|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
15-1188 |
5.51e-174 |
|
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: 545.34 E-value: 5.51e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLGEKTS-NLRVKTLRDLIHgaPVGKPAANRAFVSMVYSEEGA-------EDRTFARVIVGGSSEYKIN 86
Cdd:pfam02463 35 GKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVEITFDNEDHelpidkeEVSIRRRVYRGGDSEYYIN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 87 NKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHR 166
Cdd:pfam02463 113 GKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 167 KKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKK 246
Cdd:pfam02463 193 EELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 247 ELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQ 326
Cdd:pfam02463 273 ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 327 EFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREI 406
Cdd:pfam02463 353 AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 407 EENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIK 486
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 487 RLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLREL 566
Cdd:pfam02463 513 LALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 567 KGAKLVIDVIRYEpphikkalqyacgnalvcdnvedarriafgghqrhktvaldgtlfqksgvisggASDLKAKARRWDE 646
Cdd:pfam02463 593 SIAVLEIDPILNL------------------------------------------------------AQLDKATLEADED 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 647 KAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRI 726
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 727 NDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQL 806
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 807 KEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHL 886
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 887 QKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCE 966
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 967 DLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFD 1046
Cdd:pfam02463 939 ELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1047 RFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYK 1126
Cdd:pfam02463 1019 LKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYK 1098
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527317371 1127 PAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTKAESLIGVYPEQGDC 1188
Cdd:pfam02463 1099 PAPFYLLDEIDAALDDQNVSRVANLLKELSK-NAQFIVISLREEMLEKADKLVGVTMVENGV 1159
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-1181 |
1.28e-85 |
|
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: 303.14 E-value: 1.28e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLGEKTSN-LRVKTLRDLIHGAPVGKPAaNRAFVSMVYSEEGA----EDRTFARVIV---GGSSEYKIN 86
Cdd:TIGR02169 35 GKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQSG-NEAYVTVTFKNDDGkfpdELEVVRRLKVtddGKYSYYYLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 87 NKVVQLHEYSEELEKLGILIKARNFlVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHR 166
Cdd:TIGR02169 114 GQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 167 KKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKK 246
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 247 ELGKMMR--------EQQQIEKEIKEKDSELNQKRPQyIKAKEntshkiKKLEAAKKSLQNAQKHYKKRKGDMDELEKEm 318
Cdd:TIGR02169 273 LLEELNKkikdlgeeEQLRVKEKIGELEAEIASLERS-IAEKE------RELEDAEERLAKLEAEIDKLLAEIEELERE- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 319 LSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHR-LKEEASKRAATLAQ---ELEKFNRDQKADQDRLDLEERKKVE 394
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELAD 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 395 TEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSR 474
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 475 QQRKAEIMESIKRLYPGSVYGRLIDLCQpTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYL 554
Cdd:TIGR02169 505 RVRGGRAVEEVLKASIQGVHGTVAQLGS-VGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKM 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 555 EVKPTDEKLRELKGA-KLVIDVIRYEPpHIKKALQYACGNALVCDNVEDARRIAfgghQRHKTVALDGTLFQKSGVISGG 633
Cdd:TIGR02169 584 RDERRDLSILSEDGViGFAVDLVEFDP-KYEPAFKYVFGDTLVVEDIEAARRLM----GKYRMVTLEGELFEKSGAMTGG 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 634 AsdlkaKARRWDEKAVDKLKEKKERLTEELKEqmkAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQtKTRHLALNLQEks 713
Cdd:TIGR02169 659 S-----RAPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIEQ-- 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 714 kLESELANFGPRINDIKRIIQSREREMKDLKEKMnqvedevfeefcreigvrniREFEEEKVKRQNEIAKKRLEFENQKT 793
Cdd:TIGR02169 728 -LEQEEEKLKERLEELEEDLSSLEQEIENVKSEL--------------------KELEARIEELEEDLHKLEEALNDLEA 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 794 RLGIQLDFEKNQLKEDQDKVHM-WEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQhlakkseVNDKNHEMEEI 872
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-------IKSIEKEIENL 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 873 RKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKlplskgtmddisQEEGSSQGEDSvsgSQRISSiya 952
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK------------IEELEAQIEKK---RKRLSE--- 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 953 REALIEIDYGDLCEDLKDAQAEEEIKQE---MNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKR 1029
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1030 AKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSrNSSAQAFLgpENPEEPYLDGINYNCVAPGKRFRPMDNLSGG 1109
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELIL--ENPDDPFAGGLELSAKPKGKPVQRLEAMSGG 1078
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527317371 1110 EKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTKAESLIGV 1181
Cdd:TIGR02169 1079 EKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAG-EAQFIVVSLRSPMIEYADRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-1198 |
3.42e-82 |
|
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: 293.50 E-value: 3.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEgaeDRTFA-----------RVIVGGSSE 82
Cdd:TIGR02168 35 GKSNIVDAIRWVLGEqSAKALRGGKMEDVIFNGSETRKPLSLAEVELVFDNS---DGLLPgadyseisitrRLYRDGESE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 83 YKINNKVVQLHEYSEELekLGILIKARNF-LVFQGAVESIAMKNPKERTALFEE---ISRsgelaqeYDKRKKEMVKAEE 158
Cdd:TIGR02168 112 YFINGQPCRLKDIQDLF--LDTGLGKRSYsIIEQGKISEIIEAKPEERRAIFEEaagISK-------YKERRKETERKLE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 159 DTQFNYHRKKNIAAERKEA----KQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRM 234
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQlkslERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 235 DKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDEL 314
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 315 EKEMLSVEKarqefeermeeesqsqgrDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVE 394
Cdd:TIGR02168 343 EEKLEELKE------------------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 395 TEAKIKQKLREIEENQKRIEKLEEYITTSK-----QSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDR 469
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 470 QES--------SRQQRKAEIMESIK-----RLYPGSVYGRLIDLCQpTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQ 536
Cdd:TIGR02168 485 AQLqarldsleRLQENLEGFSEGVKallknQSGLSGILGVLSELIS-VDEGYEAAIEAALGGRLQAVVVENLNAAKKAIA 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 537 YIKEQRGEPETFLPLDYLE----VKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQ 612
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKgteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRP 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 613 RHKTVALDGTLFQKSGVISGGASDLKAK--ARRwdeKAVDKLKEKKERLTEELKE-QMKAKRKEAELRQVQSQAHGLQMR 689
Cdd:TIGR02168 644 GYRIVTLDGDLVRPGGVITGGSAKTNSSilERR---REIEELEEKIEELEEKIAElEKALAELRKELEELEEELEQLRKE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 690 LKYSQsdleqtktrhlalnlQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFcreigvRNIRE 769
Cdd:TIGR02168 721 LEELS---------------RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE------EELAE 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 770 FEEEKVKRQNEIAKKRLEFENQKTRLGIQldfeKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQ 849
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 850 DLKnqhlakkSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDIS 929
Cdd:TIGR02168 856 SLA-------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 930 QEEGSSQgedsvsgsQRISSIyaREALIEiDYGDLCEDLkdAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKL 1009
Cdd:TIGR02168 929 LRLEGLE--------VRIDNL--QERLSE-EYSLTLEEA--EALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEY 995
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1010 ESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQ-AFLGPENPEEPyldG 1088
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAElRLTDPEDLLEA---G 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1089 INYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLK 1168
Cdd:TIGR02168 1073 IEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSK-NTQFIVITHN 1151
|
1210 1220 1230
....*....|....*....|....*....|.
gi 527317371 1169 EEFYTKAESLIGV-YPEQGdcvISKVLTFDL 1198
Cdd:TIGR02168 1152 KGTMEVADQLYGVtMQEKG---VSKIVSVDL 1179
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1095-1198 |
5.46e-66 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 223.22 E-value: 5.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1095 APGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTK 1174
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFSK 224
|
90 100
....*....|....*....|....
gi 527317371 1175 AESLIGVYPEQgDCVISKVLTFDL 1198
Cdd:cd03275 225 ADALVGVYRDQ-ECNSSKVLTLDL 247
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
14-126 |
5.92e-59 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 203.19 E-value: 5.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 14 RGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLH 93
Cdd:cd03275 33 SGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAVYEDDDGEEKTFRRIITGGSSSYRINGKVVSLK 112
|
90 100 110
....*....|....*....|....*....|...
