL---------ADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEA 423
Cdd:TIGR02169 633 RRLmgkyRMVTLEGELFeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 424 EKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYrdnSDKTLEANEMLLEKLRQRIHDKavalERAIDEKFSALEEKE 503
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS---LEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 504 KELRQLRlaVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIiqql 583
Cdd:TIGR02169 786 ARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL---- 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 584 qtslhdrNKEVEDLsatllcklgpgQSEIAEelcqrLQRKERMLQDLLSDRNKQVLEHEMEiqglLQSVSTREQESQAAA 663
Cdd:TIGR02169 860 -------NGKKEEL-----------EEELEE-----LEAALRDLESRLGDLKKERDELEAQ----LRELERKIEELEAQI 912
|
730 740
....*....|....*....|.
gi 525313637 664 EKLVQALMERNSELQALRQYL 684
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEEL 933
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
257-694 |
1.82e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 257 ILQEKLNEMSYEL-KCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMlhQSQLGQLhssegtspa 335
Cdd:COG4717 46 MLLERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--EAELEEL--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 336 QQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKeaswkhnQELRKALQQLQEELQNKS 415
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE-------AELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 416 QQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEK 495
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 496 FSALEEKEKELRQLRLAVRErdHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqWLKEEMETKFSRWQKE 575
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLA--LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL-GLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 576 QESIIQQLQTSLHDRNKEV-----EDLSATLLCKLGPGQSEIAEELCQRLQRKERmLQDLLSDRNKQVLEHEMEIQGLLQ 650
Cdd:COG4717 345 RIEELQELLREAEELEEELqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 525313637 651 SVSTREQESQaaAEKLVQALMERNSELQALRQYLGGRDSLMSQA 694
Cdd:COG4717 424 ALDEEELEEE--LEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-484 |
2.72e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 34 QQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNS-----QNEAELRRQFEERQQETEHVYELLENK 108
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 109 IQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQvkpDQYTEALAQRDKRIEELNQSLAA--QE 186
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL---AELEEELEEAQEELEELEEELEQleNE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 187 RLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVsdSHLAELQEKIQQTEATNKILQEKLNEMS 266
Cdd:COG4717 236 LEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL--LALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 267 YELKcaqesSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALLDLQS 346
Cdd:COG4717 314 EELE-----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 347 ALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEAswkhnQELRKALQQLQEELQNKSQQLRAWEAeky 426
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL-----EELEEELEELEEELEELREELAELEA--- 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313637 427 nEIRTQEQniqhlNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDK 484
Cdd:COG4717 461 -ELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1841-2018 |
2.92e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1841 ADLLEEHLGEIRNLRQRLEESICINDRLREQLEHRLTSTARGRGSTSNFYSQGLESIPQLCNENRVLREDNRRLQAQLSH 1920
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1921 VSREHSQET---ESLREALLSSRSHLQELEKELEHQKVERQQLLEDLREKQQEVLHFREERLSLQENDSRLQHKLVLLQQ 1997
Cdd:COG1196 321 LEEELAELEeelEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180
....*....|....*....|.
gi 525313637 1998 QCEEKQQLFESLQSELQIYEA 2018
Cdd:COG1196 401 QLEELEEAEEALLERLERLEE 421
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
169-547 |
3.05e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 169 AQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE---------PTSMEVQPMTEELLKQQKLNSHETtitqqsvsds 239
Cdd:PRK04863 782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAfsrfigshlAVAFEADPEAELRQLNRRRVELER---------- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 240 HLAELQEKIQQTEATNKILQEKLNEMSyelKCAQESSQKQDgtiqnlkETLKSRERETEElyQVIEGQNdtmAKLREMLH 319
Cdd:PRK04863 852 ALADHESQEQQQRSQLEQAKEGLSALN---RLLPRLNLLAD-------ETLADRVEEIRE--QLDEAEE---AKRFVQQH 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 320 QSQLGQLhssegtspaQQQVALLDlqsalfCSQLEIQKLQRVVRQKERQLADAKQCV----QFVEAAAH----ESEQQKE 391
Cdd:PRK04863 917 GNALAQL---------EPIVSVLQ------SDPEQFEQLKQDYQQAQQTQRDAKQQAfaltEVVQRRAHfsyeDAAEMLA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 392 ASWKHNQELRKALQQLQEELQNKSQQLRAWEAE--KYNEIRTQeqniqhLNHSLSHKEQLLQEFRELLQyrdnsDKTLEA 469
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQlaQYNQVLAS------LKSSYDAKRQMLQELKQELQ-----DLGVPA 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 470 NEMLLEKLRQRiHDKAVALERAIDEKFSALEEK----EKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKG 545
Cdd:PRK04863 1051 DSGAEERARAR-RDELHARLSANRSRRNQLEKQltfcEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNG 1129
|
..
gi 525313637 546 LE 547
Cdd:PRK04863 1130 VE 1131
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
358-849 |
3.30e-06 |
|
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: 52.44 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 358 LQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRaweaEKYNEIRTQEQNIQ 437
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR----EQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 438 HLNHSLSHKEQLL-----------QEFRELLQYRDNSDKTLEANEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKEL 506
Cdd:pfam05557 87 ALNKKLNEKESQLadarevisclkNELSELRRQIQRAELELQSTNSELEELQER-LDLLKAKASEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 507 RQLRLAVRERDHDLERLRD----VLSSNE--ATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEE---METKFSRWQKEQE 577
Cdd:pfam05557 166 AEAEQRIKELEFEIQSQEQdseiVKNSKSelARIPELEKELERLREHNKHLNENIENKLLLKEEvedLKRKLEREEKYRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 578 SII------QQLQTSLHDRNKEVEDLSATLlcklgPGQSEIAEELCQrLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQS 651
Cdd:pfam05557 246 EAAtlelekEKLEQELQSWVKLAQDTGLNL-----RSPEDLSRRIEQ-LQQREIVLKEENSSLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 652 VS----------TREQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQ---------------------- 699
Cdd:pfam05557 320 LAqylkkiedlnKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQllerieeaedmtqkmqahneem 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 700 -----QAEVTPTG-RLGKQTDQGSMQIPSRDDST--SLTAKEDVSIPRStlgDLDTVAGLEKELSNAKEELEL-MAKKER 770
Cdd:pfam05557 400 eaqlsVAEEELGGyKQQAQTLERELQALRQQESLadPSYSKEEVDSLRR---KLETLELERQRLREQKNELEMeLERRCL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 771 ESQMELS---ALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIP--AMERLTQEVLLLREKVASVE 845
Cdd:pfam05557 477 QGDYDPKktkVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPetTSTMNFKEVLDLRKELESAE 556
|
....
gi 525313637 846 SQGQ 849
Cdd:pfam05557 557 LKNQ 560
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
63-622 |
3.68e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 63 QDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLaKNEAARMAALVEAEKECNLELSE 142
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQEL-EEILHELESRLEEEEERSQQLQN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 143 KLKGVTKNWEDVPgDQVKPDQYTEALAQRDK-----RIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMevqpMTEE 217
Cdd:pfam01576 97 EKKKMQQHIQDLE-EQLDEEEAARQKLQLEKvtteaKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN----LAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 218 LLKQQKL----NSHETTITqqsvsdshlaELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSR 293
Cdd:pfam01576 172 EEKAKSLsklkNKHEAMIS----------DLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 294 ERETEELYQVIEGQ----NDTMAKLREML-HQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKL-------QRV 361
Cdd:pfam01576 242 EEELQAALARLEEEtaqkNNALKKIRELEaQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaqQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 362 VRQKERQLADAKQCVQfVEAAAHESeQQKEASWKHNQELRKALQQLQEELQNKS------QQLRAWEAEKYNEIRTQEQN 435
Cdd:pfam01576 322 RSKREQEVTELKKALE-EETRSHEA-QLQEMRQKHTQALEELTEQLEQAKRNKAnlekakQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 436 IQHLNHSLSHKEQLLQEfrelLQYRDNSDktleanemllEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRE 515
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQE----LQARLSES----------ERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 516 RDHDLERLRDVLSsnEATMQSMESLLRAKGLEVEQLSTTCQnlqwLKEEMETKfsrwqKEQESIIQQLQTSLHDRNKEVE 595
Cdd:pfam01576 466 LESQLQDTQELLQ--EETRQKLNLSTRLRQLEDERNSLQEQ----LEEEEEAK-----RNVERQLSTLQAQLSDMKKKLE 534
|
570 580
....*....|....*....|....*..
