|
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 ... |
3-1210 |
0e+00 |
|
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: 583.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTS-NLRVKTLRDLIHgaPVGKPAANRAFVS 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 82 MVYSEEGA-------EDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTAL 154
Cdd:pfam02463 79 ITFDNEDHelpidkeEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEA 314
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 315 AKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELE 394
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 395 KFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEIN 474
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 475 KELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGR 554
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 555 DCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEpphikkalqyacgnalvcdnvedarriafgghq 634
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL--------------------------------- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 635 rhktvaldgtlfqksgvisggASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKY 714
Cdd:pfam02463 606 ---------------------AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 715 SQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEE 794
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 795 EKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLK 874
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 875 NQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEE 954
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 955 GSSQGEESVSGSQRTSSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESV 1034
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1035 RDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYN 1114
Cdd:pfam02463 985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIS 1064
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1115 CVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFY 1194
Cdd:pfam02463 1065 ARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSK-NAQFIVISLREEML 1143
|
1210
....*....|....*.
gi 258613892 1195 TKAESLIGVYPEQGDC 1210
Cdd:pfam02463 1144 EKADKLVGVTMVENGV 1159
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1203 |
7.84e-98 |
|
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: 338.58 E-value: 7.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSN-LRVKTLRDLIHGAPVGKPAaNRAFVS 81
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQSG-NEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 82 MVYSEEGA----EDRTFARVIV---GGSSEYKINNKVVQLHEYSEELEKLGILIKARNFlVFQGAVESIAMKNPKERTAL 154
Cdd:TIGR02169 80 VTFKNDDGkfpdELEVVRRLKVtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMR--------EQQQIEKEIKEKDSELNQKRPQyIKAKEnts 306
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKIGELEAEIASLERS-IAEKE--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 307 hkiKKLEAAKKSLQNAQKHYKKRKGDMDELEKEmLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHR-LKEEASKR 385
Cdd:TIGR02169 315 ---RELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKDY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 386 AATLAQ---ELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:TIGR02169 391 REKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 463 VEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQpTQKKYQIAVTKVLGKNM 542
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS-VGERYATAIEVAAGNRL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 543 DAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGA-KLVIDVIRYEPpHIKKALQYACGNALVCDN 621
Cdd:TIGR02169 550 NNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGViGFAVDLVEFDP-KYEPAFKYVFGDTLVVED 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 622 VEDARRIAfgghQRHKTVALDGTLFQKSGVISGGAsdlkaKARRWDEKAVDKLKEKKERLTEELKEqmkAKRKEAELRQV 701
Cdd:TIGR02169 629 IEAARRLM----GKYRMVTLEGELFEKSGAMTGGS-----RAPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSE 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 702 QSQAHGLQMRLKYSQSDLEQtKTRHLALNLQEkskLESELANFGPRINDIKRIIQSREREMKDLKEKMnqvedevfeefc 781
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASR-KIGEIEKEIEQ---LEQEEEKLKERLEELEEDLSSLEQEIENVKSEL------------ 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 782 reigvrniREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHM-WEQTVKKDENEIEKLKKEEQRHM 860
Cdd:TIGR02169 761 --------KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEKEYLE 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 861 KIIDETMAQLQDLKNQhlakkseVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKl 940
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQ-------IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK- 904
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 941 plskgtmddisqeegssQGEESVSGSQRTSSIYAREALIEIDYGDLCEDLKDAQAEEEIKQE---MNTLQQKLNEQQSVL 1017
Cdd:TIGR02169 905 -----------------IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEI 967
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1018 QRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSrNSSAQAF 1097
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELI 1046
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1098 LgpENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQ 1177
Cdd:TIGR02169 1047 L--ENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREK 1124
|
1210 1220
....*....|....*....|....*.
gi 258613892 1178 STcNFQAIVISLKEEFYTKAESLIGV 1203
Cdd:TIGR02169 1125 AG-EAQFIVVSLRSPMIEYADRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-1220 |
5.70e-92 |
|
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: 322.01 E-value: 5.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFVS 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEqSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 82 MVYSEEgaeDRTFA-----------RVIVGGSSEYKINNKVVQLHEYSEELekLGILIKARNF-LVFQGAVESIAMKNPK 149
Cdd:TIGR02168 81 LVFDNS---DGLLPgadyseisitrRLYRDGESEYFINGQPCRLKDIQDLF--LDTGLGKRSYsIIEQGKISEIIEAKPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 150 ERTALFEE---ISRsgelaqeYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEA----KQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:TIGR02168 156 ERRAIFEEaagISK-------YKERRKETERKLERTRENLDRLEDILNELERQlkslERQAEKAERYKELKAELRELELA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAK 302
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 303 ENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKarqefeermeeesqsqgrDLTLEENQVKKYHRLKEEA 382
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE------------------ELESLEAELEELEAELEEL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 383 SKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSK-----QSLEEQKKLEG 457
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 458 ELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQES--------SRQQRKAEIMESIK-----RLYPGSVYGRLIDLCQ 524
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLqarldsleRLQENLEGFSEGVKallknQSGLSGILGVLSELIS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 525 pTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLE----VKPTDEKLRELKGAKLVIDVIRY 600
Cdd:TIGR02168 531 -VDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgteiQGNDREILKNIEGFLGVAKDLVK 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 601 EPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAK--ARRwdeKAVDKLKEKK 678
Cdd:TIGR02168 610 FDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSilERR---REIEELEEKI 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 679 ERLTEELKE-QMKAKRKEAELRQVQSQAHGLQMRLKYSQsdleqtktrhlalnlQEKSKLESELANFGPRINDIKRIIQS 757
Cdd:TIGR02168 687 EELEEKIAElEKALAELRKELEELEEELEQLRKELEELS---------------RQISALRKDLARLEAEVEQLEERIAQ 751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 758 REREMKDLKEKMNQVEDEVFEEFcreigvRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQldfeKNQLKEDQDKVHM 837
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAE------EELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAAN 821
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 838 WEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKnqhlakkSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIET 917
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 918 KLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEESvsgsqrtssiYAREALIEiDYGDLCEDLkdAQAEE 997
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID----------NLQERLSE-EYSLTLEEA--EALEN 961
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 998 EIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESV 1077
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQV 1041
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1078 ATNIDEIYKALSRNSSAQ-AFLGPENPEEPyldGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLD 1156
Cdd:TIGR02168 1042 NENFQRVFPKLFGGGEAElRLTDPEDLLEA---GIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILD 1118
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 1157 EIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTKAESLIGV-YPEQGdcvISKVLTFDL 1220
Cdd:TIGR02168 1119 EVDAPLDDANVERFANLLKEFSK-NTQFIVITHNKGTMEVADQLYGVtMQEKG---VSKIVSVDL 1179
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
4-148 |
8.54e-85 |
|
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: 275.99 E-value: 8.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMV 83
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 84 YSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNP 148
Cdd:cd03275 81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1117-1220 |
8.15e-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: 222.83 E-value: 8.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1117 APGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTK 1196
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFSK 224
|
90 100
....*....|....*....|....
gi 258613892 1197 AESLIGVYPEQgDCVISKVLTFDL 1220
Cdd:cd03275 225 ADALVGVYRDQ-ECNSSKVLTLDL 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-771 |
5.69e-59 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 220.96 E-value: 5.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKGRQIIgPFQR-FTAIIGPNGSGKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFV 80
Cdd:COG1196 2 RLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 81 SMVYS-EEGAEDRTFARVIV------GGSSEYKINNKVVQLHEYSEELEKLGIliKARNF-LVFQGAVESIAMKNPKERT 152
Cdd:COG1196 81 SLTFDnSDGTLPIDYDEVTItrrlyrSGESEYYINGKPCRLKDIQDLFLDTGL--GPESYsIIGQGMIDRIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 153 ALFEE---ISRsgelaqeYDKRKKEmvkAE---EDTQFNYHRKKNIAAE----RKEAKQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:COG1196 159 AIIEEaagISK-------YKERKEE---AErklEATEENLERLEDILGElerqLEPLERQAEKAERYRELKEELKELEAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAK 302
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 303 ENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEA 382
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 383 SKRAATLAQELEKFNRDQKADQDRLDLEERkkveteakikqKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLER-----------LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 463 VEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVY-----------GRLIDLCQPTQKKYQ 531
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaalllaglrglAGAVAVLIGVEAAYE 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 532 IAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRE----LKGAKLVIDVIRYEPPHIKK 607
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgaiGAAVDLVASDLREADARYYV 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 608 ALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKE 687
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL---EAEAELEELAERLAEEELE 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 688 QMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKE 767
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 258613892 768 KMNQ 771
Cdd:COG1196 775 EIEA 778
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
513-628 |
3.27e-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: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 513 GSVYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVK-PTDEKLRELK-- 589
Cdd:smart00968 1 PGVLGRVADLISV-DPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRsPAGSKLREALlp 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 258613892 590 ---GAKLVIDVIRYePPHIKKALQYACGNALVCDNVEDARRI 628
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 ... |
1117-1203 |
1.41e-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: 116.80 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1117 APGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTK 1196
Cdd:cd03278 103 APGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSK-ETQFIVITHRKGTMEA 181
|
....*..
gi 258613892 1197 AESLIGV 1203
Cdd:cd03278 182 ADRLYGV 188
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1118-1204 |
4.64e-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: 4.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1118 PGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQsTCNFQAIVISLKEEFYTKA 1197
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKER-TKNAQFIVISLRNNMFELA 196
|
....*..
gi 258613892 1198 ESLIGVY 1204
Cdd:cd03274 197 DRLVGIY 203
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
515-629 |
8.00e-28 |
|
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: 108.89 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 515 VYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLV 594
Cdd:pfam06470 4 VLGRLADLIEV-DEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGAGPL 82
|
90 100 110
....*....|....*....|....*....|....*
gi 258613892 595 IDVIRYEPPhIKKALQYACGNALVCDNVEDARRIA 629
Cdd:pfam06470 83 LDLVEYDDE-YRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1128-1208 |
1.63e-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: 104.70 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1128 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQ 1207
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVLFVH 174
|
.
gi 258613892 1208 G 1208
Cdd:cd03239 175 G 175
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-145 |
3.97e-25 |
|
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: 104.69 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKGRQIIGPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPvGKPAANRAFVS 81
Cdd:cd03274 2 IITKLVLENFKSYAGEQVIGPFhKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSA-GHPNLDSCSVE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258613892 82 MvyseegaedrTFARVIVggsseykinnkvvqlheySEELEKLGILIKARNFLVFQGAVESIAM 145
Cdd:cd03274 81 V----------HFQEIID------------------KPLLKSKGIDLDHNRFLILQGEVEQIAQ 116
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-100 |
4.23e-24 |
|
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: 101.00 E-value: 4.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 4 LKLIEIENFKSYKGRQIIgPFQR-FTAIIGPNGSGKSNLMDAISFVLGEKTS-NLRVKTLRDLIHGAPVGKPAANRAFVS 81
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPgLTAIVGPNGSGKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSETRKPANFAEVT 79
|
90
....*....|....*....