gi 527317371 94 EYSEELEKLGILIKARNFLVFQGAVESIAMKNP 126
Cdd:cd03275 113 EYNEELEKINILVKARNFLVFQGDVESIASKNP 145
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-749 |
7.12e-49 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 189.38 E-value: 7.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYS-EEGAEDRTFARVIV------GGSSEYKIN 86
Cdd:COG1196 36 GKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFAGSSSRKPLGRAEVSLTFDnSDGTLPIDYDEVTItrrlyrSGESEYYIN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 87 NKVVQLHEYSEELEKLGIliKARNF-LVFQGAVESIAMKNPKERTALFEE---ISRsgelaqeYDKRKKEmvkAE---ED 159
Cdd:COG1196 116 GKPCRLKDIQDLFLDTGL--GPESYsIIGQGMIDRIIEAKPEERRAIIEEaagISK-------YKERKEE---AErklEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 160 TQFNYHRKKNIAAE----RKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMD 235
Cdd:COG1196 184 TEENLERLEDILGElerqLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 236 KVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELE 315
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 316 KEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERkkvet 395
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER----- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 396 eakikqKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQ 475
Cdd:COG1196 419 ------LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 476 QRKAEIMESIKRLYPGSVY-----------GRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGE 544
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKaalllaglrglAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 545 PETFLPLDYLEVKPTDEKLRE----LKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALD 620
Cdd:COG1196 573 RATFLPLDKIRARAALAAALArgaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 621 GTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQT 700
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALL---EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 527317371 701 KTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQ 749
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
491-606 |
3.98e-32 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 121.57 E-value: 3.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 491 GSVYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVK-PTDEKLRELK-- 567
Cdd:smart00968 1 PGVLGRVADLISV-DPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRsPAGSKLREALlp 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 527317371 568 ---GAKLVIDVIRYePPHIKKALQYACGNALVCDNVEDARRI 606
Cdd:smart00968 80 epgFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1095-1181 |
1.19e-29 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 117.18 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1095 APGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTK 1174
Cdd:cd03278 103 APGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSK-ETQFIVITHRKGTMEA 181
|
....*..
gi 527317371 1175 AESLIGV 1181
Cdd:cd03278 182 ADRLYGV 188
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1096-1182 |
4.33e-29 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 115.86 E-value: 4.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1096 PGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQsTCNFQAIVISLKEEFYTKA 1175
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKER-TKNAQFIVISLRNNMFELA 196
|
....*..
gi 527317371 1176 ESLIGVY 1182
Cdd:cd03274 197 DRLVGIY 203
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
493-607 |
1.08e-27 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 108.50 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 493 VYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLV 572
Cdd:pfam06470 4 VLGRLADLIEV-DEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGAGPL 82
|
90 100 110
....*....|....*....|....*....|....*
gi 527317371 573 IDVIRYEPPhIKKALQYACGNALVCDNVEDARRIA 607
Cdd:pfam06470 83 LDLVEYDDE-YRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1106-1186 |
1.19e-25 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 105.08 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1106 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQ 1185
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVLFVH 174
|
.
gi 527317371 1186 G 1186
Cdd:cd03239 175 G 175
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1106-1186 |
1.04e-19 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 87.42 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1106 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQ 1185
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKVI 157
|
.
gi 527317371 1186 G 1186
Cdd:cd03227 158 T 158
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1106-1191 |
5.61e-16 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 78.88 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1106 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALD--NT-NIGKVanyIKEQSTcNFQAIVISLKEEFYTKAESLIGVY 1182
Cdd:cd03273 167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDlsHTqNIGRM---IKTHFK-GSQFIVVSLKEGMFNNANVLFRTR 242
|
....*....
gi 527317371 1183 PEQGDCVIS 1191
Cdd:cd03273 243 FVDGTSTVT 251
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1103-1181 |
2.21e-15 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 77.30 E-value: 2.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527317371 1103 MDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTKAESLIGV 1181
Cdd:cd03272 156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSD-GAQFITTTFRPELLEVADKFYGV 233
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-487 |
2.06e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 134 EEISRSGELAQ-EYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 212
Cdd:PTZ00121 1339 EEAKKAAEAAKaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 213 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE---------NT 283
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkaeeakKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 284 SHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKR 363
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 364 AATLAQELEKFNRDQKADQDRLDLEERK------KVETEAKIK-QKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 436
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeeaKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 527317371 437 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKR 487
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-487 |
2.54e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 134 EEISRSGELAQEYDKRK-KEMVKAEEDTQFNYHRKKniAAERKEAKQEKEEADRYQRLKDEVVR-AQVQLQLFKLYHNEV 211
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKaDEAKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKkAEEAKKAAEAAKAEA 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 212 EIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE--NTSHKIKK 289
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEakKKAEEKKK 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 290 LEAAKKSLQNAQK--HYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYH---RLKEEASKRA 364
Cdd:PTZ00121 1433 ADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeaKKAAEAKKKA 1512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 365 ATL--------AQELEKFNRDQKADQDR-----------LDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY------ 419
Cdd:PTZ00121 1513 DEAkkaeeakkADEAKKAEEAKKADEAKkaeekkkadelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeea 1592
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527317371 420 -ITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK--ELNQVMEQLGDARIDRQESSRQQRKAEIMESIKR 487
Cdd:PTZ00121 1593 rIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKaeEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
15-118 |
2.74e-11 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 65.01 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLG-EKTSNLRVKTLRDLIHGApvGKPAANRAFVSMVY-------SEEGAEDR---TFAR-VIVGGSSE 82
Cdd:cd03273 37 GKSNILDAICFVLGiTNLSTVRASNLQDLIYKR--GQAGITKASVTIVFdnsdksqSPIGFENYpeiTVTRqIVLGGTNK 114
|
90 100 110
....*....|....*....|....*....|....*.
gi 527317371 83 YKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAV 118
Cdd:cd03273 115 YLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
122-486 |
6.06e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 122 AMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNiAAERKEAKQEKEEADRYQRLKDEVVRAQvql 201
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKAD--- 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 202 QLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE 281
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 282 -------NTSHKIKKLEAAKKSlQNAQKHYKKRKGD----MDELEK--EMLSVEKARQEFEERMEEESQSQGRDlTLEEN 348
Cdd:PTZ00121 1515 akkaeeaKKADEAKKAEEAKKA-DEAKKAEEKKKADelkkAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAK-KAEEA 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 349 QVKKYHRLKEEASKRAATLAQELEKfnRDQKADQDRLDLEERKKVE----TEAKIKQKLREI----EENQKRIEKLEEYI 420
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEqlkkKEAEEKKKAEELkkaeEENKIKAAEEAKKA 1670
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527317371 421 TTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKelnqvMEQLGDARIDRQESSRQQRKAEIMESIK 486
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
122-483 |
6.99e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 122 AMKNPKERTALFEEISRSGELAQEYDKRKKemvKAEEDTQFNYHRKKNIAAER-KEAKQEKEEADRYQRLKDEVVRAQVQ 200
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKK---KAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 201 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKE---KDSELNQKRPQYI 277
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 278 KAKE-NTSHKIKKLEAAKKSLQNAQKHYKK----RKGDMDELEKEM--LSVEKARQEFEERMEEESQSQGRDLTLEENQV 350
Cdd:PTZ00121 1553 KAEElKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 351 KKYHRLK--EEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE 428
Cdd:PTZ00121 1633 KKVEQLKkkEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 429 EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIME 483
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-753 |
2.91e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 134 EEISRSGELAQEYDKRKKEMV-------KAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEvvRAQVQLQLFKL 206
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAArkaeeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN--EEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 207 YHNEVEIEKLNKELASKNKEIEK--DKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQyikAKENTS 284
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA---AKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 285 HKIKKLEAAKKSLQNAQKHYK--KRKGDMDELEKEmlsvekarqefeermeeESQSQGRDLTLEENQVKKYHRLKEEASK 362
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKE-----------------EAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 363 RAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE-----------EQK 431
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEakkadeakkkaEEA 1482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 432 KLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIA 511
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 512 VTKVLGKNMDAiiVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYAC 591
Cdd:PTZ00121 1563 KKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 592 GNALVCDNVEDARRIAFGGHQRHKTVAldgtlfQKSGVISGGASDLKaKARRWDEKAVDKLKEKKE--RLTEELKEQMKA 669
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEA------KKAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEeaKKAEELKKKEAE 1713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 670 KRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQ 749
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
....