gi 525313637 596 DLSATLlcklgpgqsEIAEELCQRLQR 622
Cdd:pfam01576 535 EDAGTL---------EALEEGKKRLQR 552
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
29-666 |
6.40e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 29 LEERMQQKYEA--SREDIYKRNIELKVEVESLKRELQDKKQHLD-------------------KTWADVENLNSQNEAEL 87
Cdd:COG3096 363 LEEQEEVVEEAaeQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqqavqalekaRALCGLPDLTPENAEDY 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 88 RRQFEERQQE-TEHVYELlenkiqllqeESRLAKNEAARmaalveAEKECNLELSEKLKG-VTKNWEDVPGDQV---KPD 162
Cdd:COG3096 443 LAAFRAKEQQaTEEVLEL----------EQKLSVADAAR------RQFEKAYELVCKIAGeVERSQAWQTARELlrrYRS 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 163 QytEALAQRDKRIE----ELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSD 238
Cdd:COG3096 507 Q--QALAQRLQQLRaqlaELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 239 SHLAELQEKIQQTEATNKI---LQEKLNEMSYELKCAQESSQKQDGTIQNLKEtlksRERETEELYQVIEGQNDTMAKLR 315
Cdd:COG3096 585 QQLEQLRARIKELAARAPAwlaAQDALERLREQSGEALADSQEVTAAMQQLLE----REREATVERDELAARKQALESQI 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 316 EMLHQ------SQLGQLHSSEG---TSPAQQQVALLDLQ--SALFC---SQLEIQKLQRVVRQKErQLADAKQCVQFVE- 380
Cdd:COG3096 661 ERLSQpggaedPRLLALAERLGgvlLSEIYDDVTLEDAPyfSALYGparHAIVVPDLSAVKEQLA-GLEDCPEDLYLIEg 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 381 ------AAAHESEQQKEASWKHNQEL--------------RKALQQLQEELQNKSQQLraweAEKYNEIRTQEQNIQHLN 440
Cdd:COG3096 740 dpdsfdDSVFDAEELEDAVVVKLSDRqwrysrfpevplfgRAAREKRLEELRAERDEL----AEQYAKASFDVQKLQRLH 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 441 HSLShkeQLLQEFRELlqyrdnsdkTLEAN-EMLLEKLRQRIhdkavaleRAIDEKFSALEEKEKELRQLRLAVRER--- 516
Cdd:COG3096 816 QAFS---QFVGGHLAV---------AFAPDpEAELAALRQRR--------SELERELAQHRAQEQQLRQQLDQLKEQlql 875
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 517 ------------DHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQ---WLKEEMETKFSRWQKEQESIIQ 581
Cdd:COG3096 876 lnkllpqanllaDETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQ 955
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 582 QL-------QTSLH-------DRNKEVEDLSATLLCKLgpgqsEIAEELCQRLQRKERMLQDLLSDRNkQVLehemeiQG 647
Cdd:COG3096 956 QIfalsevvQRRPHfsyedavGLLGENSDLNEKLRARL-----EQAEEARREAREQLRQAQAQYSQYN-QVL------AS 1023
|
730
....*....|....*....
gi 525313637 648 LLQSVSTREQESQAAAEKL 666
Cdd:COG3096 1024 LKSSRDAKQQTLQELEQEL 1042
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-538 |
1.25e-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: 50.15 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 331 GTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEE 410
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 411 LQNKSQQLRAWEAEKYNEIRTQEQNIQH-------LNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQrihd 483
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313637 484 kavALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSME 538
Cdd:COG4942 168 ---ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-698 |
1.51e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 35 QKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEE---RQQETEHVYELLENKIQL 111
Cdd:PTZ00121 1176 KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEakkDAEEAKKAEEERNNEEIR 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 112 LQEESRLAknEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQ 191
Cdd:PTZ00121 1256 KFEEARMA--HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 192 LSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKlNEMSYELKC 271
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKK 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 272 AQESSQKQDGTIQNLKETLKSRE---------------------RETEELYQVIE---------GQNDTMAKLREMLHQS 321
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEakkkaeeakkadeakkkaeeaKKAEEAKKKAEeakkadeakKKAEEAKKADEAKKKA 1492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 322 QLGQLHSSEGTSPAQQQVALLDLQSALfcsqlEIQKLQRVVRQKERQLADAKQCVQFVEAAaheSEQQKEASWKHNQELR 401
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAE-----EAKKADEAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKKAEEKK 1564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 402 KALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEfrELLQYRDNSDKTLEANEMLLEKLRQRI 481
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 482 HD---KAVALERAIDE-KFSALEEKEKELRQLRLA--VRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEV------- 548
Cdd:PTZ00121 1643 AEekkKAEELKKAEEEnKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkkaeelk 1722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 549 ---EQLSTTCQNLQWLKEEMETKFSRWQKEQE--SIIQQLQTSLHDRNKEVEDLSATLLcklgpgQSEIAEELCQRLQRK 623
Cdd:PTZ00121 1723 kaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEekKKIAHLKKEEEKKAEEIRKEKEAVI------EEELDEEDEKRRMEV 1796
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313637 624 ERMLQDLLSdrNKQVLEhEMEIQGLLQSVSTREQESQAAAEKLVQALMERNsELQALRQYLGGRDSLMSQAPISN 698
Cdd:PTZ00121 1797 DKKIKDIFD--NFANII-EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKE 1867
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-527 |
1.54e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 165 TEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLlhlleeptsmevqpmTEELLKQQKLNSHETTITQQSVSDSHLAEL 244
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL---------------QERREALQRLAEYSWDEIDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 245 QEKIQQTEATNKILQEkLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLG 324
Cdd:COG4913 674 EAELERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 325 QLHSSEGTSPAQQQVAlLDLQSalfcsqlEIQKLQRVVRQKERQLADAKQcvQFVEAAAHESeQQKEASWKHNQELRKAL 404
Cdd:COG4913 753 ERFAAALGDAVERELR-ENLEE-------RIDALRARLNRAEEELERAMR--AFNREWPAET-ADLDADLESLPEYLALL 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 405 QQLQEE------------LQNKSQQLRAWEAEK-YNEIRTQEQNIQHLNHSLSHkeqllqefrelLQYRDNSDKTLEANE 471
Cdd:COG4913 822 DRLEEDglpeyeerfkelLNENSIEFVADLLSKlRRAIREIKERIDPLNDSLKR-----------IPFGPGRYLRLEARP 890
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313637 472 MLLE---KLRQRIHDkavALERAIDEKFSALEEKEKELRQL--RLAVRERDHDLERLRDVL 527
Cdd:COG4913 891 RPDPevrEFRQELRA---VTSGASLFDEELSEARFAALKRLieRLRSEEEESDRRWRARVL 948
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
351-527 |
2.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 351 SQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEEL-QNKSQQLRAWEAekynEI 429
Cdd:COG4913 272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLER----EI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 430 RTQEQNIQHLNHSLSHKEQLLQEF--------RELLQYRDNSDKTLEAnemlLEKLRQRIHDKAVALERAIDEKFSALEE 501
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALglplpasaEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRE 423
|
170 180
....*....|....*....|....*.
gi 525313637 502 KEKELRQLRLAVRERDHDLERLRDVL 527
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDAL 449
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
163-682 |
3.02e-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: 49.58 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 163 QYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHLA 242
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 243 ELQEKIQQTEATNKILQEKLNEmsyelkcaQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDtmaKLREMLHQSQ 322
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEE--------QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK---AAPLAAHIKA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 323 LGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFveAAAHESEQQKEASWKHNQELRK 402
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI--RDAHEVATSIREISCQQHTLTQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 403 ALQQLQEELQNKSQQLRAWEAEKYN--------EIRTQEQNIQHLNHSLSHKEQLLQEFRELLQ--YRDNSDKTLEANEM 472
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDIlqreqatiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 473 LLEKLRQRIHDKAVALERAidekfSALEEKEKELRQLRLAVRERDHDLER-LRDVLSSNEATMQSM------ESLLRAKG 545
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTK-----EQIHLQETRKKAVVLARLLELQEEPCpLCGSCIHPNPARQDIdnpgplTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 546 LEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATL-----LCKLGPGQSEIAEELCQRL 620
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrLQDLTEKLSEAEDMLACEQ 614
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313637 621 QRKERMLQDLLSDRNK-QVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQ 682
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVrLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-262 |
3.38e-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: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 50 ELKVEVESLKRELQDKKQHLDKTWADVENLNSQneaelRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAAL 129
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 130 VEAEKEcnlELSEKLKGVTKNWE----------DVPGDQVKPDQYTEALAQ-RDKRIEELNQSLAAQERLVEQLSREKQQ 198
Cdd:COG4942 99 LEAQKE---ELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313637 199 LLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSdshLAELQEKIQQTEATNKILQEKL 262
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAE---LAELQQEAEELEALIARLEAEA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
335-547 |
3.47e-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: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 335 AQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNK 414
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 415 SQQLRAWEAEKY--------------NEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQR 480
Cdd:COG4942 103 KEELAELLRALYrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313637 481 IHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLE 547
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-682 |
3.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 54 EVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQLLQ--EESRLA----KNEAARMA 127
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARkaEEARKAedakKAEAARKA 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 128 ALV-EAEKECNLELSEKLKGVTKNWEDVPGDQVKPdqytealAQRDKRIEELNQSLAAQERLVEQLSREKQQllhLLEEP 206
Cdd:PTZ00121 1185 EEVrKAEELRKAEDARKAEAARKAEEERKAEEARK-------AEDAKKAEAVKKAEEAKKDAEEAKKAEEER---NNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 207 TSMEVQPMTEELLKQQKLNSHETTITQQsVSDSHLAELQEKIQQTEATNKIlqEKLNEMSYELKCAQESSQKQdgtiQNL 286
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADE-LKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKA----EEA 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 287 KETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKE 366
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 367 RQLADAKQCVQFVEAAAHESEQQKEASW--KHNQELRKAlqqlqEELQNKSQQLR-AWEAEKYNEIRTQEQNIQHLNHSL 443
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEakKKAEEAKKA-----DEAKKKAEEAKkAEEAKKKAEEAKKADEAKKKAEEA 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 444 SHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAiDEKFSALEEKEKELRQLRLAVR--ERDHDLE 521
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA-EEAKKADEAKKAEEKKKADELKkaEELKKAE 1561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 522 RLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTslhdRNKEVEDLSATL 601
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL----KKAEEEKKKVEQ 1637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 602 LCKLGPGQSEIAEELCQRLQ----RKERMLQDLLSDRNK-QVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSE 676
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
....*.
gi 525313637 677 LQALRQ 682
Cdd:PTZ00121 1718 AEELKK 1723
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
446-700 |
4.35e-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: 48.22 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 446 KEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIhdkaVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRD 525
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 526 VLSSNEATMQSMESLLRAK-GLEVEQLSTTCQNLQWLKEemetkFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLlck 604
Cdd:COG4942 105 ELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKY-----LAPARREQAEELRADLAELAALRAELEAERAEL--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 605 lgpgqseiaEELCQRLQRKERMLQDLLSDRNKqvlehemeiqgLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYL 684
Cdd:COG4942 177 ---------EALLAELEEERAALEALKAERQK-----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*.