gi 258613892 82 MVYSEegaEDRTFArvIVG 100
Cdd:cd03278 80 LTFDN---SDGRYS--IIS 93
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
3-140 |
1.75e-23 |
|
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: 101.22 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKGRQIIGPFQR-FTAIIGPNGSGKSNLMDAISFVLG-EKTSNLRVKTLRDLIHGApvGKPAANRAFV 80
Cdd:cd03273 2 HIKEIILDGFKSYATRTVISGFDPqFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYKR--GQAGITKASV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258613892 81 SMVY-------SEEGAEDR---TFAR-VIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAV 140
Cdd:cd03273 80 TIVFdnsdksqSPIGFENYpeiTVTRqIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
4-84 |
4.05e-23 |
|
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: 97.76 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGApvGKPAANRAFVSMV 83
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGG--VKAGINSASVEIT 78
|
.
gi 258613892 84 Y 84
Cdd:cd03239 79 F 79
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1128-1208 |
1.06e-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: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1128 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQ 1207
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKVI 157
|
.
gi 258613892 1208 G 1208
Cdd:cd03227 158 T 158
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
4-145 |
4.93e-16 |
|
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: 79.23 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 4 LKLIEIENFKSYKGRQIIGPFQ-RFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIH-GApvgKPAANRAFVS 81
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSpKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHeGS---GPSVMSAYVE 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 82 MVY--SEE----GAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAM 145
Cdd:cd03272 78 IIFdnSDNrfpiDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTN 147
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1128-1213 |
6.29e-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: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1128 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALD--NT-NIGKVanyIKEQSTcNFQAIVISLKEEFYTKAESLIGVY 1204
Cdd:cd03273 167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDlsHTqNIGRM---IKTHFK-GSQFIVVSLKEGMFNNANVLFRTR 242
|
....*....
gi 258613892 1205 PEQGDCVIS 1213
Cdd:cd03273 243 FVDGTSTVT 251
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1125-1203 |
2.50e-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: 76.92 E-value: 2.50e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613892 1125 MDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTKAESLIGV 1203
Cdd:cd03272 156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSD-GAQFITTTFRPELLEVADKFYGV 233
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
7-84 |
8.39e-13 |
|
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: 67.38 E-value: 8.39e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613892 7 IEIENFKSYKGRQIIGPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTlrdlihgapVGKPAANRAFVSMVY 84
Cdd:cd03227 2 IVLGRFPSYFVPNDVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS---------GVKAGCIVAAVSAEL 71
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-127 |
5.95e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 66.19 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNlRVKTLRDLIHgapvgkPAANRAFVSMV 83
Cdd:COG0419 2 LLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLIN------VGSEEASVELE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 258613892 84 YSEEGAEDR------TFARVIVGGSSE-YKINNKVVQLHEYSEELEKLGIL 127
Cdd:COG0419 75 FEHGGKRYRierrqgEFAEFLEAKPSErKEALKRLLGLEIYEELKERLKEL 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-509 |
1.82e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 156 EEISRSGELAQ-EYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:PTZ00121 1339 EEAKKAAEAAKaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE---------NT 305
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkaeeakKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 306 SHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKR 385
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 386 AATLAQELEKFNRDQKADQDRLDLEERK------KVETEAKIK-QKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 458
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeeaKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 258613892 459 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-509 |
2.07e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 156 EEISRSGELAQEYDKRK-KEMVKAEEDTQFNYHRKKniAAERKEAKQEKEEADRYQRLKDEVVR-AQVQLQLFKLYHNEV 233
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKaDEAKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKkAEEAKKAAEAAKAEA 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 234 EIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE--NTSHKIKK 311
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEakKKAEEKKK 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 312 LEAAKKSLQNAQK--HYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYH---RLKEEASKRA 386
Cdd:PTZ00121 1433 ADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeaKKAAEAKKKA 1512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 387 ATL--------AQELEKFNRDQKADQDR-----------LDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY------ 441
Cdd:PTZ00121 1513 DEAkkaeeakkADEAKKAEEAKKADEAKkaeekkkadelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeea 1592
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258613892 442 -ITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK--ELNQVMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1593 rIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKaeEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-508 |
5.24e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 144 AMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNiAAERKEAKQEKEEADRYQRLKDEVVRAQvql 223
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKAD--- 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 224 QLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE 303
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 304 -------NTSHKIKKLEAAKKSlQNAQKHYKKRKGD----MDELEK--EMLSVEKARQEFEERMEEESQSQGRDlTLEEN 370
Cdd:PTZ00121 1515 akkaeeaKKADEAKKAEEAKKA-DEAKKAEEKKKADelkkAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAK-KAEEA 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 371 QVKKYHRLKEEASKRAATLAQELEKfnRDQKADQDRLDLEERKKVE----TEAKIKQKLREI----EENQKRIEKLEEYI 442
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEqlkkKEAEEKKKAEELkkaeEENKIKAAEEAKKA 1670
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258613892 443 TTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKelnqvMEQLGDARIDRQESSRQQRKAEIMESIK 508
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-505 |
5.90e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 144 AMKNPKERTALFEEISRSGELAQEYDKRKKemvKAEEDTQFNYHRKKNIAAER-KEAKQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKK---KAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKE---KDSELNQKRPQYI 299
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 300 KAKE-NTSHKIKKLEAAKKSLQNAQKHYKK----RKGDMDELEKEM--LSVEKARQEFEERMEEESQSQGRDLTLEENQV 372
Cdd:PTZ00121 1553 KAEElKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 373 KKYHRLK--EEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE 450
Cdd:PTZ00121 1633 KKVEQLKkkEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 451 EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIME 505
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-48 |
1.02e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 64.95 E-value: 1.02e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 258613892 4 LKLIEIENFKSYkgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFV 48
Cdd:COG4637 2 ITRIRIKNFKSL--RDLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-775 |
1.89e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 156 EEISRSGELAQEYDKRKKEMV-------KAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEvvRAQVQLQLFKL 228
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAArkaeeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN--EEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 229 YHNEVEIEKLNKELASKNKEIEK--DKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQyikAKENTS 306
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA---AKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 307 HKIKKLEAAKKSLQNAQKHYK--KRKGDMDELEKEmlsvekarqefeermeeESQSQGRDLTLEENQVKKYHRLKEEASK 384
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKE-----------------EAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 385 RAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE-----------EQK 453
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEakkadeakkkaEEA 1482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 454 KLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIA 533
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 534 VTKVLGKNMDAiiVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYAC 613
Cdd:PTZ00121 1563 KKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 614 GNALVCDNVEDARRIAFGGHQRHKTVAldgtlfQKSGVISGGASDLKaKARRWDEKAVDKLKEKKE--RLTEELKEQMKA 691
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEA------KKAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEeaKKAEELKKKEAE 1713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 692 KRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQ 771
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
....
gi 258613892 772 VEDE 775
Cdd:PTZ00121 1794 MEVD 1797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-854 |
1.01e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELnqkrPQYIKAKENTSHKIKKLEAA 315
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL----PELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKaRQEFEERMEEESQSQGRDLTLEENQVKKYHRLKE---EASKRAATLAQE 392
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEE-RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 393 LEKFNRDQKADQDRLDLEERKKVETEaKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELT-EEVEMAKRRID 471
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 472 EINKELNQVMEQLGD--ARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIdlcqptqkkyqiavtkvlgknmdaiivDS 549
Cdd:PRK03918 395 ELEKAKEEIEEEISKitARIGELKKEIKELKKAIEELKKAKGKCPVCGREL---------------------------TE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 550 EKTGRDCIQYIKEQRGEPEtflpldylEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYA-----CGNALVCDNVED 624
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEK--------ELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkeLEEKLKKYNLEE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 625 ARRIAfgghqrHKTVALDGTLFQKSGVISGGASDLKA-----KARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELR 699
Cdd:PRK03918 520 LEKKA------EEYEKLKEKLIKLKGEIKSLKKELEKleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 700 -QVQSQAHGLQMRLKYSQSDLEQTktrhlalnLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQvedevfE 778
Cdd:PRK03918 594 lKELEPFYNEYLELKDAEKELERE--------EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE------E 659
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258613892 779 EFcreigvrniREFEEEKVKRQNEIAKKRLEFEnqktrlgiQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKK 854
Cdd:PRK03918 660 EY---------EELREEYLELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-183 |
3.70e-09 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 57.89 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 7 IEIENFKSYKGrQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAP-VGKPAANRAFVSMVYS 85
Cdd:pfam13476 1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIrIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 86 EEGAE-----DRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVF---QGAVESIAMKNPKER-TALFE 156
Cdd:pfam13476 80 NNDGRytyaiERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVflgQEREEEFERKEKKERlEELEK 159
|
170 180
....*....|....*....|....*..
gi 258613892 157 EISRSGELAQEYDKRKKEMVKAEEDTQ 183
Cdd:pfam13476 160 ALEEKEDEKKLLEKLLQLKEKKKELEE 186
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-113 |
4.94e-09 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 59.78 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGekTSNLRVKTLRDLI-HGAPvgkpaanRAFVS 81
Cdd:COG1195 1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYLLAT--GRSFRTARDAELIrFGAD-------GFRVR 70
|
90 100 110
....*....|....*....|....*....|..