gi 527317371 750 VEDE 753
Cdd:PTZ00121 1794 MEVD 1797
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
15-78 |
9.98e-10 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 59.40 E-value: 9.98e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 15 GKSNLMDAISFVLGEKTS-NLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEegaEDRTFArvIVG 78
Cdd:cd03278 34 GKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSETRKPANFAEVTLTFDN---SDGRYS--IIS 93
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
214-832 |
1.52e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 214 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELnqkrPQYIKAKENTSHKIKKLEAA 293
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL----PELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 294 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKaRQEFEERMEEESQSQGRDLTLEENQVKKYHRLKE---EASKRAATLAQE 370
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEE-RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 371 LEKFNRDQKADQDRLDLEERKKVETEaKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELT-EEVEMAKRRID 449
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 450 EINKELNQVMEQLGD--ARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIdlcqptqkkyqiavtkvlgknmdaiivDS 527
Cdd:PRK03918 395 ELEKAKEEIEEEISKitARIGELKKEIKELKKAIEELKKAKGKCPVCGREL---------------------------TE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 528 EKTGRDCIQYIKEQRGEPEtflpldylEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYA-----CGNALVCDNVED 602
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEK--------ELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkeLEEKLKKYNLEE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 603 ARRIAfgghqrHKTVALDGTLFQKSGVISGGASDLKA-----KARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELR 677
Cdd:PRK03918 520 LEKKA------EEYEKLKEKLIKLKGEIKSLKKELEKleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 678 -QVQSQAHGLQMRLKYSQSDLEQTktrhlalnLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQvedevfE 756
Cdd:PRK03918 594 lKELEPFYNEYLELKDAEKELERE--------EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE------E 659
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527317371 757 EFcreigvrniREFEEEKVKRQNEIAKKRLEFEnqktrlgiQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKK 832
Cdd:PRK03918 660 EY---------EELREEYLELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
123-487 |
1.03e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 123 MKNPKERTALFEEISRSGELAQEYD--KRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQrlKDEVVRAQVQ 200
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADE 1526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 201 LQLFKLYHNEVEIEKLN-KELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKrpQYIKA 279
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 280 KENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERmeeesqsqgrdltlEENQVKKYH-RLKE 358
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE--------------EENKIKAAEeAKKA 1670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 359 EASKRAATLAQELEKFNRdQKADQDRLDLEERKKVEteakikQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELT 438
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEK-KAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 527317371 439 EEVEMAKRRIDEINKelnqvMEQLGDARIDRQESSRQQRKAEIMESIKR 487
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-847 |
2.29e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 287 IKKLEAAKKSLQNAQKHYKKRKGDMDELE-----KEMLSVEKARQEFeermeeesQSQGRDLTLEENQVKKYHRLKEEAS 361
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAeleylRAALRLWFAQRRL--------ELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 362 KRAATLAQELEKFNRD-QKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLegeltee 440
Cdd:COG4913 316 ARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE------- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 441 vemAKRRIDEINKELNQVMEQLGDARIDRQESSRQQR--KAEI--MESIKRLYPGSVY--------------------GR 496
Cdd:COG4913 389 ---AAALLEALEEELEALEEALAEAEAALRDLRRELRelEAEIasLERRKSNIPARLLalrdalaealgldeaelpfvGE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 497 LIDLcQPTQKKYQIAVTKVLGKNMDAIIVDsEKTGRDCIQYIKEQRGEPEtflpLDYLEVKPTDEKLRELKG------AK 570
Cdd:COG4913 466 LIEV-RPEEERWRGAIERVLGGFALTLLVP-PEHYAAALRWVNRLHLRGR----LVYERVRTGLPDPERPRLdpdslaGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 571 LVIDVIRYEP---PHIKKALQYACgnalvCDNVEDARRiafggHQRHKTVA----LDGTLFQKsgvisggasDLKAKARR 643
Cdd:COG4913 540 LDFKPHPFRAwleAELGRRFDYVC-----VDSPEELRR-----HPRAITRAgqvkGNGTRHEK---------DDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 644 -----WD-EKAVDKLKEKKERLTEELKE-QMKAKRKEAELRQVQSQAHGLQMRLKYS--QSDLEQTKTRHLALNlQEKSK 714
Cdd:COG4913 601 ryvlgFDnRAKLAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELE-AELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 715 LE---SELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEvfeefcreigvrnIREFEEEKvkrqnEIAKKRLEFENQ 791
Cdd:COG4913 680 LDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-------------LEQAEEEL-----DELQDRLEAAED 741
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 527317371 792 KTRLGIQLDFEKNQLKEDQDKVhmwEQTVKKD-ENEIEKLKKEEQRHMKIIDETMAQ 847
Cdd:COG4913 742 LARLELRALLEERFAAALGDAV---ERELRENlEERIDALRARLNRAEEELERAMRA 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
637-1013 |
3.55e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 637 LKAKARRwdEKAVDKLKEKKERLT------EELKEQMKAKRKEAElrqVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQ 710
Cdd:COG1196 168 SKYKERK--EEAERKLEATEENLErledilGELERQLEPLERQAE---KAERYRELKEELKELEAELLLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 711 EKSKLESELANfgpRINDIKRIIQSREREMKDLKEKMNQVEDEVfeefcreigvrnirefeEEKVKRQNEIAKKRLEFEN 790
Cdd:COG1196 243 ELEAELEELEA---ELEELEAELAELEAELEELRLELEELELEL-----------------EEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 791 QKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEME 870
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 871 EIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQgedsvsgsQRISSI 950
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA--------EEEAEL 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527317371 951 YAREALIEIdygdlcEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVR 1013
Cdd:COG1196 455 EEEEEALLE------LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
173-486 |
4.07e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.83 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 173 ERKEAKQEKEEADRYQRLKDEVVRAqvqlqlfklyhnevEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMM 252
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQ--------------EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 253 REQQQIEK-EIKEKDSELNQKRPQYIKAKENTSHKIKKL--EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFE 329
Cdd:pfam17380 345 ERERELERiRQEERKRELERIRQEEIAMEISRMRELERLqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 330 ERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLaQELEKFNRDQKADQDRLDLEERKKVETEAK----IKQKLRE 405
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 406 -----IEENQKR--IEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRideinkelnQVMEQLGDARIDRQESSRQQRK 478
Cdd:pfam17380 504 rkqamIEEERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR---------RIQEQMRKATEERSRLEAMERE 574
|
....*...
gi 527317371 479 AEIMESIK 486
Cdd:pfam17380 575 REMMRQIV 582
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
134-486 |
6.22e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 134 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE- 212
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKr 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 213 IEKLNKELASKNKEIEKDKKRMDKVEDELKEkkkelgkmMREQQQIEKEIKEKDSELNQKRPQYIKAK----ENTSHKIK 288
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKELEEKLKKYNLEELEKKaeeyEKLKEKLI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 289 KLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLkeeaskraatlA 368
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE-----------Y 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 369 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKL------EEYITTSKQSLEEQKKLEGeLTEEVE 442
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseEEYEELREEYLELSRELAG-LRAELE 683
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 527317371 443 MAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIK 486
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELR 727
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
265-901 |
1.20e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 265 KDSELNQKRPQyiKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEkEMLSVEKARQEFEERMEEESQSQGRDLT 344
Cdd:PTZ00121 1077 KDFDFDAKEDN--RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 345 LEENQVKKYHRLKEEASKraatlAQELEKFNRDQKADQDRlDLEERKKVETEAKIKQKLREieENQKRIEKLEEYitTSK 424
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARK-----AEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKA--EEERKAEEARKA--EDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 425 QSLEEQKKLEgELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRlypgSVYGRLIDLCQPT 504
Cdd:PTZ00121 1224 KKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK----AEEKKKADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 505 QKKYQIAVTKVLGKNMDAiIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIK 584
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 585 KALQYACGNALVCDNVEDARRIAFGGHQRHKTValdgtlfQKSGVISGGASDLKAKARrwDEKAVDKLKEKKE--RLTEE 662
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADEL-------KKAAAAKKKADEAKKKAE--EKKKADEAKKKAEeaKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 663 LKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSRE-REMK 741
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKaDEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 742 DLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQL-DFEKNQLKE-----DQDKVHM 815
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEvmklyEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 816 WEQTVKKDENEI--EKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDK------NHEMEEIRKKLGGANKEMTHLQ 887
Cdd:PTZ00121 1609 AEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKAEEDEK 1688
|
650
....*....|....