gi 525313637 685 GGRDSLMSQAPISNQQ 700
Cdd:COG4942 237 AAAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
15-494 |
5.97e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 15 LKKENFSLKLRIYFLEERMQQKYEASR--EDIYKRNIELK------VEVESLKRELQDKKQHLDKTWADVENLNSQNEAE 86
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 87 LR---------RQFEERQQETEHVYELLENKIQLLQEesrlAKNEAARMAALVEAEKECNLE-LSEKLKGVTKNWEDVpg 156
Cdd:PRK03918 330 IKeleekeerlEELKKKLKELEKRLEELEERHELYEE----AKAKKEELERLKKRLTGLTPEkLEKELEELEKAKEEI-- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 157 dQVKPDQYTEALAQRDKRIEELNQSLAA-------------------QERLVEQLSREKQQLLHLLEEPTSMEVQPMTEE 217
Cdd:PRK03918 404 -EEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 218 LLKQQKLNSHETTITQQSVSDsHLAELQEKiqqteaTNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERET 297
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAE-QLKELEEK------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELK 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 298 EELYQVIEGQNDTMAKLREMLHQ------SQLGQLHS--SEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQL 369
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKEleelgfESVEELEErlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 370 ADAKQCVQfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEaekyNEIRTQEQNIQHLNHSLSHKEQL 449
Cdd:PRK03918 636 AETEKRLE--ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELE----KRREEIKKTLEKLKEELEEREKA 709
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 525313637 450 LQEFRELlqyrdnsDKTLEANEMLLEKLRQRihdKAVALERAIDE 494
Cdd:PRK03918 710 KKELEKL-------EKALERVEELREKVKKY---KALLKERALSK 744
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
81-546 |
6.31e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 81 SQNEAE-LRRQFEERQQETEHVYELLENKIQLLQEEsrlAKNEAARMAALVEAEkecnlELSEKLKGVTKNWEDVPGD-- 157
Cdd:pfam07111 195 AQKEAElLRKQLSKTQEELEAQVTLVESLRKYVGEQ---VPPEVHSQTWELERQ-----ELLDTMQHLQEDRADLQATve 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 158 --QVKPDQYTEALAQRDkriEELNQSLAAQERLVEQLSREKQQLLHLLEEPT-SMEVQpmteelLKQQKLnSHETTITQQ 234
Cdd:pfam07111 267 llQVRVQSLTHMLALQE---EELTRKIQPSDSLEPEFPKKCRSLLNRWREKVfALMVQ------LKAQDL-EHRDSVKQL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 235 SVsdsHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERET----EELYQVIEGQNDT 310
Cdd:pfam07111 337 RG---QVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTasaeEQLKFVVNAMSST 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 311 MAKLREMLHQSQ----------------LGQLHSSEGTSPAQQQVALLDLQS-----------ALFCSQLEIQKLQRVVR 363
Cdd:pfam07111 414 QIWLETTMTRVEqavaripslsnrlsyaVRKVHTIKGLMARKVALAQLRQEScpppppappvdADLSLELEQLREERNRL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 364 QKERQLAdAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAW---------EAEKYNEIRTQEQ 434
Cdd:pfam07111 494 DAELQLS-AHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVArqgqqesteEAASLRQELTQQQ 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 435 NI--QHLNHSLSHKEQLLQEfrellQYRDNSDKTLEAnemlleklrQRIHDKAVALERAIDEKFSALEEKEKELRqlRLA 512
Cdd:pfam07111 573 EIygQALQEKVAEVETRLRE-----QLSDTKRRLNEA---------RREQAKAVVSLRQIQHRATQEKERNQELR--RLQ 636
|
490 500 510
....*....|....*....|....*....|....
gi 525313637 513 VRERDHDLERLRDVLSSNEATMQSMESLLRAKGL 546
Cdd:pfam07111 637 DEARKEEGQRLARRVQELERDKNLMLATLQQEGL 670
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
237-425 |
6.75e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 237 SDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAK-LR 315
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 316 EMLHQ----SQLGQLHSSEGTSPAQQQVALLD-LQSAlfcSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQK 390
Cdd:COG3883 94 ALYRSggsvSYLDVLLGSESFSDFLDRLSALSkIADA---DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190
....*....|....*....|....*....|....*
gi 525313637 391 EASWKHNQELRKALQQLQEELQNKSQQLRAWEAEK 425
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
31-682 |
7.04e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 31 ERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQ 110
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 111 LLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVE 190
Cdd:PTZ00121 1192 ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 191 QLSREKQQllhlLEEPTSMEVQPMTEELLKQQKLNSHEtTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELK 270
Cdd:PTZ00121 1272 IKAEEARK----ADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 271 CAQESSQKQDGTIQNLKETLKSRERETEELYQviegQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQqvalLDLQSALFC 350
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKKADEAKKKAEEDKKKADE----LKKAAAAKK 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 351 SQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQK-EASWKHNQELRKAlqqlqEELQNKSQqlrawEAEKYNEI 429
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaEEAKKKAEEAKKA-----DEAKKKAE-----EAKKADEA 1488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 430 RTQEQNIQHLNHSLSHKEQLLQEFRELLQYRD--NSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKeLR 507
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-AE 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 508 QLRLAVRERDHDLERLRDVLSSNEATMQS-MESLLRAKGLEVEQLSTtcqnlqwlKEEMETKFSRWQKEQE--SIIQQLQ 584
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEvMKLYEEEKKMKAEEAKK--------AEEAKIKAEELKKAEEekKKVEQLK 1639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 585 TSLHDRNKEVEDLSatllcKLGPGQSEIAEELCQRLQRKERMLQDLLSD-----RNKQVLEHEMEIQGLLQSVSTREQES 659
Cdd:PTZ00121 1640 KKEAEEKKKAEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEAKKAeedekKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
650 660
....*....|....*....|...
gi 525313637 660 QAAAEKLVQALMERNSELQALRQ 682
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKK 1737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
474-932 |
8.22e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 474 LEKLRQRIHDKAVALERAIDEKFSALEEKEKE------------LRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLL 541
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQieekeekdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 542 ---RAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEqesiIQQLQTSLHDRNKEVEDLSATllCKLGPGQSEIAEELCQ 618
Cdd:PRK02224 244 eehEERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLLAE--AGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 619 RLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISN 698
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 699 QQAEVTPTgRLGKQTDQGSMQIPSRDDS----TSLTAK---------------------------EDVSIPRSTLGDLDT 747
Cdd:PRK02224 398 ERFGDAPV-DLGNAEDFLEELREERDELrereAELEATlrtarerveeaealleagkcpecgqpvEGSPHVETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 748 VAGLEKELSNAKEELELMAKK-ER-----ESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDP 821
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERlERaedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 822 EDipAMERLTQEVLLLREKVASVESQGQEISgNRRQQL------LLMLEGLVDERSRLNEALQA------ERQLYSSlvk 889
Cdd:PRK02224 557 RE--AAAEAEEEAEEAREEVAELNSKLAELK-ERIESLerirtlLAAIADAEDEIERLREKREAlaelndERRERLA--- 630
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 525313637 890 fhahpESSERDRTLQVE-----LEGAQVLRSRLEEVLGRSLERLNRLE 932
Cdd:PRK02224 631 -----EKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELR 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
13-621 |
1.10e-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: 47.86 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 13 NDLKKENFSLKLRIYFLEERMQQKYEASrediyKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAE---LRR 89
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKA-----KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEstdLQE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 90 QFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLkgvtknwEDVPGDQVkpdQYTEALA 169
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQ-------EDLESERA---ARNKAEK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 170 QRDKRIEELN----------QSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEelLKQQKLNSHETTITQQSVSDS 239
Cdd:pfam01576 293 QRRDLGEELEalkteledtlDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQE--MRQKHTQALEELTEQLEQAKR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 240 HLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLH 319
Cdd:pfam01576 371 NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLN 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 320 QSQLGQLHSSEGTSPAQQQvaLLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQE 399
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQ--LQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 400 LRKALQQ--------------LQEELQNKSQQL--RAWEAEKYNEIRTQEQ--------NIQHLNHSLSHKEQLLQEFRE 455
Cdd:pfam01576 529 MKKKLEEdagtlealeegkkrLQRELEALTQQLeeKAAAYDKLEKTKNRLQqelddllvDLDHQRQLVSNLEKKQKKFDQ 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 456 LL-QYRDNSDKTLEANEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKELRQLRLavrerdhdleRLRDVLSSNEATM 534
Cdd:pfam01576 609 MLaEEKAISARYAEERDRAEAEAREK-ETRALSLARALEEALEAKEELERTNKQLRA----------EMEDLVSSKDDVG 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 535 QSMESLLRAKGLEVEQLSTTCQNLQWLKEEM---ETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLLCKLGPGQSE 611
Cdd:pfam01576 678 KNVHELERSKRALEQQVEEMKTQLEELEDELqatEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAE 757
|
650
....*....|
gi 525313637 612 IAEELCQRLQ 621
Cdd:pfam01576 758 LEDERKQRAQ 767
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
232-976 |
1.13e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 232 TQQSVSDSHLAELQEKIQQTEATNKIlQEKLNEMSYELKCAQESSQKQDGTIQNLKEtlksRERETEELYQVIEGQNDTM 311
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACEI-RDQITSKEAQLESSREIVKSYENELDPLKN----RLKEIEHNLSKIMKLDNEI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 312 AKL--REMLHQSQLGQLHssegtspaqqqvalLDLQSALFCSQLEIQKL----QRVVRQKERQLADAKQCVQFVEAAAHE 385
Cdd:TIGR00606 272 KALksRKKQMEKDNSELE--------------LKMEKVFQGTDEQLNDLyhnhQRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 386 SEQQKeaswkhnQELRKALQQLQEELQNKSQQLRAWEAEKY-NEIRTQEQNIQHLNHSlshkEQLLQEFRELLQYRDNSD 464
Cdd:TIGR00606 338 LNQEK-------TELLVEQGRLQLQADRHQEHIRARDSLIQsLATRLELDGFERGPFS----ERQIKNFHTLVIERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 465 --------KTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERD---HDLERLRDVLSSNEAT 533
