|
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 ... |
155-1406 |
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: 682.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 155 FINELVLENFKSYAgKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANK-MRQDRLSDLIHkSEAFPSLQSCSVA 233
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKsLRSERLSDLIH-SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 234 VHFqyviDESSGTSRIDEEKpgLIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQMKP 313
Cdd:pfam02463 79 ITF----DNEDHELPIDKEE--VSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 314 KAEKESDDGLLEYLEDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETALEFLEKEKQLTLLRS 393
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 394 KLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSL 473
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 474 EERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIR 553
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 554 HEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEK 633
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 634 NFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKVLTALSRLQKSGRINGFHGRLGDLGVIDDSFDVAISTACPRL 713
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 714 DDVVVDTVECAQHCIDYLRKNKLGYARFILLDRLRQFNLQPISTPENVPRLFdlvkpknpkfsnafysvlrdtlvaqnlk 793
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN---------------------------- 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 794 qannvaygkkrfrvvtvdgklidisgtmsgggnhvakglmklgtnqsdkvddytpeEVDKIERELSERENNFRVASDTVH 873
Cdd:pfam02463 605 --------------------------------------------------------LAQLDKATLEADEDDKRAKVVEGI 628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 874 EMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEMAYVKAVSDKAQLNVVMKNLERLRGEYNDLQSETK 953
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 954 TKKEKIKGLQDEIMKIGGIKLQMQNSKVESVCQKLDILVAKLKKVKSASKKSGGDVVKFQKLLQNSERDVELSSDELKVI 1033
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV 788
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1034 EEQLKHTKLALAENDTNMNETLNLKVELKEQSEQLKEQMEDMEESINEFKSIEIEMKNKLEKLNSLLTYIKSEITQQEKG 1113
Cdd:pfam02463 789 EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1114 LNELSIRDVTHTLGMLDDNKMDSVKEDVKNNQELDQEYRSCETQDESEIKDAETSCDNYHPMNIDETSDEVSRGIPRLSE 1193
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1194 DELRELDVELIESKINELSYYVEETNVDIGVLEEYARRLAEFKRRKLDLNNAVQKRDEVKEQLGILKKKRFDEFMAGFNI 1273
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS 1028
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1274 ISMTLKEMYQMITMGGNAELELVDSLDPFSEGVTFSVMPPKKSWRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEI 1353
Cdd:pfam02463 1029 INKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEI 1108
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|...
gi 29427672 1354 DAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAQQLVGVYKRDNRTKS 1406
Cdd:pfam02463 1109 DAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
155-1411 |
2.25e-113 |
|
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: 385.58 E-value: 2.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 155 FINELVLENFKSYAGKQVVgPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANK-MRQDRLSDLIHKSEAFPSLQSCSVA 233
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 234 VHFqyviDESSGTSRIDEEkpgLIITRKAFKNNS-SKYYINEKESSYTEVTKLLKNEGIDLDHKRFlILQGEVENIAQMK 312
Cdd:TIGR02169 80 VTF----KNDDGKFPDELE---VVRRLKVTDDGKySYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 313 PKAEKEsddglleYLEDIIGTANYKPLIEERMGQIEnlneVCLEKENRFEIVDREKNS----LESGKETALEFLEKEKQL 388
Cdd:TIGR02169 152 PVERRK-------IIDEIAGVAEFDRKKEKALEELE----EVEENIERLDLIIDEKRQqlerLRREREKAERYQALLKEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 389 TLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLER-RELE 467
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 468 GTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEH-------ETEIKDLTQLLEKERSILDDI---- 536
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEErkrrdklTEEYAELKEELEDLRAELEEVdkef 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 537 ---KLSLKDKTKNISA---EIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQEL 610
Cdd:TIGR02169 381 aetRDELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 611 QDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKvlnahRQRAMEARSSLSKAQnkSKVLTAlsrlqksgRINGFHG 690
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA-----QARASEERVRGGRAV--EEVLKA--------SIQGVHG 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 691 RLGDLGVIDDSFDVAISTAC-PRLDDVVVDTVECAQHCIDYLRKNKLGYARFILLDRLRQFN--LQPISTPENVPRLFDL 767
Cdd:TIGR02169 526 TVAQLGSVGERYATAIEVAAgNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERrdLSILSEDGVIGFAVDL 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 768 VKpKNPKFSNAFYSVLRDTLVAQNLKQANNVAygkKRFRVVTVDGKLIDISGTMSGGgnhvakglmklgtnqsdkvddyt 847
Cdd:TIGR02169 606 VE-FDPKYEPAFKYVFGDTLVVEDIEAARRLM---GKYRMVTLEGELFEKSGAMTGG----------------------- 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 848 peevdkiERELSERENNFRVASDTVHEMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEmayvkavsd 927
Cdd:TIGR02169 659 -------SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE--------- 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 928 kAQLNVVMKNLERLRGEYNDLQSetktkkekikglqdeimkiggiKLQMQNSKVESVCQKLDILVAKLKKVKSaskksgg 1007
Cdd:TIGR02169 723 -KEIEQLEQEEEKLKERLEELEE----------------------DLSSLEQEIENVKSELKELEARIEELEE------- 772
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1008 DVVKFQKLLQNSERD-----VELSSDELKVIEEQLKHTKLALAENDTNMNETLNLKVELKEQSEQLKEQMEDMEESINEF 1082
Cdd:TIGR02169 773 DLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1083 KSIEIEMKNKLEKLNSLLTYIKSEITQQEKGLNELSirdvthtlgmlddNKMDSVKEDVKNNQELDQEYRSCETQDESEI 1162
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLK-------------KERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1163 KDAETSCDNyhpmnIDETSDEVSRGIPRLSEDELRELDVELIESKINELSYYVEETN-VDIGVLEEYARRLAEFKRRKLD 1241
Cdd:TIGR02169 920 SELKAKLEA-----LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpVNMLAIQEYEEVLKRLDELKEK 994
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1242 LNNAVQKRDEVKEQLGILKKKRFDEFMAGFNIISMTLKEMYQMITmGGNAELELVDSLDPFSEGVTFSVMPPKKSWRNIT 1321
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAKPKGKPVQRLE 1073
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1322 NLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAQQLVGV-YKR 1400
Cdd:TIGR02169 1074 AMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVtMRR 1153
|
1290
....*....|.