gi 258613892 82 MVYSEEGAEDRTFARVIVGGSSEYKINNKVVQ 113
Cdd:COG1195 71 AEVERDGREVRLGLGLSRGGKKRVRINGKPVR 102
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7-880 |
5.16e-09 |
|
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: 60.75 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 7 IEIENFKSYKGRQII--GPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLR--VKTLRDLIHGAPVGKPA-------- 74
Cdd:TIGR00618 6 LTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSevIRSLNSLYAAPSEAAFAelefslgt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 75 -ANRAFVSMVYSEEGAEDRTFARVIVG--GSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKER 151
Cdd:TIGR00618 86 kIYRVHRTLRCTRSHRKTEQPEQLYLEqkKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 152 TALFE----------------EISRSGELAQEYDKRKKEMVK--AEEDTQFNYHRKKNIAAERK---EAKQEKEEADRYQ 210
Cdd:TIGR00618 166 KELLMnlfpldqytqlalmefAKKKSLHGKAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKhlrEALQQTQQSHAYL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 211 RLKDEVVRAQVQLQ--LFKLYHNEVEIEKLNKELASKNKEIEKDKKrmdkvEDELKEKKKELGKMMREQQQIEKEIKEKD 288
Cdd:TIGR00618 246 TQKREAQEEQLKKQqlLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQSKM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 289 SELNQKRPQYIKAKENTShKIKKLEAAKKSLQNAQKHYK----KRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRD 364
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLHSQEIHIRdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 365 LTLEENQVKKYHRLKEEASKRAatLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITT 444
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRD--LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 445 SKQSLE---EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSR-QQRKAEIMESIKRLYpgsvygrli 520
Cdd:TIGR00618 478 KEQIHLqetRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSEEDVY--------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 521 DLCQPTQKKYQIAvtkvlgKNMDAIIVDSEKTGRDCIQYIKEQRgePETFLPLDylEVKPTDEKLRELKGAKLVIDVIRY 600
Cdd:TIGR00618 549 HQLTSERKQRASL------KEQMQEIQQSFSILTQCDNRSKEDI--PNLQNITV--RLQDLTEKLSEAEDMLACEQHALL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 601 EPPHIKKALQYACGNALVCDNVEDARRIAFGG------HQRHKTVALDGTLFQKSgviSGGASDLKAKARRWDEKAVDKL 674
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQQCSQELALKLTALHAlqltltQERVREHALSIRVLPKE---LLASRQLALQKMQSEKEQLTYW 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 675 KEKKERLTEELKEQMKAKRKEAELRQVQSQA-HGLQMRLKYSQSDLEQ----------TKTRHLALNLQEKSKLESELAN 743
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENAsSSLGSDLAAREDALNQslkelmhqarTVLKARTEAHFNNNEEVTAALQ 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 744 FGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEfcreigvrnIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDF 823
Cdd:TIGR00618 776 TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE---------IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613892 824 EKNQLKEDQDKVHMWEQTVKKDENEIEKLKK-----------EEQRHMKIIDETMAQ-LQDLKNQHLAK 880
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKlnginqikiqfDGDALIKFLHEITLYaNVRLANQSEGR 915
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-509 |
8.07e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 145 MKNPKERTALFEEISRSGELAQEYD--KRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQrlKDEVVRAQVQ 222
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADE 1526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 223 LQLFKLYHNEVEIEKLN-KELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKrpQYIKA 301
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 302 KENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERmeeesqsqgrdltlEENQVKKYH-RLKE 380
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE--------------EENKIKAAEeAKKA 1670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 381 EASKRAATLAQELEKFNRdQKADQDRLDLEERKKVEteakikQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELT 460
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEK-KAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 258613892 461 EEVEMAKRRIDEINKelnqvMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
309-869 |
1.26e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 309 IKKLEAAKKSLQNAQKHYKKRKGDMDELE-----KEMLSVEKARQEFeermeeesQSQGRDLTLEENQVKKYHRLKEEAS 383
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAeleylRAALRLWFAQRRL--------ELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 384 KRAATLAQELEKFNRD-QKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLegeltee 462
Cdd:COG4913 316 ARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE------- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 463 vemAKRRIDEINKELNQVMEQLGDARIDRQESSRQQR--KAEI--MESIKRLYPGSVY--------------------GR 518
Cdd:COG4913 389 ---AAALLEALEEELEALEEALAEAEAALRDLRRELRelEAEIasLERRKSNIPARLLalrdalaealgldeaelpfvGE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 519 LIDLcQPTQKKYQIAVTKVLGKNMDAIIVDsEKTGRDCIQYIKEQRGEPEtflpLDYLEVKPTDEKLRELKG------AK 592
Cdd:COG4913 466 LIEV-RPEEERWRGAIERVLGGFALTLLVP-PEHYAAALRWVNRLHLRGR----LVYERVRTGLPDPERPRLdpdslaGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 593 LVIDVIRYEP---PHIKKALQYACgnalvCDNVEDARRiafggHQRHKTVA----LDGTLFQKsgvisggasDLKAKARR 665
Cdd:COG4913 540 LDFKPHPFRAwleAELGRRFDYVC-----VDSPEELRR-----HPRAITRAgqvkGNGTRHEK---------DDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 666 -----WD-EKAVDKLKEKKERLTEELKE-QMKAKRKEAELRQVQSQAHGLQMRLKYS--QSDLEQTKTRHLALNlQEKSK 736
Cdd:COG4913 601 ryvlgFDnRAKLAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELE-AELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 737 LE---SELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEvfeefcreigvrnIREFEEEKvkrqnEIAKKRLEFENQ 813
Cdd:COG4913 680 LDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-------------LEQAEEEL-----DELQDRLEAAED 741
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 258613892 814 KTRLGIQLDFEKNQLKEDQDKVhmwEQTVKKD-ENEIEKLKKEEQRHMKIIDETMAQ 869
Cdd:COG4913 742 LARLELRALLEERFAAALGDAV---ERELRENlEERIDALRARLNRAEEELERAMRA 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-1035 |
1.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 659 LKAKARRwdEKAVDKLKEKKERLT------EELKEQMKAKRKEAElrqVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQ 732
Cdd:COG1196 168 SKYKERK--EEAERKLEATEENLErledilGELERQLEPLERQAE---KAERYRELKEELKELEAELLLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 733 EKSKLESELANfgpRINDIKRIIQSREREMKDLKEKMNQVEDEVfeefcreigvrnirefeEEKVKRQNEIAKKRLEFEN 812
Cdd:COG1196 243 ELEAELEELEA---ELEELEAELAELEAELEELRLELEELELEL-----------------EEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 813 QKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEME 892
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 893 EIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEESVSGSQRTSSI 972
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258613892 973 YAREALieidygdlcedlkdAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVR 1035
Cdd:COG1196 463 ELLAEL--------------LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
195-508 |
2.70e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.21 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 195 ERKEAKQEKEEADRYQRLKDEVVRAqvqlqlfklyhnevEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMM 274
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQ--------------EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 275 REQQQIEK-EIKEKDSELNQKRPQYIKAKENTSHKIKKL--EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFE 351
Cdd:pfam17380 345 ERERELERiRQEERKRELERIRQEEIAMEISRMRELERLqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 352 ERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLaQELEKFNRDQKADQDRLDLEERKKVETEAK----IKQKLRE 427
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 428 -----IEENQKR--IEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRideinkelnQVMEQLGDARIDRQESSRQQRK 500
Cdd:pfam17380 504 rkqamIEEERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR---------RIQEQMRKATEERSRLEAMERE 574
|
....*...
gi 258613892 501 AEIMESIK 508
Cdd:pfam17380 575 REMMRQIV 582
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-508 |
5.01e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE- 234
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKr 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEkkkelgkmMREQQQIEKEIKEKDSELNQKRPQYIKAK----ENTSHKIK 310
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKELEEKLKKYNLEELEKKaeeyEKLKEKLI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 311 KLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLkeeaskraatlA 390
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE-----------Y 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 391 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKL------EEYITTSKQSLEEQKKLEGeLTEEVE 464
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseEEYEELREEYLELSRELAG-LRAELE 683
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 258613892 465 MAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIK 508
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELR 727
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-55 |
5.83e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 56.16 E-value: 5.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 258613892 3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSN 55
Cdd:COG3593 2 KLEKIKIKNFRSIK-DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
287-923 |
7.54e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 287 KDSELNQKRPQyiKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEkEMLSVEKARQEFEERMEEESQSQGRDLT 366
Cdd:PTZ00121 1077 KDFDFDAKEDN--RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 367 LEENQVKKYHRLKEEASKraatlAQELEKFNRDQKADQDRlDLEERKKVETEAKIKQKLREieENQKRIEKLEEYitTSK 446
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARK-----AEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKA--EEERKAEEARKA--EDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 447 QSLEEQKKLEgELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRlypgSVYGRLIDLCQPT 526
Cdd:PTZ00121 1224 KKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK----AEEKKKADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 527 QKKYQIAVTKVLGKNMDAiIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIK 606
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 607 KALQYACGNALVCDNVEDARRIAFGGHQRHKTValdgtlfQKSGVISGGASDLKAKARrwDEKAVDKLKEKKE--RLTEE 684
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADEL-------KKAAAAKKKADEAKKKAE--EKKKADEAKKKAEeaKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 685 LKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSRE-REMK 763
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKaDEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 764 DLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQL-DFEKNQLKE-----DQDKVHM 837
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEvmklyEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 838 WEQTVKKDENEI--EKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDK------NHEMEEIRKKLGGANKEMTHLQ 909
Cdd:PTZ00121 1609 AEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKAEEDEK 1688
|
650
....*....|....
gi 258613892 910 KEVTAIETKLEQKR 923
Cdd:PTZ00121 1689 KAAEALKKEAEEAK 1702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
188-1041 |
8.70e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 188 RKKNIAAER-KEAKQEKEEADRYQRLKDEVVRaqvqlqlfklyhnEVEIEKLNKELASKNKEIEK--DKKRMDKVEDELK 264
Cdd:PTZ00121 1084 KEDNRADEAtEEAFGKAEEAKKTETGKAEEAR-------------KAEEAKKKAEDARKAEEARKaeDARKAEEARKAED 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 265 EKKKELGKMMREQQQIEKEIKEKDS---ELNQKRPQYIKAKE-NTSHKIKKLEAAKKSlQNAQKHYKKRKGDMDELEKEM 340
Cdd:PTZ00121 1151 AKRVEIARKAEDARKAEEARKAEDAkkaEAARKAEEVRKAEElRKAEDARKAEAARKA-EEERKAEEARKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 341 LSVEKARQEFEERMEEESQSQGRDL-TLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRlDLEERKKVETEA 419
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIrKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK-KAEEKKKADEAK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 420 KIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKlegelteEVEMAKRRIDEINKELNQVMEQlgdARIDRQESSRQQR 499
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK-------AAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKK 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 500 KAEIMEsikrlypgsvygrlidlcqptQKKYQIAVTKVLGKNmdaiiVDSEKTGRDCIQYIKEQRGEPEtflpldylEVK 579
Cdd:PTZ00121 1379 KADAAK---------------------KKAEEKKKADEAKKK-----AEEDKKKADELKKAAAAKKKAD--------EAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 580 PTDEKLRELKGAKLVIDVIRYEPPHIKKAlqyacgnalvcdnvEDARRIAFGGHQRHKTVALDGTlfQKSGVISGGASDL 659
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKA--------------EEAKKAEEAKKKAEEAKKADEA--KKKAEEAKKADEA 1488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 660 KAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLES 739
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 740 ELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEvfeefcREIGVRNIREFEEEKVK----RQNEIAKKRLEFENQKT 815
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE------KKMKAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKE 1642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 816 RLGIQlDFEKNQLKEDQDKVHMWEQTVKKDEN--EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNhEMEE 893
Cdd:PTZ00121 1643 AEEKK-KAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEE 1720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 894 IRKKLGGANKEMTHLQKEVTAIETKLEQKRSD---RHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEESVSGSQRTS 970
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258613892 971 S-IYAREALIEI--DYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQET 1041
Cdd:PTZ00121 1801 KdIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
7-49 |
1.80e-07 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 54.66 E-value: 1.80e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 258613892 7 IEIENFKSYKGRQII------GPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:COG1106 5 FSIENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFLR 53
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-65 |
1.91e-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: 52.99 E-value: 1.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258613892 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVL-GEKTSNLR-VKTLRDLI 65
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKgGAHDPKLI 64
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
3-137 |
2.02e-07 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 54.78 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFvLGeKTSNLRVKTLRDLI-HGAPvgkpaanRAFVS 81
Cdd:PRK00064 2 YLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-PGRSHRTARDKELIrFGAE-------AAVIH 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258613892 82 MVYSEEGAEDRTFARVIVGGSSEYKIN-NKVVQLHEYSEEL-------EKLGILIKA----RNFL---VFQ 137
Cdd:PRK00064 72 GRVEKGGRELPLGLEIDKKGGRKVRINgEPQRKLAELAGLLnvvlftpEDLRLVKGGpserRRFLdrlLFQ 142
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-477 |
2.09e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQlfklyhnevEI 235
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK---------KA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKEntSHKIKKLEAA 315
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEA 1667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARqefeermeeesqsqgrdltlEENQVKKYHRLKEEASKRAATLAQELEK 395
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE--------------------EAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 396 fnRDQKADQDRLDLEERKKVETEAKIKqklrEIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK 475
Cdd:PTZ00121 1728 --NKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
..
