|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
160-719 |
1.69e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 160 LFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQA 239
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 240 QRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERE 319
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 320 RILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLV 399
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 400 KHKDDSSKAYRERTDAQISDLEQRLADcaekmksLQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKTARLEE 479
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLL-------LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 480 ELLAVQRDRETEankyqdNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVS--VEIAKALEETRKQREE 557
Cdd:COG1196 543 ALAAALQNIVVE------DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGaaVDLVASDLREADARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 558 LQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQQEVL 637
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 638 RQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGTVTVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTL 717
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
..
gi 121308974 718 QK 719
Cdd:COG1196 777 EA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-599 |
5.51e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 5.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 50 RDDFSSQIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSSMRKLQDQNEsfQTNRAKMAEAMSLALEKKD 129
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE--LLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 130 QEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTA 209
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 210 RLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKS 289
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 290 MEHLQSEHNKLKLQHEQHKNKVAVTEEERERilSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGELLQ 369
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEAD--YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 370 EKTSHTTAVSSLEAQVSRQN----ASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHT 445
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAkagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 446 DKLQMEWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKyqdnlRLLEEEKNSLLRSKGETDSTVESLTA 525
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE-----AELEELAERLAEEELELEEALLAEEE 704
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121308974 526 ELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQA 599
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-718 |
1.08e-18 |
|
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: 91.66 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 55 SQIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSsMRKLQDQNESFQTNRAKmAEAMSLALEKKDQEWME 134
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-LANLERQLEELEAQLEE-LESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 135 KLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKvkhmLLRREEQLNQREKELKLRGEELNTARLTLG 214
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 215 KTQDKLYELGEEHE--EICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEH 292
Cdd:TIGR02168 421 QEIEELLKKLEEAElkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 293 LQSEHNKLK-LQHEQHK---------NKVAVTEEERERILSDLQEKAASLE-RRLEANFSQDEHLQELLKEKSSL----- 356
Cdd:TIGR02168 501 LEGFSEGVKaLLKNQSGlsgilgvlsELISVDEGYEAAIEAALGGRLQAVVvENLNAAKKAIAFLKQNELGRVTFlplds 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 357 --EQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYR------------------------ 410
Cdd:TIGR02168 581 ikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALElakklrpgyrivtldgdlvrpggv 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 411 -----ERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQmewsEERERLQQQVSTQRQRGLEKTARLEEELLAVQ 485
Cdd:TIGR02168 661 itggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLA 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 486 RDRETEANkyqdnlrlLEEEKNSLLRSKGETDSTVESLTAELEQSRAEmssrqtvsveiakaLEETRKQREELQQQVSKM 565
Cdd:TIGR02168 737 RLEAEVEQ--------LEERIAQLSKELTELEAEIEELEERLEEAEEE--------------LAEAEAEIEELEAQIEQL 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 566 TESLVKAEQEVSRLsqdlgvkEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREH---NSQLTSLQQEVLRQTQQ 642
Cdd:TIGR02168 795 KEELKALREALDEL-------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIeelSEDIESLAAEIEELEEL 867
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121308974 643 LSSYQSRVSDLESEVLSLTAHSHADECEGEQngtvTVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQ 718
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEE----LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-745 |
2.21e-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: 87.42 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 125 LEKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKLRGE 204
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 205 ELNTARLTLGKTQDKLyelgeehEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAE 284
Cdd:TIGR02168 296 EISRLEQQKQILRERL-------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 285 ALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLE------- 357
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleeleee 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 358 --------QRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQ--ISDLEQRLAD- 426
Cdd:TIGR02168 449 leelqeelERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsgLSGILGVLSEl 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 427 --CAEKMK---------SLQQQLKDSQMHTDKLQ--MEWSEERERLQQQVSTQRQRGLEKTARL----EEELLAVQRDRE 489
Cdd:TIGR02168 529 isVDEGYEaaieaalggRLQAVVVENLNAAKKAIafLKQNELGRVTFLPLDSIKGTEIQGNDREilknIEGFLGVAKDLV 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 490 TEANKYQDNL--------------------RLLEEEKN-------------SLLRSKGETDSTVESLTAELEQSRAEMSS 536
Cdd:TIGR02168 609 KFDPKLRKALsyllggvlvvddldnalelaKKLRPGYRivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 537 RQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECES--- 613
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElee 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 614 RRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEV--LSLTAHSHADECEGEQNGTVTVSD-LDQLQKVNK 690
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtlLNEEAANLRERLESLERRIAATERrLEDLEEQIE 848
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 121308974 691 DLEQQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPDSEMKErLQDGRQERSAE 745
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL-LRSELEELSEE 902
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
52-737 |
2.37e-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: 87.42 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 52 DFSSQIQRRNDQIRKLEaklsdyaEQLRLMQKTKEKLEIALEKYQdssmRKLQDQNESFQTNRAKMAEamslaLEKKDQE 131
Cdd:TIGR02168 292 ALANEISRLEQQKQILR-------ERLANLERQLEELEAQLEELE----SKLDELAEELAELEEKLEE-----LKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 132 WMEKLASLEQEKLSLTSRLDEMTEQSLSLfqkRDDLDELEgfqqQELAKVKHMLLRREEQLNQREKELKLRGEELNTARL 211
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETL---RSKVAQLE----LQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 212 TLGKTQDKlyelgeeheEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSME 291
Cdd:TIGR02168 429 KLEEAELK---------ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 292 HLQSEHNKLK-LQHEQHK---------NKVAVTEEERERILSDLQEKAASLE-RRLEANFSQDEHLQELLKEKSSL---- 356
Cdd:TIGR02168 500 NLEGFSEGVKaLLKNQSGlsgilgvlsELISVDEGYEAAIEAALGGRLQAVVvENLNAAKKAIAFLKQNELGRVTFlpld 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 357 ---EQRLEEARGELLQEKTSHTTAVSSLE-----------------------------AQVSRQNASIIDLQTLVKHKDD 404
Cdd:TIGR02168 580 sikGTEIQGNDREILKNIEGFLGVAKDLVkfdpklrkalsyllggvlvvddldnalelAKKLRPGYRIVTLDGDLVRPGG 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 405 SSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQmewsEERERLQQQVSTQRQRGLEKTARLEEELLAV 484
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 485 QRdRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSK 564
Cdd:TIGR02168 736 AR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 565 MTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECEsrrlEAEEKEREHNSQLTSLQQEVLRQTQQLS 644
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALA 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 645 SYQSRVSDLESEVLSLTAHSHADEcegeqngtvtvSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKELKLK 724
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELR-----------RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
730
....*....|...
gi 121308974 725 PDPDSEMKERLQD 737
Cdd:TIGR02168 960 ENKIEDDEEEARR 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
124-624 |
6.47e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 124 ALEKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKLRG 203
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 204 EELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNA 283
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 284 EALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEA 363
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 364 RGELLQEKTSHTTAVSSLEAQ---------VSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSL 434
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYegflegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 435 QQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEktARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKG 514
Cdd:COG1196 563 IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA--VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 515 ETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALK 594
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500 510
....*....|....*....|....*....|
gi 121308974 595 EELQAARSSLSSLQAECESRRLEAEEKERE 624
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEE 750
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
63-765 |
1.29e-14 |
|
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: 78.57 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 63 QIRKLEAKLSDYAEQLRLMQKTKEKLEialeKYQDSSMRKlqdqNESFQTNRAKMAEAMSLALEKKDQEwmekLASLEQE 142
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAE----RYQALLKEK----REYEGYELLKEKEALERQKEAIERQ----LASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 143 KLSLTSRLDEMTEQSLSLFQKRDDLD-ELEGFQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTLGKTQDKLY 221
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNkKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 222 ELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLK 301
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 302 LQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGELLQ---EKTSHTTAV 378
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRvekELSKLQREL 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 379 SSLEAQVSRQNASIIDLQTLVKHKDDSSK----------------------AYRERTDAQISDLEQRLADCAEKMKSLQ- 435
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryataievAAGNRLNNVVVEDDAVAKEAIELLKRRKa 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 436 --------QQLKDSQMHTDKLQM-----------EWSEERERLQQQV-----------STQRQRGLEKTARLEEELL--- 482
Cdd:TIGR02169 573 gratflplNKMRDERRDLSILSEdgvigfavdlvEFDPKYEPAFKYVfgdtlvvedieAARRLMGKYRMVTLEGELFeks 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 483 --------------AVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKAL 548
Cdd:TIGR02169 653 gamtggsraprggiLFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 549 EETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHN-S 627
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIeA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 628 QLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHShADECEGEQNGTVTVSDLDQ----LQKVNKDLEQQLAEKNKTI 703
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGKKEELEEeleeLEAALRDLESRLGDLKKER 891
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121308974 704 KQLQQRLAELKRTLQkELKLKPDPDSEMKERLQDGRQERSAEKTVLETPMPTAAPSPALGLS 765
Cdd:TIGR02169 892 DELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS 952
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
305-662 |
4.63e-14 |
|
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: 76.65 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 305 EQHKNKVAVTEEERERILSDLQEKAASLERrLEANFSQDEHLQELLKEKSSLEQRleeargELLQEKTSHTTAVSSLEAQ 384
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLER-LRREREKAERYQALLKEKREYEGY------ELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 385 VSRQNASIIDLQtlvkhkddsskayrertdAQISDLEQRLADCAEKMKSLQQQLKDsqmhtdklqmEWSEERERLQQQV- 463
Cdd:TIGR02169 246 LASLEEELEKLT------------------EEISELEKRLEEIEQLLEELNKKIKD----------LGEEEQLRVKEKIg 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 464 STQRQRglEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVE 543
Cdd:TIGR02169 298 ELEAEI--ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 544 IAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKER 623
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 121308974 624 EHNS---QLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTA 662
Cdd:TIGR02169 456 KLEQlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-509 |
1.61e-12 |
|
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: 71.63 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 155 EQSLSLFQKRDDLDELEG---FQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTLGKTQDKLYELGEEHEEIC 231
Cdd:TIGR02168 667 KTNSSILERRREIEELEEkieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 232 RTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKlqheqhknkv 311
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN---------- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 312 avteeereRILSDLQEKAASLERRLEAnfsQDEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNAS 391
Cdd:TIGR02168 817 --------EEAANLRERLESLERRIAA---TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 392 IIDLQTLVKHKDDsskayrerTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHtdklqmewseeRERLQQQVSTQRQRGL 471
Cdd:TIGR02168 886 EEALALLRSELEE--------LSEELRELESKRSELRRELEELREKLAQLELR-----------LEGLEVRIDNLQERLS 946
|
330 340 350
....*....|....*....|....*....|....*...
gi 121308974 472 EKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSL 509
Cdd:TIGR02168 947 EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
126-671 |
3.27e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 126 EKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDElegfqqqelakvkhMLLRREEqlnqREKELKLRGEE 205
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE--------------VLEEHEE----RREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 206 LNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSE-------KEEAERRVVDLERREQELQQLIQQVSEDFQK 278
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 279 AQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERErilsDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQ 358
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE----DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 359 RLEEARGELLQEKTSHTTAVSSLEAQVsRQNASIID---LQTLVKHKDDSSKAYR-ERTDAQISDLEQRLADCAEKMKSL 434
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERV-EEAEALLEagkCPECGQPVEGSPHVETiEEDRERVEELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 435 QQQLKdsqmhTDKLQMEWSEERERLQQQVSTQRQRGLEKTARLEEellavQRDRETEANKYQDNLRLLEEEKNSLLRSKG 514
Cdd:PRK02224 495 EERLE-----RAEDLVEAEDRIERLEERREDLEELIAERRETIEE-----KRERAEELRERAAELEAEAEEKREAAAEAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 515 ETDSTVESLTAELEQSRAEMSSRqtvsVEIAKALEETRKQREELQQQVSKMTESLvKAEQEVSRLSQD-LGVKEEEVNAL 593
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKER----IESLERIRTLLAAIADAEDEIERLREKR-EALAELNDERRErLAEKRERKREL 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 594 KEELQAAR-SSLSSLQAECESRRLEAEEKEREHNSQLTSLQQE---VLRQTQQLSSYQSRVSDLESEVLSL-TAHSHADE 668
Cdd:PRK02224 640 EAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEALeALYDEAEE 719
|
...
gi 121308974 669 CEG 671
Cdd:PRK02224 720 LES 722
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
63-645 |
5.60e-12 |
|
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: 69.71 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 63 QIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQdSSMRKLQDQNESFQTNRAKMAEAMS-------------LALEKKD 129
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLL-AEIEELEREIEEERKRRDKLTEEYAelkeeledlraelEEVDKEF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 130 QEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTA 209
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 210 RLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQ----------QVSEDFQKA 279
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgSVGERYATA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 280 QSNA-------------EALEKSMEHLQSEH---------NKLKLQH----------------------EQHKNKVA--- 312
Cdd:TIGR02169 541 IEVAagnrlnnvvveddAVAKEAIELLKRRKagratflplNKMRDERrdlsilsedgvigfavdlvefdPKYEPAFKyvf 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 313 ----VTE--EERERIL---------SDLQEKAASL------ERRLEANF-SQDEHLQELLKEKSSLEQRLEEargeLLQE 370
Cdd:TIGR02169 621 gdtlVVEdiEAARRLMgkyrmvtleGELFEKSGAMtggsraPRGGILFSrSEPAELQRLRERLEGLKRELSS----LQSE 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 371 KTSHTTAVSSLEAQVSRQNASIIDLQ---TLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDK 447
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 448 LQMEWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAEL 527
Cdd:TIGR02169 777 LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 528 EQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSL 607
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
650 660 670
....*....|....*....|....*....|....*...