Cdd:TIGR00606 407 aktaaqlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 534 MQSME--SLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQL-----QTSLHDRNKEVEDLSATLLCKLG 606
Cdd:TIGR00606 487 LSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmltkdKMDKDEQIRKIKSRHSDELTSLL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 607 P--GQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQAL--MERNSELQALRQ 682
Cdd:TIGR00606 567 GyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCgsQDEESDLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 683 YLggRDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVS-IPRSTLGDLDTVAGLEKELSNAKEE 761
Cdd:TIGR00606 647 EI--EKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISdLQSKLRLAPDKLKSTESELKKKEKR 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 762 LELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPE----DIPAMERLTQEVLLL 837
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 838 REKVASVESQGQEISGNRR-QQLLLMLEGLVDERSRLNEALQAERQLYSSLVKFHAHPESSERD-RTLQVELEGAQVLRS 915
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElKSEKLQIGTNLQRRQ 884
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313637 916 RLEEvlgRSLERLNRLETLAAIGGAAAGDDTEDTSTEFTDSIEEEAAHHSHQQLVKVALEK 976
Cdd:TIGR00606 885 QFEE---QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDK 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1912-2060 |
1.20e-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: 47.74 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1912 RRLQAQLSHVSREHS---QETESLREALLSSRSHLQELEKELEHQKVERQQLLEDLREKQQEVLHFREERLSLQENDSRL 1988
Cdd:TIGR02168 263 QELEEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313637 1989 QHKLVLLQQQCEEKQQLFESLQSELQIYEALYGNSKKGLKAysldachqipLSSDLSHLVAEVRALRGQLEQ 2060
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----------LRSKVAQLELQIASLNNEIER 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
294-682 |
1.61e-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: 47.04 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 294 ERETEELYQVIEGQ---NDTMAKLREMLHQSQLgqlhssEGTSPAQQqvALLDLQSALFCSQleiqklQRVVRQKERQLA 370
Cdd:pfam17380 286 ERQQQEKFEKMEQErlrQEKEEKAREVERRRKL------EEAEKARQ--AEMDRQAAIYAEQ------ERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 371 DAKQcvqfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAwEAEKYNEIRTQEQNIQhlnhslshkEQLL 450
Cdd:pfam17380 352 RIRQ-----EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKILEEERQ---------RKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 451 QEFRELLQYRDNSDktlEANEMLLEKLRqrihdkavaleraidekfsalEEKEKELRQLRLAVRERDHDLERLRDVLSSN 530
Cdd:pfam17380 417 QQKVEMEQIRAEQE---EARQREVRRLE---------------------EERAREMERVRLEEQERQQQVERLRQQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 531 EATMQSMESLLRAKGLEVEqlsttcQNLQWLKEEMETKfSRWQKEQESIIQQLQTSLHDRnkevedlsatllcklgpgQS 610
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEE------QRRKILEKELEER-KQAMIEEERKRKLLEKEMEER------------------QK 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313637 611 EIAEELCQRLQRKERmlqdllsdRNKQVLEHEMEIQgllqsvstrEQESQAAAEKLVQALMERNSELqaLRQ 682
Cdd:pfam17380 528 AIYEEERRREAEEER--------RKQQEMEERRRIQ---------EQMRKATEERSRLEAMEREREM--MRQ 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
489-861 |
2.45e-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: 46.60 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 489 ERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDvlssneatmqSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETK 568
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR----------EREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 569 FSRWQKEQESI---IQQLQTSLHDRNKEVEDLSATLlcklgpgqSEIAEELcqrlqrkERMLQDLLSDRNKQVLEHEMEI 645
Cdd:TIGR02169 239 KEAIERQLASLeeeLEKLTEEISELEKRLEEIEQLL--------EELNKKI-------KDLGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 646 QGLLQSVSTREQESQAAAEKLVQALMERNSEL-------QALRQYLGGRDSLMSQapISNQQAEvtptgRLGKQTDQGSM 718
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieeleREIEEERKRRDKLTEE--YAELKEE-----LEDLRAELEEV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 719 qipsrdDSTSLTAKEDVSIPRSTLGDL-DTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADM 797
Cdd:TIGR02169 377 ------DKEFAETRDELKDYREKLEKLkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313637 798 ESLTRNI-QIKEDLIKDLQMQLVDPEDIPAME-RLTQEVLLLREKVASVESQGQEISGNRRQQLLL 861
Cdd:TIGR02169 451 KKQEWKLeQLAADLSKYEQELYDLKEEYDRVEkELSKLQRELAEAEAQARASEERVRGGRAVEEVL 516
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
182-702 |
2.90e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 182 LAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTeelLKQQKLNSHETTITQQSVSDSHLAELQEKIQQteatnkiLQEK 261
Cdd:PRK10246 372 FSQQTSDREQLRQWQQQLTHAEQKLNALPAITLT---LTADEVAAALAQHAEQRPLRQRLVALHGQIVP-------QQKR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 262 LNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEgQNDTMAKLREMLHQSQLGQLHSSEGTS--PAQQQV 339
Cdd:PRK10246 442 LAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDLEAQRAQLQAGQPCPLCGSTshPAVEAY 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 340 ALLDLQSalfcSQLEIQKLQRVVRQ-KERQLADAKQcvqfVEAAAHESEQQKEASwkhnQELRKALQQLQEELQNKSQQL 418
Cdd:PRK10246 521 QALEPGV----NQSRLDALEKEVKKlGEEGAALRGQ----LDALTKQLQRDESEA----QSLRQEEQALTQQWQAVCASL 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 419 raweaekyNEIRTQEQNIQH-LNHSLSHKEQLLQefrelLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAI----- 492
Cdd:PRK10246 589 --------NITLQPQDDIQPwLDAQEEHERQLRL-----LSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALagyal 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 493 -----DEKFSALEEKEKEL-----RQLRL-AVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEV--EQLSTTCQnLQ 559
Cdd:PRK10246 656 tlpqeDEEASWLATRQQEAqswqqRQNELtALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVheQCLSLHSQ-LQ 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 560 WLKEEMETKFSRWQKEQESIIQQLQTSLHDrnkeveDLSATLLCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVL 639
Cdd:PRK10246 735 TLQQQDVLEAQRLQKAQAQFDTALQASVFD------DQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALA 808
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 640 EHEMEIQGLLQSVSTREQeSQAAAEKLVQALME---RNSEL-QALRQYLGGRD---SLMSQAPISNQQAE 702
Cdd:PRK10246 809 QHQQHRPDGLDLTVTVEQ-IQQELAQLAQQLREnttRQGEIrQQLKQDADNRQqqqALMQQIAQATQQVE 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
352-1036 |
2.92e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 352 QLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQ-KEASWKHNQELRKALQQLQeeLQNKSQQLRAWEAEKYNEIR 430
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQtQQSHAYLTQKREAQEEQLK--KQQLLKQLRARIEELRAQEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 431 TQEQNIQHLNHSlSHKEQLLQEFRELLQYRDNSDK---TLEANEMLLEKLRQriHDKAVALERAIDEKFSALEEKEkeLR 507
Cdd:TIGR00618 278 VLEETQERINRA-RKAAPLAAHIKAVTQIEQQAQRihtELQSKMRSRAKLLM--KRAAHVKQQSSIEEQRRLLQTL--HS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 508 QLRLAVRERDHDLERlRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLqtsl 587
Cdd:TIGR00618 353 QEIHIRDAHEVATSI-REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 588 HDRNKEVEDLSATLLCKLGPG---QSEIAEE-LCQRLQRKERMLQDLLSDRnKQVLEHEMEIQGLLQSVSTREQESQAAA 663
Cdd:TIGR00618 428 HAKKQQELQQRYAELCAAAITctaQCEKLEKiHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 664 EKlvqALMERNSELQALRQyLGGRDSLMSQ---APISNQQAEVTPTGRLGKQTDQG---SMQIPSRDDSTSLTAKEDVSI 737
Cdd:TIGR00618 507 CG---SCIHPNPARQDIDN-PGPLTRRMQRgeqTYAQLETSEEDVYHQLTSERKQRaslKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 738 PRStlgdldtVAGLEKELSNAKEELELMAKKERESQMELSAlqsmmavQEEELQVQAADMESLTRNIQIKEDLIKDLQmq 817
Cdd:TIGR00618 583 KED-------IPNLQNITVRLQDLTEKLSEAEDMLACEQHA-------LLRKLQPEQDLQDVRLHLQQCSQELALKLT-- 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 818 lvdpedipAMERLTQEVLLLREKVASVES-QGQEISGNRRQQLLLMLEGLVDE----RSRLNEALQAERQLYSSLVKFHA 892
Cdd:TIGR00618 647 --------ALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKMQSEKEQltywKEMLAQCQTLLRELETHIEEYDR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 893 H-PESSERDRTLQVELEGAQVLrsrLEEVLGrSLERLNRlETLAAIGGAAAGDDTEDTSTEFTDSIEEE-AAHHSHQQLV 970
Cdd:TIGR00618 719 EfNEIENASSSLGSDLAAREDA---LNQSLK-ELMHQAR-TVLKARTEAHFNNNEEVTAALQTGAELSHlAAEIQFFNRL 793
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313637 971 KVALEKSLATVETQNPSFSPPspmGGDSNRCLQEEMLHLRAEFHQHLEEKRKAEEELKELKAQIEE 1036
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPS---DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
31-308 |
3.18e-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: 45.88 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 31 ERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRR-QFEERQQETEHV-YELLENK 108
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERiRQEERKRELERIrQEEIAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 109 IQLLQEESRLA-----KNEAARMaalvEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQyTEALAQRDKRIEELNQSLA 183
Cdd:pfam17380 374 ISRMRELERLQmerqqKNERVRQ----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ-EEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 184 AQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQT-------EATNK 256
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKllekemeERQKA 528
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 525313637 257 ILQEKLNEMSYELKCAQESS------QKQDGTIQNLKETLKSRERETEELYQVIEGQN 308
Cdd:pfam17380 529 IYEEERRREAEEERRKQQEMeerrriQEQMRKATEERSRLEAMEREREMMRQIVESEK 586
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
162-430 |
3.22e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 162 DQYTEALAQRDKRIEELNQSLAAQERLVEQLsREKQQLLHLleeptSMEVQPMTEELlkqqklnsheTTITQQsvsdshL 241
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEF-RQKNGLVDL-----SEEAKLLLQQL----------SELESQ------L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 242 AELQEKIQQTEATNKILQEKLNEMSYELkcaqeSSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREmlhqs 321
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDAL-----PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA----- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 322 qlgQLHSSEGTSPAQQQVALLDLQSalfcsqlEIQKLQRVVRQKERQLADAKQcvQFVEAAAHESEQQKeaswkHNQELr 401
Cdd:COG3206 299 ---QIAALRAQLQQEAQRILASLEA-------ELEALQAREASLQAQLAQLEA--RLAELPELEAELRR-----LEREV- 360
|
250 260
....*....|....*....|....*....