gi 29427672 1401 DNRTKSTTIKN 1411
Cdd:TIGR02169 1154 NGESQVFGLKL 1164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-1397 |
1.03e-98 |
|
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: 343.96 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 155 FINELVLENFKSYAGKQVVgPFHTSFSAVVGPNGSGKSNVIDSMLFVFG-FRANKMRQDRLSDLIHK-SEAFPSLQSCSV 232
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTI-NFDKGITGIVGPNGCGKSNIVDAIRWVLGeQSAKALRGGKMEDVIFNgSETRKPLSLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 233 AVhfqyVIDESSGTSRIDEeKPGLIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDldhKRFL--ILQGEVENIAQ 310
Cdd:TIGR02168 80 EL----VFDNSDGLLPGAD-YSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLG---KRSYsiIEQGKISEIIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 311 MKPkaekesdDGLLEYLEDIIGTANYKPLIEERMGQI----ENLNEVcleKENRFEIvDREKNSLESGKETALEFLEKEK 386
Cdd:TIGR02168 152 AKP-------EERRAIFEEAAGISKYKERRKETERKLertrENLDRL---EDILNEL-ERQLKSLERQAEKAERYKELKA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 387 QLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERREL 466
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 467 EGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKN 546
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 547 I---SAEIIRHEkelepwdLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKthKQELQDLILDLKKKLNS 623
Cdd:TIGR02168 381 LetlRSKVAQLE-------LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 624 LKDERSQGEKnftsahlKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKVLTALSR------------LQKSGRINGFHGR 691
Cdd:TIGR02168 452 LQEELERLEE-------ALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsegvkalLKNQSGLSGILGV 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 692 LGDLGVIDDSFDVAISTACP-RLDDVVVDTVECAQHCIDYLRKNKLGYARFILLDRLRQFNLQP------ISTPENVPRL 764
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGndreilKNIEGFLGVA 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 765 FDLVKPKnPKFSNAFYSVLRDTLVAQNLKQANNVA-YGKKRFRVVTVDGKLIDISGTMSGGGNHVAKGLMKLgtnqsdkv 843
Cdd:TIGR02168 605 KDLVKFD-PKLRKALSYLLGGVLVVDDLDNALELAkKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILER-------- 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 844 ddytpeevdkiERELSERENNFRVASDTVHEMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEmayvk 923
Cdd:TIGR02168 676 -----------RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----- 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 924 avsdkaqlnvvmKNLERLRGEYNDLQSETKTKKEKIKGLQDEImkiggIKLQMQNSKVESVCQKLdilvaklkkvksask 1003
Cdd:TIGR02168 740 ------------AEVEQLEERIAQLSKELTELEAEIEELEERL-----EEAEEELAEAEAEIEEL--------------- 787
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1004 ksggdvvkfQKLLQNSERDVELSSDELKVIEEQLKHTKLALAENDTNMNETLNLKVELKEQSEQLKEQMEDMEESINEFK 1083
Cdd:TIGR02168 788 ---------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1084 SIEIEMKNKLEKLNSLLTYIKSEITQQEKGLNELSIRDvthtlgmldDNKMDSVKEDVKNNQELDQEYRSCETQDESEIk 1163
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSEL---------EELSEELRELESKRSELRRELEELREKLAQLE- 928
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1164 daetscdnyhpMNIDETSDEVSRGIPRLSED------------ELRELDVELIESKINELSYYVEET-NVDIGVLEEYAR 1230
Cdd:TIGR02168 929 -----------LRLEGLEVRIDNLQERLSEEysltleeaealeNKIEDDEEEARRRLKRLENKIKELgPVNLAAIEEYEE 997
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1231 ---RLAEFKRRKLDLNNAVQKRDEVKEQLGILKKKRFDEfmaGFNIISMTLKEMYQMITMGGNAELELVDSLDPFSEGVT 1307
Cdd:TIGR02168 998 lkeRYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD---TFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIE 1074
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1308 FSVMPPKKSWRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNM 1387
Cdd:TIGR02168 1075 IFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGT 1154
|
1290
....*....|
gi 29427672 1388 FELAQQLVGV 1397
Cdd:TIGR02168 1155 MEVADQLYGV 1164
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
154-317 |
4.51e-67 |
|
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: 225.25 E-value: 4.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 154 LFINELVLENFKSYAGKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLIHKSEAFPSLQSCSVA 233
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHPNLDSCSVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 234 VHFQYVIDESsgtsrideekpgliitrkafknnsskyyinekessytevtkLLKNEGIDLDHKRFLILQGEVENIAQMKP 313
Cdd:cd03274 81 VHFQEIIDKP-----------------------------------------LLKSKGIDLDHNRFLILQGEVEQIAQMPK 119
|
....
gi 29427672 314 KAEK 317
Cdd:cd03274 120 KSWK 123
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1311-1407 |
5.74e-67 |
|
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: 224.87 E-value: 5.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1311 MPPKKSWRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFEL 1390
Cdd:cd03274 116 QMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFEL 195
|
90
....*....|....*..