gi 258613892 476 EL 477
Cdd:PTZ00121 1802 DI 1803
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
4-505 |
2.11e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 4 LKLIEIENFKSYKGRQIIGPfQRFTAIIGPNGSGKSNLMDAISFVLgekTSNLRVKTLRDLIhgapvgKPAANRAFVSMV 83
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFD-TGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMI------KKGKNNLEVELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 84 YSEEGAEDRTFARVIVGG-----SSEYKINNKVVQ--LHEYSEELEKLGILIKARNFL----VFQGAVESIAMKNPKERT 152
Cdd:PRK01156 73 FRIGGHVYQIRRSIERRGkgsrrEAYIKKDGSIIAegFDDTTKYIEKNILGISKDVFLnsifVGQGEMDSLISGDPAQRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 153 ALFEEISRSGELAQEYDKRKKEMvkaeedtqfnyhrkKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLfKLYHNE 232
Cdd:PRK01156 153 KILDEILEINSLERNYDKLKDVI--------------DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEK-SHSITL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 233 VEIEKLNKELASKNKEIEKDKKRMDkvedelkekkkELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKL 312
Cdd:PRK01156 218 KEIERLSIEYNNAMDDYNNLKSALN-----------ELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKII 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 313 EAAKKSLQNAQKHYKKRKGDMDELeKEMLSVEKArqefeermeeesqsqgrdltleenQVKKYHRLKEEASKRAATLAQE 392
Cdd:PRK01156 287 NDPVYKNRNYINDYFKYKNDIENK-KQILSNIDA------------------------EINKYHAIIKKLSVLQKDYNDY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 393 LEKFNRDQKADQDRLDLEerkkvETEAKIKQKLREIEENQKRIEKLEeyittskqslEEQKKLEGELTEEVEMAKRRIDE 472
Cdd:PRK01156 342 IKKKSRYDDLNNQILELE-----GYEMDYNSYLKSIESLKKKIEEYS----------KNIERMSAFISEILKIQEIDPDA 406
|
490 500 510
....*....|....*....|....*....|...
gi 258613892 473 INKELNQVMEQLGDarIDRQESSRQQRKAEIME 505
Cdd:PRK01156 407 IKKELNEINVKLQD--ISSKVSSLNQRIRALRE 437
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-99 |
2.60e-07 |
|
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: 52.66 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1 MGFLKLiEIENFKSYKGRQII----GPFQRFTAIIGPNGSGKSNLMDAISFVL-GEKTSNLRVKTLRDLIHgapvgkPAA 75
Cdd:cd03279 1 MKPLKL-ELKNFGPFREEQVIdftgLDNNGLFLICGPTGAGKSTILDAITYALyGKTPRYGRQENLRSVFA------PGE 73
|
90 100 110
....*....|....*....|....*....|....
gi 258613892 76 NRAFVSMVYS----------EEGAEDRTFARVIV 99
Cdd:cd03279 74 DTAEVSFTFQlggkkyrverSRGLDYDQFTRIVL 107
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-510 |
2.83e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 4 LKLIEIENFKSYKGRQIigpfqRFTA----IIGPNGSGKSNLMDAISFVL-GEKTSNLRVKTLRDLIhgapvgKPAANRA 78
Cdd:PRK03918 3 IEELKIKNFRSHKSSVV-----EFDDginlIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFT------RIGGSGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 79 FVSMVYSEEGaEDRTFARVIVGGSSEYKINNKVVQLHEYSEEL-EKLGILIKARNFL----VFQGAVESIaMKNPKERTA 153
Cdd:PRK03918 72 EIELKFEKNG-RKYRIVRSFNRGESYLKYLDGSEVLEEGDSSVrEWVERLIPYHVFLnaiyIRQGEIDAI-LESDESREK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 154 LFEEISRSGELAQEYD---KRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRaQVQLQLFKLYH 230
Cdd:PRK03918 150 VVRQILGLDDYENAYKnlgEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP-ELREELEKLEK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 231 NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELkekkkelgkmmreqQQIEKEIKEKDSELNqkrpqyikakentshKIK 310
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKI--------------RELEERIEELKKEIE---------------ELE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 311 KLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKaRQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLA 390
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK-RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 391 QELEKFNrDQKADQDRLD-LEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRR 469
Cdd:PRK03918 359 ERHELYE-EAKAKKEELErLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 258613892 470 IDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:PRK03918 438 CPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-768 |
3.20e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 333 MDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRL---KEEASKRAATLAQELEKFNRD----QKADQD 405
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREEleklEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 406 RLDLEERKKVETE--------AKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEG--------ELTEEVEMAKRR 469
Cdd:COG4717 128 LPLYQELEALEAElaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 470 IDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGknMDAIIVds 549
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG--VLFLVL-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 550 ektGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYAcgnalvcDNVEDARRIA 629
Cdd:COG4717 284 ---GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL-------DRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 630 FGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAvDKLKEKKERLtEELKEQMKAKRKEAELRQVQSQAHGLQ 709
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEEL-EELEEQLEELLGELEELLEALDEEELE 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258613892 710 MRLKYSQSDLEQTKTRHLALnLQEKSKLESELANFGP--RINDIKRIIQSREREMKDLKEK 768
Cdd:COG4717 432 EELEELEEELEELEEELEEL-REELAELEAELEQLEEdgELAELLQELEELKAELRELAEE 491
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-65 |
6.13e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 52.31 E-value: 6.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258613892 3 FLKLIEIENFKSYKGRQI-IGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLI 65
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIdFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1122-1203 |
6.26e-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: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1122 FRPMDNLSGGEKTVAALALLFAIHSYKPA--PFFVLDEIDAALDNTNI-GKVANYIKEQ-STCNFQAIVISLKEEFYTKA 1197
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERkSQKNFQLIVITHDEELVDAA 189
|
....*.
gi 258613892 1198 ESLIGV 1203
Cdd:cd03240 190 DHIYRV 195
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-510 |
7.64e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 149 KERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNiaaERKEAKQEKEEA-DRYQRLKDEVVRAQVQLQLFK 227
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE---ELEELEEELEELeAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 228 LYHnevEIEKLNKELASKNKEIEKDKKRMDKVEDelkekkkelgkMMREQQQIEKEIKEKDSELNQ--------KRPQYI 299
Cdd:COG4717 130 LYQ---ELEALEAELAELPERLEELEERLEELRE-----------LEEELEELEAELAELQEELEElleqlslaTEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 300 KAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQS------------------- 360
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllslilti 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 361 -----------------QGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRL-----DLEERKKVETE 418
Cdd:COG4717 276 agvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 419 AKIKQKLREIEENQKRIEKL-EEYITTSKQSLE---EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQES 494
Cdd:COG4717 356 AEELEEELQLEELEQEIAALlAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE 435
|
410
....*....|....*.
gi 258613892 495 SRQQRKAEIMESIKRL 510
Cdd:COG4717 436 ELEEELEELEEELEEL 451
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
163-439 |
8.07e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 163 ELAQEYDKRKKeMVKAEEDTQFNYHRKKNIAAERKEAKQEKE-EADRYQRLKDEVVRAQVQLQLFKLYHNEV-EIEKLNK 240
Cdd:pfam17380 307 EKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERErELERIRQEERKRELERIRQEEIAMEISRMrELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 241 ELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEiKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKK--S 318
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE-QEEARQREVRRLEEERAREMERVRLEEQERQQQveR 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 319 LQNAQKHYKKRKGDMDELEKEMLSVEKAR-----QEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQ-- 391
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRrkileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERrk 544
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 258613892 392 ELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLE 439
Cdd:pfam17380 545 QQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
281-503 |
8.82e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 281 EKEIKEKDSELNQKRPQYIKAKENT--SHKIKKLEAAKKSLQNAQKhykkrkgdMDELEKEMLSVEKARQEFEERMEEES 358
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQ--------LVELSTEVQSLIREIKDAKEQDSPLE 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 359 QSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRL-DLEERKKVETEAKIKQKLREIEENQKRIEK 437
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIqDGKDDYLKQKETELNTVNAQLEECEKHQEK 995
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258613892 438 LEEYITTSKQSLEEQKKLEGELTEEVEMAKRR--IDEINKELNQVMEQLGDARIDRQESSRQQRKAEI 503
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENI 1063
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1119-1188 |
1.09e-06 |
|
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: 1.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258613892 1119 GKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNiGKVA--NYIKE-QSTCNFQAIVIS 1188
Cdd:cd03276 101 KAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN-RKIStdLLVKEaKKQPGRQFIFIT 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-476 |
1.52e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQ-EKEEADRYQRLKDEVVRAQVQlQLFKLYHNEVE 234
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQyiKAKENTSHKIKKLEA 314
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEALKKEAE 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 315 AKKSLQNAQKHYKKRKGDMDELEKEMlSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELE 394
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 395 KFNRD--QKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDE 472
Cdd:PTZ00121 1779 AVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNN 1858
|
....