gi 527317371 888 KEVTAIETKLEQKR 901
Cdd:PTZ00121 1689 KAAEALKKEAEEAK 1702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
166-1019 |
1.96e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 166 RKKNIAAER-KEAKQEKEEADRYQRLKDEVVRaqvqlqlfklyhnEVEIEKLNKELASKNKEIEK--DKKRMDKVEDELK 242
Cdd:PTZ00121 1084 KEDNRADEAtEEAFGKAEEAKKTETGKAEEAR-------------KAEEAKKKAEDARKAEEARKaeDARKAEEARKAED 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 243 EKKKELGKMMREQQQIEKEIKEKDS---ELNQKRPQYIKAKE-NTSHKIKKLEAAKKSlQNAQKHYKKRKGDMDELEKEM 318
Cdd:PTZ00121 1151 AKRVEIARKAEDARKAEEARKAEDAkkaEAARKAEEVRKAEElRKAEDARKAEAARKA-EEERKAEEARKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 319 LSVEKARQEFEERMEEESQSQGRDL-TLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRlDLEERKKVETEA 397
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIrKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK-KAEEKKKADEAK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 398 KIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKlegelteEVEMAKRRIDEINKELNQVMEQlgdARIDRQESSRQQR 477
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK-------AAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKK 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 478 KAEIMEsikrlypgsvygrlidlcqptQKKYQIAVTKVLGKNmdaiiVDSEKTGRDCIQYIKEQRGEPEtflpldylEVK 557
Cdd:PTZ00121 1379 KADAAK---------------------KKAEEKKKADEAKKK-----AEEDKKKADELKKAAAAKKKAD--------EAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 558 PTDEKLRELKGAKLVIDVIRYEPPHIKKAlqyacgnalvcdnvEDARRIAFGGHQRHKTVALDGTlfQKSGVISGGASDL 637
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKA--------------EEAKKAEEAKKKAEEAKKADEA--KKKAEEAKKADEA 1488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 638 KAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLES 717
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 718 ELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEvfeefcREIGVRNIREFEEEKVK----RQNEIAKKRLEFENQKT 793
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE------KKMKAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKE 1642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 794 RLGIQlDFEKNQLKEDQDKVHMWEQTVKKDEN--EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNhEMEE 871
Cdd:PTZ00121 1643 AEEKK-KAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEE 1720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 872 IRKKLGGANKEMTHLQKEVTAIETKLEQKRSD---RHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQR-I 947
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKkI 1800
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527317371 948 SSIYAREALIEI--DYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQET 1019
Cdd:PTZ00121 1801 KDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-455 |
2.55e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 134 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQlfklyhnevEI 213
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK---------KA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 214 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKEntSHKIKKLEAA 293
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEA 1667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 294 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARqefeermeeesqsqgrdltlEENQVKKYHRLKEEASKRAATLAQELEK 373
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE--------------------EAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 374 fnRDQKADQDRLDLEERKKVETEAKIKqklrEIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK 453
Cdd:PTZ00121 1728 --NKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
..
gi 527317371 454 EL 455
Cdd:PTZ00121 1802 DI 1803
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-746 |
4.44e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 311 MDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRL---KEEASKRAATLAQELEKFNRD----QKADQD 383
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREEleklEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 384 RLDLEERKKVETE--------AKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEG--------ELTEEVEMAKRR 447
Cdd:COG4717 128 LPLYQELEALEAElaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 448 IDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGknMDAIIVds 527
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG--VLFLVL-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 528 ektGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYAcgnalvcDNVEDARRIA 607
Cdd:COG4717 284 ---GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL-------DRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 608 FGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAvDKLKEKKERLtEELKEQMKAKRKEAELRQVQSQAHGLQ 687
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEEL-EELEEQLEELLGELEELLEALDEEELE 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527317371 688 MRLKYSQSDLEQTKTRHLALnLQEKSKLESELANFGP--RINDIKRIIQSREREMKDLKEK 746
Cdd:COG4717 432 EELEELEEELEELEEELEEL-REELAELEAELEQLEEdgELAELLQELEELKAELRELAEE 491
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1100-1181 |
5.69e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1100 FRPMDNLSGGEKTVAALALLFAIHSYKPA--PFFVLDEIDAALDNTNI-GKVANYIKEQ-STCNFQAIVISLKEEFYTKA 1175
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERkSQKNFQLIVITHDEELVDAA 189
|
....*.
gi 527317371 1176 ESLIGV 1181
Cdd:cd03240 190 DHIYRV 195
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1097-1166 |
9.22e-07 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 50.67 E-value: 9.22e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527317371 1097 GKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNiGKVA--NYIKE-QSTCNFQAIVIS 1166
Cdd:cd03276 101 KAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN-RKIStdLLVKEaKKQPGRQFIFIT 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
127-488 |
1.04e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 127 KERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNiaaERKEAKQEKEEA-DRYQRLKDEVVRAQVQLQLFK 205
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE---ELEELEEELEELeAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 206 LYHnevEIEKLNKELASKNKEIEKDKKRMDKVEDelkekkkelgkMMREQQQIEKEIKEKDSELNQ--------KRPQYI 277
Cdd:COG4717 130 LYQ---ELEALEAELAELPERLEELEERLEELRE-----------LEEELEELEAELAELQEELEElleqlslaTEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 278 KAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQS------------------- 338
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllslilti 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 339 -----------------QGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRL-----DLEERKKVETE 396
Cdd:COG4717 276 agvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 397 AKIKQKLREIEENQKRIEKL-EEYITTSKQSLE---EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQES 472
Cdd:COG4717 356 AEELEEELQLEELEQEIAALlAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE 435
|
410
....*....|....*.
gi 527317371 473 SRQQRKAEIMESIKRL 488
Cdd:COG4717 436 ELEEELEELEEELEEL 451
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
259-481 |
1.12e-06 |
|
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: 53.13 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 259 EKEIKEKDSELNQKRPQYIKAKENT--SHKIKKLEAAKKSLQNAQKhykkrkgdMDELEKEMLSVEKARQEFEERMEEES 336
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQ--------LVELSTEVQSLIREIKDAKEQDSPLE 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 337 QSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRL-DLEERKKVETEAKIKQKLREIEENQKRIEK 415
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIqDGKDDYLKQKETELNTVNAQLEECEKHQEK 995
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527317371 416 LEEYITTSKQSLEEQKKLEGELTEEVEMAKRR--IDEINKELNQVMEQLGDARIDRQESSRQQRKAEI 481
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENI 1063
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
141-417 |
1.13e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 141 ELAQEYDKRKKeMVKAEEDTQFNYHRKKNIAAERKEAKQEKE-EADRYQRLKDEVVRAQVQLQLFKLYHNEV-EIEKLNK 218
Cdd:pfam17380 307 EKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERErELERIRQEERKRELERIRQEEIAMEISRMrELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 219 ELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEiKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKK--S 296
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE-QEEARQREVRRLEEERAREMERVRLEEQERQQQveR 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 297 LQNAQKHYKKRKGDMDELEKEMLSVEKAR-----QEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQ-- 369
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRrkileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERrk 544
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 527317371 370 ELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLE 417
Cdd:pfam17380 545 QQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1106-1166 |
1.61e-06 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 49.17 E-value: 1.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527317371 1106 LSGGEKTVAALALLFAihsYKPaPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVIS 1166
Cdd:cd00267 81 LSGGQRQRVALARALL---LNP-DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVT 137
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-454 |
1.67e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 134 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQ-EKEEADRYQRLKDEVVRAQVQlQLFKLYHNEVE 212
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 213 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQyiKAKENTSHKIKKLEA 292
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEALKKEAE 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 293 AKKSLQNAQKHYKKRKGDMDELEKEMlSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELE 372
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 373 KFNRD--QKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDE 450
Cdd:PTZ00121 1779 AVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNN 1858
|
....
gi 527317371 451 INKE 454
Cdd:PTZ00121 1859 ENGE 1862
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
15-62 |
1.77e-06 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 49.61 E-value: 1.77e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 527317371 15 GKSNLMDAISFVLGEKTSNLRVKTLRDLIHGApvGKPAANRAFVSMVY 62
Cdd:cd03239 34 GKSNIVDAICFVLGGKAAKLRRGSLLFLAGGG--VKAGINSASVEITF 79
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
841-1036 |
2.57e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 841 IDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDiklpl 920
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 921 skGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAE-EEIKQEMNTLQQKLNEQQSVLQRIA 999
Cdd:COG3883 100 --GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAElEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 527317371 1000 APNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQA 1036
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
15-123 |
3.24e-06 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 49.95 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLGEKTSNLRVKTLRDLIH-GApvgKPAANRAFVSMVY--SEE----GAEDRTFARVIVGGSSEYKINN 87
Cdd:cd03272 35 GKSNFFAAIRFVLSDEYTHLREEQRQALLHeGS---GPSVMSAYVEIIFdnSDNrfpiDKEEVRLRRTIGLKKDEYFLDK 111
|
90 100 110
....*....|....*....|....*....|....*.
gi 527317371 88 KVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAM 123
Cdd:cd03272 112 KNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTN 147
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
15-123 |
3.88e-06 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 49.22 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPvGKPAANRAFVSMvyseegaedrTFARVIVggsseykinnkvvqlhe 94
Cdd:cd03274 37 GKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSA-GHPNLDSCSVEV----------HFQEIID----------------- 88
|
90 100
....*....|....*....|....*....