gi 121308974 608 QAEcesrrLEAEEKEREHNSQLTSLQQEVLRQTQQLSS 645
Cdd:TIGR02169 937 EDP-----KGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-653 |
4.48e-11 |
|
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: 67.00 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 278 KAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSS-- 355
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAel 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 356 --LEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKhKDDSSKAYRERTDAQISDLEQRLADCAEKMKS 433
Cdd:TIGR02168 263 qeLEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE-RLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 434 LQQQLKDSQmhtdklqmewsEERERLQQQvstqrqrgLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLlrsk 513
Cdd:TIGR02168 342 LEEKLEELK-----------EELESLEAE--------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 514 getDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEEtrKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNAL 593
Cdd:TIGR02168 399 ---NNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 594 KEELQAARSSLSSLQAecesrRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDL 653
Cdd:TIGR02168 474 EQALDAAERELAQLQA-----RLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
422-737 |
5.88e-11 |
|
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: 66.62 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 422 QRLADCAEKMKSLQQQLKDSQMHTDKLQM-EWSEERERLQQQvstqrqrgLEKTARLEEELLAVQRDRETEANKYQDNLR 500
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLeELREELEELQEE--------LKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 501 LLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQqqvskmtESLVKAEQEVSRLS 580
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA-------EELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 581 QDLGVKEEEVNALKEELQAARSSLSSLQAECE---SRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEV 657
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 658 LSLTAHSHADECEGEQNGtvtvsdLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQkELKLKPDPDSEMKERLQD 737
Cdd:TIGR02168 431 EEAELKELQAELEELEEE------LEELQEELERLEEALEELREELEEAEQALDAAERELA-QLQARLDSLERLQENLEG 503
|
|
| Grip |
smart00755 |
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245; |
788-833 |
8.66e-11 |
|
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
Pssm-ID: 197860 Cd Length: 46 Bit Score: 57.62 E-value: 8.66e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 121308974 788 EINFEYLKHVVLKFMSSREAEAFQLIRAVSVLLHFSKEEEDMLKQT 833
Cdd:smart00755 1 EANFEYLKNVLLQFLTLRESERETLLPVISTVLQLSPEEMQKLLEV 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
133-712 |
1.34e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 133 MEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEG-----FQQQELAKVKHMLLRREEQLNQREKELKLRGEELN 207
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 208 TARLTLGKTQDKLYELGEEHEEicrtnsQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALE 287
Cdd:COG4913 320 ALREELDELEAQIRGNGGDRLE------QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 288 KSMEHLQSEhnklkLQHEQHKNKVAVTEEEREriLSDLQEKAASLERRleaNFSQDEHLQELLKE-KSSLEQRLEEAR-- 364
Cdd:COG4913 394 EALEEELEA-----LEEALAEAEAALRDLRRE--LRELEAEIASLERR---KSNIPARLLALRDAlAEALGLDEAELPfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 365 GELLQ------------EKTSHTTAVSSL-EAQVSRQNASIID-------LQTLVKHKDDSSKAYRERTDAQISD----- 419
Cdd:COG4913 464 GELIEvrpeeerwrgaiERVLGGFALTLLvPPEHYAAALRWVNrlhlrgrLVYERVRTGLPDPERPRLDPDSLAGkldfk 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 420 -------LEQRLAD-----CAEKmkslQQQLKDSQMH-TDKLQMEWSEERERLQQQVSTQRQRGL-----EKTARLEEEL 481
Cdd:COG4913 544 phpfrawLEAELGRrfdyvCVDS----PEELRRHPRAiTRAGQVKGNGTRHEKDDRRRIRSRYVLgfdnrAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 482 LAVQRDRETEANKYQDN---LRLLEEEKNSL--LRSKGETDSTVESLTAELEQSRAEMssrqtvsveiaKALEETRKQRE 556
Cdd:COG4913 620 AELEEELAEAEERLEALeaeLDALQERREALqrLAEYSWDEIDVASAEREIAELEAEL-----------ERLDASSDDLA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 557 ELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQQEV 636
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121308974 637 LRQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGTVTVSDLDQLQKVNKDLEQQ-LAEKNKTIKQLQQRLAE 712
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDgLPEYEERFKELLNENSI 845
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-723 |
8.87e-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: 62.77 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 411 ERTDAQISDLEQRLADCAEKMKSLQQQLKDSQmhtdKLQmEWSEERERLQQQVSTQR-QRGLEKTARLEEELLAVQRDRE 489
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAE----RYK-ELKAELRELELALLVLRlEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 490 teanKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESL 569
Cdd:TIGR02168 257 ----ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 570 VKAEQEVSRLSQDLGVKEEEVNALKEELQAARS---SLSSLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSY 646
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 647 QSRVSDLESEVLSL-TAHSHADECEGEQNGTVTVSDLDQLQKVNKDLEQQLAEKNKTI--------------KQLQQRLA 711
Cdd:TIGR02168 413 EDRRERLQQEIEELlKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELeeaeqaldaaerelAQLQARLD 492
|
330
....*....|..
gi 121308974 712 ELKRTLQKELKL 723
Cdd:TIGR02168 493 SLERLQENLEGF 504
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
286-657 |
1.01e-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: 62.44 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 286 LEKSMEHLQSE-HNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQE--------LLKEKSSL 356
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEqarnqnsmYMRQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 357 EQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCA---EKMKS 433
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlekEQNKR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 434 LQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQrdreteankyqdnlrlleeeknsllrSK 513
Cdd:pfam15921 403 LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQ--------------------------GK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 514 GETDSTVESLTAELEQSRAEMssRQTVSVEIAK--ALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVN 591
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEML--RKVVEELTAKkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121308974 592 ALKEElqaaRSSLSSLQAECESRRLEAEEKERE---HNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEV 657
Cdd:pfam15921 535 HLKNE----GDHLRNVQTECEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-567 |
2.74e-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: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 199 LKLRGEELNTARL--TLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQqliqqvsedf 276
Cdd:TIGR02169 660 RAPRGGILFSRSEpaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE---------- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 277 QKAQSNAEALEKSMEHLQSEHNKLkLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQ--DEHLQELLKEKS 354
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEI-ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiQAELSKLEEEVS 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 355 SLEQRLEEARGELlqektshtTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSL 434
Cdd:TIGR02169 809 RIEARLREIEQKL--------NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 435 QQQLKDSQMHTDKLQMEWSEERERLQQQvSTQRQRGLEKTARLEEELLAVqrdreteankyQDNLRLLEEEKNSLLRSKG 514
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKAKLEAL-----------EEELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 121308974 515 ETDStVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTE 567
Cdd:TIGR02169 949 EELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
50-763 |
8.94e-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: 59.36 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 50 RDDFSSQIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSSMRKLQDQNESFQTNRAKMAEAMSLalekkd 129
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRM------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 130 qeWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDElegfqqqELAKVKHMLLRREEQLNQREKELKLRGEELNTA 209
Cdd:pfam15921 340 --YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD-------QLQKLLADLHKREKELSLEKEQNKRLWDRDTGN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 210 RLTLGKTQDklyELGEEHEEICRTNSQLQAQRDELlseKEEAERRVVDLERREQELQQliqqVSEDFQKAQSNAEALEKS 289
Cdd:pfam15921 411 SITIDHLRR---ELDDRNMEVQRLEALLKAMKSEC---QGQMERQMAAIQGKNESLEK----VSSLTAQLESTKEMLRKV 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 290 MEHLQSEHNKLKlQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANF-------SQDEHLQELLKEKSSLEQRLEE 362
Cdd:pfam15921 481 VEELTAKKMTLE-SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLqelqhlkNEGDHLRNVQTECEALKLQMAE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 363 ARG--ELLQEKTSHTTAVSSLEAQVSrqNASIIDLQTLVKHKDDSS------KAYRERTDAQISDLEQRLADCA-EKMKS 433
Cdd:pfam15921 560 KDKviEILRQQIENMTQLVGQHGRTA--GAMQVEKAQLEKEINDRRlelqefKILKDKKDAKIRELEARVSDLElEKVKL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 434 LQQqlkdsqmhtdklqmewSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLlrsk 513
Cdd:pfam15921 638 VNA----------------GSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKL---- 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 514 getDSTVESLTAELEQSRAEMSSRQ-------TVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLsqdlgvk 586
Cdd:pfam15921 698 ---KMQLKSAQSELEQTRNTLKSMEgsdghamKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFL------- 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 587 EEEVNALKEELQAARSSLSSLQAECESRRleaeEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHA 666
Cdd:pfam15921 768 KEEKNKLSQELSTVATEKNKMAGELEVLR----SQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 667 DECEGEQNGTVTVSDLdqlqKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQDGRQERSAEK 746
Cdd:pfam15921 844 DVKELQGPGYTSNSSM----KPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEP 919
|
730
....*....|....*..
gi 121308974 747 TVLETPMPTAAPSPALG 763
Cdd:pfam15921 920 TVQLSKAEDKGRAPSLG 936
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
114-750 |
1.13e-08 |
|
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: 59.21 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 114 RAKMAEAMSLALEKKDQEwmEKLASLEQEKLSLTSRLDEMTEQSLSLFQ-KRDDLDELEGFQQQELAK-------VKHML 185
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKK--EALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLEleeeyllYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 186 LRREEQLNQREKELKLRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQEL 265
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 266 QQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEH 345
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 346 LQELLKEKSSLEQR----LEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLqTLVKHKDDSSKAYRERTDAQISDLE 421
Cdd:pfam02463 393 KEEELELKSEEEKEaqllLELARQLEDLLKEEKKEELEILEEEEESIELKQGKL-TEEKEELEKQELKLLKDELELKKSE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 422 QRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERL-------QQQVSTQRQRGLEKTARLEEELLAVQRDRETEANK 494
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLkvllaliKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 495 YQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKAL-------------------------- 548
Cdd:pfam02463 552 EVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaqldkatleadeddkrakvvegilkd 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 549 -------EETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEK 621
Cdd:pfam02463 632 teltklkESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 622 EREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGTVTVSdldqLQKVNKDLEQQLAEKNK 701
Cdd:pfam02463 712 LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS----LKEKELAEEREKTEKLK 787
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 121308974 702 TIKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQDGRQERSAEKTVLE 750
Cdd:pfam02463 788 VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
237-712 |
1.56e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 237 LQAQRDELLSEKEEAERRvvdlERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEE 316
Cdd:PRK02224 211 LESELAELDEEIERYEEQ----REQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 317 ERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARgellqektshtTAVSSLEAQVSRQNASIIDLQ 396
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR-----------VAAQAHNEEAESLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 397 TLVKHKDDSSKAYR---ERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLqqqvstqrqrglek 473
Cdd:PRK02224 356 ERAEELREEAAELEselEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER-------------- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 474 tARLEEELLAVQRDRETEANKYQDNLRLLEE----------EKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTvSVE 543
Cdd:PRK02224 422 -DELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEE-RLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 544 IAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSlsslQAECESRRLEAEEKER 623
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA----AAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 624 EHNSQLTSLQQEvLRQTQQLSSYQSRVSDLESEVLSLTahshadecegeqngtvtvSDLDQLQKVNKDLEQQLAEKNKTI 703
Cdd:PRK02224 576 ELNSKLAELKER-IESLERIRTLLAAIADAEDEIERLR------------------EKREALAELNDERRERLAEKRERK 636
|
....*....
gi 121308974 704 KQLQQRLAE 712
Cdd:PRK02224 637 RELEAEFDE 645
|
|
| GRIP |
pfam01465 |
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ... |
788-830 |
3.26e-08 |
|
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.
Pssm-ID: 460221 [Multi-domain] Cd Length: 44 Bit Score: 50.04 E-value: 3.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 121308974 788 EINFEYLKHVVLKFMSSREA-EAFQLIRAVSVLLHFSKEEEDML 830
Cdd:pfam01465 1 GANLEYLKNVLLQFLESKESsERKQLLPVIATLLKFSPEEEQKI 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
53-576 |
4.44e-08 |
|
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: 56.95 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 53 FSSQIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEK-----------LEIALEKYQDSSMRKLQDQNE--SFQTNRAKMAE 119
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKflteikkkekeLEKLNNKYNDLKKQKEELENElnLLEKEKLNIQK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 120 AMSLALEK--KDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLfqkRDDLDELegfqQQELAKVKHMLLRREEQLNQREK 197
Cdd:TIGR04523 188 NIDKIKNKllKLELLLSNLKKKIQKNKSLESQISELKKQNNQL---KDNIEKK----QQEINEKTTEISNTQTQLNQLKD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 198 ELKLRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRD-----ELLSEKEEAERRVVDLERREQELQQLIQQV 272
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 273 SEDFQKaqsnaeaLEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILS---DLQEKAASLERRLEANFSQDEHLQEL 349
Cdd:TIGR04523 341 NEQISQ-------LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQeikNLESQINDLESKIQNQEKLNQQKDEQ 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 350 LKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYR---ERTDAQISDLEQRLAD 426
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsiNKIKQNLEQKQKELKS 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 427 CAEKMKSLQQQLKDSQMHTDKLQMEWSEERERlQQQVSTQRQRGLEKTARLEEELLAVQRDR-----ETEANKYQDNLRL 501
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDELNKDDFELkkenlEKEIDEKNKEIEE 572
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121308974 502 LEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEV 576
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
524-747 |
8.40e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 524 TAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSS 603
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 604 LSSLQAEcESRRLEAEEKEREHNSQLTSLQQE----VLRQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGTVTV 679
Cdd:COG4942 99 LEAQKEE-LAELLRALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121308974 680 SDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQDGRQERSAEKT 747
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
187-737 |
9.82e-08 |
|
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: 55.95 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 187 RREEQLNQREKELKLRGEELNTARLTLGKTQDKLYELGEEH---EEICRTNSQLQAQRDE----LLSEKEEAERRVVDLE 259
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKnalQEQLQAETELCAEAEEmrarLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 260 RREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEEReRILSDLQEKaaslerrlean 339
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDI-LLLEDQNSK----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 340 fsqdehlqeLLKEKSSLEQRLEEARGELLQEKTShttaVSSLEAQVSRQNASIIDLQTLVKHKDDSskayRERTDAQISD 419
Cdd:pfam01576 150 ---------LSKERKLLEERISEFTSNLAEEEEK----AKSLSKLKNKHEAMISDLEERLKKEEKG----RQELEKAKRK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 420 LEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLQQQvSTQRQRGLEKTARLEEELLAVQRDRETEA---NKYQ 496
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEE-TAQKNNALKKIRELEAQISELQEDLESERaarNKAE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 497 DNLRLLEEEKNSLlrsKGETDSTVESLTAELEQSraemSSRQTVSVEIAKALE-ETRKQREELQQQVSKMTESLVKAEQE 575
Cdd:pfam01576 292 KQRRDLGEELEAL---KTELEDTLDTTAAQQELR----SKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 576 VSRLSQDLGVKEEEVNALKEELQAARSSLSSLQaeceSRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLES 655
Cdd:pfam01576 365 LEQAKRNKANLEKAKQALESENAELQAELRTLQ----QAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 656 EVLSLTAHSHADECEGEQNGTVTVSDLDQLQKVNKDLEQ-------------QLAEKNKTIKQLQQRLAELKRTLQKELK 722
Cdd:pfam01576 441 ELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEetrqklnlstrlrQLEDERNSLQEQLEEEEEAKRNVERQLS 520
|
570
....*....|....*
gi 121308974 723 LKPDPDSEMKERLQD 737
Cdd:pfam01576 521 TLQAQLSDMKKKLEE 535
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
338-615 |
1.30e-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: 54.77 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 338 ANFSQDEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAQvsrqnasiidlqtlvkhkddsskayrertDAQI 417
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----------------------------ERRI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 418 SDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLQQQVstqrqRGLEKTARLEEELLAVQRDRETEANKYQD 497
Cdd:COG4942 65 AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL-----RALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 498 NLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEmssrqtvsveIAKALEETRKQREELQQQVSkmteslvKAEQEVS 577
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAE----------LEALLAELEEERAALEALKA-------ERQKLLA 202
|
250 260 270
....*....|....*....|....*....|....*...