gi 29427672 1391 AQQLVGVYKRDNRTKST 1407
Cdd:cd03274 196 ADRLVGIYKTNNCTKSV 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-1397 |
4.03e-59 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 222.12 E-value: 4.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 155 FINELVLENFKSYAGKQVVgPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANK-MRQDRLSDLIHK-SEAFPSLQSCSV 232
Cdd:COG1196 2 RLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKsLRGGKMEDVIFAgSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 233 AVHFqyviDESSGTSRIDEEKpgLIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDldhKRF--LILQGEVENIAQ 310
Cdd:COG1196 81 SLTF----DNSDGTLPIDYDE--VTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLG---PESysIIGQGMIDRIIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 311 MKPKAekesddgLLEYLEDIIGTANYKPLIEE---RMGQI-ENLNEVclekENRFEIVDREKNSLESGKETALEFLEKEK 386
Cdd:COG1196 152 AKPEE-------RRAIIEEAAGISKYKERKEEaerKLEATeENLERL----EDILGELERQLEPLERQAEKAERYRELKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 387 QLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERREL 466
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 467 EGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSilddiklslkdktkn 546
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE--------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 547 isaeiirhekelepwdlQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKD 626
Cdd:COG1196 366 -----------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 627 ERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKskvltalsrlqksgringfhgrlgdlgviddsfdvai 706
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE------------------------------------- 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 707 stacprlddvvvdtvecaqhcidYLRKNKLGYARFILLDRLRQfnlqpistpenvprlfdlvkpknpkfsnafysvlRDT 786
Cdd:COG1196 472 -----------------------AALLEAALAELLEELAEAAA----------------------------------RLL 494
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 787 LVAQNLKQANNVAYGKKRFRVVTVDGKLIDISGTMSGGGNhvakglmklgtnqsdkvddytpEEVDKIERELSERENNFR 866
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA----------------------AYEAALEAALAAALQNIV 552
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 867 VASDTVH-EMEEELKKLRDH--EPDLESQISKAEMEADSLASELTLAEQQVKEAEMAYVKAVSDKAQLNVVMKNLERLRG 943
Cdd:COG1196 553 VEDDEVAaAAIEYLKAAKAGraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 944 EYNDLQSETKTKKEKIKGLQDEIMKIGGIKLQMQNSKVESvcqkldilvaklkkvksaskksggdvvkfqkLLQNSERDV 1023
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-------------------------------ALLEAEAEL 681
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1024 ELSSDELKVIEEQLKHTKLALAENDTNMNETLNLKVELKEQSEQLKEQMEDMEESInefksieiemknkleklnslltyi 1103
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL------------------------ 737
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1104 kseitqqekglnelsirdvthtlgmlddnkmdsvkedvknnQELDQEYRSCETQDESEIKDAEtscdnyhpmnidetsde 1183
Cdd:COG1196 738 -----------------------------------------LEELLEEEELLEEEALEELPEP----------------- 759
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1184 vsrgiprLSEDELRElDVELIESKINELSyyveetNVDIGVLEEYAR---RLAEFKRRKLDLNNAVQK-RDEVKEqlgiL 1259
Cdd:COG1196 760 -------PDLEELER-ELERLEREIEALG------PVNLLAIEEYEEleeRYDFLSEQREDLEEARETlEEAIEE----I 821
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1260 KKKRFDEFMAGFNIISMTLKEMYQMITMGGNAELELVDSLDPFSEGVTFSVMPPKKSWRNITNLSGGEKTLSSLALVFAL 1339
Cdd:COG1196 822 DRETRERFLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAI 901
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....*...
gi 29427672 1340 HKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAQQLVGV 1397
Cdd:COG1196 902 FRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYGV 959
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
159-313 |
1.07e-33 |
|
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: 130.77 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 159 LVLENFKSYAGKQVVGPFHtSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLIHKSE-AFPSLQSCSVAVHFQ 237
Cdd:cd03275 4 LELENFKSYKGRHVIGPFD-RFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARvGKPDSNSAYVTAVYE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29427672 238 YvidessgtsriDEEKPGLIitRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQMKP 313
Cdd:cd03275 83 D-----------DDGEEKTF--RRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1311-1409 |
1.36e-33 |
|
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: 130.38 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1311 MPPKKSWRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKE-RTKNAQFIVISLRNNMFE 1389
Cdd:cd03275 144 NPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREqAGPNFQFIVISLKEEFFS 223
|
90 100
....*....|....*....|
gi 29427672 1390 LAQQLVGVYKRDNRTKSTTI 1409
Cdd:cd03275 224 KADALVGVYRDQECNSSKVL 243
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
686-798 |
2.49e-31 |
|
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: 119.26 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 686 NGFHGRLGDLGVIDDSFDVAISTAC-PRLDDVVVDTVECAQHCIDYLRKNKLGYARFILLDRLR-------QFNLQPIST 757
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALgGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKprspagsKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 29427672 758 PENVPRLFDLVKPKnPKFSNAFYSVLRDTLVAQNLKQANNV 798
Cdd:smart00968 81 PGFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1323-1405 |
3.72e-31 |
|
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: 120.88 E-value: 3.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1323 LSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKN-AQFIVISLRNNMFELAQQLVGVYKRD 1401
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 29427672 1402 NRTK 1405
Cdd:cd03239 175 GVST 178
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1311-1397 |
1.42e-30 |
|
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: 119.88 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1311 MPPKKSwRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFEL 1390
Cdd:cd03278 103 APGKKV-QRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEA 181
|
....*..
gi 29427672 1391 AQQLVGV 1397
Cdd:cd03278 182 ADRLYGV 188
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
685-799 |
9.37e-29 |
|
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: 111.97 E-value: 9.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 685 INGFHGRLGDLGVIDDSFDVAISTAC-PRLDDVVVDTVECAQHCIDYLRKNKLGYARFILLDRLRQFNLQPISTPEN-VP 762
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALgGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGgAG 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 29427672 763 RLFDLVKPKnPKFSNAFYSVLRDTLVAQNLKQANNVA 799
Cdd:pfam06470 81 PLLDLVEYD-DEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
154-319 |
6.23e-25 |
|
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: 105.46 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 154 LFINELVLENFKSYAGKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRA-NKMRQDRLSDLIHKSEafpslQSCSV 232
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKRG-----QAGIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 233 AVHFQYVIDESS-GTSRI-DEEKPGLIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQ 310
Cdd:cd03273 76 KASVTIVFDNSDkSQSPIgFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLN 155
|
....*....
gi 29427672 311 MKpKAEKES 319
Cdd:cd03273 156 MG-GVWKES 163
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1323-1404 |
7.17e-24 |
|
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: 99.36 E-value: 7.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1323 LSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERT-KNAQFIVISLRNNMFELAQQLVGVYKRD 1401
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIKKVI 157
|
...
gi 29427672 1402 NRT 1404
Cdd:cd03227 158 TGV 160
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
156-237 |
2.00e-21 |
|
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: 93.14 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 156 INELVLENFKSYAGKQVVGPFHtSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLiHKSEAFPSLQSCSVAVH 235
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSN-SFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFL-AGGGVKAGINSASVEIT 78
|
..