gi 525313637 402 KALQQLQEELQNKSQQLRAWEAEKYNEIR 430
Cdd:COG3206 361 EVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1844-2025 |
3.23e-04 |
|
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: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1844 LEEHLGEIRNLRQRLEESICINDRLREQLEHRLTSTARGRGSTSNFYSQGLESIPQLCNENRVLREDNRRLQAQLshvsr 1923
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1924 ehsQETESLREALLSSRSHLQELEKELEHQKVERQQLLEDLREKQQEVLHFREERLSLQENDSRLQHKLVLLQQQCEEKQ 2003
Cdd:COG1196 414 ---ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
170 180
....*....|....*....|..
gi 525313637 2004 QLFESLQSELQIYEALYGNSKK 2025
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKA 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
398-933 |
3.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 398 QELRKALQQLQEELQNKSQQLRAWE-----AEKYNEIRTQEQNIQHLNHSLSH--KEQLLQEFRELLQYRDNSDKTLEAN 470
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEpirelAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 471 EMLLEKLRQRIHDKAVALERAIDE-KFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVE 549
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 550 QLSTTCQNLQwlkEEMETKFSRWQKEqesiIQQLQTSLHDRNKEVEDLSATLLCkLGPGQSEIAEELCQRLQRKERMLQ- 628
Cdd:COG4913 391 ALLEALEEEL---EALEEALAEAEAA----LRDLRRELRELEAEIASLERRKSN-IPARLLALRDALAEALGLDEAELPf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 629 --DLLsdrnkQVLEHEME----IQGLLQSVSTR-----EQESQAAA--------EKLV-QALMERNSELQA--------- 679
Cdd:COG4913 463 vgELI-----EVRPEEERwrgaIERVLGGFALTllvppEHYAAALRwvnrlhlrGRLVyERVRTGLPDPERprldpdsla 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 680 -------------LRQYLGGRDSLM---SQAPISNQQAEVTPTGrLGKQtdqgsmqipsrddSTSLTAKEDVSIPRST-- 741
Cdd:COG4913 538 gkldfkphpfrawLEAELGRRFDYVcvdSPEELRRHPRAITRAG-QVKG-------------NGTRHEKDDRRRIRSRyv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 742 LGD--LDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAA--DMESLTRNIQIKEDLIKDLQmq 817
Cdd:COG4913 604 LGFdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeiDVASAEREIAELEAELERLD-- 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 818 lvdpEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQqlllmlegLVDERSRLNEALQAERQLYSSLVKFHAHPESS 897
Cdd:COG4913 682 ----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGR--------LEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
570 580 590
....*....|....*....|....*....|....*...
gi 525313637 898 ERDRTLQVELEGAQV--LRSRLEEVLGRSLERLNRLET 933
Cdd:COG4913 750 LLEERFAAALGDAVEreLRENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1841-2060 |
3.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1841 ADLLEEHLGEIRNLRQRLEesicindRLREQLEHrltstargrgstsnfysqgLESIPQLCNENRVLREDNRRLQAQLSH 1920
Cdd:COG4913 227 ADALVEHFDDLERAHEALE-------DAREQIEL-------------------LEPIRELAERYAAARERLAELEYLRAA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1921 VSREHSQ-ETESLREALLSSRSHLQELEKELEHQKVERQQLLEDLREKQQEvlhfreerlsLQEND----SRLQHKLVLL 1995
Cdd:COG4913 281 LRLWFAQrRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ----------IRGNGgdrlEQLEREIERL 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313637 1996 QQQCEEKQQLFESLQSELQIYEALYGNSKKGLKAYS------LDACHQI--PLSSDLSHLVAEVRALRGQLEQ 2060
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRaeaaalLEALEEEleALEEALAEAEAALRDLRRELRE 423
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
356-577 |
4.40e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 44.75 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 356 QKLQRVVRQKERQLADAKqcvqfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEkyneirTQEQN 435
Cdd:pfam09787 14 QKAARILQSKEKLIASLK------EGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTE------LQELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 436 IQHLNHSLSHKEQLlQEFRELLQYRDNSDKTLEANemlLEKLRQRIHdkavaleraidekfSALEEKEKELRQLRLAVRE 515
Cdd:pfam09787 82 AQQQEEAESSREQL-QELEEQLATERSARREAEAE---LERLQEELR--------------YLEEELRRSKATLQSRIKD 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313637 516 RDHDLERLRDVL---SSNEATMQSMESLLR-------AKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQE 577
Cdd:pfam09787 144 REAEIEKLRNQLtskSQSSSSQSELENRLHqltetliQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGS 215
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
385-536 |
5.57e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.36 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 385 ESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKY------NEIRTQEQNIQHLNHslsHKEQLLQEFRELLQ 458
Cdd:pfam13851 44 RNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQslknlkARLKVLEKELKDLKW---EHEVLEQRFEKVER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 459 YRDNsdkTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDL----ERLRDVLSSNEATM 534
Cdd:pfam13851 121 ERDE---LYDKFEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQLNEVLAAANLDPDALqavtEKLEDVLESKNQLI 197
|
..
gi 525313637 535 QS 536
Cdd:pfam13851 198 KD 199
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-300 |
6.97e-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: 45.06 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 8 LSQHLNDLKKENFSLKLRIyfleERMQQKYEASREDIYkrniELKVEVESLKRELQDKKQHLDKTWADVEnlnsqneaEL 87
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELKELEARIE--------EL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 88 RRQFEERQQETEHVY-ELLENKIQLLQEESRLAKNEAARM-AALVEAEKECNLELSEKlkgvTKNWEDVPGDQVKPDQYT 165
Cdd:TIGR02169 771 EEDLHKLEEALNDLEaRLSHSRIPEIQAELSKLEEEVSRIeARLREIEQKLNRLTLEK----EYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 166 EALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEpTSMEVQPMTEELLK-QQKLNSHETTITQQsvsDSHLAEL 244
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-LKKERDELEAQLRElERKIEELEAQIEKK---RKRLSEL 922
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 525313637 245 QEKIQQTEATNKILQEKLNEMSYELKCaqessqkqDGTIQNLKETLKSRERETEEL 300
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEE--------ELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1841-2060 |
7.53e-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: 45.05 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1841 ADLLEEHLGEIRNLRQRLEESICINDRLREQLEhRLTSTARGRGSTSNFYSQGLESIPQLCNENRVLREDNRRLQAQLSH 1920
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1921 VSREHSQETESLREALLSSRSHLQELEKELEHQKVERQQLLEDLREKQQEVLHFREERLSLQENDSRLQHKLVLLQQQCE 2000
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 2001 EKQQLFESLQSELQIYEALYGNSKKGLKAYSLDachQIPLSSDLSHLVAEVRALRGQLEQ 2060
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSE---LEELSEELRELESKRSELRRELEE 919
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-516 |
8.43e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 333 SPAQQQVALLDLQSALfcsqLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEaswkhnqELRKALQQLQEELQ 412
Cdd:COG1579 1 AMPEDLRALLDLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 413 NKSQQLRAWEaEKYNEIRTQEQnIQHLNHSLSH----KEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIhdkaVAL 488
Cdd:COG1579 70 EVEARIKKYE-EQLGNVRNNKE-YEALQKEIESlkrrISDLEDEILELMERIEELEEELAELEAELAELEAEL----EEK 143
|
170 180
....*....|....*....|....*...