gi 121308974 578 RLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRR 615
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
127-742 |
1.61e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 127 KKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLfQKRDDLDELEGFQQQELAKVKHMLLRREEQlnqREKELKLRGEEL 206
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAK-KKAEDARKAEEARKAEDARKAEEARKAEDA---KRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 207 NTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQ--RDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAE 284
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 285 ALEKsmEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEAR 364
Cdd:PTZ00121 1244 KAEE--ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 365 GellqektshttavsslEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQmh 444
Cdd:PTZ00121 1322 K----------------KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-- 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 445 tdKLQMEWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSL--LRSKGETDSTVES 522
Cdd:PTZ00121 1384 --KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdeAKKKAEEAKKAEE 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 523 LTAELEQSRAEMSSRQTV-----SVEIAKALEETRKQREELQQ--QVSKMTESLVKAEQevSRLSQDLGVKEEEVNAlkE 595
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAeeakkADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEE--AKKADEAKKAEEAKKA--D 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 596 ELQAARSSLSSLQAECESRRLEAEEKER-EHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQN 674
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 675 GTVTVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQ--RLAELKRTLQKELKLKPDPDSEMKERLQDGRQER 742
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-599 |
2.56e-07 |
|
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: 54.64 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 55 SQIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSSmrKLQDQNESFQTNRAKMAEAMSLALEKKDQEWME 134
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI--KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 135 KLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRRE------EQLNQREKELKLRGEELNT 208
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllsnlKKKIQKNKSLESQISELKK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 209 ARLTLGKTQDKLY-ELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERreqeLQQLIQQVSEDFQKAQSNAEALE 287
Cdd:TIGR04523 226 QNNQLKDNIEKKQqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKSEISDLN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 288 KSMEhlQSEHNKLKLQHEQHKNKVAVTE---EERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEAR 364
Cdd:TIGR04523 302 NQKE--QDWNKELKSELKNQEKKLEEIQnqiSQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 365 GELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSS----------KAYRERTDAQISDLEQRLADCAEKMKSL 434
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellekeierlKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 435 QQQLKDSQMHTDKLQMEWSEERERLQQQV-------------STQRQRGLEKTARLEE---ELLAVQRDRETEANKYQDN 498
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQkelkskekelkklNEEKKELEEKVKDLTKkisSLKEKIEKLESEKKEKESK 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 499 LRLLEEEKNS---------LLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESL 569
Cdd:TIGR04523 540 ISDLEDELNKddfelkkenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
570 580 590
....*....|....*....|....*....|
gi 121308974 570 VKAEQEVSRLSQDLGVKEEEVNALKEELQA 599
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-622 |
3.90e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 54 SSQIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEialekyqdssmrKLQDQNESFQTNRAKMAEAMSlALEKKDQEWM 133
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELEELKEEIE------------ELEKELESLEGSKRKLEEKIR-ELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 134 EKLASLEqEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREkELKLRGEELNTARLTL 213
Cdd:PRK03918 273 KEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE-EKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 214 GKTQDKLYELGEEHEEICRTNSQLQAQRDELLS-EKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEH 292
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 293 LQSEHNKLKLQHEQhknkvaVTEEERERILSDLQEKAASLERRleanfsqdehLQELLKEKSSLEQRLEEARGELLQEKT 372
Cdd:PRK03918 431 LKKAKGKCPVCGRE------LTEEHRKELLEEYTAELKRIEKE----------LKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 373 SHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYRE--RTDAQISDLEQRLadcaEKMKSLQQQLKDSQMHTDKLQM 450
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKliKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 451 EWSEERERLqqqvstqRQRGLEKTARLEEELlavqRDRETEANKY---QDNLRLLEEEKNSLlrskgetdstvESLTAEL 527
Cdd:PRK03918 571 ELAELLKEL-------EELGFESVEELEERL----KELEPFYNEYlelKDAEKELEREEKEL-----------KKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 528 EQSRAEMSsrqtvsvEIAKALEETRKQREELQQQVSKmtESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSL 607
Cdd:PRK03918 629 DKAFEELA-------ETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
570
....*....|....*
gi 121308974 608 QAECESRRLEAEEKE 622
Cdd:PRK03918 700 KEELEEREKAKKELE 714
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
429-742 |
4.43e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 429 EKMKSLQQQLKDSQMHTDKLQ---MEWSEERERLQQQVStQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEE 505
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEdilNELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 506 KNSLLRskgETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGV 585
Cdd:TIGR02168 251 AEEELE---ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 586 KEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQQevlrQTQQLSSYQSRVSDLESEVLSLTAhsh 665
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNN--- 400
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121308974 666 adecegeqngtvtvsdldQLQKvnkdLEQQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQDGRQER 742
Cdd:TIGR02168 401 ------------------EIER----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-612 |
5.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 150 LDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTLGKTQDKL--YELGEEH 227
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 228 EEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKA----QSNAEALEKSMEHLQSEHNKLKLQ 303
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeellEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 304 HEQHKNKVAVTEEERERILSDLQEKAASLER-RLEANFSQDEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLE 382
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAaALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 383 AQVSRQNASIIDLQTLVKhKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLQQQ 462
Cdd:COG4717 288 LLFLLLAREKASLGKEAE-ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 463 VSTQRQRGLEKTARLE-----EELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDStvESLTAELEQSRAEMSsr 537
Cdd:COG4717 367 ELEQEIAALLAEAGVEdeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELE-- 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121308974 538 qtvsvEIAKALEETRKQREELQQQVSKMTESlvkaeQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECE 612
Cdd:COG4717 443 -----ELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
58-639 |
6.23e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 58 QRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSSMRKLQDQNESFQTNRAKMAEamslalEKKDQEWMEKLA 137
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE------AKKKADAAKKKA 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 138 SLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTLGKTQ 217
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 218 D--KLYELGEEHEEI-----CRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSM 290
Cdd:PTZ00121 1468 EakKADEAKKKAEEAkkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 291 EHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLER-RLEANFSQDEhlqELLKEKSSLEQRLEEARGELLQ 369
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEaRIEEVMKLYE---EEKKMKAEEAKKAEEAKIKAEE 1624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 370 EKTshttavsslEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQ 449
Cdd:PTZ00121 1625 LKK---------AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 450 MEWSEER--ERLQQQVSTQRQRGLEKTARLEEELLAVQ--RDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTA 525
Cdd:PTZ00121 1696 KEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKAEeaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 526 ELEQSRAEmssrqtvsvEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDlgVKEEEVNALKEELQAARSSLS 605
Cdd:PTZ00121 1776 EKEAVIEE---------ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIND--SKEMEDSAIKEVADSKNMQLE 1844
|
570 580 590
....*....|....*....|....*....|....
gi 121308974 606 SLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQ 639
Cdd:PTZ00121 1845 EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
57-573 |
6.62e-07 |
|
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: 53.43 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 57 IQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSSMRKLQDQNES----FQTNRAKMAEAMSLALEKKDQEW 132
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQatidTRTSAFRDLQGQLAHAKKQQELQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 133 MEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKV---KHMLLRREEQLNQREKELKLRGEELNTA 209
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQEtrkKAVVLARLLELQEEPCPLCGSCIHPNPA 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 210 RLTLG-------KTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVS-----EDFQ 277
Cdd:TIGR00618 517 RQDIDnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPnlqniTVRL 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 278 KAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERilsDLQEKAASLERrLEANFSQDEHLQELLKEKSsLE 357
Cdd:TIGR00618 597 QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHA-LQLTLTQERVREHALSIRV-LP 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 358 QRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQ 437
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 438 LKdsqmhtdklqmeWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRS-KGET 516
Cdd:TIGR00618 752 AR------------TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDIL 819
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 517 DSTVESLTAELEQSRAEMSSRQTVSVEIA---KALEETRKQREELQQQVSKMTESLVKAE 573
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSATLGEIThqlLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
459-657 |
6.78e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 459 LQQQVSTQRQRGLEKTARLEEELLAVQ---RDRETEANKYQdnlrlleeEKNSLLRSKGETDSTVESLT---AELEQSRA 532
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRkelEEAEAALEEFR--------QKNGLVDLSEEAKLLLQQLSeleSQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 533 EMSSRQTVSVEIAKALEETRKQREELQQ--QVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSS---- 606
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeaqr 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 121308974 607 LQAECESRRLEAEEKEREHNSQLTSLQQEVlrqtQQLSSYQSRVSDLESEV 657
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREV 360
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
320-719 |
1.00e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 320 RILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGEL--LQEKTSHTTAVSSLEAQVSRQNASIIDLQT 397
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeeLREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 398 LVKHKDDSSKAYRERTDAQiSDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRglEKTARL 477
Cdd:COG4717 144 LPERLEELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE--LEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 478 EEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRS------KGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEET 551
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 552 RKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKERE---HNSQ 628
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 629 LTSLQQ--EVLRQTQQLSSYQSRVSDLESEVLSLtahshadecEGEQNGTVTVSDLDQLQKVNKDLEQQLAEKNKTIKQL 706
Cdd:COG4717 381 VEDEEElrAALEQAEEYQELKEELEELEEQLEEL---------LGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410
....*....|...
gi 121308974 707 QQRLAELKRTLQK 719
Cdd:COG4717 452 REELAELEAELEQ 464
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
51-719 |
1.20e-06 |
|
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: 52.28 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 51 DDFSSQIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQ--DSSMRKLQDQNESFQTNRAKMAEaMSLALEKK 128
Cdd:TIGR00618 208 LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEeqLKKQQLLKQLRARIEELRAQEAV-LEETQERI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 129 DQ--------EWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDL--DELEGFQQQELAKVKHMLLRREEQLNQREKE 198
Cdd:TIGR00618 287 NRarkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHvkQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 199 LKLRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQK 278
Cdd:TIGR00618 367 IREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 279 AQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQ--EKAASLERRLEANFSQDEHLQELLKEKSSL 356
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLArlLELQEEPCPLCGSCIHPNPARQDIDNPGPL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 357 EQRLEEargeLLQEKTSHTTAVSSLEAQV----------SRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLAD 426
Cdd:TIGR00618 527 TRRMQR----GEQTYAQLETSEEDVYHQLtserkqraslKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 427 CAEKMKSLqqqLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEK 506
Cdd:TIGR00618 603 LSEAEDML---ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 507 NSLlrskgetdSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKmteslvkaeqevsrLSQDLGVK 586
Cdd:TIGR00618 680 LAL--------QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS--------------LGSDLAAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 587 EEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVlsltaHSHA 666
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI-----GQEI 812
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 121308974 667 DECEGEQNGTVtvsdlDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQK 719
Cdd:TIGR00618 813 PSDEDILNLQC-----ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
471-759 |
1.25e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 471 LEKTAR---LEEELLAVQRDRETEANKYQDNLRLLEEEKNSLL------RSKGETDSTVESLTAELEQSRAEMSSRQTVS 541
Cdd:COG3206 96 LERVVDklnLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVIeisytsPDPELAAAVANALAEAYLEQNLELRREEARK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 542 VE--IAKALEETRKQREELQQQVSKMTES--LVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLE 617
Cdd:COG3206 176 ALefLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 618 AEEKERehNSQLTSLQQEVLRQTQQLSSYQSRVSD-------LESEVLSLTAHSHAdecEGEQNGTVTVSDLDQLQKVNK 690
Cdd:COG3206 256 LPELLQ--SPVIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQLQQ---EAQRILASLEAELEALQAREA 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121308974 691 DLEQQLAEKNKTIKQLQQRLAELKRtLQKELKLKPDPDSEMKERLQDGRQERSAEKT---VLETPMPTAAPS 759
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRR-LEREVEVARELYESLLQRLEEARLAEALTVGnvrVIDPAVVPLKPV 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
395-606 |
1.60e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 395 LQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMewSEERERLQQQVSTQRQRGLEKT 474
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLL--LQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 475 ARLE--EELLAVQRDRETEAN------KYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSR-QTVSVEIA 545
Cdd:COG3206 240 ARLAalRAQLGSGPDALPELLqspviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121308974 546 KALEETRKQREELQQQVSKMTE---SLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSS 606
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEArlaELPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
554-784 |
1.84e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 554 QREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQ 633
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 634 Q--------EVLRQTQQLSSYQSRVSDLESEV---LSLTAHSHADECEGEQNGTVTVSDLDQLQKVNKDLEQQLAEKNKT 702
Cdd:COG3883 97 RsggsvsylDVLLGSESFSDFLDRLSALSKIAdadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 703 IKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQDGRQERSAEKTVLETPMPTAAPSPALGLSQTPGPITPNTTVTNSSD 782
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
..