gi 29427672 236 FQ 237
Cdd:cd03239 79 FD 80
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
156-249 |
3.61e-21 |
|
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: 92.91 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 156 INELVLENFKSYAGKQVVgPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANK-MRQDRLSDLIHK-SEAFPSLQSCSVA 233
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKsLRGEKMSDVIFAgSETRKPANFAEVT 79
|
90
....*....|....*.
gi 29427672 234 VHFqyviDESSGTSRI 249
Cdd:cd03278 80 LTF----DNSDGRYSI 91
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1317-1402 |
5.46e-19 |
|
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: 88.12 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1317 WR-NITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAQQLV 1395
Cdd:cd03273 160 WKeSLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLF 239
|
....*..
gi 29427672 1396 GVYKRDN 1402
Cdd:cd03273 240 RTRFVDG 246
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1318-1406 |
8.57e-19 |
|
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: 87.32 E-value: 8.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1318 RNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAQQLVGV 1397
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
....*....
gi 29427672 1398 yKRDNRTKS 1406
Cdd:cd03272 234 -KFRNKVST 241
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
158-245 |
2.67e-15 |
|
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: 75.09 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 158 ELVLENFKSYAGKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQdrlsdlihKSEAFPSLQSCSVAVHFQ 237
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR--------RSGVKAGCIVAAVSAELI 72
|
....*...
gi 29427672 238 YVIDESSG 245
Cdd:cd03227 73 FTRLQLSG 80
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
156-312 |
2.33e-12 |
|
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: 68.44 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 156 INELVLENFKSYAGKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLIHKSeAFPSLQSCSVAVH 235
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEG-SGPSVMSAYVEII 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29427672 236 FqyviDESSGtsRIDEEKPGLIItRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQMK 312
Cdd:cd03272 80 F----DNSDN--RFPIDKEEVRL-RRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMK 149
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
341-627 |
7.74e-12 |
|
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: 70.05 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 341 EERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETAL------EFLEKEKQLTLLRSKLFQFKllQSNSKLASTLEKI 414
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWnkelksELKNQEKKLEEIQNQISQNN--KIISQLNEQISQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 415 SSSNKDLEDEKMKFQESLK----KVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKT 490
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 491 LKSTKHSISEAENMLEELRGQQTEHETEIKDLtqllekersilDDIKLSLKDKTKNISAEIIRHEKELEPWDLQLQEKES 570
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNL-----------DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 29427672 571 QIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDE 627
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
340-670 |
3.11e-11 |
|
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: 68.12 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 340 IEERMGQIENLNEVCLEKENRFEIVDREKNSLESG----------KETALEFLEKEKQLTLLRSKlfqfKLLQSNSKLAS 409
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESEnsekqreleeKQNEIEKLKKENQSYKQEIK----NLESQINDLES 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 410 TLEKISSSNKDLEDEKMKFQES----LKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKME 485
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEkellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 486 KAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQ---LLEKERSILDDIKLSLKDKTKNISAEIIRHEKELEPWD 562
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKkisSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 563 LqlqekESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKL 642
Cdd:TIGR04523 559 L-----EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
330 340
....*....|....*....|....*...
gi 29427672 643 KEMQKVLNAHRQRAMEARSSLSKAQNKS 670
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
156-238 |
1.60e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 59.25 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 156 INELVLENFKSYAGKQVVgPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRlSDLIHKSEAfpslqSCSVAVH 235
Cdd:COG0419 2 LLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLR-SDLINVGSE-----EASVELE 74
|
...
gi 29427672 236 FQY 238
Cdd:COG0419 75 FEH 77
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
872-1410 |
2.31e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.23 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 872 VHEMEEELKKLRDHEPDlESQISKAEMEADSLASELTlaeqQVKEAEMAYVKAVSDKAQLNvvmKNLERLRGEYNDLQSE 951
Cdd:PRK01156 321 INKYHAIIKKLSVLQKD-YNDYIKKKSRYDDLNNQIL----ELEGYEMDYNSYLKSIESLK---KKIEEYSKNIERMSAF 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 952 TKTKKEKIKGLQDEIMKIGG---IKLQMQNSKVESVCQKLDILVAKLKKVKSASKKSGGD----VVKFQKLLQNSERDVE 1024
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNeinVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIIN 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1025 LSSDELKVIEEQLKHTKLALAENDTNMNETLNLKVELK----EQSEQLKEQMEDMEESINEFKSIEIEMKNKLEKLNSLL 1100
Cdd:PRK01156 473 HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIK 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1101 TYIKS---EITQQ--EKGLNELSIRDVT--HTLGMLDDNKMDSVKEDVKNNQELDQEYRSCETQDESEIKDAETSCDNYH 1173
Cdd:PRK01156 553 NRYKSlklEDLDSkrTSWLNALAVISLIdiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1174 PM------------NIDETSDEVSRGIPRLS--EDELRELDVEL--IESKINELSYYVEETNVDIGVLEEYAR----RLA 1233
Cdd:PRK01156 633 NKyneiqenkilieKLRGKIDNYKKQIAEIDsiIPDLKEITSRIndIEDNLKKSRKALDDAKANRARLESTIEilrtRIN 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1234 EFKRRKLDLNNAVQKRDEVKEQLGILKKKRfdEFMAGFNIISMTLKEMYQMITMGGNAELELVD-SLDPFSEGVTFSVMP 1312
Cdd:PRK01156 713 ELSDRINDINETLESMKKIKKAIGDLKRLR--EAFDKSGVPAMIRKSASQAMTSLTRKYLFEFNlDFDDIDVDQDFNITV 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1313 PKKSW-RNITNLSGGEKTLSSLALVFALHKY--KPTPLYVMDEIDAALDFRNVSIVANYIKERTKNA----QFIVISLRN 1385
Cdd:PRK01156 791 SRGGMvEGIDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSsdipQVIMISHHR 870
|
570 580
....*....|....*....|....*
gi 29427672 1386 NMFELAQQLVGVYKRDNRTKSTTIK 1410
Cdd:PRK01156 871 ELLSVADVAYEVKKSSGSSKVIPLR 895
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1323-1400 |
4.51e-09 |
|
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: 56.87 E-value: 4.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29427672 1323 LSGGEKTLSSLALVFALhkyKPtPLYVMDEIDAALDFRNVSIVANYIKE-RTKNAQFIVISLRNNMFELAQQLVGVYKR 1400
Cdd:cd00267 81 LSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
406-672 |
5.71e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 406 KLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLE---ERTKNLVS 482
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 483 KMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQL--LEKERSILDDIKLSLKDKTKNISAEIIRHEKELEP 560
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 561 WDLQLQE---KESQIQLAESELSLLEETQAKLKKNVETLEEkILAKKTHKQELQDLILDL-KKKLNSLKDERSQGEKNFT 636
Cdd:PRK03918 326 IEERIKEleeKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIE 404
|
250 260 270
....*....|....*....|....*....|....*.