gi 527317371 95 ySEELEKLGILIKARNFLVFQGAVESIAM 123
Cdd:cd03274 89 -KPLLKSKGIDLDHNRFLILQGEVEQIAQ 116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-479 |
8.35e-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: 49.38 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 253 REQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEK---ARQEFE 329
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 330 ERMEEESQSQGRDLTLEenqvkkyHRLKEEASKRAATLAQELEKFNRDQKADQDRLdleerkkVETEAKIKQKLREIEEN 409
Cdd:COG4942 107 AELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527317371 410 QKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKA 479
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
134-488 |
9.48e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 134 EEISRSGELAQEYDKRKKEMVKAEEdtqfnyhRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEI 213
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEE-------RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 214 EKLNKELAS---KNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKenTSHKIKKL 290
Cdd:PRK03918 387 EKLEKELEElekAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEE--YTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 291 EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEA---SKRAATL 367
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklKGEIKSL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 368 AQELEKFNrDQKADQDRLDLEERKKVETEAKIKQKLRE-----IEENQKRIEKLEEY------ITTSKQSLEEQKKLEGE 436
Cdd:PRK03918 545 KKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKELEPFyneyleLKDAEKELEREEKELKK 623
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 527317371 437 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 488
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-904 |
2.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 119 ESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKdevvraq 198
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIAR------- 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 199 vqlqlfklyhnevEIEKLNKELASKNKEiekDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIK 278
Cdd:PTZ00121 1159 -------------KAEDARKAEEARKAE---DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 279 AKEntSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSqgrDLTLEENQVKKYHRLKE 358
Cdd:PTZ00121 1223 AKK--AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DELKKAEEKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 359 EASKRAATLAQEleKFNRDQKADQDRLDLEERKKVETEAKIKQ---------KLREIEENQKRIEKLEEYITTSKQSLEE 429
Cdd:PTZ00121 1298 AEEKKKADEAKK--KAEEAKKADEAKKKAEEAKKKADAAKKKAeeakkaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 430 QKKLEGELTEEVEmAKRRIDEINK---ELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDlcqPTQK 506
Cdd:PTZ00121 1376 AKKKADAAKKKAE-EKKKADEAKKkaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD---EAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 507 KyqiavtkvlgknmdaiiVDSEKTGRDCIQYIKEQRGEPEtfLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKA 586
Cdd:PTZ00121 1452 K-----------------AEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 587 lqyacgnalvcDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKEQ 666
Cdd:PTZ00121 1513 -----------DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK---KAEEKKKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 667 mkAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHlalnlQEKSKLESELANfgpRINDIKRIIQSREREMKDLKEK 746
Cdd:PTZ00121 1579 --ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKK 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 747 MNQVEDEvfEEFCREIGVRNIREFEEEkvKRQNEIAKKRLEFENQKtrlgiqldfeKNQLKEDQDKVHMWEQTVKKDENE 826
Cdd:PTZ00121 1649 AEELKKA--EEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKA----------AEALKKEAEEAKKAEELKKKEAEE 1714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 827 I---EKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKN---HEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQK 900
Cdd:PTZ00121 1715 KkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....
gi 527317371 901 RSDR 904
Cdd:PTZ00121 1795 EVDK 1798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
209-447 |
2.68e-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: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 209 NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRpqyikakentshkiK 288
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------------K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 289 KLEAAKKSLQNAQKHYKK------RKGDMDELeKEMLSVEKARQEFEERMEEESQSQGRdltleENQVKKYHRLKEEASK 362
Cdd:COG4942 91 EIAELRAELEAQKEELAEllralyRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPAR-----REQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 363 RAATLAQE---LEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTE 439
Cdd:COG4942 165 LRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*...
gi 527317371 440 EVEMAKRR 447
Cdd:COG4942 245 AAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
259-480 |
5.46e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 259 EKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEK---ARQEFEERMEEE 335
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 336 SQSQGRDLTLEENQVkkyhrlkeeASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEK 415
Cdd:COG3883 95 LYRSGGSVSYLDVLL---------GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 416 LEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAE 480
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
654-1073 |
6.15e-05 |
|
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: 47.41 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 654 EKKERLTEELKEQMKAKRKEAELRQVQSQAHglQMRLKYSQSDLEQTKTRhlALNLQEKSKLESElanfgprinDIKRII 733
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEK--ENKMKDLTFLLEESRDK--ANQLEEKTKLQDE---------NLKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 734 QSRE---REMKDLKEKMNQ-VEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKR-------LEFENQKTRLGIQLDFE 802
Cdd:pfam05483 289 EKKDhltKELEDIKMSLQRsMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 803 KNQLKEDQDKVHMWEQTVKKDENEIEKLkkeeqrhMKIIDETMAQLQDLKNQhLAKKSEVNDKNHEMEEIRKKLGGANKE 882
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEM-------TKFKNNKEVELEELKKI-LAEDEKLLDEKKQFEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 883 MTHL----QKEVTAIETKLEQKRSDRHNLLQacKMQDIKLPLSKGTMDDISQEEGSsqgeDSVSGSQRISSIYAREALIE 958
Cdd:pfam05483 441 LIFLlqarEKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNIELTAHC----DKLLLENKELTQEASDMTLE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 959 IDYGDlcEDLKDAQAEEE-IKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAF 1037
Cdd:pfam05483 515 LKKHQ--EDIINCKKQEErMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
410 420 430
....*....|....*....|....*....|....*....
gi 527317371 1038 EQikkeRFDRFNACFESVATNIDEIY---KALSRNSSAQ 1073
Cdd:pfam05483 593 EN----KCNNLKKQIENKNKNIEELHqenKALKKKGSAE 627
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
254-489 |
6.49e-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: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 254 EQQQIEKEIKEKDSELNQKRPqyIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERME 333
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 334 EESQSQGRdLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRI 413
Cdd:pfam17380 375 SRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRL 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527317371 414 EKLE--EYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDrQESSRQQRKAEIMESIKRLY 489
Cdd:pfam17380 454 EEQErqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIY 530
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
251-373 |
6.76e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 251 MMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEE 330
Cdd:PRK12704 66 IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 527317371 331 RMEEESQSQGRDLTLEEnqvkkyhrLKEEASKRAATLAQELEK 373
Cdd:PRK12704 146 RISGLTAEEAKEILLEK--------VEEEARHEAAVLIKEIEE 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-497 |
7.24e-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: 46.68 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 391 KKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVmeqlgDARIDRQ 470
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----EKEIAEL 95
|
90 100
....*....|....*....|....*..
gi 527317371 471 ESSRQQRKAEIMESIKRLYPGSVYGRL 497
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPL 122
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
638-906 |
7.25e-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: 47.04 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 638 KAKARRWDEKAVDKLKEKKERL-TEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLE 716
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 717 SElanfgprindikriiQSREREMKDLKEKMNQVEDEVFEefcreigvrniREFEEEKVKRQNEIAKKRLEFENQKTRLG 796
Cdd:pfam17380 362 LE---------------RIRQEEIAMEISRMRELERLQME-----------RQQKNERVRQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 797 IQLDFEKNQLKEDQDKVHMWEQTVKKDEN--EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRK 874
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQREVRRLEEERarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
250 260 270
....*....|....*....|....*....|....*
gi 527317371 875 KLggaNKEMTHLQKEVTAIETK---LEQKRSDRHN 906
Cdd:pfam17380 496 IL---EKELEERKQAMIEEERKrklLEKEMEERQK 527
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
91-488 |
7.41e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 91 QLHEYSEELEKLGILIKARNFLVfQGAVES--IAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKk 168
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSEC-QGQMERqmAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 169 niAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYH----------NEVEIEKLNKELASKNKEIEKDKKRMDKVE 238
Cdd:pfam15921 498 --VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknegdhlrnVQTECEALKLQMAEKDKVIEILRQQIENMT 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 239 DELKEKKKELGKMMREQQQIEKEIKEKDSELNqkrpQYIKAKENTSHKIKKLEA-------AKKSLQNAQKHYKKRKGDM 311
Cdd:pfam15921 576 QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ----EFKILKDKKDAKIRELEArvsdlelEKVKLVNAGSERLRAVKDI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 312 DELEKEMLSVEKarqefeermeeESQSQGRDLTLEENQVKKYHRLK-EEASKRAATLAQELEKFNRDQKADQDRLDLEE- 389
Cdd:pfam15921 652 KQERDQLLNEVK-----------TSRNELNSLSEDYEVLKRNFRNKsEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEg 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 390 ------RKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQS----LEEQKKLEGEL----TEEVEMA----------- 444
Cdd:pfam15921 721 sdghamKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhflKEEKNKLSQELstvaTEKNKMAgelevlrsqer 800
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 527317371 445 --KRRIDEINKELNQVMEQLGDAR--IDRQESSRQQRKAEIMESIKRL 488
Cdd:pfam15921 801 rlKEKVANMEVALDKASLQFAECQdiIQRQEQESVRLKLQHTLDVKEL 848
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
349-489 |
9.40e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 349 QVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQK---------LREIEENQKRIEKLEEY 419
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 420 ITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLgDARIDRQESSRQQRKAEIMESIKRLY 489
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL-EAELEELEAEREELAAKIPPELLALY 180
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1099-1152 |
1.11e-04 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 44.89 E-value: 1.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527317371 1099 RFRPMDNL--------SGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYI 1152
Cdd:cd03277 112 KFREGEQLqeldphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDML 173
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1088-1186 |
1.14e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1088 GINYncVAPGkrfRPMDNLSGGEKTVAALALLFAIHSykPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISL 1167
Cdd:cd03238 75 GLGY--LTLG---QKLSTLSGGELQRVKLASELFSEP--PGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147
|
90
....*....|....*....