gi 121308974 783 IT 784
Cdd:COG3883 257 AA 258
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
286-726 |
1.89e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 286 LEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEER---ERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQR--- 359
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQnnq 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 360 LEEARGELLQEKTSHTTAVSSLEAQVSrqnaSIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQlk 439
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLN----QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ-- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 440 dSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDS- 518
Cdd:TIGR04523 304 -KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSy 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 519 --TVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEE 596
Cdd:TIGR04523 383 kqEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 597 LQAARSSLSSLQAECESRRLEAEEKEREhnsqLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGT 676
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKE----LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 121308974 677 VTVSDLDQLQKVNKD-----LEQQLAEKNKTIKQLQQRLAELKRTlQKELKLKPD 726
Cdd:TIGR04523 539 KISDLEDELNKDDFElkkenLEKEIDEKNKEIEELKQTQKSLKKK-QEEKQELID 592
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
548-750 |
3.40e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 548 LEETRKQREELQQQVSK------MTESLVKAEQEVS-----RLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRL 616
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryreLKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 617 EAEEKEREHNS---QLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAhshadecegeqngtvtvsDLDQLQKVNKDLE 693
Cdd:COG1196 275 ELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEE------------------ELAELEEELEELE 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 121308974 694 QQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQDGRQERSAEKTVLE 750
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
454-659 |
3.87e-06 |
|
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: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 454 EERERLQQQVSTQRQRgLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAE 533
Cdd:COG4942 27 AELEQLQQEIAELEKE-LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 534 ---------MSSRQT-----VSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQA 599
Cdd:COG4942 106 laellralyRLGRQPplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 600 ARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLS 659
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
547-746 |
4.38e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 547 ALEETRKQREELQQQVSKmTESLVKAEQEVSRLSQDLGVKEeeVNALKEELQAARSSLSSLQAECESRRLEAEEKE---R 623
Cdd:TIGR02168 194 ILNELERQLKSLERQAEK-AERYKELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEeklE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 624 EHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGTvtvsDLDQLQKVNKDLEQQLAEKNKTI 703
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA----QLEELESKLDELAEELAELEEKL 346
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 121308974 704 KQLQQRLAELKRTLQKELKLKPdpdsEMKERLQDGRQERSAEK 746
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELE----ELESRLEELEEQLETLR 385
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
209-575 |
4.58e-06 |
|
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: 50.28 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 209 ARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEK 288
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 289 SMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGELL 368
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 369 QEKTSHTTAVSSLEAQVSrqnasiidlqTLVKHKDDSSKAYRERTDAQISDLEQRLAdcAEKMKSLQQQLKDSQMHTDKL 448
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDT----------QVLQLQDTITTLTQKLTTAHRKEAENEAL--LEELRSLQERLNASERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 449 QMEWSE---ERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLta 525
Cdd:pfam07888 257 GEELSSmaaQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERL-- 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 121308974 526 eleqsRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQE 575
Cdd:pfam07888 335 -----QEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKE 379
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
189-714 |
5.78e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 189 EEQLNQREKELKLRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQL 268
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 269 IQQVSEDFQKAQSnaeaLEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERI---LSDLQEKAASLERRLEANFSQDEH 345
Cdd:TIGR04523 203 LSNLKKKIQKNKS----LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqLNQLKDEQNKIKKQLSEKQKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 346 LQELLKEKSSLEQRLEEARGELLQEKTSHTTavSSLEAQVSRQNASIIDLQTlvkhkddsskayrertdaQISDLEQRLA 425
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQN------------------QISQNNKIIS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 426 DCAEKMKSLQQQLKDSQMHTDKLQMEWsEERERLQQQVSTQRQRGLEKTARLE---EELLAVQRDRETEANKYQDNLRLL 502
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQREL-EEKQNEIEKLKKENQSYKQEIKNLEsqiNDLESKIQNQEKLNQQKDEQIKKL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 503 EEEKNSLLRSkgetdstVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQD 582
Cdd:TIGR04523 418 QQEKELLEKE-------IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 583 LGVKEEEVNALKEE----------LQAARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQT--QQLSSYQSRV 650
Cdd:TIGR04523 491 LKSKEKELKKLNEEkkeleekvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEI 570
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121308974 651 SDLESEVLSLTA-HSHADEcegeqngtvtvsDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELK 714
Cdd:TIGR04523 571 EELKQTQKSLKKkQEEKQE------------LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
435-750 |
1.16e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 435 QQQLKDSQMHTDKLQMEWSE-----ERERLQQQVSTQRQRGLEKTARL--EEELLAVQRDRETEANKYQDNLRLLEEEKN 507
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEkarevERRRKLEEAEKARQAEMDRQAAIyaEQERMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 508 SLLRSKGETDSTVESLtaELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKmteSLVKAEQEVSRlsqdlgvkE 587
Cdd:pfam17380 368 EEIAMEISRMRELERL--QMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM---EQIRAEQEEAR--------Q 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 588 EEVNALKEElqaarsslsslqAECESRRLEAEEKEREHnsqltslQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHAD 667
Cdd:pfam17380 435 REVRRLEEE------------RAREMERVRLEEQERQQ-------QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 668 --ECEGEQNGTVTVSDLDQLQKVNKDLEQQlaeKNKTIKQLQQRLAELKRTLQKELklkpdpdsEMKERLQDGRQERSAE 745
Cdd:pfam17380 496 ilEKELEERKQAMIEEERKRKLLEKEMEER---QKAIYEEERRREAEEERRKQQEM--------EERRRIQEQMRKATEE 564
|
....*
gi 121308974 746 KTVLE 750
Cdd:pfam17380 565 RSRLE 569
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
485-733 |
1.45e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.92 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 485 QRDRETEANKYQD------NLRLLEEEKNSLlrskgETDSTVESLT-AELEQSRAEMSSRQTVSVEIAKALEETRKQREE 557
Cdd:COG5022 812 YRSYLACIIKLQKtikrekKLRETEEVEFSL-----KAEVLIQKFGrSLKAKKRFSLLKKETIYLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 558 LQQQVSKMTES---LVKAEQEVSRLSQDLGVKEEEVNALKEEL-----QAARSSLSSLQAECESRRLEAEEKEREHNSQL 629
Cdd:COG5022 887 LKIDVKSISSLklvNLELESEIIELKKSLSSDLIENLEFKTELiarlkKLLNNIDLEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 630 TSLQQEVLRQTQQLSSYQSRVSDLESEVLSL--TAHSHADECEGEQNGTVTVsdldqlqkvnKDLEQQLAEKNKTIKQLQ 707
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFkkELAELSKQYGALQESTKQL----------KELPVEVAELQSASKIIS 1036
|
250 260
....*....|....*....|....*.
gi 121308974 708 QRLAELKRtLQKELKLKPDPDSEMKE 733
Cdd:COG5022 1037 SESTELSI-LKPLQKLKGLLLLENNQ 1061
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
546-718 |
1.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 546 KALEETRKQRE------ELQQQVSKMTESLVKAEQEVSRLsqDLGVKEEEVNALKEELQAARSSLSSLQAE---CESRRL 616
Cdd:COG4913 242 EALEDAREQIEllepirELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAElerLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 617 EAEEKEREHNSQ--------LTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGTVTVSDLDQLQKV 688
Cdd:COG4913 320 ALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|
gi 121308974 689 NKDLEQQLAEKNKTIKQLQQRLAELKRTLQ 718
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
348-736 |
1.63e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 348 ELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYR-----ERTDAQISDLEQ 422
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRqqekiERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 423 RLADCAEKMKSLQQQLKDSQMHTDKLQmewsEERERLQQQVSTQRQRglektarleeelLAVQrdrETEANKYQDNLRLL 502
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAE----EEVDELKSQLADYQQA------------LDVQ---QTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 503 EEEKNSLlrskGETDSTVESLTAELEQSRAE--------------MSSRQTVSVEIAKALEETRK--------------- 553
Cdd:PRK04863 424 ERAKQLC----GLPDLTADNAEDWLEEFQAKeqeateellsleqkLSVAQAAHSQFEQAYQLVRKiagevsrseawdvar 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 554 --------------QREELQQQVSKMTESLVKaEQEVSRLSQDLGVK-------EEEVNALKEELQAARSSLSSLQAECE 612
Cdd:PRK04863 500 ellrrlreqrhlaeQLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRlgknlddEDELEQLQEELEARLESLSESVSEAR 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 613 SRRLEaeekEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLEsevlsltahshadECEGEQngTVTVSDLDQLQkvnkdl 692
Cdd:PRK04863 579 ERRMA----LRQQLEQLQARIQRLAARAPAWLAAQDALARLR-------------EQSGEE--FEDSQDVTEYM------ 633
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 121308974 693 eQQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQ 736
Cdd:PRK04863 634 -QQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLN 676
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-433 |
1.93e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 174 QQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTLGKTQDKLYELGEE----HEEICRTNSQLQAQRDELLSEKE 249
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaalEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 250 EAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEhlqsehnklklqheqhknkvavteeERERILSDLQEKA 329
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP-------------------------ARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 330 ASLERRLEANFSQDEHLQELLKEkssleqrLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQtlvkhkddsskAY 409
Cdd:COG4942 160 AELAALRAELEAERAELEALLAE-------LEEERAALEALKAERQKLLARLEKELAELAAELAELQ-----------QE 221
|
250 260
....*....|....*....|....
gi 121308974 410 RERTDAQISDLEQRLADCAEKMKS 433
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
113-724 |
1.95e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 113 NRAKMAEAMSLALEKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEqL 192
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE-L 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 193 NQREKELKLRGEELNtarltlgktqdKLYELGEEHEEicrtnsqLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQV 272
Cdd:PRK03918 272 KKEIEELEEKVKELK-----------ELKEKAEEYIK-------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 273 SEDfqkaQSNAEALEKSMEHLQSEHNKLKLQHEQHkNKVAVTEEERERILSDLQEKA-ASLERRLEANFSQDEHLQELLK 351
Cdd:PRK03918 334 EEK----EERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 352 EkssleqrLEEARGELLQEKTSHTTAVSSLEAqvSRQNASIIDLQTLVKHKDDSSKAYRertdAQISDLEQRLADCAEKM 431
Cdd:PRK03918 409 K-------ITARIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHRKELLEEYT----AELKRIEKELKEIEEKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 432 KSLQQQLKdsqmhtdKLQMEWSEERErlqqqVSTQRQRgLEKTARLEEELlavqrdRETEANKYQDNLRLLEEEKNSLLR 511
Cdd:PRK03918 476 RKLRKELR-------ELEKVLKKESE-----LIKLKEL-AEQLKELEEKL------KKYNLEELEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 512 SKGETDSTVESLT--AELEQSRAEMSSR-QTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLS---QDLGV 585
Cdd:PRK03918 537 LKGEIKSLKKELEklEELKKKLAELEKKlDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKdaeKELER 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 586 KEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNsqltslQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHsh 665
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS------EEEYEELREEYLELSRELAGLRAELEELEKR-- 688
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121308974 666 adecegeqngtvtvsdLDQLQKVNKDLEQQLAE---KNKTIKQLQQRLAELKRTLQKELKLK 724
Cdd:PRK03918 689 ----------------REEIKKTLEKLKEELEErekAKKELEKLEKALERVEELREKVKKYK 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-368 |
2.23e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 56 QIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQdSSMRKLQDQNESFQTNRAKMAEAMSlALEKKDQEWMEK 135
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS-RKIGEIEKEIEQLEQEEEKLKERLE-ELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 136 LASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQ-----QQELAKVKHMLLRREEQLNQREKELKLRGEELNTAR 210
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 211 LTLGKTQDKLYELGEEHEEICRtnsqlqaQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSM 290
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEK-------EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 291 EHLQSEHNKLKLQHEQHKNKVAVTEEE----------------RERILSDLQEKAASLERRLEA----NFSQDEHLQELL 350
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEElseiedpkgedeeipeEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVL 985
|
330 340
....*....|....*....|.
gi 121308974 351 KEKSSLE---QRLEEARGELL 368
Cdd:TIGR02169 986 KRLDELKekrAKLEEERKAIL 1006
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
48-651 |
3.35e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 48 SSRDDFSSQIQRRNDQIRKLEAKLSDYAEQLrlmqktkEKLEIALEKYQDSSMRKL---QDQNESFQTNRAKMAEAMSLA 124
Cdd:pfam12128 294 TLDDQWKEKRDELNGELSAADAAVAKDRSEL-------EALEDQHGAFLDADIETAaadQEQLPSWQSELENLEERLKAL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 125 LEKK---DQEWMEKLASLEQEKLSLTSRLDEMTEQS-----LSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQRE 196
Cdd:pfam12128 367 TGKHqdvTAKYNRRRSKIKEQNNRDIAGIKDKLAKIreardRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 197 KELKLRgeeLNTARLT------LGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQ 270
Cdd:pfam12128 447 GELKLR---LNQATATpelllqLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALD 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 271 QVSED-FQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKV--AVTEEERERILS------DLQE----KAASLERRLE 337
Cdd:pfam12128 524 ELELQlFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLdpEVWDGSVGGELNlygvklDLKRidvpEWAASEEELR 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 338 ANFSQ-DEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAqvsrqnaSIIDLQTLVKHKDDSSKAYRERTDAQ 416
Cdd:pfam12128 604 ERLDKaEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKN-------ARLDLRRLFDEKQSEKDKKNKALAER 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 417 ISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQrglEKTARLEEELLA--VQRDRETEAnk 494
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD---AQLALLKAAIAArrSGAKAELKA-- 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 495 yqdnlrlLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSrqtVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQ 574
Cdd:pfam12128 752 -------LETWYKRDLASLGVDPDVIAKLKREIRTLERKIER---IAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIER 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 575 EVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAE---------CESRRLeAEEKEREHNSQLTSLQQEVLRQTQQLSS 645
Cdd:pfam12128 822 AISELQQQLARLIADTKLRRAKLEMERKASEKQQVRlsenlrglrCEMSKL-ATLKEDANSEQAQGSIGERLAQLEDLKL 900
|
....*.