gi 29427672 637 SAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKV 672
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKCPV 440
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
304-627 |
1.20e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 304 EVENIAQMKPKAEKESDDGLLEYLEDIIGTANYKPLIEERMGQIENLNE------VC---LEKENRFEIVDREKNSLESG 374
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpVCgreLTEEHRKELLEEYTAELKRI 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 375 KETALEFLEKEKQL----TLLRSKLFQFKLLQSNSKLASTLEKISSSNK-----DLEDEKMKFQESLKKVDEIKAQRKEI 445
Cdd:PRK03918 465 EKELKEIEEKERKLrkelRELEKVLKKESELIKLKELAEQLKELEEKLKkynleELEKKAEEYEKLKEKLIKLKGEIKSL 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 446 KDRIsscsSKEKTLVLERRELEGTRVSLEERTKNLVSKME----KAEKTLKSTKHSISEAENMLEELRGQQTE---HETE 518
Cdd:PRK03918 545 KKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLELKDAEKElerEEKE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 519 IKDLTQLLEKERSILDDIKLSLKDKTKNISA-EIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLE 597
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
330 340 350
....*....|....*....|....*....|....*.
gi 29427672 598 EKILAKKTHKQELQDL------ILDLKKKLNSLKDE 627
Cdd:PRK03918 701 EELEEREKAKKELEKLekalerVEELREKVKKYKAL 736
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
473-630 |
3.07e-08 |
|
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: 56.09 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 473 LEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKlslkdKTKNISAeii 552
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYEA--- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29427672 553 rHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKkthKQELQDLILDLKKKLNSLKDERSQ 630
Cdd:COG1579 94 -LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAEREE 167
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
355-671 |
3.30e-08 |
|
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: 58.19 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 355 LEKENRFEIVDREKN-SLESGKETALEflEKEKQLTLL----RSKLFQF--KLLQSNSKLASTLEKISSSNKDLEDEKMK 427
Cdd:pfam05483 227 LEEEYKKEINDKEKQvSLLLIQITEKE--NKMKDLTFLleesRDKANQLeeKTKLQDENLKELIEKKDHLTKELEDIKMS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 428 FQESL---KKVDE--------IKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKH 496
Cdd:pfam05483 305 LQRSMstqKALEEdlqiatktICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 497 SISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDiklslKDKTKNISAEIIRHEKELEpwdLQLQEKESQIQLAE 576
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE-----KKQFEKIAEELKGKEQELI---FLLQAREKEIHDLE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 577 SELSLLEETQAKLKKNVETLEEKI------------------LAKKTHKQELQDLILDLKKKLNSLKDERSQGEK----- 633
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELekeklknieltahcdkllLENKELTQEASDMTLELKKHQEDIINCKKQEERmlkqi 536
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 29427672 634 -NFTSAHLKLK-EMQKVLNAHRQRAMEARSSLSKAQNKSK 671
Cdd:pfam05483 537 eNLEEKEMNLRdELESVREEFIQKGDEVKCKLDKSEENAR 576
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
272-632 |
3.45e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 272 INEKESSYTEVTKLLKNEGIDLDHKRflilqGEVENIaqmkpKAEKESDDGLLEYLEdiigtaNYKPLIEERMGQIENLN 351
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELR-----EELEKL-----EKEVKELEELKEEIE------ELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 352 EVCLEKENRFEIVDREKNSLESgKETALEFLeKEKQLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQES 431
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEE-KVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 432 LKKVDEIKAQRKEIKDRISSCSSKEKTLVlERRELEGTRVSLEERTKNLvsKMEKAEKTLKSTKHSISEAENMLEELRGQ 511
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 512 QTEHETEIKDLTQLLEK-----------ERSILDDIKLSLKDK----TKNISAEIIRHEKELEPWDLQLQEKESQIqLAE 576
Cdd:PRK03918 414 IGELKKEIKELKKAIEElkkakgkcpvcGRELTEEHRKELLEEytaeLKRIEKELKEIEEKERKLRKELRELEKVL-KKE 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 577 SELSLLEETQAKLKKNVETLE----EKILAKKTHKQELQDLILDLKKKLNSLKDERSQGE 632
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
154-650 |
3.55e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 154 LFINELVLENFKSYAGKQVVgpFHTSFSAVVGPNGSGKSNVIDSMLFVFgfrANKMRQDRLSDLIHKSEAfpslqscSVA 233
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMIKKGKN-------NLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 234 VHFQYVIDESSGTSRIDEEKPGLIITRKAF--KNNSSKYYINEKESSYTEVTKLLKNEGIDLDhkRFLILQGEVENIAQM 311
Cdd:PRK01156 69 VELEFRIGGHVYQIRRSIERRGKGSRREAYikKDGSIIAEGFDDTTKYIEKNILGISKDVFLN--SIFVGQGEMDSLISG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 312 KPKAEKESDDGLLEY---------LEDII-----GTANYKPLIEE---RMGQIENLNEVCLEKENRFEIVDREKNSLESg 374
Cdd:PRK01156 147 DPAQRKKILDEILEInslernydkLKDVIdmlraEISNIDYLEEKlksSNLELENIKKQIADDEKSHSITLKEIERLSI- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 375 ketalEFLEKEKQLTLLRSKLfqfkllqsnSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSS 454
Cdd:PRK01156 226 -----EYNNAMDDYNNLKSAL---------NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVY 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 455 KEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKS-------------TKHSISEAENMLEELRGQQTEHETEIKD 521
Cdd:PRK01156 292 KNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKlsvlqkdyndyikKKSRYDDLNNQILELEGYEMDYNSYLKS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 522 LTQLLEKERSILDDIK-----LSLKDKTKNISAEIIRheKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETL 596