gi 527317371 1168 KEEFYTKAESLIGVYPEQG 1186
Cdd:cd03238 148 NLDVLSSADWIIDFGPGSG 166
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-488 |
1.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 349 QVKKYHRLKEEASKRAATLAQELEKFnrdQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE 428
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELA---ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527317371 429 EQKKLEGELTEEVEMAKRRIDEI-NKELNQVMEQLGDARIDRQEssRQQRKAEIMESIKRL 488
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEE--RERRRARLEALLAAL 371
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
128-478 |
1.72e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.19 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 128 ERTALFEEISRSGELaQEYDKRKKEMVKaeEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLY 207
Cdd:PTZ00108 1012 SNKVRFIKHVINGEL-VITNAKKKDLVK--ELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSY 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 208 H----------NEVEIEKLNKELASKNKEIEKDKKRmdkvedelkekkkELGKM-MREQQQIEKEIKEKDSELNQKRPQY 276
Cdd:PTZ00108 1089 DyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNT-------------TPKDMwLEDLDKFEEALEEQEEVEEKEIAKE 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 277 IKAKENTSHKIKKLeaAKKSLQNAQKhyKKRKGDMDELEKEMLSVEKARQEFEERMEEESQ-------SQGRDLTLEENQ 349
Cdd:PTZ00108 1156 QRLKSKTKGKASKL--RKPKLKKKEK--KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKpdnkksnSSGSDQEDDEEQ 1231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 350 VKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEE 429
Cdd:PTZ00108 1232 KTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVK 1311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 527317371 430 QKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRK 478
Cdd:PTZ00108 1312 KRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKK 1360
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
355-487 |
1.75e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 355 RLKEEASKRAATLAQELEkfnRDQKadqdrlDLEERKKVETEAKIKQKLREIEENQKRIEKLEE-------YITTSKQSL 427
Cdd:PRK12704 42 RILEEAKKEAEAIKKEAL---LEAK------EEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrkleLLEKREEEL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 428 EEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLG-----DARIDRQESSRQQRKAEIMESIKR 487
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeEAKEILLEKVEEEARHEAAVLIKE 177
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
314-463 |
2.27e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 314 LEKEMlsvEKARQEFEERMEEESQSQGRDLTLEENQVKKY----HRLKEEASKRAATLAqELEKFNRDQKADQDRLDLEE 389
Cdd:COG2433 382 LEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLeeqvERLEAEVEELEAELE-EKDERIERLERELSEARSEE 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 390 RKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKE-LNQVMEQLG 463
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEaIRRLEEEYG 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
818-1050 |
2.38e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 818 QTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKL 897
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 898 EQKRSDRHNLLQACKMQdiklplskGTMDDISQEEGSSQGEDSVSGSQRISSIY-AREALIEiDYGDLCEDLKDAQAE-E 975
Cdd:COG4942 100 EAQKEELAELLRALYRL--------GRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAE-ELRADLAELAALRAElE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 976 EIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNA 1050
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
668-899 |
2.40e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 668 KAKRKEAELRQVQSQahglqmrLKYSQSDLEQTKtrhlalnlQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKM 747
Cdd:COG4942 21 AAAEAEAELEQLQQE-------IAELEKELAALK--------KEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 748 NQVEDEvfeefcreigvrnIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEI 827
Cdd:COG4942 86 AELEKE-------------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527317371 828 EKLKKE-------EQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQ 899
Cdd:COG4942 153 EELRADlaelaalRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
15-474 |
3.03e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLgekTSNLRVKTLRDLIhgapvgKPAANRAFVSMVYSEEGAEDRTFARVIVGG-----SSEYKINNKV 89
Cdd:PRK01156 35 GKSSIVDAIRFAL---FTDKRTEKIEDMI------KKGKNNLEVELEFRIGGHVYQIRRSIERRGkgsrrEAYIKKDGSI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 90 VQ--LHEYSEELEKLGILIKARNFL----VFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMvkaeedtqfn 163
Cdd:PRK01156 106 IAegFDDTTKYIEKNILGISKDVFLnsifVGQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVI---------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 164 yhrkKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLfKLYHNEVEIEKLNKELASKNKEIEKDKKRMDkvedelke 243
Cdd:PRK01156 176 ----DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEK-SHSITLKEIERLSIEYNNAMDDYNNLKSALN-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 244 kkkELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELeKEMLSVEK 323
Cdd:PRK01156 243 ---ELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK-KQILSNID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 324 ArqefeermeeesqsqgrdltleenQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLE--ERKKVETEAKIKQ 401
Cdd:PRK01156 319 A------------------------EINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEgyEMDYNSYLKSIES 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527317371 402 KLREIEENQKRIEKLEEYITtskQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSR 474
Cdd:PRK01156 375 LKKKIEEYSKNIERMSAFIS---EILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
356-486 |
3.66e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 356 LKEEASKRA-ATLAQELEKFNR-DQKADQDRLDLEERKKvETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEqkkl 433
Cdd:PRK00409 499 LPENIIEEAkKLIGEDKEKLNElIASLEELERELEQKAE-EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK---- 573
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 527317371 434 egELTEEVEMAKRRIDEINKELNQvMEQLGDARIDRQESSRQQRK----AEIMESIK 486
Cdd:PRK00409 574 --EAQQAIKEAKKEADEIIKELRQ-LQKGGYASVKAHELIEARKRlnkaNEKKEKKK 627
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
144-453 |
5.65e-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: 44.33 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 144 QEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQrlkdEVVRAQVQLQLFKLYHNEVEIEKLNKELASK 223
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA----EELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 224 NKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKH 303
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 304 YKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQD 383
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 384 RLDLEERKKVETEAKIKQKLREIEENQkriEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK 453
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELELASAK---QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
213-455 |
7.11e-04 |
|
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: 44.06 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 213 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQiekeikEKDsELNQKRPQYIKAKENtshKIKKLEA 292
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS------EKD-KKNKALAERKDSANE---RLNSLEA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 293 AKKSLQNAQKHYKKR-KGDMDELEKEMLSVEKArqefeermeeesqsqgrdltLEENQVKKYHRLKEEASKRAATLAQEL 371
Cdd:pfam12128 690 QLKQLDKKHQAWLEEqKEQKREARTEKQAYWQV--------------------VEGALDAQLALLKAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 372 EKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY---------------ITTSKQSLEEQKKLEGE 436
Cdd:pfam12128 750 KALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYfdwyqetwlqrrprlATQLSNIERAISELQQQ 829
|
250
....*....|....*....