gi 121308974 646 YQSRVS 651
Cdd:pfam12128 901 KRDYLS 906
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-720 |
3.75e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 236 QLQAQRDELlsekEEAERRVVDLERREQELQQLIQQvSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQH-----EQHKNK 310
Cdd:COG4913 229 ALVEHFDDL----ERAHEALEDAREQIELLEPIREL-AERYAAARERLAELEYLRAALRLWFAQRRLELleaelEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 311 VAVTEEERERI---LSDLQEKAASLERRLEANFSQDehLQELLKEKSSLEQRLEEARGELLQektsHTTAVSSLEAQVSR 387
Cdd:COG4913 304 LARLEAELERLearLDALREELDELEAQIRGNGGDR--LEQLEREIERLERELEERERRRAR----LEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 388 QNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADcaekmksLQQQLKdsqmhtdklqmEWSEERERLQQQVSTQR 467
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD-------LRRELR-----------ELEAEIASLERRKSNIP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 468 QRGLEKTARLEEEL-------------------------------------LAVQRDRETEANKYQDNLRL--------L 502
Cdd:COG4913 440 ARLLALRDALAEALgldeaelpfvgelievrpeeerwrgaiervlggfaltLLVPPEHYAAALRWVNRLHLrgrlvyerV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 503 EEEKNSLLRSKGETDSTVESLTAELEQSRA----EMSSRQTV-SVEIAKALEETRK------------------------ 553
Cdd:COG4913 520 RTGLPDPERPRLDPDSLAGKLDFKPHPFRAwleaELGRRFDYvCVDSPEELRRHPRaitragqvkgngtrhekddrrrir 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 554 -----------QREELQQQVSKMTESLVKAEQEVSRLSQ-----------------------DLGVKEEEVNALKEELQA 599
Cdd:COG4913 600 sryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAeldalqerrealqrlaeyswdeiDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 600 ARSSLSSLQA------ECESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVlSLTAHSHADECEGEQ 673
Cdd:COG4913 680 LDASSDDLAAleeqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA-RLELRALLEERFAAA 758
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 121308974 674 NGTvtvsdlDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKE 720
Cdd:COG4913 759 LGD------AVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
235-720 |
3.91e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 235 SQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVT 314
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 315 EEERERilSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVsslEAQVSRQNASIID 394
Cdd:COG4717 129 PLYQEL--EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT---EEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 395 LQtlvkhkddsskAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKT 474
Cdd:COG4717 204 LQ-----------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 475 ARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQ 554
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 555 REELQQQVSKMTesLVKAEQEVSRLSQDLGVKEEE----VNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNsqLT 630
Cdd:COG4717 353 LREAEELEEELQ--LEELEQEIAALLAEAGVEDEEelraALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 631 SLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEqngtvtVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRL 710
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE------LAELLQELEELKAELRELAEEWAALKLALELL 502
|
490
....*....|
gi 121308974 711 AELKRTLQKE 720
Cdd:COG4717 503 EEAREEYREE 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
151-469 |
4.15e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 151 DEMTEQSLSLFQKRDDLDELEgfQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTLGKTQDKLYE-----LGE 225
Cdd:pfam17380 268 NEFLNQLLHIVQHQKAVSERQ--QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAeqermAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 226 EHEEICRTNSQLQAQRDELLSEKEEAER--RVVDLERREQELQQLIQQVSEDFQKAQS----NAEALEKSMEHLQSEHNK 299
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEisRMRELERLQMERQQKNERVRQELEAARKvkilEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 300 LKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHL--QELLKEKSSLEQRLEEARGELLQEKTSHTTA 377
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERkrKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 378 VSSLEAQVSRqnasiidlQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQmEWSEERE 457
Cdd:pfam17380 506 QAMIEEERKR--------KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE-AMERERE 576
|
330
....*....|..
gi 121308974 458 RLQQQVSTQRQR 469
Cdd:pfam17380 577 MMRQIVESEKAR 588
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
410-721 |
4.21e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 410 RERTDAQISDLEQRLADCAEKMKSLQQQLKD-------------SQMHTDKLQMEWSEER-------------------- 456
Cdd:PRK11281 75 IDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkddndeetretlSTLSLRQLESRLAQTLdqlqnaqndlaeynsqlvsl 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 457 ----ERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLeEEKNSLLRSKGETDSTVESLtaeLEQSRA 532
Cdd:PRK11281 155 qtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALL-NAQNDLQRKSLEGNTQLQDL---LQKQRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 533 EMSSRQTV---------SVEIAKALEETRKQREELQQQ---VSKMTESLVKAEQEVSR-LSQDLGVKEEEVNALKEELQA 599
Cdd:PRK11281 231 YLTARIQRlehqlqllqEAINSKRLTLSEKTVQEAQSQdeaARIQANPLVAQELEINLqLSQRLLKATEKLNTLTQQNLR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 600 ARSSLSSLQaecesrrleaeEKEREHNSQLTSL------------QQEVLRQTQQLSSYQSRVSDLESEVLSLT------ 661
Cdd:PRK11281 311 VKNWLDRLT-----------QSERNIKEQISVLkgslllsrilyqQQQALPSADLIEGLADRIADLRLEQFEINqqrdal 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121308974 662 --AHSHADECEGEQNGTVTVSDLDQLQKV-----------NKDLEQQLAEKNkTIKQLQQRLAELKRTLQKEL 721
Cdd:PRK11281 380 fqPDAYIDKLEAGHKSEVTDEVRDALLQLlderrelldqlNKQLNNQLNLAI-NLQLNQQQLLSVSDSLQSTL 451
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
415-632 |
5.08e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 415 AQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKTA---RLEEELLAVQRDREte 491
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAeieELTDELLNLVMDIE-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 492 anKYQDNLRLLEEEKnSLLRSKGETDSTVESL----------TAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQ 561
Cdd:PHA02562 252 --DPSAALNKLNTAA-AKIKSKIEQFQKVIKMyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 562 VSKMTESLVK------------------------AEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLqaecesrrle 617
Cdd:PHA02562 329 MDEFNEQSKKllelknkistnkqslitlvdkakkVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL---------- 398
|
250
....*....|....*
gi 121308974 618 aeEKEREHNSQLTSL 632
Cdd:PHA02562 399 --VKEKYHRGIVTDL 411
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
502-648 |
5.08e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 502 LEEEKNSLLRSkgetdsTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQ 581
Cdd:PRK09039 71 LERQGNQDLQD------SVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQ 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121308974 582 DlgvkeeeVNALKEELQAARSSLSslqaecesrrlEAEEKEREHNSQLTSLQQEV----LRQTQQLSSYQS 648
Cdd:PRK09039 145 Q-------IAALRRQLAALEAALD-----------ASEKRDRESQAKIADLGRRLnvalAQRVQELNRYRS 197
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
161-394 |
5.54e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 161 FQKRDDLDELEGfQQQELAKVKHMLLRREEQLNQREKELKLRGEELNT------ARLTLGKTQDKLYELGEEHEEICRTN 234
Cdd:COG4913 606 FDNRAKLAALEA-ELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswDEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 235 S---QLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKV 311
Cdd:COG4913 685 DdlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 312 AVTEEERERILSDLQEKAASLERRLEANFSQ---------------DEHLQELLKEKSSLEQ-RLEEARGELLQEKTSHT 375
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLDRLEEdGLPEYEERFKELLNENS 844
|
250 260
....*....|....*....|
gi 121308974 376 TA-VSSLEAQVSRQNASIID 394
Cdd:COG4913 845 IEfVADLLSKLRRAIREIKE 864
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
92-753 |
6.83e-05 |
|
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: 46.71 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 92 LEKYQDSSMRKLQDQNESFQTNRAKMaEAMSLALEKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELE 171
Cdd:pfam01576 350 MRQKHTQALEELTEQLEQAKRNKANL-EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 172 GFQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEA 251
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 252 ERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAAS 331
Cdd:pfam01576 509 EEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVD 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 332 L--ERRLEANFS--QDEHLQELLKEKSSLEQRLEE---ARGELLQEKTSHTTAVSSLEA------QVSRQNASI-IDLQT 397
Cdd:pfam01576 589 LdhQRQLVSNLEkkQKKFDQMLAEEKAISARYAEErdrAEAEAREKETRALSLARALEEaleakeELERTNKQLrAEMED 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 398 LVKHKDDSSKAYRERTDAQISdLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKTARL 477
Cdd:pfam01576 669 LVSSKDDVGKNVHELERSKRA-LEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQL 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 478 EEELlavqRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREE 557
Cdd:pfam01576 748 VKQV----RELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDE 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 558 LQQQVSKMTESLVKAEQEVSRLSQDLGVKEEevnaLKEELQAARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQQEVL 637
Cdd:pfam01576 824 ILAQSKESEKKLKNLEAELLQLQEDLAASER----ARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELE 899
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 638 RQTQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGtvtvSDLDQLQKVNKDLEQQLAEKNKTIKQLQQrlAELKRTL 717
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSE----SARQQLERQNKELKAKLQEMEGTVKSKFK--SSIAALE 973
|
650 660 670
....*....|....*....|....*....|....*.
gi 121308974 718 QKELKLKPDPDSEMKERLQDGRQERSAEKTVLETPM 753
Cdd:pfam01576 974 AKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLL 1009
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
134-364 |
7.14e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 134 EKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLdelegfqQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTL 213
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKAL-------LKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 214 GKTQDKLYELGEEHEEICRTNSQLQAQ-RDELLSEKEEAERRVVDLERREQELQQLIQQVsEDFQKAQSNAEALEKSMEH 292
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121308974 293 LQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKeksSLEQRLEEAR 364
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA---RLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
246-458 |
8.35e-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: 45.91 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 246 SEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDL 325
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 326 QEKAASLERRLEANF--SQDEHLQELLKEKSSLE--------QRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDL 395
Cdd:COG4942 100 EAQKEELAELLRALYrlGRQPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121308974 396 QTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERER 458
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
56-469 |
1.05e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 56 QIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDssmrklqdqnesfqtnraKMAEAMSLALEKKDQEWMEK 135
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE------------------LREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 136 LASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEG----FQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARL 211
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAelaeLQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 212 TLGKTQDKLYELGEEHEEIcrTNSQLQAQRDELLSEKEE---AERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEK 288
Cdd:COG4717 214 ELEEAQEELEELEEELEQL--ENELEAAALEERLKEARLlllIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 289 SMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLE------- 361
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 362 ----------------EARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLqtLVKHKDDSSKAYRERTDAQISDLEQRLA 425
Cdd:COG4717 372 iaallaeagvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEEL--LEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 121308974 426 DCAEKMKSLQQQLKdsQMHTDKLQMEWSEERERLQQQVSTQRQR 469
Cdd:COG4717 450 ELREELAELEAELE--QLEEDGELAELLQELEELKAELRELAEE 491
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
343-721 |
1.42e-04 |
|
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: 45.71 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 343 DEHLQELLkeksSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYR-----ERTDAQI 417
Cdd:COG3096 281 RELSERAL----ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRqqekiERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 418 SDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQmewsEERERLQQQVStQRQRGLEktarleeellaVQrdrETEANKYQD 497
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAE----EEVDSLKSQLA-DYQQALD-----------VQ---QTRAIQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 498 NLRLLEEEKNSLlrskGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKAL---EETRKQREELQQQVSKMT-------- 566
Cdd:COG3096 418 AVQALEKARALC----GLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQFEKAYELVCKIAgeversqa 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 567 ------------------ESLVKAEQEVSRLSQDLGvKEEEVNALKEELQ-------AARSSLSSLQAECESRRLEAEEK 621
Cdd:COG3096 494 wqtarellrryrsqqalaQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCqrigqqlDAAEELEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 622 EREHNSQLTSLQQEVLRQTQQLSSYQSRvsdlesEVLSLTAHShADECEGEQNGtVTVSDLDQLQkvnkDLEQQLAEKNK 701
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKELAAR------APAWLAAQD-ALERLREQSG-EALADSQEVT----AAMQQLLERER 640
|
410 420
....*....|....*....|
gi 121308974 702 TIKQLQQRLAELKRTLQKEL 721
Cdd:COG3096 641 EATVERDELAARKQALESQI 660
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
485-656 |
1.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 485 QRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTvsvEIAKALEETRKQREELQQQV-- 562
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---EIAEAEAEIEERREELGERAra 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 563 ----------------SKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHN 626
Cdd:COG3883 95 lyrsggsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|
gi 121308974 627 SQLTSLQQEVLRQTQQLSSYQSRVSDLESE 656
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
543-750 |
2.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 543 EIAKALEETRKQREELqqqvSKMTESLVKAEQEVSRLsqdlgvkeEEVNALKEELQAARSSLSSLQAECESRRLEAEEKE 622
Cdd:COG4913 222 DTFEAADALVEHFDDL----ERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 623 REH-NSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAhshadecEGEQNGTvtvSDLDQLQKVNKDLEQQLAEKNK 701
Cdd:COG4913 290 LELlEAELEELRAELARLEAELERLEARLDALREELDELEA-------QIRGNGG---DRLEQLEREIERLERELEERER 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 121308974 702 TIKQLQQRLAELK----------RTLQKELKLKPDPDSEMKERLQDGRQERSAEKTVLE 750
Cdd:COG4913 360 RRARLEALLAALGlplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-244 |
2.67e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 47 SSSRDDFSSQIQRRNDQIRKLEAKLSDYAEQLRLmqktkekleIALEKYQDSSMRKLQDQNESFQTNRAKMAEAMSLALE 126
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEEFRQKNGL---------VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 127 KKDQEWMEK-----------LASLEQEKLSLTSRLDEM----TEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQ 191
Cdd:COG3206 245 LRAQLGSGPdalpellqspvIQQLRAQLAELEAELAELsaryTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 121308974 192 LNQREKELKLRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDEL 244
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
309-656 |
2.79e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 309 NKVAVTEEERErilsDLQEKAASLERRLEANFSQDEHLQELLKEKSSL------EQRLEEARGELLQEKTSHTTAVSSLE 382
Cdd:PRK04863 786 KRIEQLRAERE----ELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVafeadpEAELRQLNRRRVELERALADHESQEQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 383 AQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQlkdsQMHTDKLQMEWS------EER 456
Cdd:PRK04863 862 QQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQH----GNALAQLEPIVSvlqsdpEQF 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 457 ERLQQQV--STQRQRGLEKTARLEEELLAVQrdretEANKYQDNLRLLEEEknsllrskgetDSTVESLTAELEQSRaem 534
Cdd:PRK04863 938 EQLKQDYqqAQQTQRDAKQQAFALTEVVQRR-----AHFSYEDAAEMLAKN-----------SDLNEKLRQRLEQAE--- 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 535 ssrqtvsveiakalEETRKQREELQQQVSKMTEslvkAEQEVSRLSQDLGVKEEEVNALKEELQAARSSL-SSLQAECES 613
Cdd:PRK04863 999 --------------QERTRAREQLRQAQAQLAQ----YNQVLASLKSSYDAKRQMLQELKQELQDLGVPAdSGAEERARA 1060
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 121308974 614 RRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESE 656
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
116-750 |
2.83e-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: 44.57 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 116 KMAEAMSLALEKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDElegfqQQELAKVKHMLLRREEQLNQR 195
Cdd:TIGR00618 201 LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE-----QLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 196 EKELKLRGEELNTARltlgktqdKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERrvvdlerreqelqqlIQQVSED 275
Cdd:TIGR00618 276 EAVLEETQERINRAR--------KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK---------------LLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 276 FQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTE---EERERILSdLQEKAASLERRLEANFSQDEHLQELLKE 352
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCqqhTLTQHIHT-LQQQKTTLTQKLQSLCKELDILQREQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 353 KSSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDaQISDLEQRLADCAEKMK 432
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 433 SLQQQLKDSQMHTDKLQMEWSEERERLQQ----QVSTQR-QRGLEKTARLEEELLAVQRDRETEANKYQDnlrlLEEEKN 507
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPARQDidnpGPLTRRmQRGEQTYAQLETSEEDVYHQLTSERKQRAS----LKEQMQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 508 SLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKA----LEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDL 583
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAedmlACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 584 GVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAH 663
Cdd:TIGR00618 647 ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 664 SHADECEGEQNGTVTVSDLDQLQ-------KVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQ 736
Cdd:TIGR00618 727 SSSLGSDLAAREDALNQSLKELMhqartvlKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
650
....*....|....