gi 258613892 473 INKE 476
Cdd:PTZ00121 1859 ENGE 1862
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1128-1188 |
1.69e-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: 1.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258613892 1128 LSGGEKTVAALALLFAihsYKPaPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVIS 1188
Cdd:cd00267 81 LSGGQRQRVALARALL---LNP-DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVT 137
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
4-49 |
1.71e-06 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 46.44 E-value: 1.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 258613892 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:pfam13555 1 LTRLQLINWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-253 |
2.16e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 51.24 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 27 FTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPV--GKPAANRAFVSMVYSEEGAEDRtfarvivGGSSE 104
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGipSLLNGIDPKEPIEFEISEFLED-------GVRYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 105 YKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAmKNPKERTALFEEISRSGELAqEYDKRKKEMVKAEEDTQF 184
Cdd:pfam13304 74 YGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPP-EAEELRLGLDVEERIELSLS-ELSDLISGLLLLSIISPL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613892 185 NYHRKKNIAAeRKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDK 253
Cdd:pfam13304 152 SFLLLLDEGL-LLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRER 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-65 |
5.51e-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: 47.62 E-value: 5.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 8 EIENF-KSYKGRQIIGPFQ------RFTAIIGPNGSGKSNLMDAISFVL----------GEKTSNLRVKTLRDLI 65
Cdd:cd00267 1 EIENLsFRYGGRTALDNVSltlkagEIVALVGPNGSGKSTLLRAIAGLLkptsgeilidGKDIAKLPLEELRRRI 75
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-510 |
7.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 156 EEISRSGELAQEYDKRKKEMVKAEEdtqfnyhRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEI 235
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEE-------RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 236 EKLNKELAS---KNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKenTSHKIKKL 312
Cdd:PRK03918 387 EKLEKELEElekAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEE--YTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 313 EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEA---SKRAATL 389
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklKGEIKSL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 390 AQELEKFNrDQKADQDRLDLEERKKVETEAKIKQKLRE-----IEENQKRIEKLEEY------ITTSKQSLEEQKKLEGE 458
Cdd:PRK03918 545 KKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKELEPFyneyleLKDAEKELEREEKELKK 623
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 258613892 459 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
275-501 |
8.46e-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: 49.76 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 275 REQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEK---ARQEFE 351
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 352 ERMEEESQSQGRDLTLEenqvkkyHRLKEEASKRAATLAQELEKFNRDQKADQDRLdleerkkVETEAKIKQKLREIEEN 431
Cdd:COG4942 107 AELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258613892 432 QKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKA 501
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAERTP 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-926 |
1.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 141 ESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKdevvraq 220
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIAR------- 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 221 vqlqlfklyhnevEIEKLNKELASKNKEiekDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIK 300
Cdd:PTZ00121 1159 -------------KAEDARKAEEARKAE---DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 301 AKEntSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSqgrDLTLEENQVKKYHRLKE 380
Cdd:PTZ00121 1223 AKK--AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DELKKAEEKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 381 EASKRAATLAQEleKFNRDQKADQDRLDLEERKKVETEAKIKQ---------KLREIEENQKRIEKLEEYITTSKQSLEE 451
Cdd:PTZ00121 1298 AEEKKKADEAKK--KAEEAKKADEAKKKAEEAKKKADAAKKKAeeakkaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 452 QKKLEGELTEEVEmAKRRIDEINK---ELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDlcqPTQK 528
Cdd:PTZ00121 1376 AKKKADAAKKKAE-EKKKADEAKKkaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD---EAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 529 KyqiavtkvlgknmdaiiVDSEKTGRDCIQYIKEQRGEPEtfLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKA 608
Cdd:PTZ00121 1452 K-----------------AEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 609 lqyacgnalvcDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKEQ 688
Cdd:PTZ00121 1513 -----------DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK---KAEEKKKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 689 mkAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHlalnlQEKSKLESELANfgpRINDIKRIIQSREREMKDLKEK 768
Cdd:PTZ00121 1579 --ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKK 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 769 MNQVEDEvfEEFCREIGVRNIREFEEEkvKRQNEIAKKRLEFENQKtrlgiqldfeKNQLKEDQDKVHMWEQTVKKDENE 848
Cdd:PTZ00121 1649 AEELKKA--EEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKA----------AEALKKEAEEAKKAEELKKKEAEE 1714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 849 I---EKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKN---HEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQK 922
Cdd:PTZ00121 1715 KkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....
gi 258613892 923 RSDR 926
Cdd:PTZ00121 1795 EVDK 1798
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
5-479 |
1.60e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 49.35 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 5 KLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRdlIHGAPVGKPAA----NRAFV 80
Cdd:COG4694 4 KIKKLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFE--IEAGGSAPNPSvrvfNRDFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 81 SM-VYSEEGAEDrtfaRVIVGGSS---EYKINNKVVQLHEYSEELEKLGILIKARNflvfqGAVESIAMKNPKERTALFE 156
Cdd:COG4694 82 EEnLRSGEEIKG----IFTLGEENielEEEIEELEKEIEDLKKELDKLEKELKEAK-----KALEKLLEDLAKSIKDDLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 157 EISRSGElaQEYDKRK-KEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADrYQRLKDEVVRAQVQLQlfklyhnEVEI 235
Cdd:COG4694 153 KLFASSG--RNYRKANlEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITP-LPDLKALLSEAETLLE-------KSAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 236 EKLNKELASKNKEIEKD------KKRMDKVEdelkekkkelgkmmRE-----QQQIEKEIKEK-DSELNQkrpQYIKAKE 303
Cdd:COG4694 223 SSAIEELAALIQNPGNSdwveqgLAYHKEEE--------------DDtcpfcQQELAAERIEAlEAYFDD---EYEKLLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 304 NTSHKIKKLEAAKKSL-----QNAQKHYKKRKGDMDELEKEMLS-VEKARQEFEERMEEESQSQGRDLTLEENQVKKyhr 377
Cdd:COG4694 286 ALKDLLEELESAINALsalllEILRTLLPSAKEDLKAALEALNAlLETLLAALEEKIANPSTSIDLDDQELLDELND--- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 378 LKEEASKRAATLAQELEKFnrDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEG 457
Cdd:COG4694 363 LIAALNALIEEHNAKIANL--KAEKEEARKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEA 440
|
490 500
....*....|....*....|..
gi 258613892 458 ELTEEVEMAkrriDEINKELNQ 479
Cdd:COG4694 441 ELSSVDEAA----DEINEELKA 458
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
863-1058 |
1.68e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 863 IDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDiklpl 942
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 943 skGTMDDISQEEGSSQGEESVSGSQRTSSIYAREALIEIDYGDLCEDLKDAQAE-EEIKQEMNTLQQKLNEQQSVLQRIA 1021
Cdd:COG3883 100 --GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAElEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 258613892 1022 APNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQA 1058
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
24-124 |
1.98e-05 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (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 including 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 47.97 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 24 FQR-FTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKT--LRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVI-V 99
Cdd:cd03241 19 FEEgLTVLTGETGAGKSILLDALSLLLGGRASADLIRSgaEKAVVEGVFDISDEEEAKALLLELGIEDDDDLIIRREIsR 98
|
90 100
....*....|....*....|....*
gi 258613892 100 GGSSEYKINNKVVQLHEYSEELEKL 124
Cdd:cd03241 99 KGRSRYFINGQSVTLKLLRELGSLL 123
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
231-469 |
2.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 231 NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRpqyikakentshkiK 310
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------------K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 311 KLEAAKKSLQNAQKHYKK------RKGDMDELeKEMLSVEKARQEFEERMEEESQSQGRdltleENQVKKYHRLKEEASK 384
Cdd:COG4942 91 EIAELRAELEAQKEELAEllralyRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPAR-----REQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 385 RAATLAQE---LEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTE 461
Cdd:COG4942 165 LRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*...
gi 258613892 462 EVEMAKRR 469
Cdd:COG4942 245 AAGFAALK 252
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-46 |
2.62e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 47.00 E-value: 2.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 258613892 7 IEIEN-FKSYKGRQIIG------PFQRFTAIIGPNGSGKSNLMDAIS 46
Cdd:COG4604 2 IEIKNvSKRYGGKVVLDdvsltiPKGGITALIGPNGAGKSTLLSMIS 48
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
676-1095 |
2.80e-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: 48.56 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 676 EKKERLTEELKEQMKAKRKEAELRQVQSQAHglQMRLKYSQSDLEQTKTRhlALNLQEKSKLESElanfgprinDIKRII 755
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEK--ENKMKDLTFLLEESRDK--ANQLEEKTKLQDE---------NLKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 756 QSRE---REMKDLKEKMNQ-VEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKR-------LEFENQKTRLGIQLDFE 824
Cdd:pfam05483 289 EKKDhltKELEDIKMSLQRsMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 825 KNQLKEDQDKVHMWEQTVKKDENEIEKLkkeeqrhMKIIDETMAQLQDLKNQhLAKKSEVNDKNHEMEEIRKKLGGANKE 904
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEM-------TKFKNNKEVELEELKKI-LAEDEKLLDEKKQFEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 905 MTHL----QKEVTAIETKLEQKRSDRHNLLQacKMQDIKLPLSKGTMDDISQEEGSSQ-GEESVSGSQRTSSIYareali 979
Cdd:pfam05483 441 LIFLlqarEKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNIELTAHCDKlLLENKELTQEASDMT------ 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 980 eIDYGDLCEDLKDAQAEEE-IKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQA 1058
Cdd:pfam05483 513 -LELKKHQEDIINCKKQEErMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKI 591
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 258613892 1059 FEQikkeRFDRFNACFESVATNIDEIY---KALSRNSSAQ 1095
Cdd:pfam05483 592 LEN----KCNNLKKQIENKNKNIEELHqenKALKKKGSAE 627
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
7-65 |
2.90e-05 |
|
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: 46.44 E-value: 2.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258613892 7 IEIENFKSYKGRQI-IGPfqRFTAIIGPNGSGKSNLMDAISFVLGEKTSNL-RVKTLRDLI 65
Cdd:cd03276 4 ITLKNFMCHRHLQIeFGP--RVNFIVGNNGSGKSAILTALTIGLGGKASDTnRGSSLKDLI 62
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
276-511 |
4.88e-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: 47.81 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 276 EQQQIEKEIKEKDSELNQKRPqyIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERME 355
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 356 EESQSQGRdLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRI 435
Cdd:pfam17380 375 SRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRL 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258613892 436 EKLE--EYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDrQESSRQQRKAEIMESIKRLY 511
Cdd:pfam17380 454 EEQErqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIY 530
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-502 |
4.98e-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: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 281 EKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEK---ARQEFEERMEEE 357
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 358 SQSQGRDLTLEENQVkkyhrlkeeASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEK 437
Cdd:COG3883 95 LYRSGGSVSYLDVLL---------GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 438 LEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAE 502
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
660-928 |
5.05e-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: 47.81 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 660 KAKARRWDEKAVDKLKEKKERL-TEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLE 738
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 739 SElanfgprindikriiQSREREMKDLKEKMNQVEDEVFEefcreigvrniREFEEEKVKRQNEIAKKRLEFENQKTRLG 818
Cdd:pfam17380 362 LE---------------RIRQEEIAMEISRMRELERLQME-----------RQQKNERVRQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 819 IQLDFEKNQLKEDQDKVHMWEQTVKKDEN--EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRK 896
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQREVRRLEEERarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
250 260 270
....*....|....*....|....*....|....*
gi 258613892 897 KLggaNKEMTHLQKEVTAIETK---LEQKRSDRHN 928
Cdd:pfam17380 496 IL---EKELEERKQAMIEEERKrklLEKEMEERQK 527
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
2-67 |
5.11e-05 |
|
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: 45.66 E-value: 5.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258613892 2 GFLKLIEIENFKSYkGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNL-RVKTLRDLI-HG 67
Cdd:cd03277 1 GSIVRIKLENFVTY-DETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLgRAKKVGEFVkRG 67
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
113-510 |
6.18e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 113 QLHEYSEELEKLGILIKARNFLVfQGAVES--IAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKk 190
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSEC-QGQMERqmAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 191 niAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYH----------NEVEIEKLNKELASKNKEIEKDKKRMDKVE 260
Cdd:pfam15921 498 --VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknegdhlrnVQTECEALKLQMAEKDKVIEILRQQIENMT 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 261 DELKEKKKELGKMMREQQQIEKEIKEKDSELNqkrpQYIKAKENTSHKIKKLEA-------AKKSLQNAQKHYKKRKGDM 333
Cdd:pfam15921 576 QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ----EFKILKDKKDAKIRELEArvsdlelEKVKLVNAGSERLRAVKDI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 334 DELEKEMLSVEKarqefeermeeESQSQGRDLTLEENQVKKYHRLK-EEASKRAATLAQELEKFNRDQKADQDRLDLEE- 411
Cdd:pfam15921 652 KQERDQLLNEVK-----------TSRNELNSLSEDYEVLKRNFRNKsEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEg 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 412 ------RKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQS----LEEQKKLEGEL----TEEVEMA----------- 466
Cdd:pfam15921 721 sdghamKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhflKEEKNKLSQELstvaTEKNKMAgelevlrsqer 800
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 258613892 467 --KRRIDEINKELNQVMEQLGDAR--IDRQESSRQQRKAEIMESIKRL 510
Cdd:pfam15921 801 rlKEKVANMEVALDKASLQFAECQdiIQRQEQESVRLKLQHTLDVKEL 848
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
413-519 |
6.48e-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: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 413 KKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVmeqlgDARIDRQ 492
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----EKEIAEL 95
|
90 100
....*....|....*....|....*..