gi 527317371 437 LTEEVEMAKRRIDEINKEL 455
Cdd:pfam12128 830 LARLIADTKLRRAKLEMER 848
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
625-1191 |
7.13e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 625 QKSGVISGGASDLKAKARRWDE--KAVDKLKEKKERLTEELK--EQMKAKRKEAELRQVQSQAHgLQMRLKYSQSDLEQT 700
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDlnNQILELEGYEMDYNSYLKsiESLKKKIEEYSKNIERMSAF-ISEILKIQEIDPDAI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 701 KTRHLALNlQEKSKLESELANFGPRINDIkriiqsREREMkDLKEKMNQVEDEVFEEFCR----EIGVRNIRE------- 769
Cdd:PRK01156 408 KKELNEIN-VKLQDISSKVSSLNQRIRAL------RENLD-ELSRNMEMLNGQSVCPVCGttlgEEKSNHIINhynekks 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 770 -FEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMA-Q 847
Cdd:PRK01156 480 rLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 848 LQDL--KNQHLAKKSEVNDkNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRS-----------------DRHNLL 908
Cdd:PRK01156 560 LEDLdsKRTSWLNALAVIS-LIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidksireieneannlnNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 909 QACKMQDIKLplsKGTMDDISQEegsSQGEDSVSGSQriSSIYAREALIEIDYGDLCEDLKDAQAE--------EEIKQE 980
Cdd:PRK01156 639 QENKILIEKL---RGKIDNYKKQ---IAEIDSIIPDL--KEITSRINDIEDNLKKSRKALDDAKANrarlestiEILRTR 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 981 MNTLQQKLNEQQSVLQRiaapnMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVatNID 1060
Cdd:PRK01156 711 INELSDRINDINETLES-----MKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKYLFEFNLDFDDI--DVD 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1061 EIYK-ALSRNSSAQAflgpenpeepyldginyncvapgkrfrpMDNLSGGEKTVAALALLFAIHSY--KPAPFFVLDEID 1137
Cdd:PRK01156 784 QDFNiTVSRGGMVEG----------------------------IDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPT 835
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 527317371 1138 AALDN---TNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVIS 1191
Cdd:PRK01156 836 AFLDEdrrTNLKDIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSKVI 892
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
127-472 |
8.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 127 KERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEE-ADRYQRLKDEVVRAQVQLQLFK 205
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKELKEKAEEYIKLSE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 206 LYHN-EVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKkKELGKMMREQQQIEKEIKEKDSELNQKRP-----QYIKA 279
Cdd:PRK03918 301 FYEEyLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEERHELYEEAKAkkeelERLKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 280 K------ENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMD----ELEKEMLSVEKA--------RQEFEERMEEESQSQGR 341
Cdd:PRK03918 380 RltgltpEKLEKELEELEKAKEEIEEEISKITARIGELKkeikELKKAIEELKKAkgkcpvcgRELTEEHRKELLEEYTA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 342 DLTLEENQVKKYHRLKEEASKRAATLAQELEKFNR----DQKADQDRlDLEERKKVETEAKIKQKLREIEENQKRIEKLE 417
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklKELAEQLK-ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 418 EYITTSKQSLEEQKKLEGELtEEVEMAKRRIDEINKELNQVMEQLGDARIDRQES 472
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKL-AELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
96-440 |
8.68e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 96 SEELEKLGILiKARNFLVFQGA--VESIAMKNPKERTALFeeiSRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAE 173
Cdd:PLN03229 390 TEELLKHRML-KFRKIGGFQEGvpVDPERKVNMKKREAVK---TPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 174 R--KEAKQEKEEA-------DRYQRLKDEVVRAQVQLQLFklyhNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEK 244
Cdd:PLN03229 466 KlkKEIDLEYTEAviamglqERLENLREEFSKANSQDQLM----HPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLN 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 245 KKELGKMMREQQQIEKEIKekdSELNQKRPQYIKAKEntshkIK-KLEAAKKSLQNAQKHykkRKGDMDELEKEmlSVEK 323
Cdd:PLN03229 542 EFSRAKALSEKKSKAEKLK---AEINKKFKEVMDRPE-----IKeKMEALKAEVASSGAS---SGDELDDDLKE--KVEK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 324 ARQEFEERMEEESQSQGRDL-------------TLEENQVKKYHRLKEEASK------RAATLAQELEKFNRDQKADQDR 384
Cdd:PLN03229 609 MKKEIELELAGVLKSMGLEVigvtkknkdtaeqTPPPNLQEKIESLNEEINKkierviRSSDLKSKIELLKLEVAKASKT 688
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 527317371 385 LDLEERKKVET-EAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 440
Cdd:PLN03229 689 PDVTEKEKIEAlEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKND 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
171-412 |
8.74e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 171 AAERKEAKQEKEEadryqrlkdevVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGK 250
Cdd:COG4942 19 ADAAAEAEAELEQ-----------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 251 MMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKI----KKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQ 326
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 327 EFEERMEEESQsqgrdltLEENQVKKYHRLKEEASKRAATLAQelekFNRDQKADQDRLDLEERKKVETEAKIKQKLREI 406
Cdd:COG4942 168 ELEAERAELEA-------LLAELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*.
gi 527317371 407 EENQKR 412
Cdd:COG4942 237 AAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
257-488 |
8.87e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 257 QIE-KEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQ---KHYKKRKGDMDELEKEMLSV-EKARQEFEER 331
Cdd:PRK02224 195 QIEeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLrETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 332 MEEESQSQGRDLTLEEnqvkkyhrLKEEASKRAATLAQElekfNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQK 411
Cdd:PRK02224 275 EELAEEVRDLRERLEE--------LEEERDDLLAEAGLD----DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 412 RIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKR-------RIDEINKELNQVMEQLGDARIDRQES-----SRQQRKA 479
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREavedrreEIEELEEEIEELRERFGDAPVDLGNAedfleELREERD 422
|
....*....
gi 527317371 480 EIMESIKRL 488
Cdd:PRK02224 423 ELREREAEL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
635-856 |
9.44e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 635 SDLKAKARRWDEKAVDKlkekkeRLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSK 714
Cdd:COG4913 255 EPIRELAERYAAARERL------AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 715 LESELANFGPRINDIKRIIQSREREMKDLKEKMNQvedevFEEFCREIGVrnirefeeekvkrqnEIAKKRLEFENQKTR 794
Cdd:COG4913 329 EAQIRGNGGDRLEQLEREIERLERELEERERRRAR-----LEALLAALGL---------------PLPASAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527317371 795 LGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKE----EQRHmKIIDETMAQLQDLKNQHL 856
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslERRK-SNIPARLLALRDALAEAL 453
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
369-488 |
1.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 369 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE---------LTE 439
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQK 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 527317371 440 EVEMAKRRIDEINKELNQVMEQLGDAR--IDRQESSRQQRKAEIMESIKRL 488
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEeeLAELEAELAELEAELEEKKAEL 147
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
771-1000 |
2.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 771 EEEKVKRQNEIAKKRLEFENQKTRLGIqLDFEKNQLK--EDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQL 848
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAE-LEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 849 QDLKNQHLAkksevndknhemeeirkkLGGANKEmtHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDI 928
Cdd:COG4913 326 DELEAQIRG------------------NGGDRLE--QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527317371 929 SQEegssqgedsvsGSQRISSIYAREALIEIDYGDLCEDLKDAQAE-EEIKQEMNTLQQ-KLN---EQQSVLQRIAA 1000
Cdd:COG4913 386 RAE-----------AAALLEALEEELEALEEALAEAEAALRDLRRElRELEAEIASLERrKSNipaRLLALRDALAE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
650-909 |
2.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 650 DKLKEKKERLTEELKEqmkAKRKEAELRQVQSQAHGLQMRLKysqsDLEQTKTRhlalnlqekskleselanfgprINDI 729
Cdd:PRK03918 193 ELIKEKEKELEEVLRE---INEISSELPELREELEKLEKEVK----ELEELKEE----------------------IEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 730 KRIIQSREREMKDLKEKMNQVEDEVFEEfcreigVRNIREFeEEKVKRQNEIAKKRLEFENQKtRLGIQLDFEKNQLKED 809
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEEL------KKEIEEL-EEKVKELKELKEKAEEYIKLS-EFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 810 QDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKsEVNDKNHEMEEIRKKLGGANKEmtHLQKE 889
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKE 392
|
250 260
....*....|....*....|
gi 527317371 890 VTAIETKLEQKRSDRHNLLQ 909
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITA 412
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-455 |
2.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 173 ERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMM 252
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 253 REQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERM 332
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 333 EEESQSQgrdltlEENQVKKYHRLKEEASKRAATLAQELEKfnrdqkaDQDRLDLEERKKVETEAKIKQKLREIEENQKR 412
Cdd:TIGR04523 562 EIDEKNK------EIEELKQTQKSLKKKQEEKQELIDQKEK-------EKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 527317371 413 IEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKEL 455
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
657-854 |
2.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 657 ERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSR 736
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 737 E--REMKDLKEKMNQVEDEVfEEFCREIgvRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQldfEKNQLKEDQDKVH 814
Cdd:COG4717 129 PlyQELEALEAELAELPERL-EELEERL--EELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 527317371 815 MWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQ 854
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-488 |
3.15e-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: 41.29 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 357 KEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 436
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 437 LT---------------------EEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKAEIMESIKRL 488
Cdd:COG4942 109 LLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRAdlAELAALRAELEAERAELEALLAEL 183
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-858 |
3.66e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 15 GKSNLMDAISFVLGEKTSNLR--VKTLRDLIHGAPVGKPA---------ANRAFVSMVYSEEGAEDRTFARVIVG--GSS 81
Cdd:TIGR00618 38 GKTTLLDAITYALYGKLPRRSevIRSLNSLYAAPSEAAFAelefslgtkIYRVHRTLRCTRSHRKTEQPEQLYLEqkKGR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 82 EYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFE----------------EISRSGELAQE 145
Cdd:TIGR00618 118 GRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMnlfpldqytqlalmefAKKKSLHGKAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 146 YDKRKKEMVK--AEEDTQFNYHRKKNIAAERK---EAKQEKEEADRYQRLKDEVVRAQVQLQ--LFKLYHNEVEIEKLNK 218
Cdd:TIGR00618 198 LLTLRSQLLTlcTPCMPDTYHERKQVLEKELKhlrEALQQTQQSHAYLTQKREAQEEQLKKQqlLKQLRARIEELRAQEA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 219 ELASKNKEIEKDKKrmdkvEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTShKIKKLEAAKKSLQ 298
Cdd:TIGR00618 278 VLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLH 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 299 NAQKHYK----KRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAatLAQELEKF 374
Cdd:TIGR00618 352 SQEIHIRdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD--LQGQLAHA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 375 NRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE---EQKKLEGELTEEVEMAKRRIDEI 451
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLqetRKKAVVLARLLELQEEPCPLCGS 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 452 NKELNQVMEQLGDARIDRQESSR-QQRKAEIMESIKRLYpgsvygrliDLCQPTQKKYQIAvtkvlgKNMDAIIVDSEKT 530
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSEEDVY---------HQLTSERKQRASL------KEQMQEIQQSFSI 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 531 GRDCIQYIKEQRgePETFLPLDylEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGG 610
Cdd:TIGR00618 575 LTQCDNRSKEDI--PNLQNITV--RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 611 ------HQRHKTVALDGTLFQKSgviSGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQA- 683
Cdd:TIGR00618 651 lqltltQERVREHALSIRVLPKE---LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAs 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 684 HGLQMRLKYSQSDLEQ----------TKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDE 753
Cdd:TIGR00618 728 SSLGSDLAAREDALNQslkelmhqarTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 754 VFEEfcreigvrnIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKK- 832
Cdd:TIGR00618 808 IGQE---------IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKl 878
|
890 900 910
....*....|....*....|....*....|....*..