gi 121308974 737 DGRQERSAEKTVLE 750
Cdd:TIGR00618 807 EIGQEIPSDEDILN 820
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
543-657 |
3.11e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 42.89 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 543 EIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKE 622
Cdd:pfam06785 66 EKSFLEEKEAKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQL 145
|
90 100 110
....*....|....*....|....*....|....*
gi 121308974 623 REHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEV 657
Cdd:pfam06785 146 AEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKV 180
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-419 |
3.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 54 SSQIQRRNDQIRKLEaKLSDYAEQLRLMQKTKEKLEialEKYQDSSMRKLQDQNESFQTNRAKMAEAMSLALEKKDQEwm 133
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAE-EAKKKAEEAKKADEAKKKAE---EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE-- 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 134 EKLASLEQEKLSLTSRLDEMTE----QSLSLFQKRDDLDELEGFQQQELAKV----KHMLLRREEQLNQREKELKLRGEE 205
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKaeekKKADELKKAEELKKAEEKKKAEEAKKaeedKNMALRKAEEAKKAEEARIEEVMK 1599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 206 LNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEA 285
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 286 LEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEAnfsqdehlQELLKEKSSLEQRLEEAR- 364
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA--------EEAKKEAEEDKKKAEEAKk 1751
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 121308974 365 GELLQEKTSHTTAVSSLEAQVSRQNASIIdLQTLVKHKDDSSKAYRERTDAQISD 419
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
527-629 |
3.71e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 527 LEQSRAEMSSRQTVSVEIAKalEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSS 606
Cdd:PRK12704 44 LEEAKKEAEAIKKEALLEAK--EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121
|
90 100
....*....|....*....|...
gi 121308974 607 LQAECESRRLEAEEKEREHNSQL 629
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQLQEL 144
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
40-713 |
5.05e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 40 DDFASDGSSSRDDFSSQIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKL-EIALEKYQDSSMRKLQDQNESFQTNRAKMA 118
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELkLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 119 EAMSLALEKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLlrrEEQLNQREKE 198
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL---SSAAKLKEEE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 199 LKLRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQK 278
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 279 AQsnaeaLEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEK-----------AASLERRLEANFSQDEHLQ 347
Cdd:pfam02463 477 TQ-----LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGgriisahgrlgDLGVAVENYKVAISTAVIV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 348 ELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADC 427
Cdd:pfam02463 552 EVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKD 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 428 AEKMKSLQQQL-KDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEK 506
Cdd:pfam02463 632 TELTKLKESAKaKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 507 NSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEV--------SR 578
Cdd:pfam02463 712 LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREkteklkveEE 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 579 LSQDLGVKEEEVNALKEELQAARSSLSSLQAEcESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVL 658
Cdd:pfam02463 792 KEEKLKAQEEELRALEEELKEEAELLEEEQLL-IEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 121308974 659 SLTAHSH----ADECEGEQNGTVTVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAEL 713
Cdd:pfam02463 871 ELLLKEEeleeQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEI 929
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
96-742 |
5.05e-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: 43.88 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 96 QDSSMRKLQDQNESFQTNRAKMAEAMSLALEKKDQEWMEK--LASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGF 173
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSReiVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 174 QQQELAKVKHMLLRREEQLNQREKELK----LRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQ--RDELLSE 247
Cdd:TIGR00606 278 KKQMEKDNSELELKMEKVFQGTDEQLNdlyhNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEqgRLQLQAD 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 248 KEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKlqheQHKNKVAVTEEERERILSDLQE 327
Cdd:TIGR00606 358 RHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA----QLCADLQSKERLKQEQADEIRD 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 328 KAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEaqVSRQNASIIDLQTLVKhkddSSK 407
Cdd:TIGR00606 434 EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS--KAEKNSLTETLKKEVK----SLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 408 AYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQ----MEWSEERERLQQQVSTQRQRGLEKTARLEEELLA 483
Cdd:TIGR00606 508 NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEqirkIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEIN 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 484 VQRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKAleetRKQREELQQQV- 562
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKS----SKQRAMLAGATa 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 563 --SKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESrRLEAEEKEREHNSQLTSLQQEVL-RQ 639
Cdd:TIGR00606 664 vySQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES-ELKKKEKRRDEMLGLAPGRQSIIdLK 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 640 TQQLSSYQSRVSDLESEVLSLTAHSHADECEGEQNGTVTVSDLDQLQKVN--KDLEQQLAEKNKTIKQLQQRL--AELKR 715
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimERFQMELKDVERKIAQQAAKLqgSDLDR 822
|
650 660
....*....|....*....|....*..
gi 121308974 716 TLQKELKLKPDPDSEMKERLQDGRQER 742
Cdd:TIGR00606 823 TVQQVNQEKQEKQHELDTVVSKIELNR 849
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
57-634 |
5.23e-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: 43.88 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 57 IQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKY----QDSSMRKLQDQNE-SFQTNRAKMAEAMSLALEKKDQE 131
Cdd:TIGR00606 400 IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLgrtiELKKEILEKKQEElKFVIKELQQLEGSSDRILELDQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 132 WMEKLASLeqEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKH---------MLLRREEQLNQREKELKLR 202
Cdd:TIGR00606 480 LRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtqmeMLTKDKMDKDEQIRKIKSR 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 203 GEELNTARLTLGKTQDKLYE-LGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEdfqkaQS 281
Cdd:TIGR00606 558 HSDELTSLLGYFPNKKQLEDwLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-----VC 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 282 NAEALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLE 361
Cdd:TIGR00606 633 GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 362 EARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTLvKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDS 441
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL-RNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 442 QMhTDKLQMEWSEERERLQQQVSTQRQRGLEKT-ARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKGETD--- 517
Cdd:TIGR00606 792 TI-MERFQMELKDVERKIAQQAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNelk 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 518 STVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEEL 597
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV 950
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 121308974 598 QAARSSLSSL----QAECESRRLEAEEKEREHNSQLTSLQQ 634
Cdd:TIGR00606 951 KNIHGYMKDIenkiQDGKDDYLKQKETELNTVNAQLEECEK 991
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
416-657 |
5.62e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 416 QISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERERL----QQQVSTQRQRGLEKT---ARLEEELLAVQRDR 488
Cdd:pfam00038 5 QLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLyslyEKEIEDLRRQLDTLTverARLQLELDNLRLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 489 ETEANKYQDNLRL---LEEEKNSLLR-------SKGETDSTVESLTAELEQSR----AEMS------SRQTVSVEI---- 544
Cdd:pfam00038 85 EDFRQKYEDELNLrtsAENDLVGLRKdldeatlARVDLEAKIESLKEELAFLKknheEEVRelqaqvSDTQVNVEMdaar 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 545 ----AKALEETRKQREELQQQVSKMTESLVKAEQEvsRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEE 620
Cdd:pfam00038 165 kldlTSALAEIRAQYEEIAAKNREEAEEWYQSKLE--ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKAS 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 121308974 621 KERehnsQLTSLQQevlRQTQQLSSYQSRVSDLESEV 657
Cdd:pfam00038 243 LER----QLAETEE---RYELQLADYQELISELEAEL 272
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
272-722 |
9.36e-04 |
|
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: 42.79 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 272 VSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVavteEERERILSDLQEKAASLERRLEAnfsQDEHLQELLK 351
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKM----KDLTFLLEESRDKANQLEEKTKL---QDENLKELIE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 352 EKSSLEQRLEEARGELLQEKTSHTTavssLEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKM 431
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQRSMSTQKA----LEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 432 KSLQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLE----KTARLEEELLAvqrDRETEANKYQDNLRLLEEEKN 507
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEleelKKILAEDEKLL---DEKKQFEKIAEELKGKEQELI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 508 SLLRSKgetDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKE 587
Cdd:pfam05483 443 FLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 588 EEVNALKEELQAARSSLSSLQaecesrrleaeEKEREHNSQLTSLQQEVLRQtqqlssyqsrvsdlESEVLSLTAHSHAD 667
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLE-----------EKEMNLRDELESVREEFIQK--------------GDEVKCKLDKSEEN 574
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 121308974 668 ECEGEQNGTVTVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKELK 722
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
111-312 |
1.02e-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: 42.44 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 111 QTNRAKMAEAMSLALEKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREE 190
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 191 QLNQREKELK------------------LRGEELNTA--RLTLGKT-----QDKLYELGEEHEEICRTNSQLQAQRDELL 245
Cdd:COG4942 98 ELEAQKEELAellralyrlgrqpplallLSPEDFLDAvrRLQYLKYlaparREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121308974 246 SEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKNKVA 312
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
432-724 |
1.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 432 KSLQQQLkdsqmhtDKLQ-MEWSEERERLQQQVSTQRQRGLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLL 510
Cdd:PRK11281 39 ADVQAQL-------DALNkQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 511 RSKGETDST--VESLTAELEQSRAEMSSRQtvsveiaKALEETRKQREELQQQV----SKMTESLVKAEQEVSRLSQDLG 584
Cdd:PRK11281 112 EETRETLSTlsLRQLESRLAQTLDQLQNAQ-------NDLAEYNSQLVSLQTQPeraqAALYANSQRLQQIRNLLKGGKV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 585 VKEEEVNALKEELQAarsSLSSLQAECESRRleaeeKEREHNSQLTSLQQ----EVLRQTQQLssyQSRVSDLESEV--- 657
Cdd:PRK11281 185 GGKALRPSQRVLLQA---EQALLNAQNDLQR-----KSLEGNTQLQDLLQkqrdYLTARIQRL---EHQLQLLQEAInsk 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121308974 658 -LSLTahshadecegEQngtvTVSDLDQLQKVNK----DLEQQLAEKNktiKQLQQRL----AELKRTLQKELKLK 724
Cdd:PRK11281 254 rLTLS----------EK----TVQEAQSQDEAARiqanPLVAQELEIN---LQLSQRLlkatEKLNTLTQQNLRVK 312
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
522-744 |
1.21e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 522 SLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQvskmtesLVKAEQEVSRLSQDLGVKEEEVNALKEELQAAR 601
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQ-------LKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 602 SSLSSLQAECE------SRRLEAEEKEREHNS-QLTSLQQEVLRQTQQLSSY-------QSRVSDLESEVLSLTAHSHAD 667