Cdd:PRK01156 372 IESLKKKIEEYSKNIErmsafISEILKIQEIDPDAIK--KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEML 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 29427672 597 EEK----ILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLN 650
Cdd:PRK01156 450 NGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE 507
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
276-613 |
5.39e-08 |
|
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: 57.82 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 276 ESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQMKPKAEKesddglleylediIGTANYKPLIEERMGQIENLNEVCL 355
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK-------------LQMAEKDKVIEILRQQIENMTQLVG 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 356 EKENRFEIVDREKNSLEsgketaleflekeKQLTLLRSKLFQFKLLQSnsKLASTLEKISSSNKDLEDEKMKF----QES 431
Cdd:pfam15921 580 QHGRTAGAMQVEKAQLE-------------KEINDRRLELQEFKILKD--KKDAKIRELEARVSDLELEKVKLvnagSER 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 432 LKKVDEIKAQRKEIKDRISSCSSKEKTL-----VLER------RELEGTRVSLEERTKNLVSKMEKAEKTLKSTK----H 496
Cdd:pfam15921 645 LRAVKDIKQERDQLLNEVKTSRNELNSLsedyeVLKRnfrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgH 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 497 SISEAENMLEEL---RGQQTEHETEIKDLTQLL---EKERSILDDIKLSLKDKTKNISAEIIRHEKELEPWDLQ---LQE 567
Cdd:pfam15921 725 AMKVAMGMQKQItakRGQIDALQSKIQFLEEAMtnaNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQerrLKE 804
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 29427672 568 KESQIQLAESELSL-LEETQAKLKKNVetlEEKILAKKTHKQELQDL 613
Cdd:pfam15921 805 KVANMEVALDKASLqFAECQDIIQRQE---QESVRLKLQHTLDVKEL 848
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
161-666 |
1.23e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 161 LENFKSYAGKQVvgPFHTSFSAVVGPNGSGKSNVIDSMLF-VFGFRAnkmRQDRLSDLIHKSEafpslQSCSVAVHF--- 236
Cdd:PRK02224 8 LENFKCYADADL--RLEDGVTVIHGVNGSGKSSLLEACFFaLYGSKA---LDDTLDDVITIGA-----EEAEIELWFeha 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 237 --QYVID-------ESSGTSRIDEEKPGLIItrkafknnsskyyiNEKESSYTEVTKLLKnegidLDHKRFL----ILQG 303
Cdd:PRK02224 78 ggEYHIErrvrlsgDRATTAKCVLETPEGTI--------------DGARDVREEVTELLR-----MDAEAFVncayVRQG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 304 EVENIAQMKPKAEKESDDGLLEY--LEDIIGTANY-----KPLIEERMGQIENLNEVCLEKE--------NRFEI----V 364
Cdd:PRK02224 139 EVNKLINATPSDRQDMIDDLLQLgkLEEYRERASDarlgvERVLSDQRGSLDQLKAQIEEKEekdlherlNGLESelaeL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 365 DREKNSLESGKETALEFLEkEKQLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKE 444
Cdd:PRK02224 219 DEEIERYEEQREQARETRD-EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 445 IKDRISSCSSKEKTLVLERRELEG-----------TRVS-----------------LEERTKNLVSKMEKAEKTLKSTKH 496
Cdd:PRK02224 298 LLAEAGLDDADAEAVEARREELEDrdeelrdrleeCRVAaqahneeaeslredaddLEERAEELREEAAELESELEEARE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 497 SISEAENMLEELRGQQTEHE-------TEIKDLTQLLEKERSILDDIKLSLKDKTKNIS--AEIIRHEKEL--------- 558
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRtaRERVEEAEALleagkcpec 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 559 ------EPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEkilakkthKQELQDLILDLKKKLNSLKDERSQGE 632
Cdd:PRK02224 458 gqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED--------LVEAEDRIERLEERREDLEELIAERR 529
|
570 580 590
....*....|....*....|....*....|....
gi 29427672 633 KNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKA 666
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
433-682 |
2.74e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 433 KKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQ 512
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 513 TEHETEIKDLTQLLEKeRSILDDIKLSLKDKTKNISAEIIRHEKELEPWDLQLQEKesqiqlaeselslLEETQAKLKKN 592
Cdd:COG4942 100 EAQKEELAELLRALYR-LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE-------------LRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 593 VETLEEKILAKKTHKQELQDLildlKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKV 672
Cdd:COG4942 166 RAELEAERAELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|
gi 29427672 673 LTALSRLQKS 682
Cdd:COG4942 242 RTPAAGFAAL 251
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1314-1382 |
3.95e-07 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 52.22 E-value: 3.95e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29427672 1314 KKSWRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTK---NAQFIVIS 1382
Cdd:cd03276 101 KAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKkqpGRQFIFIT 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
345-627 |
5.98e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 345 GQIENLNEVCLEKENRFEIVDREKNSLESGKETAL-EFLEKEKQLTLLRSKLFQFKLL--------QSNSKLASTLEKIS 415
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEkEKLNIQKNIDKIKNKLLKLELLlsnlkkkiQKNKSLESQISELK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 416 SSNKDLEDEKMKFQESL-KKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNL--------VSKMEK 486
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEInEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlkseisDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 487 AEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQL---LEKERSILDDIKLSL---------------------KD 542
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisqLKKELTNSESENSEKqreleekqneieklkkenqsyKQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 543 KTKNISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLE-------ETQAKLKKNVETLEEKILAKKTHKQELQDLIL 615
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEkeierlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
330
....*....|..