gi 527317371 833 ----------EEQRHMKIIDETMAQ-LQDLKNQHLAK 858
Cdd:TIGR00618 879 nginqikiqfDGDALIKFLHEITLYaNVRLANQSEGR 915
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
686-899 |
4.82e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 686 LQMRLKYSQsdleqtKTRHLALNLQEKSKLESELANfgpriNDIKRIIQSREREMKDLKEKMNQVEDEVfeefcreigvR 765
Cdd:pfam07888 32 LQNRLEECL------QERAELLQAQEAANRQREKEK-----ERYKRDREQWERQRRELESRVAELKEEL----------R 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 766 NIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETM 845
Cdd:pfam07888 91 QSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 527317371 846 AQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQ 899
Cdd:pfam07888 171 AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
644-909 |
5.22e-03 |
|
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: 41.25 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 644 WDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAhgLQMRLKYSQSDLEQTKTRHLalnlQEKSKLESELANFG 723
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA--IKTSEEHYLKEVEDLKTELE----KEKLKNIELTAHCD 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 724 PRINDIKRIIQSREREMKDLKekmNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEK 803
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELK---KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 804 NQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEM 883
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKF 652
|
250 260
....*....|....*....|....*.
gi 527317371 884 THLqkeVTAIETKLEQKRSDRHNLLQ 909
Cdd:pfam05483 653 EEI---IDNYQKEIEDKKISEEKLLE 675
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
340-480 |
5.27e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.76 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 340 GRDLTLEENQVKKYHRLKEEASKRAATLAQELEKfnrdqkaDQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY 419
Cdd:pfam05262 191 EKGVNFRRDMTDLKERESQEDAKRAQQLKEELDK-------KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527317371 420 ITTskQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKAE 480
Cdd:pfam05262 264 ADT--SSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKEL 324
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
165-297 |
5.28e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 165 HRKKNIAAERKEAKQEKEEA-DRYQRLKDEVVRAQVQLQLFKLYHNEVE--IEKL---------NKELASKNKEIEKDKK 232
Cdd:COG1579 24 HRLKELPAELAELEDELAALeARLEAAKTELEDLEKEIKRLELEIEEVEarIKKYeeqlgnvrnNKEYEALQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527317371 233 RMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSL 297
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
205-487 |
6.62e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 205 KLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTS 284
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 285 HKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKE------ 358
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktteis 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 359 EASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKriEKLEEYITTSKQSLEEQKKLEGELT 438
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 527317371 439 EEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQ-QRKAEIMESIKR 487
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRElEEKQNEIEKLKK 377
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
291-488 |
6.98e-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: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 291 EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRdLTLEENQ----VKKYHRLKEEASKRAAT 366
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERelerIRQEERKRELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 367 LAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREiEENQKRIekleeyittsKQSLEEQKKLEGELTEEVEMAKR 446
Cdd:pfam17380 370 IAMEISRMRELERLQMERQQKNERVRQELEAARKVKILE-EERQRKI----------QQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 527317371 447 RIDEinkELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 488
Cdd:pfam17380 439 RLEE---ERAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
358-465 |
7.18e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 358 EEASKRAATLAQELEKFNRDQKADQDRLDLEERK---KVETEAKIKQKlREIEENQKRIEKL-EEYITTSKQSLEEQKKL 433
Cdd:cd22656 131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKAlkdLLTDEGGAIAR-KEIKDLQKELEKLnEEYAAKLKAKIDELKAL 209
|
90 100 110
....*....|....*....|....*....|....*
gi 527317371 434 EGELTEEVEMAKR---RIDEINKELNQVMEQLGDA 465
Cdd:cd22656 210 IADDEAKLAAALRliaDLTAADTDLDNLLALIGPA 244
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
191-445 |
7.58e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 191 KDEVVRAqvqLQLFKLYH-NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMR-EQQQIEKEIKEKDSE 268
Cdd:PRK05771 18 KDEVLEA---LHELGVVHiEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvSVKSLEELIKDVEEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 269 LNQKRPQyIKAKENtshKIKKLEAAKKSLQNAQKHYKKRKG-DMD---ELEKEMLSVEKARQEFEERMEEESQSQGRDLt 344
Cdd:PRK05771 95 LEKIEKE-IKELEE---EISELENEIKELEQEIERLEPWGNfDLDlslLLGFKYVSVFVGTVPEDKLEELKLESDVENV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 345 LEENQVKKYHR-----LKEEASKRAATLAqelekfnrdqKADQDRLDLEERKKVETEakIKQKLREIEENQKRIEKLEEY 419
Cdd:PRK05771 170 EYISTDKGYVYvvvvvLKELSDEVEEELK----------KLGFERLELEEEGTPSEL--IREIKEELEEIEKERESLLEE 237
|
250 260
....*....|....*....|....*..
gi 527317371 420 ITTSKQSLEE-QKKLEGELTEEVEMAK 445
Cdd:PRK05771 238 LKELAKKYLEeLLALYEYLEIELERAE 264
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
657-1156 |
8.71e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 657 ERLTEELKEqmkAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLAL--------NLQEKSKLESELANFGPRIND 728
Cdd:COG4717 74 KELEEELKE---AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllqllpLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 729 IKRIIQSREREMKDLKEKMNQVED--EVFEEFCREIGVRNIREFEEeKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQL 806
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAElqEELEELLEQLSLATEEELQD-LAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 807 KEDQDKVHMWEQTVKKDENEI----------------------------------------EKLKKEEQRHMKIIDETma 846
Cdd:COG4717 230 EQLENELEAAALEERLKEARLllliaaallallglggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEEL-- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 847 qlqdlknQHLAKKSEVNDKnhEMEEIRKKLG----GANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSK 922
Cdd:COG4717 308 -------QALPALEELEEE--ELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 923 GTMDDISQ-EEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAP 1001
Cdd:COG4717 379 AGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1002 N------------MKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNAcfesvatNIDEIYKALSRN 1069
Cdd:COG4717 459 EaeleqleedgelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLE-------RASEYFSRLTDG 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1070 SSAQAFLgpenPEEPYLDGINYNCvapgkRFRPMDNLSGGEKTVAALALLFA-IHSYKPAPF-FVLDEIDAALDNTNIGK 1147
Cdd:COG4717 532 RYRLIRI----DEDLSLKVDTEDG-----RTRPVEELSRGTREQLYLALRLAlAELLAGEPLpLILDDAFVNFDDERLRA 602
|
....*....
gi 527317371 1148 VANYIKEQS 1156
Cdd:COG4717 603 ALELLAELA 611
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
646-901 |
9.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 646 EKAVDKLKEKKERLTE----ELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQS------DLEQTKTRHLALN------L 709
Cdd:PRK03918 227 EKEVKELEELKEEIEElekeLESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSefyeeyL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 710 QEKSKLESELANFGPRINDIKRIIQ---SREREMKDLKEKMNQVEDEVfeefcreigvrnirEFEEEKVKRQNEIAKKRL 786
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKeleEKEERLEELKKKLKELEKRL--------------EELEERHELYEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 787 EFENQKTRLGiqlDFEKNQLKEDQDKVhmwEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLA--------- 857
Cdd:PRK03918 373 ELERLKKRLT---GLTPEKLEKELEEL---EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelt 446
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 527317371 858 ---KKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKR 901
Cdd:PRK03918 447 eehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1101-1176 |
9.34e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527317371 1101 RPMDNLSGGEKTVAALALLFAIHSY------KPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVIS----LKEE 1170
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALALSEVlqnrggARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVIShveeLKER 198
|
....*.
gi 527317371 1171 FYTKAE 1176
Cdd:cd03279 199 IPQRLE 204
|
|
|