gi 525313637 489 ERAIDEKFSALEEKEKELRQLRLAVRER 516
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAAK 171
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
7-528 |
8.70e-04 |
|
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: 44.73 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 7 TLSQHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIyKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNsQNEAE 86
Cdd:pfam05557 38 ALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA-ELNRLKKKYLEALNKKLNEKESQLADAREVISCLK-NELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 87 LRRQFEERQQETEHvyelLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVtKNWEDVPGDQVKPDQYTE 166
Cdd:pfam05557 116 LRRQIQRAELELQS----TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI-KELEFEIQSQEQDSEIVK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 167 ALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSME-----VQPMTEELLK--------QQKLNSHETTITQ 233
Cdd:pfam05557 191 NSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklerEEKYREEAATlelekeklEQELQSWVKLAQD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 234 QSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELK----CAQESSQKQDGTIQNLKETLKSREReTEELYQVIEGQND 309
Cdd:pfam05557 271 TGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARqlekARRELEQELAQYLKKIEDLNKKLKR-HKALVRRLQRRVL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 310 TMAKLREMLHQ------SQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQklqrvVRQKERQLADAKQCVQFVEA-- 381
Cdd:pfam05557 350 LLTKERDGYRAilesydKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQ-----LSVAEEELGGYKQQAQTLERel 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 382 -AAHESEQQKEASWKHNQ--ELRKALQQLQEELQNKSQQLRAWEAEkyneirTQEQNIQHLNHSLSHKEQLLQEfRELLQ 458
Cdd:pfam05557 425 qALRQQESLADPSYSKEEvdSLRRKLETLELERQRLREQKNELEME------LERRCLQGDYDPKKTKVLHLSM-NPAAE 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 459 YRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLS 528
Cdd:pfam05557 498 AYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
227-693 |
9.07e-04 |
|
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: 44.43 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 227 HETTITQQSVSDSH-------LAELQEKIQQTEATNKILQEKLNEMSyelkcAQESSQKQDgtIQNLKETLKSRERETEE 299
Cdd:pfam10174 270 REEEIKQMEVYKSHskfmknkIDQLKQELSKKESELLALQTKLETLT-----NQNSDCKQH--IEVLKESLTAKEQRAAI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 300 LYQVIEGQNDTMAKLREMLH--QSQLGQLHSSEGTspaqQQVALLDLQSALFCS-------QLEIQKLQRVVRQKERQLA 370
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNkkTKQLQDLTEEKST----LAGEIRDLKDMLDVKerkinvlQKKIENLQEQLRDKDKQLA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 371 DAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLL 450
Cdd:pfam10174 419 GLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 451 QEFRELLQ-------YRDNSDKTLEAN-------EMLLEKLRQRIHDKAVAlERAIDEKFSALEEKEKELRQLRLAVRER 516
Cdd:pfam10174 499 IDLKEHASslassglKKDSKLKSLEIAveqkkeeCSKLENQLKKAHNAEEA-VRTNPEINDRIRLLEQEVARYKEESGKA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 517 DHDLERLRDVL-------SSNEATMQSMESLLRAKGLEveqLSTTCQNLQWLKEEMETKfsrwqkeqesIIQQLQTSLHD 589
Cdd:pfam10174 578 QAEVERLLGILrevenekNDKDKKIAELESLTLRQMKE---QNKKVANIKHGQQEMKKK----------GAQLLEEARRR 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 590 RNKEVEDLSATLLCKLGPGQSEIAEEL----------CQRLQRKERMLQDLLSDRNKQVLEH-EMEIQGLLQSVStrEQE 658
Cdd:pfam10174 645 EDNLADNSQQLQLEELMGALEKTRQELdatkarlsstQQSLAEKDGHLTNLRAERRKQLEEIlEMKQEALLAAIS--EKD 722
|
490 500 510
....*....|....*....|....*....|....*.
gi 525313637 659 SQAAAEKLVQALMERNS-ELQALRQYlggRDSLMSQ 693
Cdd:pfam10174 723 ANIALLELSSSKKKKTQeEVMALKRE---KDRLVHQ 755
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1-305 |
9.44e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1 MSNGYRTLSQHLNDLKKENFSLKlriyflEERMQQKYEAsrediykrNIELKVEVESLKRELQDKKQHLDKTWADVENLN 80
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGEN------AESSKRLNEN--------ANNLIKQFENTKEKIAEYTKSIDIKKATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 81 SQNEAELRRQFEERQQETEHvyELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLE-LSEKLKGVTKNWEDVPgdQV 159
Cdd:COG5185 317 QLAAAEAEQELEESKRETET--GIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSkSSEELDSFKDTIESTK--ES 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 160 KPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEpTSMEVQPMTEELLKQQKLNSHETTITQQSVSDS 239
Cdd:COG5185 393 LDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE-VSKLLNELISELNKVMREADEESQSRLEEAYDE 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 240 HLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNL----KETLKSRERETEELYQVIE 305
Cdd:COG5185 472 INRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKldqvAESLKDFMRARGYAHILAL 541
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
42-597 |
1.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 42 EDIYKRNIELKVEVESLkRELQDKKQHLDKTWADvenLNSQNEAELRRQFEERQQEtehvYELLENKIQLLQEEsrLAKN 121
Cdd:COG4913 238 ERAHEALEDAREQIELL-EPIRELAERYAAARER---LAELEYLRAALRLWFAQRR----LELLEAELEELRAE--LARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 122 EAARmaALVEAEKEcnlELSEKLKGVTKNWEDVPGDQVkpdqytEALAQrdkRIEELNQSLAAQERLVEQLsrekQQLLH 201
Cdd:COG4913 308 EAEL--ERLEARLD---ALREELDELEAQIRGNGGDRL------EQLER---EIERLERELEERERRRARL----EALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 202 LLEEPTsmevqPMTEELLKQQKLNSHEttitQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKcAQESSQKQ-D 280
Cdd:COG4913 370 ALGLPL-----PASAEEFAALRAEAAA----LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-SLERRKSNiP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 281 GTIQNLKETLKS--RERETE-----ELYQVIEGQND--------------TM-------AKLREMLHQSQLGQLHSSEGT 332
Cdd:COG4913 440 ARLLALRDALAEalGLDEAElpfvgELIEVRPEEERwrgaiervlggfalTLlvppehyAAALRWVNRLHLRGRLVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 333 SPAQQQVALLDLQSALFCSQLEIQK------LQRVVRQK--------ERQLADAKQCV-------QFVEAAAHESEQQKE 391
Cdd:COG4913 520 RTGLPDPERPRLDPDSLAGKLDFKPhpfrawLEAELGRRfdyvcvdsPEELRRHPRAItragqvkGNGTRHEKDDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 392 ASWKHNQELRKALQQLQEELQNKSQQLRAWEAEkYNEIRTQEQNIQhlnhslshkeQLLQEFRELLQYRDNSDKTLEANE 471
Cdd:COG4913 600 SRYVLGFDNRAKLAALEAELAELEEELAEAEER-LEALEAELDALQ----------ERREALQRLAEYSWDEIDVASAER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 472 ML--LEKLRQRI---HDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAkgL 546
Cdd:COG4913 669 EIaeLEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--E 746
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 525313637 547 EVEQLSTTCQNLqwLKEEMETKFSRWQKEQesiIQQLQTSLHDRNKEVEDL 597
Cdd:COG4913 747 LRALLEERFAAA--LGDAVERELRENLEER---IDALRARLNRAEEELERA 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1844-2014 |
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: 43.90 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1844 LEEHLGEIRNLRQRLEESICINDRLREQLEHRLTSTARGRGS-----------------TSNFYSQGLESI--------- 1897
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselkelearieeleeDLHKLEEALNDLearlshsri 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1898 PQLCNENRVLREDNRRLQAQLSHVSREHSQETEsLREALLSSRSHLQELEKELEHQKVERQQLLEDLR-----------E 1966
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTL-EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkeeleeeleE 872
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 525313637 1967 KQQEVLHFREERLSLQENDSRLQHKLVLLQ---QQCEEKQQLFESLQSELQ 2014
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELErkiEELEAQIEKKRKRLSELK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1905-2014 |
1.76e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1905 RVLREDNRRLQAQL-SHVSREHSQETESLREALLSSRSHLQELEKELEHQKVERQQLLEDLREKQQEVLHFREERLSLQE 1983
Cdd:COG1196 216 RELKEELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110
....*....|....*....|....*....|.
gi 525313637 1984 NDSRLQHKLVLLQQQCEEKQQLFESLQSELQ 2014
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELA 326
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
739-1123 |
2.02e-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: 43.51 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 739 RSTLGDLDTVAGLEKELSNAKEELELMAKKE---RESQMELSALQsmmavqeeeLQVQAADMESLTRNIQIKEDLIKDLQ 815
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAeryKELKAELRELE---------LALLVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 816 MQLVDPEdiPAMERLTQEVLLLREKVASVESQGQEISGNrrqqlllmLEGLVDERSRLNEALQaerqlysslvkfhahpE 895
Cdd:TIGR02168 253 EELEELT--AELQELEEKLEELRLEVSELEEEIEELQKE--------LYALANEISRLEQQKQ----------------I 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 896 SSERDRTLQVELEGAQVLRSRLEEVLGRSLERLNRLEtlaaiggaaagddteDTSTEFTDSIEEEAAHHSHQQLVKVALE 975
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELE---------------EKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 976 KSLATvetqnpsfsppspmggdsnrcLQEEMLHLRAEFHQHLEEKRKAEEELKELKAQIEEAGFS-SVSHIRNTMLSLCL 1054
Cdd:TIGR02168 372 SRLEE---------------------LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRrERLQQEIEELLKKL 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313637 1055 ENAELKEQMGEAMSDGWEIEEDKEKGEVMVETVVTKEGLSEsSLQAEFRKLQGKLKNAHNIINLLKEQL 1123
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
377-668 |
2.19e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 377 QFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNksqqlraweAEK----YNEIRTQEqnIQHLNHSLSHKEQLLQE 452
Cdd:PLN02939 103 QRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQN---------AEKnillLNQARLQA--LEDLEKILTEKEALQGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 453 FREL---LQYRDNSDKT-------LEANEMLLEKLRQRIHDKAV---ALERAIDEKFSALEEKEKELRQLRLAVR----- 514
Cdd:PLN02939 172 INILemrLSETDARIKLaaqekihVEILEEQLEKLRNELLIRGAtegLCVHSLSKELDVLKEENMLLKDDIQFLKaelie 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 515 -----ERDHDLERLRDVLssnEATMQSMESLLRAKGLEVEQLSTTCQNLQWLK-EEMETKFSRWQKEQESIIQQLQTSlH 588
Cdd:PLN02939 252 vaeteERVFKLEKERSLL---DASLRELESKFIVAQEDVSKLSPLQYDCWWEKvENLQDLLDRATNQVEKAALVLDQN-Q 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 589 DRNKEVEDLSATLlckLGPGQSEIAEELCQRLQRKERMLQDLLsdrnkQVLEHEMEIQGLLQSVSTreQESQAAAEKLVQ 668
Cdd:PLN02939 328 DLRDKVDKLEASL---KEANVSKFSSYKVELLQQKLKLLEERL-----QASDHEIHSYIQLYQESI--KEFQDTLSKLKE 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
447-677 |
2.23e-03 |
|
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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 447 EQLLQEFRELLQYRDNSDKTLEANEML--LEKLRQRIHDKAVALE--RAIDEKFS------ALEEKEKELRQLRLAVRER 516
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLepIRELAERYAAARERLAelEYLRAALRlwfaqrRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 517 DHDLERLRDVLSSNEATMQSMESLLRAKGLE-VEQLSttcQNLQWLKEEMETKFSRWQkEQESIIQQLQTSLHDRNKEVE 595
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDrLEQLE---REIERLERELEERERRRA-RLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 596 DLSATLlcklgPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNS 675
Cdd:COG4913 384 ALRAEA-----AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
..