Cdd:PRK11637 110 ASIAKLEQQQAaqerllAAQLDAAFRQGEHTGlQLILSGEESQRGERILAYFgylnqarQETIAELKQTREELAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 668 ECEGEQNGTVtvsdLDQLQKVNKDLEQQLAEKNKTIKQL-------QQRLAELKrtlQKELKLKpdpDSEMK-ERLQDGR 739
Cdd:PRK11637 190 EEKQSQQKTL----LYEQQAQQQKLEQARNERKKTLTGLesslqkdQQQLSELR---ANESRLR---DSIARaEREAKAR 259
|
....*
gi 121308974 740 QERSA 744
Cdd:PRK11637 260 AEREA 264
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
63-629 |
1.26e-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: 42.47 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 63 QIRKLEAKLSDYAEQLRLMQKTKEKLE--IALEKYQDSSMRKLQDQNESFQTNRAKMAEAMSLALEKKDQEWMEKLASLE 140
Cdd:pfam01576 490 RLRQLEDERNSLQEQLEEEEEAKRNVErqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 141 QEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQ---QELAKVKHMLLRREEQLNQREKElklrGEELNTARLTLGKtq 217
Cdd:pfam01576 570 KLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdQMLAEEKAISARYAEERDRAEAE----AREKETRALSLAR-- 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 218 dKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERrvvdlerreqelqqliqqvsedfqkaqsNAEALEKSMEHLQSEH 297
Cdd:pfam01576 644 -ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGK----------------------------NVHELERSKRALEQQV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 298 NKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEhlqellKEKSSLEQRLEEARGELLQEKTSHTTA 377
Cdd:pfam01576 695 EEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE------EKRRQLVKQVRELEAELEDERKQRAQA 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 378 VSSleaqvsrQNASIIDLQTLVKHKDDSSKAYRErtdaqisdleqrladCAEKMKSLQQQLKDSQMHTDKLQMewSEERE 457
Cdd:pfam01576 769 VAA-------KKKLELDLKELEAQIDAANKGREE---------------AVKQLKKLQAQMKDLQRELEEARA--SRDEI 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 458 RLQQQVSTQRQRGLE-KTARLEEELLAVQRDR---ETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAE 533
Cdd:pfam01576 825 LAQSKESEKKLKNLEaELLQLQEDLAASERARrqaQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSN 904
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 534 MSSrqtvsveIAKALEETRKQREELQQQVSKMTESLVKAE---QEVSRLSQDLGVK-EEEVNALKEELQAARSSLSSLQA 609
Cdd:pfam01576 905 TEL-------LNDRLRKSTLQVEQLTTELAAERSTSQKSEsarQQLERQNKELKAKlQEMEGTVKSKFKSSIAALEAKIA 977
|
570 580
....*....|....*....|
gi 121308974 610 ECEsRRLEAEEKEREHNSQL 629
Cdd:pfam01576 978 QLE-EQLEQESRERQAANKL 996
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
502-645 |
1.79e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 41.67 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 502 LEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKaLEETRKQREELQQQVSKMTESLvkaeqevSRLSQ 581
Cdd:pfam10186 21 LYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLK-LRLLKSEVAISNERLNEIKDKL-------DQLRR 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121308974 582 DLGVKEEEVNALKEELQAARSSLSSLQAECESRRleaeekerehNSQLTSLQQEVLRQTQQLSS 645
Cdd:pfam10186 93 EIAEKKKKIEKLRSSLKQRRSDLESASYQLEERR----------ASQLAKLQNSIKRIKQKWTA 146
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
529-734 |
1.80e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 529 QSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVkaeQEVSRLSQdlgvKEEEVNALKEELQAARSSLSSLQ 608
Cdd:COG5022 807 GSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLI---QKFGRSLK----AKKRFSLLKKETIYLQSAQRVEL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 609 AECESRRLEAEEKEREHNSQLTS-LQQEVLRQTQQLSsyqsrvSDLESEVLSLTAHSHADEC--------EGEQNGTVTV 679
Cdd:COG5022 880 AERQLQELKIDVKSISSLKLVNLeLESEIIELKKSLS------SDLIENLEFKTELIARLKKllnnidleEGPSIEYVKL 953
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121308974 680 SDLDQLQKVNKDLEQQLAEKNKTIK-------QLQQRLAELKRT------LQKELKLKPDPDSEMKER 734
Cdd:COG5022 954 PELNKLHEVESKLKETSEEYEDLLKkstilvrEGNKANSELKNFkkelaeLSKQYGALQESTKQLKEL 1021
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
188-634 |
1.83e-03 |
|
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: 42.25 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 188 REEQLNQREKELKLRGEeLNTARLTLGKTQDKLYELGEEHEEICRTNSQL----QAQRDEL------LSEKEEAERRVVD 257
Cdd:COG3096 277 ANERRELSERALELRRE-LFGARRQLAEEQYRLVEMARELEELSARESDLeqdyQAASDHLnlvqtaLRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 258 LERREQELQQLIQQVSEdfqkAQSNAEALEKSMEHLQSEHNKLKLQ--------HEQHKNKV----AVTEEERERILSDL 325
Cdd:COG3096 356 LEELTERLEEQEEVVEE----AAEQLAEAEARLEAAEEEVDSLKSQladyqqalDVQQTRAIqyqqAVQALEKARALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 326 QE-KAASLERRLEAnfsQDEHLQELLKEKSSLEQRL---EEARGELLQEktshTTAVSSLEAQVSRQNASIIDLQTLVKH 401
Cdd:COG3096 432 PDlTPENAEDYLAA---FRAKEQQATEEVLELEQKLsvaDAARRQFEKA----YELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 402 KDDSSKAYRERT-DAQISDLEQRLAdcaekmkslQQQlkdsqmhtdklqmewseERERLQQQVSTQRQRGLEKTARLEEE 480
Cdd:COG3096 505 RSQQALAQRLQQlRAQLAELEQRLR---------QQQ-----------------NAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 481 LlavqrdreteankyqdnlrlleeeknsllrskgetdstvesltAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQ 560
Cdd:COG3096 559 L-------------------------------------------AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121308974 561 QVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAEcesrRLEAEEKEREHNSQLTSLQQ 634
Cdd:COG3096 596 ELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVE----RDELAARKQALESQIERLSQ 665
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
275-746 |
2.07e-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: 41.75 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 275 DFQKAQSNAEALEKSMEHLQSEHNKLKLQHEQHKN---KVAVTEEERERILSDLQEKAASL-----ERRLEAN---FSQD 343
Cdd:pfam12128 235 GIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSdetLIASRQEERQETSAELNQLLRTLddqwkEKRDELNgelSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 344 EHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLQTlvKHKDDSSKAYR------ERTDAQI 417
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTG--KHQDVTAKYNRrrskikEQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 418 SDLEQRLADCAEkmkSLQQQLKDSQMHTDKLQMEWseeRERLQQQVSTQRQRGLEKTARLEEelLAVQRDRETEANKYQD 497
Cdd:pfam12128 393 AGIKDKLAKIRE---ARDRQLAVAEDDLQALESEL---REQLEAGKLEFNEEEYRLKSRLGE--LKLRLNQATATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 498 NLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAeqevs 577
Cdd:pfam12128 465 QLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF----- 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 578 rLSQDLGVKEEEVNALKEELQAARSSL------SSLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQS--- 648
Cdd:pfam12128 540 -LRKEAPDWEQSIGKVISPELLHRTDLdpevwdGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSare 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 649 RVSDLESEVLSLTAHSHADECEGEQNGTVTVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPD 728
Cdd:pfam12128 619 KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
490
....*....|....*...
gi 121308974 729 SEMKERLQDGRQERSAEK 746
Cdd:pfam12128 699 QAWLEEQKEQKREARTEK 716
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
446-623 |
2.36e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 446 DKLQMEWSEERERLQQQVSTQRQRGLEKtaRLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLRSKgetdsTVESLTA 525
Cdd:NF033838 53 NESQKEHAKEVESHLEKILSEIQKSLDK--RKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSK-----TKKELDA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 526 ELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARS--S 603
Cdd:NF033838 126 AFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDeeK 205
|
170 180
....*....|....*....|
gi 121308974 604 LSSLQAECESRRLEAEEKER 623
Cdd:NF033838 206 IKQAKAKVESKKAEATRLEK 225
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
273-478 |
2.42e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 273 SEDFQKAQSNAEALEKSMEHLQSEHNKLKLQHEqhkNKVAVTEEERERILSDLQEKAASLERRLEanfSQDEHLQELLKE 352
Cdd:PRK05771 42 NERLRKLRSLLTKLSEALDKLRSYLPKLNPLRE---EKKKVSVKSLEELIKDVEEELEKIEKEIK---ELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 353 KSSLEQRLEEAR------GELLQEKTSHTTAVSSleAQVSRQNASIIDLQT------------------LVKHKDDSSKA 408
Cdd:PRK05771 116 IKELEQEIERLEpwgnfdLDLSLLLGFKYVSVFV--GTVPEDKLEELKLESdvenveyistdkgyvyvvVVVLKELSDEV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 409 YRE---------------RTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEERE-RLQQQVSTQRQRGLE 472
Cdd:PRK05771 194 EEElkklgferleleeegTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEiELERAEALSKFLKTD 273
|
....*.
gi 121308974 473 KTARLE 478
Cdd:PRK05771 274 KTFAIE 279
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
405-741 |
2.58e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 405 SSKAYRERTDAQISDLEQRLADCAekmKSLQQQLKDSQMHTDKLQMEWSEERERLQQQVSTQRQRGLEKTARLEEELLAV 484
Cdd:PLN02939 60 SSNSKLQSNTDENGQLENTSLRTV---MELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 485 QRDRETeankyqdNLRLLEEEKNSLLRSKGETDSTVESLTAE---LEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQ 561
Cdd:PLN02939 137 IQNAEK-------NILLLNQARLQALEDLEKILTEKEALQGKiniLEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 562 VSKMTESlvkAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECEsrRLEAEEKER--------EHNSQLTSLQ 633
Cdd:PLN02939 210 LLIRGAT---EGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEE--RVFKLEKERslldaslrELESKFIVAQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 634 QEVLR-QTQQLSSYQSRVSDLESEVLSLTAHShadecegEQNGTVTVSDLDQLQKVNKdLEQQLAEKNktIKQLQQRLAE 712
Cdd:PLN02939 285 EDVSKlSPLQYDCWWEKVENLQDLLDRATNQV-------EKAALVLDQNQDLRDKVDK-LEASLKEAN--VSKFSSYKVE 354
|
330 340
....*....|....*....|....*....
gi 121308974 713 LkrtLQKELKLkpdpdseMKERLQDGRQE 741
Cdd:PLN02939 355 L---LQQKLKL-------LEERLQASDHE 373
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
295-513 |
2.67e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 295 SEHNKLklqheqHKNKVAVTEEEreriLSDLQEKAASLERRLEanfSQDEHLQELLKEKSSLEQRLEEARGELLQEKTSH 374
Cdd:PHA02562 166 SEMDKL------NKDKIRELNQQ----IQTLDMKIDHIQQQIK---TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 375 TTAVSSLEAQVSRQNASIID----------LQTLVKHKDDS----SKAYRERTDA-----QISDLEQRLADCAEKMKSLQ 435
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDpsaalnklntAAAKIKSKIEQfqkvIKMYEKGGVCptctqQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 436 QQLKDSQMHTDKLQMEWSEERER------LQQQVSTQRQ-----RGLEKTARLEEELLAVQR-DRETEANKYQDNLRLLE 503
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEQskklleLKNKISTNKQslitlVDKAKKVKAAIEELQAEFvDNAEELAKLQDELDKIV 392
|
250
....*....|
gi 121308974 504 EEKNSLLRSK 513
Cdd:PHA02562 393 KTKSELVKEK 402
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
441-736 |
2.94e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 441 SQMHTDKLQMEWSEERER--LQQQVSTQRQRGLEKTARLEEELLAVQ--RDRETEAN--------------KYQDNLRLL 502
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARieLEKKASALKRQLDRESDRNQELQKRIRllEKREAEAEealreqaelnrlkkKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 503 EEEKNSLLRSKGETDSTVESLTAELEQS----RAEMSSRQTVSVEIAKALEETRK---QREELQQQVSKMTESLVKAEQE 575
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQiqraELELQSTNSELEELQERLDLLKAkasEAEQLRQNLEKQQSSLAEAEQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 576 VSRLSQDLGVKEEEvnalKEELQAARSSLSSLQaecesrRLEAE-EKEREHNSQLTSLQQEVLRQTQQLSSYQSR----- 649
Cdd:pfam05557 172 IKELEFEIQSQEQD----SEIVKNSKSELARIP------ELEKElERLREHNKHLNENIENKLLLKEEVEDLKRKleree 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 650 -----VSDLESEVLSLTAHSHADECEGEQNGTVTVSDLD------QLQKVNK-------DLEQQLAEKNKTIKQLQQRLA 711
Cdd:pfam05557 242 kyreeAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDlsrrieQLQQREIvlkeensSLTSSARQLEKARRELEQELA 321
|
330 340
....*....|....*....|....*
gi 121308974 712 ELKRTLQkELKLKPDPDSEMKERLQ 736
Cdd:pfam05557 322 QYLKKIE-DLNKKLKRHKALVRRLQ 345
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
411-709 |
3.11e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 411 ERTDAQISDLEQRLADCAEKMKS----LQQQLKDSQMHTDKLQMEWSE--ERERLQQQVSTQRQRGLEKTARLEEELLAV 484
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKqkfyLRQSVIDLQTKLQEMQMERDAmaDIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 485 QRDRETEANKYQDNLRLLEEEKNSLLRSKGETDSTVESLTAELEQSRAEMSSR--QTVSVEIAKALEE------------ 550
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILREldteisylkgri 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 551 --TRKQREELQQQVSKMTESLVKAEQEvsRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESRRLEAEEKEREHNSQ 628
Cdd:pfam15921 241 fpVEDQLEALKSESQNKIELLLQQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 629 LTSLQQEVLRQTQQL----SSYQSRVSDLESEVLSLTAHSHADECEGEQNGTVTVSDLDQLQKVNKDL---EQQLAEKNK 701
Cdd:pfam15921 319 LSDLESTVSQLRSELreakRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkrEKELSLEKE 398
|
....*...