gi 29427672 616 DLKKKLNSLKDE 627
Cdd:TIGR04523 465 SLETQLKVLSRS 476
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
309-671 |
8.26e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 309 AQMKPKAEKESDDGLLEYLEDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDR--EKNSLESGKETALEFLEKE- 385
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeEKKKADEAKKKAEEAKKADe 1448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 386 -KQLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERR 464
Cdd:PTZ00121 1449 aKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 465 ELEGTRVSLEERTKNLVSKME---KAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSL- 540
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADelkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMk 1608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 541 -----KDKTKNISAEIIRHEKELEPWDLQLQEKESQiQLAESELSLLEETQAKLKKnvETLEEKILAKKTHKQELQDLIL 615
Cdd:PTZ00121 1609 aeeakKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-EKKKAEELKKAEEENKIKA--AEEAKKAEEDKKKAEEAKKAEE 1685
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 29427672 616 DLKKKLNSLKDERSQGEKnftSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSK 671
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKK---AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
395-621 |
9.76e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 395 LFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISscsskekTLVLERRELEGTRVSLE 474
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 475 ERTKNLVSKMEKAEKTLKSTKHSISE---------AENMLEELRGQQ--TEHETEIKDLTQLLEKERSILDDIKLSLKDK 543
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAEllralyrlgRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29427672 544 TKNIsAEIIRHEKELEpwdLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKL 621
Cdd:COG4942 163 AALR-AELEAERAELE---ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
372-599 |
1.06e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 372 ESGKETALEFLekekqLTLLRSKLFQ-----FKLLQSNSKLAST-LEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEI 445
Cdd:COG4717 33 EAGKSTLLAFI-----RAMLLERLEKeadelFKPQGRKPELNLKeLKELEEELKEAEEKEEEYAELQEELEELEEELEEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 446 KDRISSCSSKEKTL--VLERRELEGTRVSLEERTKNLVSKMEKAEKTLKStkhsISEAENMLEELRGQQTEHETEIKDLT 523
Cdd:COG4717 108 EAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29427672 524 QLLEKErsilddiklslkdktknISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEK 599
Cdd:COG4717 184 EQLSLA-----------------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
362-647 |
1.31e-06 |
|
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: 53.19 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 362 EIVDREKNSLESGKETALEFLEKEKQLTLLRSKLFQfKLLQSNSKLASTLEKISSSNKDLEDE-----------KMKFQE 430
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ-ELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnllKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 431 SLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERREL----EGTRVSLEERTKNLVSKMEKAEKTLKStkhSISEAENMLE 506
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELrvqaENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 507 ELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIRHE---KELEPWDLQLQEKESQIQLAESELSLLE 583
Cdd:pfam05483 244 LLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDhltKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29427672 584 ETQAKLKKNVET-LEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQK 647
Cdd:pfam05483 324 KTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
413-650 |
1.33e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 413 KISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLK 492
Cdd:TIGR04523 55 ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 493 STKHSISEAENMLEELRGQQTEHETEIKDLTQL---LEKERSILDDIKLSLKDKTKNISAEIIRHEKELepwdLQLQEKE 569
Cdd:TIGR04523 135 ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQkeeLENELNLLEKEKLNIQKNIDKIKNKLLKLELLL----SNLKKKI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 570 SQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVL 649
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
.
gi 29427672 650 N 650
Cdd:TIGR04523 291 N 291
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
390-630 |
1.33e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.01 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 390 LLRSKLFQFKLLQSNSKLASTLEKISSSNK----DLEDEKMkfQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRE 465
Cdd:PRK05771 1 LAPVRMKKVLIVTLKSYKDEVLEALHELGVvhieDLKEELS--NERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 466 LEgtRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQqtehETEIK-------DLTQLLEKER------SI 532
Cdd:PRK05771 79 VS--VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE----IERLEpwgnfdlDLSLLLGFKYvsvfvgTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 533 LDDIKLSLKDKTKNISAEIIRHEKELEP---WDLQLQEKESQIQLAESELSLLEEtqaklkKNVETLEEKILAKKTHKQE 609
Cdd:PRK05771 153 PEDKLEELKLESDVENVEYISTDKGYVYvvvVVLKELSDEVEEELKKLGFERLEL------EEEGTPSELIREIKEELEE 226
|
250 260
....*....|....*....|.
gi 29427672 610 LQDLILDLKKKLNSLKDERSQ 630
Cdd:PRK05771 227 IEKERESLLEELKELAKKYLE 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
505-665 |
1.64e-06 |
|
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: 50.69 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 505 LEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKNISaeiiRHEKELEPWDLQLQEKESQIQLAES--ELSLL 582
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK----RLELEIEEVEARIKKYEEQLGNVRNnkEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 583 EETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAhlkLKEMQKVLNAHRQRAMEARSS 662
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELAAK 171
|
...