gi 258613892 493 ESSRQQRKAEIMESIKRLYPGSVYGRL 519
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPL 122
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
273-395 |
6.50e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 273 MMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEE 352
Cdd:PRK12704 66 IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 258613892 353 RMEEESQSQGRDLTLEEnqvkkyhrLKEEASKRAATLAQELEK 395
Cdd:PRK12704 146 RISGLTAEEAKEILLEK--------VEEEARHEAAVLIKEIEE 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-510 |
6.91e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 4 LKLIEIENFKSYKGRQIIGPfQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKtlrdlihgapVGKPAANRAFVSMV 83
Cdd:COG4717 3 IKELEIYGFGKFRDRTIEFS-PGLNVIYGPNEAGKSTLLAFIRAMLLERLEKEADE----------LFKPQGRKPELNLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 84 YSEEGAEDRTFARvivggSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGE 163
Cdd:COG4717 72 ELKELEEELKEAE-----EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 164 LAQEYDKRKKEMVKAEEDtqfnyhrkknIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELA 243
Cdd:COG4717 147 RLEELEERLEELRELEEE----------LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 244 SKNKEIEKDKKRMDKVEDElkekkkelgkmmREQQQIEKEIKEKDSELN--------QKRPQYIKAKENTSHKIKKLEAA 315
Cdd:COG4717 217 EAQEELEELEEELEQLENE------------LEAAALEERLKEARLLLLiaaallalLGLGGSLLSLILTIAGVLFLVLG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEE-----NQVKKYHRLKEEASKRAATLa 390
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllellDRIEELQELLREAEELEEEL- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 391 qELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEEnqkRIEKLEEYITTSKQSLEEQKKL--EGELTEEVEMAKR 468
Cdd:COG4717 364 -QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE---ELEELEEQLEELLGELEELLEAldEEELEEELEELEE 439
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 258613892 469 RIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
371-511 |
7.17e-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: 45.69 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 371 QVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQK---------LREIEENQKRIEKLEEY 441
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 442 ITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLgDARIDRQESSRQQRKAEIMESIKRLY 511
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL-EAELEELEAEREELAAKIPPELLALY 180
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
3-90 |
1.05e-04 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 46.19 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 3 FLKLIEIENFKSYKgrQIIGPFQ-RFTAIIGPNGSGKSNLMDAIsFVLGEkTSNLRVKTLRDLI-HGAPvgkpaanRAFV 80
Cdd:TIGR00611 2 YLSRLELTDFRNYD--AVDLELSpGVNVIVGPNGQGKTNLLEAI-YYLAL-GRSHRTSRDKPLIrFGAE-------AFVI 70
|
90
....*....|
gi 258613892 81 SMVYSEEGAE 90
Cdd:TIGR00611 71 EGRVSKGDRE 80
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
371-510 |
1.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 371 QVKKYHRLKEEASKRAATLAQELEKFnrdQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE 450
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELA---ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258613892 451 EQKKLEGELTEEVEMAKRRIDEI-NKELNQVMEQLGDARIDRQEssRQQRKAEIMESIKRL 510
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEE--RERRRARLEALLAAL 371
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-46 |
1.13e-04 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 45.42 E-value: 1.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 258613892 6 LIEIENFK-SYKGRQIIGP--FQ----RFTAIIGPNGSGKSNLMDAIS 46
Cdd:COG1120 1 MLEAENLSvGYGGRPVLDDvsLSlppgEVTALLGPNGSGKSTLLRALA 48
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1121-1174 |
1.20e-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: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258613892 1121 RFRPMDNL--------SGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYI 1174
Cdd:cd03277 112 KFREGEQLqeldphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDML 173
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1110-1208 |
1.27e-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: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1110 GINYncVAPGkrfRPMDNLSGGEKTVAALALLFAIHSykPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISL 1189
Cdd:cd03238 75 GLGY--LTLG---QKLSTLSGGELQRVKLASELFSEP--PGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147
|
90
....*....|....*....
gi 258613892 1190 KEEFYTKAESLIGVYPEQG 1208
Cdd:cd03238 148 NLDVLSSADWIIDFGPGSG 166
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
377-509 |
1.59e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 377 RLKEEASKRAATLAQELEkfnRDQKadqdrlDLEERKKVETEAKIKQKLREIEENQKRIEKLEE-------YITTSKQSL 449
Cdd:PRK12704 42 RILEEAKKEAEAIKKEAL---LEAK------EEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrkleLLEKREEEL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 450 EEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLG-----DARIDRQESSRQQRKAEIMESIKR 509
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeEAKEILLEKVEEEARHEAAVLIKE 177
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
150-500 |
1.75e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.19 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 150 ERTALFEEISRSGELaQEYDKRKKEMVKaeEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLY 229
Cdd:PTZ00108 1012 SNKVRFIKHVINGEL-VITNAKKKDLVK--ELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSY 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 230 H----------NEVEIEKLNKELASKNKEIEKDKKRmdkvedelkekkkELGKM-MREQQQIEKEIKEKDSELNQKRPQY 298
Cdd:PTZ00108 1089 DyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNT-------------TPKDMwLEDLDKFEEALEEQEEVEEKEIAKE 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 299 IKAKENTSHKIKKLeaAKKSLQNAQKhyKKRKGDMDELEKEMLSVEKARQEFEERMEEESQ-------SQGRDLTLEENQ 371
Cdd:PTZ00108 1156 QRLKSKTKGKASKL--RKPKLKKKEK--KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKpdnkksnSSGSDQEDDEEQ 1231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 372 VKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEE 451
Cdd:PTZ00108 1232 KTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVK 1311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 258613892 452 QKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRK 500
Cdd:PTZ00108 1312 KRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKK 1360
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
336-485 |
1.99e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 336 LEKEMlsvEKARQEFEERMEEESQSQGRDLTLEENQVKKY----HRLKEEASKRAATLAqELEKFNRDQKADQDRLDLEE 411
Cdd:COG2433 382 LEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLeeqvERLEAEVEELEAELE-EKDERIERLERELSEARSEE 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 412 RKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKE-LNQVMEQLG 485
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEaIRRLEEEYG 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
690-921 |
2.04e-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: 45.14 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 690 KAKRKEAELRQVQSQahglqmrLKYSQSDLEQTKtrhlalnlQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKM 769
Cdd:COG4942 21 AAAEAEAELEQLQQE-------IAELEKELAALK--------KEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 770 NQVEDEvfeefcreigvrnIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEI 849
Cdd:COG4942 86 AELEKE-------------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613892 850 EKLKKE-------EQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQ 921
Cdd:COG4942 153 EELRADlaelaalRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
840-1072 |
2.33e-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: 45.14 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 840 QTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKL 919
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 920 EQKRSDRHNLLQA-CKMQDIKLPLSKGTMDDISQEEGSSQGEESVSGSQRTSSIYAREALIEIdygdlcEDLKDAQAEEe 998
Cdd:COG4942 100 EAQKEELAELLRAlYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL------AALRAELEAE- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258613892 999 iKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNA 1072
Cdd:COG4942 173 -RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-46 |
2.52e-04 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 43.19 E-value: 2.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 258613892 8 EIEN-FKSYKGRQIIGPFQ------RFTAIIGPNGSGKSNLMDAIS 46
Cdd:cd03214 1 EVENlSVGYGGRTVLDDLSlsieagEIVGILGPNGAGKSTLLKTLA 46
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
7-49 |
2.58e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 44.19 E-value: 2.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 258613892 7 IEIENFKSYKGRQIigPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:COG4938 4 ISIKNFGPFKEAEL--ELKPLTLLIGPNGSGKSTLIQALLLLL 44
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
378-508 |
3.68e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 378 LKEEASKRA-ATLAQELEKFNR-DQKADQDRLDLEERKKvETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEqkkl 455
Cdd:PRK00409 499 LPENIIEEAkKLIGEDKEKLNElIASLEELERELEQKAE-EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK---- 573
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 258613892 456 egELTEEVEMAKRRIDEINKELNQvMEQLGDARIDRQESSRQQRK----AEIMESIK 508
Cdd:PRK00409 574 --EAQQAIKEAKKEADEIIKELRQ-LQKGGYASVKAHELIEARKRlnkaNEKKEKKK 627
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
4-75 |
3.78e-04 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 43.83 E-value: 3.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258613892 4 LKLIEIENFKSYKGRQIigPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTsnLRVKTLRDLIHgapVGKPAA 75
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFePGVTVLVGENAQGKTNLLEAISLLATGKS--HRTSRDKELIR---WGAEEA 66
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
647-1213 |
5.23e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 647 QKSGVISGGASDLKAKARRWDE--KAVDKLKEKKERLTEELK--EQMKAKRKEAELRQVQSQAHgLQMRLKYSQSDLEQT 722
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDlnNQILELEGYEMDYNSYLKsiESLKKKIEEYSKNIERMSAF-ISEILKIQEIDPDAI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 723 KTRHLALNlQEKSKLESELANFGPRINDIkriiqsREREMkDLKEKMNQVEDEVFEEFCR----EIGVRNIRE------- 791
Cdd:PRK01156 408 KKELNEIN-VKLQDISSKVSSLNQRIRAL------RENLD-ELSRNMEMLNGQSVCPVCGttlgEEKSNHIINhynekks 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 792 -FEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMA-Q 869
Cdd:PRK01156 480 rLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 870 LQDL--KNQHLAKKSEVNDkNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRS-----------------DRHNLL 930
Cdd:PRK01156 560 LEDLdsKRTSWLNALAVIS-LIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidksireieneannlnNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 931 QACKMQDIKLplsKGTMDDISQEegsSQGEESVSGSQRTSSIYAREalIEIDYGDLCEDLKDAQAE--------EEIKQE 1002
Cdd:PRK01156 639 QENKILIEKL---RGKIDNYKKQ---IAEIDSIIPDLKEITSRIND--IEDNLKKSRKALDDAKANrarlestiEILRTR 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1003 MNTLQQKLNEQQSVLQRiaapnMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVatNID 1082
Cdd:PRK01156 711 INELSDRINDINETLES-----MKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKYLFEFNLDFDDI--DVD 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1083 EIYK-ALSRNSSAQAflgpenpeepyldginyncvapgkrfrpMDNLSGGEKTVAALALLFAIHSY--KPAPFFVLDEID 1159
Cdd:PRK01156 784 QDFNiTVSRGGMVEG----------------------------IDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPT 835
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 258613892 1160 AALDN---TNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVIS 1213
Cdd:PRK01156 836 AFLDEdrrTNLKDIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSKVI 892
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-80 |
5.25e-04 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 43.15 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 1 MGFLKLIEIEN--FkSYKGRQII---------GpfqRFTAIIGPNGSGKSNLMDAIsfvLGE-KTSNLRVKtlrdlIHGA 68
Cdd:COG1121 1 MMMMPAIELENltV-SYGGRPVLedvsltippG---EFVAIVGPNGAGKSTLLKAI---LGLlPPTSGTVR-----LFGK 68
|
90
....*....|..