gi 121308974 702 TIKQLQQR 709
Cdd:pfam15921 399 QNKRLWDR 406
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
322-663 |
3.20e-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: 41.35 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 322 LSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSLEAQVSRQNASIIDLqtlvkh 401
Cdd:pfam10174 382 IRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERL------ 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 402 KDDSSKAYRERTDaQISDLEQRLADCAEKMKSLQQQLkdsqmhtdklqMEWSEERERLQQQVSTQRQRGLEKTARLEEEL 481
Cdd:pfam10174 456 KEQREREDRERLE-ELESLKKENKDLKEKVSALQPEL-----------TEKESSLIDLKEHASSLASSGLKKDSKLKSLE 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 482 LAVQRDREtEANKYQDNLRLLEEEKNSLlRSKGETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQ 561
Cdd:pfam10174 524 IAVEQKKE-ECSKLENQLKKAHNAEEAV-RTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKK 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 562 VSKMteslvkaEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSlqaecESRRLEAEEKEREHNSQLTSLQQEVLRQTQ 641
Cdd:pfam10174 602 IAEL-------ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLE-----EARRREDNLADNSQQLQLEELMGALEKTRQ 669
|
330 340
....*....|....*....|..
gi 121308974 642 QLSSYQSRVSDLESEVLSLTAH 663
Cdd:pfam10174 670 ELDATKARLSSTQQSLAEKDGH 691
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
56-737 |
3.32e-03 |
|
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: 41.19 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 56 QIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSSMRKLQDQNESFQ-TNRAKMAEAMSL-----ALEKKD 129
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQrTVREKERELVDCqreleKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 130 QEWMEKLASLEQEKLSLTSRLDEMTEQSL---SLFQKRDDLDELEGFQQQELAKVK----HMLLRR--EEQLNQREKELK 200
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRardSLIQSLATRLELDGFERGPFSERQiknfHTLVIErqEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 201 LRGEELNTARLTLGKTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQ 280
Cdd:TIGR00606 416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 281 SNA-EALEKSMEHLQSEHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKE---KSSL 356
Cdd:TIGR00606 496 TETlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnKKQL 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 357 EQRLEEARGELLQekTSHTTAVSSLEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQ 436
Cdd:TIGR00606 576 EDWLHSKSKEINQ--TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSK 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 437 QLKDSQMHTDkLQMEWSEERERLQQQVSTQRQRGLEKTARLEEellaVQRDRETEANKYQDNLRLLEEEKNSLLRSKGET 516
Cdd:TIGR00606 654 QRAMLAGATA-VYSQFITQLTDENQSCCPVCQRVFQTEAELQE----FISDLQSKLRLAPDKLKSTESELKKKEKRRDEM 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 517 DSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVskmtESLVKAEQEVSRLSQDLGVKEEEVNALKE- 595
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL----GTIMPEEESAKVCLTDVTIMERFQMELKDv 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 596 ----ELQAARSSLSSLQAECESRRLEAEEKEREHN---SQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHADE 668
Cdd:TIGR00606 805 erkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ 884
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121308974 669 CEGEQNGTVtVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKELKLKPDPDSEMKERLQD 737
Cdd:TIGR00606 885 QFEEQLVEL-STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
125-708 |
3.93e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 125 LEKKDQEWMEKLASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQ---QELAKVKHMLLRREEQLNQREKELKL 201
Cdd:pfam05557 18 KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEealREQAELNRLKKKYLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 202 RGEELNTARLTLGKtqdklyELGEEHEEICRTNSQLQAQRdellSEKEEAERRVVDLERREQELQQLIqqvsEDFQKAQS 281
Cdd:pfam05557 98 QLADAREVISCLKN------ELSELRRQIQRAELELQSTN----SELEELQERLDLLKAKASEAEQLR----QNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 282 NAEALEKSMEHLQSEHNklklQHEQHKNKVAVTEEERERIlsdlqekaASLERRLEANFSQDEHLQELLKEKSSLEQRLE 361
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQ----SQEQDSEIVKNSKSELARI--------PELEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 362 EARGELLQEKTSHTTAVSsLEAQVSRQNAsiiDLQTLVKHKDDSSKAYRERTDA--QISDLEQRLADCAEKMKSLQQQLK 439
Cdd:pfam05557 232 DLKRKLEREEKYREEAAT-LELEKEKLEQ---ELQSWVKLAQDTGLNLRSPEDLsrRIEQLQQREIVLKEENSSLTSSAR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 440 dsqmHTDKLQMEwseererLQQQVSTQRQRGLEKTARLEEEllavqrdrETEANKYQDNLRLLEEEKNSLlrskgetDST 519
Cdd:pfam05557 308 ----QLEKARRE-------LEQELAQYLKKIEDLNKKLKRH--------KALVRRLQRRVLLLTKERDGY-------RAI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 520 VESLTAELEQSRAemssrqtvSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQA 599
Cdd:pfam05557 362 LESYDKELTMSNY--------SPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 600 ARSSLS-----SLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSS--------------YQSRVSDLE---SEV 657
Cdd:pfam05557 434 ADPSYSkeevdSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKtkvlhlsmnpaaeaYQQRKNQLEklqAEI 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 121308974 658 LSLTAHSHADECEGEQNGTVTVSDLDQLQKVNKDLEQQLAEKNKTIKQLQQ 708
Cdd:pfam05557 514 ERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKE 564
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
514-745 |
4.38e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 514 GETDSTVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQRE------------------ELQQQVSKMTESLVKAEQE 575
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqallkekreyegyELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 576 VSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAECESrrlEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLES 655
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 656 EVLSLTAHSHADECE--------GEQNGTVT--VSDLDQLQKVNKDLEQQLAEKNKTIKQLQQRLAELKRTLQKeLKLKP 725
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEieelereiEEERKRRDklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK-LKREI 401
|
250 260
....*....|....*....|
gi 121308974 726 DPDSEMKERLQDGRQERSAE 745
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEE 421
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
66-666 |
4.45e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 66 KLEAKLSDYAEQLRLMQKTKEKLEiALEKYQDSSMRKLQDQNESFQTnrakMAEAMSLALEKKDQEWMEKLASLEQEKLS 145
Cdd:pfam01576 184 KHEAMISDLEERLKKEEKGRQELE-KAKRKLEGESTDLQEQIAELQA----QIAELRAQLAKKEEELQAALARLEEETAQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 146 LTSRLDEMTEQSLSLFQKRDDLdELEGFQQQELAKVKHMLlrrEEQLNQREKELKLRGEELNTARLTLGKTQDKLYELGE 225
Cdd:pfam01576 259 KNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDL---GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 226 EHEEICRTN-SQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSmeHLQSEHNKLKLQH 304
Cdd:pfam01576 335 ALEEETRSHeAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA--KQDSEHKRKKLEG 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 305 EQHKNKVAVTEEERERilSDLQEKAASLERRLEANFSQDEHLQ----ELLKEKSSLEQRLEEARgELLQEKTSHTTAVSS 380
Cdd:pfam01576 413 QLQELQARLSESERQR--AELAEKLSKLQSELESVSSLLNEAEgkniKLSKDVSSLESQLQDTQ-ELLQEETRQKLNLST 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 381 LEAQVSRQNASIIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEWSEE----- 455
Cdd:pfam01576 490 RLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKaaayd 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 456 -----RERLQQQ-----VSTQRQR----GLEKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKN----SLLRSKGETD 517
Cdd:pfam01576 570 klektKNRLQQElddllVDLDHQRqlvsNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKEtralSLARALEEAL 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 518 STVESLTAELEQSRAEMSSRQTVSVEIAKALEETRKQREELQQQVSKMTESLVKAEQEvsrlsqdLGVKEEEVNALKEEL 597
Cdd:pfam01576 650 EAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDE-------LQATEDAKLRLEVNM 722
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121308974 598 QAARsslSSLQAECESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEVLSLTAHSHA 666
Cdd:pfam01576 723 QALK---AQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDA 788
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
382-629 |
4.61e-03 |
|
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: 40.49 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 382 EAQVSRQNAsiIDLQTLVKHKDDSSKAYRERTDAQISDLEQRLADcaEKMKSLQQQLKDSQMHT-DKLQMEWSEERERLQ 460
Cdd:pfam17380 320 EAEKARQAE--MDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQEEIAMEISRMRElERLQMERQQKNERVR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 461 QQVSTQRQRGL---EKTARLEEELLAVQRDRETEANKYQDNLRLLEEEKNSLLR----SKGETDSTVESLTAELEQSR-- 531
Cdd:pfam17380 396 QELEAARKVKIleeERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMErvrlEEQERQQQVERLRQQEEERKrk 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 532 -----AEMSSRQTVSVEIAKALE---ETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSS 603
Cdd:pfam17380 476 kleleKEKRDRKRAEEQRRKILEkelEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
250 260
....*....|....*....|....*.
gi 121308974 604 LSSLQAECESRRLEAEEKEREHNSQL 629
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREMMRQI 581
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
56-370 |
4.71e-03 |
|
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: 40.73 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 56 QIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSSMRKLQDQNESFQTNRAKMAEAMSLALEKKDQEWMEK 135
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 136 LASLEQEKLSLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKlrgEELNTARLTLGK 215
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK---EEQKLEKLAEEE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 216 TQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMEHLQS 295
Cdd:pfam02463 856 LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE 935
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121308974 296 EHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQDEHLQELLKEKSSLEQRLEEARGELLQE 370
Cdd:pfam02463 936 EPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
309-657 |
4.90e-03 |
|
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: 40.71 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 309 NKVAVTEEERERILSDLQEKAASLER--RLEANFSQ--------------DEHLQELLKEKSSLEQRLEEARGELLQekt 372
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQKlqRLHQAFSQfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQ--- 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 373 sHTTAVSSLEAQVSRQNAsiidLQTLVKHKDDSSKAYRertdaqISDLEQRLADCAEKMKSLQQQLKDSQMHTDKLQMEW 452
Cdd:COG3096 862 -LRQQLDQLKEQLQLLNK----LLPQANLLADETLADR------LEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQ 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 453 S--EERERLQQQVST--QRQRGLEKTARLEEELlaVQRdreTEANKYQDNLRLLeeeknsllrskGETDSTVESLTAELE 528
Cdd:COG3096 931 SdpEQFEQLQADYLQakEQQRRLKQQIFALSEV--VQR---RPHFSYEDAVGLL-----------GENSDLNEKLRARLE 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 529 QsraemssrqtvsveiakALEETRKQREELQQQVSKMTEslvkAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQ 608
Cdd:COG3096 995 Q-----------------AEEARREAREQLRQAQAQYSQ----YNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEA 1053
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 121308974 609 AEC-ESRRLEAEEKEREHNSQLTSLQQEVLRQTQQLSSYQSRVSDLESEV 657
Cdd:COG3096 1054 EERaRIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDY 1103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
56-229 |
5.47e-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: 40.13 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 56 QIQRRNDQIRKLEAKLSDYAEQLRLMQKTKEKLEIALEKYQDSSMRKLQDQNESFQTNRAKM-AEAMSLALEKKDQEWME 134
Cdd:COG4942 63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALlLSPEDFLDAVRRLQYLK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 135 KLASLEQEKL-SLTSRLDEMTEQSLSLFQKRDDLDELEGFQQQELAKVKHMLLRREEQLNQREKELKLRGEELNTARLTL 213
Cdd:COG4942 143 YLAPARREQAeELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
170
....*....|....*.
gi 121308974 214 GKTQDKLYELGEEHEE 229
Cdd:COG4942 223 EELEALIARLEAEAAA 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-394 |
7.25e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 189 EEQLNQREKELKLRGEELNTARltlgkTQDKLYELGEEHEEICRTNSQLQAQRDELLSEKEEAERRVVDLERREQELQQL 268
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 269 IQQVSED--FQKAQSNAEALEKSMEHLQS----EHNKLKLQHEQHKNKVAVTEEERERILSDLQEKAASLERRLEANFSQ 342
Cdd:COG3206 256 LPELLQSpvIQQLRAQLAELEAELAELSArytpNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 121308974 343 DEHLQELLKEKSSLEQRLEEARGELLQEKTSHTTAVSSL-EAQVSRQ----NASIID 394
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLeEARLAEAltvgNVRVID 392
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
252-620 |
7.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 252 ERRVVDLERREQELQQLIQQVSEDFQKAQSNAEALEKSMehlqSEHNKLKLQH--EQHKNKVAVTEEERERILSDLQEKA 329
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFI----GSHLAVAFEAdpEAELRQLNRRRVELERALADHESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 330 ASLERRLEANFSQDEHLQELLKEKS-----SLEQRLEEARGELLQEK------TSHTTAVSSLEAQVS--RQNASIIDLq 396
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALNRLLPRLNlladeTLADRVEEIREQLDEAEeakrfvQQHGNALAQLEPIVSvlQSDPEQFEQ- 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 397 tlVKHKDDSSKAYRERTDAQI---------------SDLEQRLADCAEKMKSLQQQLKDSQmhtdklqmewsEERERLQQ 461
Cdd:PRK04863 940 --LKQDYQQAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQRLEQAE-----------QERTRARE 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121308974 462 QVSTQRQRGLEKTArleeellaVQRDRETEANKYQDNLRLLEEEKNSLlrskgetdsTVESLTAELEQSRAEMSsrqtvs 541
Cdd:PRK04863 1007 QLRQAQAQLAQYNQ--------VLASLKSSYDAKRQMLQELKQELQDL---------GVPADSGAEERARARRD------ 1063
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121308974 542 vEIAKALEETRKQREELQQQVSKMTESLVKAEQEVSRLSQDLGVKEEEVNALKEELQAARSSLSSLQAEcesRRLEAEE 620
Cdd:PRK04863 1064 -ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVE---RRLHRRE 1138
|
|
| |