gi 525313637 676 EL 677
Cdd:COG4913 459 EL 460
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
84-666 |
2.42e-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: 43.24 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 84 EAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEkecnlELSEKLKGVTKNWEDVPGDqvkpdq 163
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE-----EMRARLAARKQELEEILHE------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 164 yteaLAQRDKRIEELNQSLAAQERlveqlsrEKQQLLHLLEEPtsmevqpMTEELLKQQKLNSHETTItqqsvsDSHLAE 243
Cdd:pfam01576 80 ----LESRLEEEEERSQQLQNEKK-------KMQQHIQDLEEQ-------LDEEEAARQKLQLEKVTT------EAKIKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 244 LQEKIQQTEATN-------KILQEKLNEMSYELKCAQESSQ-------KQDGTIQNLKETLKSRE---RETEELYQVIEG 306
Cdd:pfam01576 136 LEEDILLLEDQNsklskerKLLEERISEFTSNLAEEEEKAKslsklknKHEAMISDLEERLKKEEkgrQELEKAKRKLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 307 QndtmaklremlhqsqlgqlhssegTSPAQQQVALLdlqsalfcsQLEIQKLQRVVRQKERQLADAkqcvqfvEAAAHES 386
Cdd:pfam01576 216 E------------------------STDLQEQIAEL---------QAQIAELRAQLAKKEEELQAA-------LARLEEE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 387 EQQKEASWKHNQELRKALQQLQEELQ------NKSQQLRAWEAEKYNEIRTQ------------------EQNIQHLNHS 442
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLEseraarNKAEKQRRDLGEELEALKTEledtldttaaqqelrskrEQEVTELKKA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 443 LSHK----EQLLQEFREllqyrdnsdKTLEANEMLLEKLRQRIHDKAvALERAIDEKFSALEEKEKELRQLRLAVRERDH 518
Cdd:pfam01576 336 LEEEtrshEAQLQEMRQ---------KHTQALEELTEQLEQAKRNKA-NLEKAKQALESENAELQAELRTLQQAKQDSEH 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 519 DLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQT------------- 585
Cdd:pfam01576 406 KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDtqellqeetrqkl 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 586 SLHDRNKEVEDLSATLLcklgpGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGL----------LQSVSTR 655
Cdd:pfam01576 486 NLSTRLRQLEDERNSLQ-----EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkkrlqreLEALTQQ 560
|
650
....*....|.
gi 525313637 656 EQESQAAAEKL 666
Cdd:pfam01576 561 LEEKAAAYDKL 571
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
8-285 |
2.58e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 8 LSQHLNDLKKEnFSLKLRIYFLEERMQQKYEASREDIYKRNIE-------LKVEVESLKRE-------------LQDKKQ 67
Cdd:PLN03229 460 LNEMIEKLKKE-IDLEYTEAVIAMGLQERLENLREEFSKANSQdqlmhpvLMEKIEKLKDEfnkrlsrapnylsLKYKLD 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 68 HLDKTWADVENLNSQNEAE-LRRQFEERQQETEHVYELLEnKIQLLQEEsrLAKNEAARMAAL--------VEAEKECNL 138
Cdd:PLN03229 539 MLNEFSRAKALSEKKSKAEkLKAEINKKFKEVMDRPEIKE-KMEALKAE--VASSGASSGDELdddlkekvEKMKKEIEL 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 139 ELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKrIEELNqslaaqerlvEQLSREKQQLLHlleeptSMEVQPMTEEL 218
Cdd:PLN03229 616 ELAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEK-IESLN----------EEINKKIERVIR------SSDLKSKIELL 678
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 219 lkqqKLNSHETTITQQSVSDSHLAELQEKIQQ--TEATNKI-LQEKLNEMSYELKCAQESSQKQDGTIQN 285
Cdd:PLN03229 679 ----KLEVAKASKTPDVTEKEKIEALEQQIKQkiAEALNSSeLKEKFEELEAELAAARETAAESNGSLKN 744
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
1899-1983 |
2.87e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 42.73 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1899 QLCNENRVLREDNRRLQAQL----------SHVSREHSQETESLREA---------LLSSRSHLQELEKELEHQKVERQQ 1959
Cdd:pfam14817 317 QFLNELAETRSRCQQLQARLqglkdeaeleSLGIGDTSQNDSLLRQVlelelqaagLAASRDTLRSECQQLNKLARERQE 396
|
90 100
....*....|....*....|....
gi 525313637 1960 LLEDLREKQQEVLHFREERLSLQE 1983
Cdd:pfam14817 397 ALRSLQKKWQRILDFRQLVSELQE 420
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
738-932 |
3.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 738 PRSTLGDLDTVAGLEKELSNAKEELELmAKKERESQMELSALQSMMAVQEEELQVQAADMESLT-----RNIQIKEDLIK 812
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED-AREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 813 DLQMQLVDPEDipAMERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLvkfHA 892
Cdd:COG4913 299 ELRAELARLEA--ELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL---GL 373
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 525313637 893 HPESSERD-----RTLQVELEGAQVLRSRLEEVLGRSLERLNRLE 932
Cdd:COG4913 374 PLPASAEEfaalrAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
408-682 |
3.42e-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: 42.85 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 408 QEELQNKSQQLRAWEaEKYNEIRTQEQNIQHLNHSLSHKEQLLQEfrellQYRDNSDKTLEANEMlleklRQRIHDKAVA 487
Cdd:pfam01576 4 EEEMQAKEEELQKVK-ERQQKAESELKELEKKHQQLCEEKNALQE-----QLQAETELCAEAEEM-----RARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 488 LERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMEsllrakgLEVEQLSTTCQNLQ---WLKEE 564
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ-------LEKVTTEAKIKKLEediLLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 565 METKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSatllcKLGPGQSEIAEELCQRLQRKERMLQDL----------LSDR 634
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLS-----KLKNKHEAMISDLEERLKKEEKGRQELekakrklegeSTDL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 525313637 635 NKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQ 682
Cdd:pfam01576 221 QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
368-684 |
3.66e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 368 QLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQlraweaekyneIRTQEQNIQHLNHSLSHKE 447
Cdd:PRK11281 25 AFARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDK-----------IDRQKEETEQLKQQLAQAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 448 QLLQEF-RELLQYRDNSDKTLEANemlLEKLRQRihdkavALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDV 526
Cdd:PRK11281 94 AKLRQAqAELEALKDDNDEETRET---LSTLSLR------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 527 LSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqwlkeemetkfsrWQKEQESIiqQLQTSLhdRNKEVEdlSATLLCKLG 606
Cdd:PRK11281 165 LYANSQRLQQIRNLLKGGKVGGKALRPSQRVL-------------LQAEQALL--NAQNDL--QRKSLE--GNTQLQDLL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313637 607 PGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMeiqgllQSVSTREQESQAAAEKLVQALMERNSELQalrQYL 684
Cdd:PRK11281 226 QKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTV------QEAQSQDEAARIQANPLVAQELEINLQLS---QRL 294
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
226-1051 |
4.71e-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: 42.52 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 226 SHETTI-TQQSVSDSHLAELQEKIQQTEATnkiLQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQvi 304
Cdd:pfam12128 269 SDETLIaSRQEERQETSAELNQLLRTLDDQ---WKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAA-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 305 egqndtmaklremLHQSQLGQLHSSegtspaqqqvalLDLQSALFCSQLEiqKLQRVVRQKERQLADAK-QCVQFVEAAA 383
Cdd:pfam12128 344 -------------ADQEQLPSWQSE------------LENLEERLKALTG--KHQDVTAKYNRRRSKIKeQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 384 HESEQQKEASWKHNQELRKALQQLQEEL--QNKSQQLRAWEAEKYNEIRTQEQNIQhLNHSLSHKEQLLQefrellqyrd 461
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELreQLEAGKLEFNEEEYRLKSRLGELKLR-LNQATATPELLLQ---------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 462 nsdktLEANEMLLEKLRQrihdkavALERAidekFSALEEKEKELRQLRLAvreRDHDLERLRD----VLSSNEATMQSM 537
Cdd:pfam12128 466 -----LENFDERIERARE-------EQEAA----NAEVERLQSELRQARKR---RDQASEALRQasrrLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 538 ESLLRAKGLEVEQLSTTCQNlqwlkeemetkfsrWQKEQESIIQQLQTSLHDRNKEVEDLSATLLCKLG----------- 606
Cdd:pfam12128 527 LQLFPQAGTLLHFLRKEAPD--------------WEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYgvkldlkridv 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 607 PGQSEIAEELCQRLQRKERMLQDlLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYLgg 686
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQS-AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK-- 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 687 rdslmSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEdvsiprSTLGDLDTVAGLEKELSNAKEEL-ELM 765
Cdd:pfam12128 670 -----NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE------ARTEKQAYWQVVEGALDAQLALLkAAI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 766 AKKERESQMELSALQSMMAvqeEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIPAMERLTQEVLLLR-----EK 840
Cdd:pfam12128 739 AARRSGAKAELKALETWYK---RDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRrprlaTQ 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 841 VASVESQGQEISGN----------RRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKFHAHPESSERDRTLQVELEGA 910