gi 258613892 69 PVGKPAANRAFV 80
Cdd:COG1121 69 PPRRARRRIGYV 80
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
235-502 |
5.36e-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: 44.44 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQiekeikEKDsELNQKRPQYIKAKENtshKIKKLEA 314
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS------EKD-KKNKALAERKDSANE---RLNSLEA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 315 AKKSLQNAQKHYKKR-KGDMDELEKEMLSVEKArqefeermeeesqsqgrdltLEENQVKKYHRLKEEASKRAATLAQEL 393
Cdd:pfam12128 690 QLKQLDKKHQAWLEEqKEQKREARTEKQAYWQV--------------------VEGALDAQLALLKAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 394 EKFNRDQKADQDRLDLEErkkvETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE-LTEEVEMAKRRIDE 472
Cdd:pfam12128 750 KALETWYKRDLASLGVDP----DVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPrLATQLSNIERAISE 825
|
250 260 270
....*....|....*....|....*....|
gi 258613892 473 INKELNQVMEqlgDARIDRQESSRQQRKAE 502
Cdd:pfam12128 826 LQQQLARLIA---DTKLRRAKLEMERKASE 852
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
166-475 |
5.52e-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: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 166 QEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQrlkdEVVRAQVQLQLFKLYHNEVEIEKLNKELASK 245
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA----EELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 246 NKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKH 325
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 326 YKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQD 405
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 406 RLDLEERKKVETEAKIKQKLREIEENQkriEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK 475
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELELASAK---QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-46 |
6.66e-04 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 41.28 E-value: 6.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 258613892 7 IEIENF-KSYKGRQIIGPFqRFT-------AIIGPNGSGKSNLMDAIS 46
Cdd:cd03221 1 IELENLsKTYGGKLLLKDI-SLTinpgdriGLVGRNGAGKSTLLKLIA 47
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
279-510 |
6.73e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 279 QIE-KEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQ---KHYKKRKGDMDELEKEMLSV-EKARQEFEER 353
Cdd:PRK02224 195 QIEeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLrETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 354 MEEESQSQGRDLTLEEnqvkkyhrLKEEASKRAATLAQElekfNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQK 433
Cdd:PRK02224 275 EELAEEVRDLRERLEE--------LEEERDDLLAEAGLD----DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 434 RIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKR-------RIDEINKELNQVMEQLGDARIDRQES-----SRQQRKA 501
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREavedrreEIEELEEEIEELRERFGDAPVDLGNAedfleELREERD 422
|
....*....
gi 258613892 502 EIMESIKRL 510
Cdd:PRK02224 423 ELREREAEL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
657-878 |
7.61e-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: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 657 SDLKAKARRWDEKAVDKlkekkeRLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNlQEKSK 736
Cdd:COG4913 255 EPIRELAERYAAARERL------AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR-EELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 737 LESELANF-GPRINDIKRIIQSREREMKDLKEKMNQvedevFEEFCREIGVrnirefeeekvkrqnEIAKKRLEFENQKT 815
Cdd:COG4913 328 LEAQIRGNgGDRLEQLEREIERLERELEERERRRAR-----LEALLAALGL---------------PLPASAEEFAALRA 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258613892 816 RLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKE----EQRHMKiIDETMAQLQDLKNQHL 878
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslERRKSN-IPARLLALRDALAEAL 453
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
391-510 |
8.02e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 391 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE---------LTE 461
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQK 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 258613892 462 EVEMAKRRIDEINKELNQVMEQLGDAR--IDRQESSRQQRKAEIMESIKRL 510
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEeeLAELEAELAELEAELEEKKAEL 147
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-434 |
8.40e-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: 43.21 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 193 AAERKEAKQEKEEadryqrlkdevVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGK 272
Cdd:COG4942 19 ADAAAEAEAELEQ-----------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 273 MMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKI----KKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQ 348
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 349 EFEERMEEESQsqgrdltLEENQVKKYHRLKEEASKRAATLAQelekFNRDQKADQDRLDLEERKKVETEAKIKQKLREI 428
Cdd:COG4942 168 ELEAERAELEA-------LLAELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*.
gi 258613892 429 EENQKR 434
Cdd:COG4942 237 AAAAER 242
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
118-462 |
8.63e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 118 SEELEKLGILiKARNFLVFQGA--VESIAMKNPKERTALFeeiSRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAE 195
Cdd:PLN03229 390 TEELLKHRML-KFRKIGGFQEGvpVDPERKVNMKKREAVK---TPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 196 R--KEAKQEKEEA-------DRYQRLKDEVVRAQVQLQLFklyhNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEK 266
Cdd:PLN03229 466 KlkKEIDLEYTEAviamglqERLENLREEFSKANSQDQLM----HPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLN 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 267 KKELGKMMREQQQIEKEIKekdSELNQKRPQYIKAKEntshkIK-KLEAAKKSLQNAQKHykkRKGDMDELEKEmlSVEK 345
Cdd:PLN03229 542 EFSRAKALSEKKSKAEKLK---AEINKKFKEVMDRPE-----IKeKMEALKAEVASSGAS---SGDELDDDLKE--KVEK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 346 ARQEFEERMEEESQSQGRDL-------------TLEENQVKKYHRLKEEASK------RAATLAQELEKFNRDQKADQDR 406
Cdd:PLN03229 609 MKKEIELELAGVLKSMGLEVigvtkknkdtaeqTPPPNLQEKIESLNEEINKkierviRSSDLKSKIELLKLEVAKASKT 688
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 258613892 407 LDLEERKKVET-EAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:PLN03229 689 PDVTEKEKIEAlEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKND 745
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
672-931 |
1.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 672 DKLKEKKERLTEELKEqmkAKRKEAELRQVQSQAHGLQMRLKysqsDLEQTKTRhlalnlqekskleselanfgprINDI 751
Cdd:PRK03918 193 ELIKEKEKELEEVLRE---INEISSELPELREELEKLEKEVK----ELEELKEE----------------------IEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 752 KRIIQSREREMKDLKEKMNQVEDEVFEEfcreigVRNIREFeEEKVKRQNEIAKKRLEFENQKtRLGIQLDFEKNQLKED 831
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEEL------KKEIEEL-EEKVKELKELKEKAEEYIKLS-EFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 832 QDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKsEVNDKNHEMEEIRKKLGGANKEmtHLQKE 911
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKE 392
|
250 260
....*....|....*....|
gi 258613892 912 VTAIETKLEQKRSDRHNLLQ 931
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITA 412
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
3-54 |
1.80e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 42.20 E-value: 1.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 258613892 3 FLKLIEIENFKSYKGRQIigPFQ-RFTAIIGPNGSGKSNLMDAISFVLGEKTS 54
Cdd:pfam13175 2 KIKSIIIKNFRCLKDTEI--DLDeDLTVLIGKNNSGKSSILEALDIFLNNKEK 52
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
27-45 |
1.95e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.98 E-value: 1.95e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
793-1022 |
2.01e-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: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 793 EEEKVKRQNEIAKKRLEFENQKTRLGIqLDFEKNQLK--EDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQL 870
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAE-LEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 871 QDLKNQHLAkksevndknhemeeirkkLGGANKEmtHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDI 950
Cdd:COG4913 326 DELEAQIRG------------------NGGDRLE--QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258613892 951 SQEegssqgeesvsGSQRTSSIYAREALIEIDYGDLCEDLKDAQAE-EEIKQEMNTLQQ-KLN---EQQSVLQRIAA 1022
Cdd:COG4913 386 RAE-----------AAALLEALEEELEALEEALAEAEAALRDLRRElRELEAEIASLERrKSNipaRLLALRDALAE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
679-876 |
2.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 679 ERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSR 758
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 759 E--REMKDLKEKMNQVEDEVfEEFCREIgvRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQldfEKNQLKEDQDKVH 836
Cdd:COG4717 129 PlyQELEALEAELAELPERL-EELEERL--EELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 258613892 837 MWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQ 876
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-477 |
2.22e-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: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 195 ERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMM 274
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 275 REQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERM 354
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 355 EEESQSQgrdltlEENQVKKYHRLKEEASKRAATLAQELEKfnrdqkaDQDRLDLEERKKVETEAKIKQKLREIEENQKR 434
Cdd:TIGR04523 562 EIDEKNK------EIEELKQTQKSLKKKQEEKQELIDQKEK-------EKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 258613892 435 IEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKEL 477
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
26-46 |
2.25e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 41.25 E-value: 2.25e-03
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
379-510 |
2.90e-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: 41.67 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 379 KEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 458
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 459 LT---------------------EEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKAEIMESIKRL 510
Cdd:COG4942 109 LLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRAdlAELAALRAELEAERAELEALLAEL 183
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
27-46 |
2.94e-03 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 40.88 E-value: 2.94e-03
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-46 |
3.29e-03 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 40.23 E-value: 3.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 258613892 8 EIENFKSYKGRQII----GPFQ--RFTAIIGPNGSGKSNLMDAIS 46
Cdd:cd03213 12 TVKSSPSKSGKQLLknvsGKAKpgELTAIMGPSGAGKSTLLNALA 56
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
708-921 |
3.35e-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: 41.42 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 708 LQMRLKYSQsdleqtKTRHLALNLQEKSKLESELANfgpriNDIKRIIQSREREMKDLKEKMNQVEDEVfeefcreigvR 787
Cdd:pfam07888 32 LQNRLEECL------QERAELLQAQEAANRQREKEK-----ERYKRDREQWERQRRELESRVAELKEEL----------R 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 788 NIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETM 867
Cdd:pfam07888 91 QSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 258613892 868 AQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQ 921
Cdd:pfam07888 171 AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
187-319 |
4.22e-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: 40.29 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 187 HRKKNIAAERKEAKQEKEEA-DRYQRLKDEVVRAQVQLQLFKLYHNEVE--IEKL---------NKELASKNKEIEKDKK 254
Cdd:COG1579 24 HRLKELPAELAELEDELAALeARLEAAKTELEDLEKEIKRLELEIEEVEarIKKYeeqlgnvrnNKEYEALQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258613892 255 RMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSL 319
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
666-931 |
4.31e-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: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 666 WDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAhgLQMRLKYSQSDLEQTKTRHLalnlQEKSKLESELANFG 745
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA--IKTSEEHYLKEVEDLKTELE----KEKLKNIELTAHCD 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 746 PRINDIKRIIQSREREMKDLKekmNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEK 825
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELK---KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 826 NQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEM 905
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKF 652
|
250 260
....*....|....*....|....*.
gi 258613892 906 THLqkeVTAIETKLEQKRSDRHNLLQ 931
Cdd:pfam05483 653 EEI---IDNYQKEIEDKKISEEKLLE 675
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
362-502 |
4.81e-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: 41.14 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 362 GRDLTLEENQVKKYHRLKEEASKRAATLAQELEKfnrdqkaDQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY 441
Cdd:pfam05262 191 EKGVNFRRDMTDLKERESQEDAKRAQQLKEELDK-------KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258613892 442 ITTskQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKAE 502
Cdd:pfam05262 264 ADT--SSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKEL 324
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
313-510 |
4.90e-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: 41.26 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 313 EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRdLTLEENQ----VKKYHRLKEEASKRAAT 388
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERelerIRQEERKRELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 389 LAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREiEENQKRIekleeyittsKQSLEEQKKLEGELTEEVEMAKR 468
Cdd:pfam17380 370 IAMEISRMRELERLQMERQQKNERVRQELEAARKVKILE-EERQRKI----------QQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 258613892 469 RIDEinkELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:pfam17380 439 RLEE---ERAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-498 |
5.06e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 16 KGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLgekTSNLRVKTLRD-LIHGAPVGKPAANRAFVSMVYSEEGAEDRTF 94
Cdd:TIGR00606 19 KDKQIIDFFSPLTILVGPNGAGKTTIIECLKYIC---TGDFPPGTKGNtFVHDPKVAQETDVRAQIRLQFRDVNGEECAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 95 ARVIVGGS----SEYKINNKVVQLHEYSEE--------------LEKLGILIKARNFLVFQGAVESI-AMKNPKERTALF 155
Cdd:TIGR00606 96 VRSMVCTQktkkTEFKTLEGVITRYKHGEKvslsskcaeidremISHLGVSKAVLNNVIFCHQEDSNwPLSEGKALKQKF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 156 EEISRSGELAQEYDKRKK------EMVKAEEDTQFNYHRKKNIAAERKE---AKQEKEEADRYQRLKDEVVRAQVQLQLF 226
Cdd:TIGR00606 176 DEIFSATRYIKALETLRQvrqtqgQKVQEHQMELKYLKQYKEKACEIRDqitSKEAQLESSREIVKSYENELDPLKNRLK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 227 KLYHNEVEIEKLNKELA---SKNKEIEKDKKRMDkvedelkekkkelGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE 303
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKalkSRKKQMEKDNSELE-------------LKMEKVFQGTDEQLNDLYHNHQRTVREKERELV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 304 NTSHKIKKLEAAKKSLQNAQKHYKKRKGDM----DELEKEMLSVEKARQEFEERMEEESQSQGRDLtleENQVKKYHRLK 379
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFS---ERQIKNFHTLV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 380 EEA-SKRAATLAQELEKFNRDQKADQDRLDLEE-----------------RKKVETEAKIKQKLREIEENQKRIEKLEEY 441
Cdd:TIGR00606 400 IERqEDEAKTAAQLCADLQSKERLKQEQADEIRdekkglgrtielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258613892 442 ITTSKQSL---EEQKKLEGELTEEVEMAKRRIDEINK--ELNQVMEQLgdariDRQESSRQQ 498
Cdd:TIGR00606 480 LRKAERELskaEKNSLTETLKKEVKSLQNEKADLDRKlrKLDQEMEQL-----NHHTTTRTQ 536
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
28-501 |
6.01e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 28 TAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAF---------VSMVYSEEGAEDRTFARVI 98
Cdd:pfam12128 20 TNICGTNAAGKTTLLRLLPLFYGEYPSRIVPGTDRDSFEDYYLPRDSSYIVYeyqrpdgqlCMAVLHSNGDGKGVQYRFI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 99 VGGSSE---YKINNKVVQLHEYSE---ELEKLGIlikARNFLVFQGAVESIAMKnpkERTALFEEISRSGELAQEYDKRK 172
Cdd:pfam12128 100 AGGYRLddfIKANNDFVKCETVAElgrFMKNAGI---QRTNLLNTREYRSIIQN---DRTLLGRERVELRSLARQFALCD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 173 KE--------MVKAEEDTQFNYHRKKNIAAER--------KEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE-I 235
Cdd:pfam12128 174 SEsplrhidkIAKAMHSKEGKFRDVKSMIVAIleddgvvpPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNtL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMReqqQIEKEIKEKDSELNQkrpqyikakentshkikKLEAA 315
Cdd:pfam12128 254 ESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLR---TLDDQWKEKRDELNG-----------------ELSAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLT-LEENQVK---KYHRLKEEASKRAATLAQ 391
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKaLTGKHQDvtaKYNRRRSKIKEQNNRDIA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 392 ELEKFNRDQKADQDRLDLEERKKVEteaKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRID 471
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQ---ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFD 470
|
490 500 510
....*....|....*....|....*....|
gi 258613892 472 EinkELNQVMEQLGDARIDRQESSRQQRKA 501
Cdd:pfam12128 471 E---RIERAREEQEAANAEVERLQSELRQA 497
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
380-487 |
6.32e-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: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 380 EEASKRAATLAQELEKFNRDQKADQDRLDLEERK---KVETEAKIKQKlREIEENQKRIEKL-EEYITTSKQSLEEQKKL 455
Cdd:cd22656 131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKAlkdLLTDEGGAIAR-KEIKDLQKELEKLnEEYAAKLKAKIDELKAL 209
|
90 100 110
....*....|....*....|....*....|....*
gi 258613892 456 EGELTEEVEMAKR---RIDEINKELNQVMEQLGDA 487
Cdd:cd22656 210 IADDEAKLAAALRliaDLTAADTDLDNLLALIGPA 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
227-509 |
6.53e-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: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 227 KLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTS 306
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 307 HKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKE------ 380
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktteis 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 381 EASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKriEKLEEYITTSKQSLEEQKKLEGELT 460
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 258613892 461 EEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQ-QRKAEIMESIKR 509
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRElEEKQNEIEKLKK 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-923 |
6.99e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 668 EKAVDKLKEKKERLTE----ELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQS------DLEQTKTRHLALN------L 731
Cdd:PRK03918 227 EKEVKELEELKEEIEElekeLESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSefyeeyL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 732 QEKSKLESELANFGPRINDIKRIIQ---SREREMKDLKEKMNQVEDEVfeefcreigvrnirEFEEEKVKRQNEIAKKRL 808
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKeleEKEERLEELKKKLKELEKRL--------------EELEERHELYEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 809 EFENQKTRLGiqlDFEKNQLKEDQDKVhmwEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLA--------- 879
Cdd:PRK03918 373 ELERLKKRLT---GLTPEKLEKELEEL---EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelt 446
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 258613892 880 ---KKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKR 923
Cdd:PRK03918 447 eehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-46 |
7.55e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 39.75 E-value: 7.55e-03
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-49 |
7.74e-03 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 39.14 E-value: 7.74e-03
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
277-963 |
8.79e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 277 QQQIEKEIKEKDSELNQKRPQYIKAKENTSHK---------IKKLEAAKKSLQNAQKHYKKRkgdMDELEKEMLSVEKAR 347
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDAMADIRRRESQSQEdlrnqlqntVHELEAAKCLKEDMLEDSNTQ---IEQLRKMMLSHEGVL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 348 QEFEERMEEESQSQGRDLTLEENQVKKYHR-LKEEASKRAATLAQELEKFNRDQKADQDRLdleERKKVETEAKIKQKLr 426
Cdd:pfam15921 187 QEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKILRELDTEISYLKGRIFPVEDQL---EALKSESQNKIELLL- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 427 eiEENQKRIEKLEEyittskqslEEQKKLEGeLTEEVEMAKRRIDEINKELNQVMEQLGDA------RIDRQESSRQQRK 500
Cdd:pfam15921 263 --QQHQDRIEQLIS---------EHEVEITG-LTEKASSARSQANSIQSQLEIIQEQARNQnsmymrQLSDLESTVSQLR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 501 AEIMESiKRLYPGSVY---GRLI----DLCQPTQKKYQIAV-TKVLGKNMDAIIVDSEKTGRDcIQYIKEQRgepETFLP 572
Cdd:pfam15921 331 SELREA-KRMYEDKIEeleKQLVlansELTEARTERDQFSQeSGNLDDQLQKLLADLHKREKE-LSLEKEQN---KRLWD 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 573 LDYLEVKPTDEKLRELKGAKLviDVIRYEPphIKKALQYACGN------ALVCDNVEDARRIAFGGHQRHKT-------- 638
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNM--EVQRLEA--LLKAMKSECQGqmerqmAAIQGKNESLEKVSSLTAQLESTkemlrkvv 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 639 ---VALDGTLFQKSGVISGGASDLKAKARRWdEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYS 715
Cdd:pfam15921 482 eelTAKKMTLESSERTVSDLTASLQEKERAI-EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEK 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 716 QSDLEQTKT-------------RHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEF-C 781
Cdd:pfam15921 561 DKVIEILRQqienmtqlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVnA 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 782 REIGVRNIREFEEEKVKRQNEIAKKRLE--------------FENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDEN 847
Cdd:pfam15921 641 GSERLRAVKDIKQERDQLLNEVKTSRNElnslsedyevlkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613892 848 EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRH 927
Cdd:pfam15921 721 SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 258613892 928 NLLQacKMQDIKLPLSKGTM-----DDISQEegssQGEESV 963
Cdd:pfam15921 801 RLKE--KVANMEVALDKASLqfaecQDIIQR----QEQESV 835
|
|
| |