Cdd:pfam12128 816 LSNIERAISELQQQlarliadtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQL 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 911 QVLRSRLEEVLGRSLERLNRLETLAAIGGAAAGDdtedtstEFTDSIEEEAAHHSHQQLVKVALEKSLATVEtqnPSFSP 990
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLA-------ETWESLREEDHYQNDKGIRLLDYRKLVPYLE---QWFDV 965
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313637 991 PSPMGGDSNRCLQEEMLHLRAEFHQHLEE-KRKAEEELKELKAQI-EEAGFSSVSHIRNTMLS 1051
Cdd:pfam12128 966 RVPQSIMVLREQVSILGVDLTEFYDVLADfDRRIASFSRELQREVgEEAFFEGVSESAVRIRS 1028
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-928 |
5.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 335 AQQQVALLDLQSALFcSQLEIQKLQRVVRQKERQLADAkqcvqfvEAAAHESEQQKEAswkHNQELRKALQQLQeelQNK 414
Cdd:COG4913 271 LAELEYLRAALRLWF-AQRRLELLEAELEELRAELARL-------EAELERLEARLDA---LREELDELEAQIR---GNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 415 SQQLRAWEAEkyneirtqeqnIQHLNHSLSHKEQLLQEFRELLQyrdNSDKTLEANEMLLEKLRQRIHDKAVALERAIDE 494
Cdd:COG4913 337 GDRLEQLERE-----------IERLERELEERERRRARLEALLA---ALGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 495 KFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRakglevEQLSTTCQNLQWLKEEME--TKFSRW 572
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA------EALGLDEAELPFVGELIEvrPEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 573 QKEQE---------------------SIIQQLQTSLH---------DRNKEVEDLSA-TLLCKL----GPGQSEIAEELC 617
Cdd:COG4913 477 RGAIErvlggfaltllvppehyaaalRWVNRLHLRGRlvyervrtgLPDPERPRLDPdSLAGKLdfkpHPFRAWLEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 618 QR-----------LQRKER--MLQDLLSDRNKQvleHEMEIQGLLQSV-----STREQ-----ESQAAAEKLVQALMERN 674
Cdd:COG4913 557 RRfdyvcvdspeeLRRHPRaiTRAGQVKGNGTR---HEKDDRRRIRSRyvlgfDNRAKlaaleAELAELEEELAEAEERL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 675 SELQALRQYLGGRDSLMSQapISNQQAEvtptgrlgkqtdqgsmqipsrddstsltakedvsiprstlgDLDtVAGLEKE 754
Cdd:COG4913 634 EALEAELDALQERREALQR--LAEYSWD-----------------------------------------EID-VASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 755 LSNAKEELELMakkeRESQMELSALQSMMAVQEEELQVQAADMESLTRNI-----QIK--EDLIKDLQMQLVDPEDIPAm 827
Cdd:COG4913 670 IAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIgrlekELEqaEEELDELQDRLEAAEDLAR- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 828 erlTQEVLLLREKVAsvesqgQEISGNRRQQlllMLEGLVDERSRLNEAL-QAERQLYSSLVKFHAHPESSERDrtLQVE 906
Cdd:COG4913 745 ---LELRALLEERFA------AALGDAVERE---LRENLEERIDALRARLnRAEEELERAMRAFNREWPAETAD--LDAD 810
|
650 660
....*....|....*....|..
gi 525313637 907 LEGAQVLRSRLEEVLGRSLERL 928
Cdd:COG4913 811 LESLPEYLALLDRLEEDGLPEY 832
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
414-964 |
5.56e-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: 42.12 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 414 KSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEfrELLQYRDnsdktleanemllekLRQRIHDKAVALERAID 493
Cdd:pfam10174 43 KERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQD--ELRAQRD---------------LNQLLQQDFTTSPVDGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 494 EKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQ 573
Cdd:pfam10174 106 DKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 574 K--EQESIIQQLQTSLHDRNKEVEDLSATLLCKL-GPGQSEIAEELCQRLQRKERMLQDLlsDRNKQVLEHEMEI---QG 647
Cdd:pfam10174 186 RiaEAEMQLGHLEVLLDQKEKENIHLREELHRRNqLQPDPAKTKALQTVIEMKDTKISSL--ERNIRDLEDEVQMlktNG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 648 LLQSVSTREQESQAAA------------EKLVQALMERNSELQALRQYLggrDSLMSQAPISNQQAEVTptgrlgkqtdq 715
Cdd:pfam10174 264 LLHTEDREEEIKQMEVykshskfmknkiDQLKQELSKKESELLALQTKL---ETLTNQNSDCKQHIEVL----------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 716 gsmqipsrddSTSLTAKEDVSIPRSTLGDLDTVAGLEKE--LSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQ 793
Cdd:pfam10174 330 ----------KESLTAKEQRAAILQTEVDALRLRLEEKEsfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 794 AADMESLTRNIQIKEDLIKDLQ--MQLVDPEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQQLllmleglvDERS 871
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKerVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL--------EELE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 872 RLNEALQAERQLYSSLvkfhaHPESSERDRTLQVELEGAQVLRSR----------LEEVLGRSLERLNRLETlaAIGGAA 941
Cdd:pfam10174 472 SLKKENKDLKEKVSAL-----QPELTEKESSLIDLKEHASSLASSglkkdsklksLEIAVEQKKEECSKLEN--QLKKAH 544
|
570 580
....*....|....*....|....*.
gi 525313637 942 AGDDTEDTSTEFTDSI---EEEAAHH 964
Cdd:pfam10174 545 NAEEAVRTNPEINDRIrllEQEVARY 570
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1902-2017 |
6.03e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.27 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1902 NENRVLREDNRRLQAQLSHVSREHsQETESLREALLSSRSHLQEL--EKELEhqkvERQQLLEDLREKQQEVLHFREERL 1979
Cdd:pfam15619 67 EEVRVLRERLRRLQEKERDLERKL-KEKEAELLRLRDQLKRLEKLseDKNLA----EREELQKKLEQLEAKLEDKDEKIQ 141
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 525313637 1980 SLQE----NDSRLQHKLVLLQQQCEEKQQLFESLQSELQIYE 2017
Cdd:pfam15619 142 DLERklelENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQ 183
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
471-682 |
7.44e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 471 EMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRlavreRDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQ 550
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 551 LSTTCQNLQWLKEEMETKFSRWQkeQESIIQQLQTSLHDRNKEVEDLSATLlcklGPGQSEIaeelcQRLQRKERMLQDL 630
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARY----TPNHPDV-----IALRAQIAALRAQ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525313637 631 LSDRNKQVLEhemEIQGLLQSVSTREQESQAAAEKL---VQALMERNSELQALRQ 682
Cdd:COG3206 307 LQQEAQRILA---SLEAELEALQAREASLQAQLAQLearLAELPELEAELRRLER 358
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1844-2018 |
7.85e-03 |
|
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: 40.90 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1844 LEEHLGEIRNLRQRLEESICINDRLREQLEHRLTSTARGRGSTSNFYSQGLESIPQLCNENRVLREDNRRLQAQLSHVSR 1923
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 1924 EHSQETESLREALLSSRSHLQELEKELEHQKV---ERQQLLEDLREKQQEV----LHFREERLSLQENDSRLQHKLVLLQ 1996
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlapARREQAEELRADLAELaalrAELEAERAELEALLAELEEERAALE 191
|
170 180
....*....|....*....|..
gi 525313637 1997 QQCEEKQQLFESLQSELQIYEA 2018
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAA 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
609-918 |
8.25e-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: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 609 QSEIAEELcQRLQRKERMLQ-DLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYLGGR 687
Cdd:TIGR02168 208 QAEKAERY-KELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 688 DSLMSQapISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKedvsipRSTLGDLDTVAGLEKELSNAKEELELMAK 767
Cdd:TIGR02168 287 QKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEELE------SKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 768 KERESQMELSALQSMMAVQEEELQVQAAD-------MESLTRNIQIKEDLIKDLQMQLvdpedipamERLTQEVLLLREK 840
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKvaqlelqIASLNNEIERLEARLERLEDRR---------ERLQQEIEELLKK 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313637 841 VASVESQGQEISGNRRQQlllMLEGLVDERSRLNEALQAERQLYSslVKFHAHPESSERDRTLQVELEGAQVLRSRLE 918
Cdd:TIGR02168 430 LEEAELKELQAELEELEE---ELEELQEELERLEEALEELREELE--EAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
103-459 |
8.38e-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: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 103 ELLENKIQLLQEESR--LAKNEAARMAALVEAE--KECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEEL 178
Cdd:pfam07888 30 ELLQNRLEECLQERAelLQAQEAANRQREKEKEryKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 179 NQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSH-ETTITQQSVSDSHLAELQEKIQQTEATNKI 257
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERaKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 258 LQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEgqndTMAKLREMLHQSQ-----LGQLHSSEGT 332
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQERLNASErkvegLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313637 333 SPAQQQVALLdlQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAahesEQQKEASWKHNQELRKALQQLQEElQ 412
Cdd:pfam07888 266 QRDRTQAELH--QARLQAAQLTLQLADASLALREGRARWAQERETLQQSA----EADKDRIEKLSAELQRLEERLQEE-R 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 525313637 413 NKSQQLRAWEAEKYNEIRTQ----EQNIQHLNHSL----SHKEQLLQEFRELLQY 459
Cdd:pfam07888 339 MEREKLEVELGREKDCNRVQlsesRRELQELKASLrvaqKEKEQLQAEKQELLEY 393
|
|
| |