gi 29427672 663 LSK 665
Cdd:COG1579 172 IPP 174
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
155-443 |
1.81e-06 |
|
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: 51.83 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 155 FINELVLENFKSYagKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLIHKsEAFPSLQSCSVAV 234
Cdd:pfam13175 2 KIKSIIIKNFRCL--KDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKD-VIKIDKEDLNIFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 235 HFQYVIDES---------SGTSRID------EEKPGLIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFL 299
Cdd:pfam13175 79 NISFSIDIEidvefllilFGYLEIKkkylclASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYIYNNYYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 300 ILQGEVENIAQMKPKAEKESDDGLLEYLEDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETAL 379
Cdd:pfam13175 159 DEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHENVLENLQIKKLLISADRNASDEDSEKIN 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29427672 380 EFLEKEKQLTllrSKLFQFKLLQSNSKLASTLEKISSSNKDLEDE-KMKFQESLKKVDEIKAQRK 443
Cdd:pfam13175 239 SLLGALKQRI---FEEALQEELELTEKLKETQNKLKEIDKTLAEElKNILFKKIDKLKDFGYPPF 300
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
430-685 |
1.89e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 430 ESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMekaeKTLKSTKHSISEaenMLEELR 509
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEA----QELREKRDELNE---KVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 510 GQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKtKNISAEIIRHEKELEPWDL----------QLQEKESQIQLAESEL 579
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSI-DKLRKEIERLEWRQQTEVLspeeekelveKIKELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 580 SLLEETQ------AKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHL------------- 640
Cdd:COG1340 157 EKNEKLKelraelKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEkadelheeiielq 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29427672 641 -KLKEMQKVLNAHRQRAMEARSSLSKAQNKSKVLTALSRLQKSGRI 685
Cdd:COG1340 237 kELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
159-658 |
2.02e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 159 LVLENFKSYAGKQVV--GPFHTSFsAVVGPNGSGKSNVIDSMLFVF----GFRANKMRQDRLSDLIHKSEAFPSLQscsV 232
Cdd:TIGR00618 6 LTLKNFGSYKGTHTIdfTALGPIF-LICGKTGAGKTTLLDAITYALygklPRRSEVIRSLNSLYAAPSEAAFAELE---F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 233 AVHFQYVIDESSGTSRIDEEKPGLIITRKAFKNNSSKYYINEKESSYTEV-TKLLKnegidLDHKRF----LILQGEVEN 307
Cdd:TIGR00618 82 SLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEViHDLLK-----LDYKTFtrvvLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 308 IAQMKPKAEKESddglleyLEDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETALEFLEKEkq 387
Cdd:TIGR00618 157 FLKAKSKEKKEL-------LMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKE-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 388 LTLLRSKLFQFKllQSNSKLASTLEKISSSNKdLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKtLVLERRELE 467
Cdd:TIGR00618 228 LKHLREALQQTQ--QSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP-LAAHIKAVT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 468 GTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKdLTQLLEKERSILD--DIKLSLKDKTK 545
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH-IRDAHEVATSIREisCQQHTLTQHIH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 546 NIsAEIIRHEKELE----PWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQ-ELQDLILD--LK 618
Cdd:TIGR00618 383 TL-QQQKTTLTQKLqslcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITcTAQCEKLEkiHL 461
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 29427672 619 KKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAME 658
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE 501
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
156-201 |
4.54e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 50.70 E-value: 4.54e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 29427672 156 INELVLENFKSYagKQVVGPFHtSFSAVVGPNGSGKSNVIDSMLFV 201
Cdd:COG4637 2 ITRIRIKNFKSL--RDLELPLG-PLTVLIGANGSGKSNLLDALRFL 44
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
155-328 |
4.65e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 50.43 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 155 FINELVLENFKSYAGKQVV-----GPFHTSFSAVVGPNGSGKSNVIDSMLFVFGF-RANKMRQDRLSD---LIHKSEAFP 225
Cdd:COG1106 1 MLISFSIENFRSFKDELTLsmvasGLRLLRVNLIYGANASGKSNLLEALYFLRNLvLNSSQPGDKLVEpflLDSESKNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 226 SlqscSVAVHF-----QYVIDESSGTSRIDEE---------KPGLIITRKAFKNNSSKYYINEKESSYT----------- 280
Cdd:COG1106 81 S----EFEILFlldgvRYEYGFELDKERIISEwlyflstaaQLNVPLLSPLYDWFDNNISLDTSSDGLTlllkedeslke 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29427672 281 EVTKLLKNegIDLDHKRFLILQGEVENIAQMKPKAEKESDDGLLEYLE 328
Cdd:COG1106 157 ELLELLKI--ADPGIEDIEVEEEEIEDLVERKLIFKHKGGNVPLPLSE 202
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
237-923 |
6.92e-06 |
|
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: 50.89 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 237 QYVIDESSGTSRIDEEKPGLIITRKAFKN------NSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLIL--QGEVENI 308
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDAMADIRRRESQsqedlrNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLshEGVLQEI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 309 AQMKPKAEKESDDGLLEYleDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETALEFL------ 382
Cdd:pfam15921 190 RSILVDFEEASGKKIYEH--DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLlqqhqd 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 383 -------EKEKQLTLLRSKLFQFKLlQSNSkLASTLEKISSSNKDLEDEKMKFQESLKK-VDEIKAQRKEIK----DRIS 450
Cdd:pfam15921 268 rieqlisEHEVEITGLTEKASSARS-QANS-IQSQLEIIQEQARNQNSMYMRQLSDLEStVSQLRSELREAKrmyeDKIE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 451 SCsskEKTLVLERRELEGTRV---SLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLtqlle 527
Cdd:pfam15921 346 EL---EKQLVLANSELTEARTerdQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL----- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 528 keRSILDDIKLSLKDKTKNISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHK 607
Cdd:pfam15921 418 --RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 608 QELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNA--HRQRAMEARSSLS-KAQNKSKVLTAL-SRLQKSG 683
Cdd:pfam15921 496 RTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdHLRNVQTECEALKlQMAEKDKVIEILrQQIENMT 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 684 RINGFHGR----------------------LGDLGVIDDSFDVAISTACPRLDDVVVDTVECAQHCIDYLRKNK-LGYAR 740
Cdd:pfam15921 576 QLVGQHGRtagamqvekaqlekeindrrleLQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKdIKQER 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 741 FILLDRLRQFNLQPISTPENvprlfdlvkpknpkfsnafYSVLRDTLvaQNLKQANNVAYGKKRFRVVTVDGKLIDISGT 820
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSED-------------------YEVLKRNF--RNKSEEMETTTNKLKMQLKSAQSELEQTRNT 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 821 ---MSGGGNH---VAKGLMKLGTNQSDKVD------DYTPEEVDKIERE---LSERENNFRVASDTV----HEMEEELKK 881
Cdd:pfam15921 715 lksMEGSDGHamkVAMGMQKQITAKRGQIDalqskiQFLEEAMTNANKEkhfLKEEKNKLSQELSTVatekNKMAGELEV 794
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 29427672 882 LRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEMAYVK 923
Cdd:pfam15921 795 LRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
346-623 |
2.99e-05 |
|
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: 48.48 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 346 QIENLNEVCLEKENRFEIVDREKNSLESGKETALEFLEKEK-QLTLLRSKLFQFKLL---------QSNSKLASTLEKIS 415
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNsEIKDLTNQDSVKELIiknldntreSLETQLKVLSRSIN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 416 SSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKStk 495
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-- 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 496 hsiseaENMLEELRGQQTEHEtEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIRHEKELEPWDLQLQEKESQIQLA 575
Cdd:TIGR04523 557 ------ENLEKEIDEKNKEIE-ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 29427672 576 ESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNS 623
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
427-671 |
3.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 427 KFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLvleRRELEgtrvSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLE 506
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEEL---NEEYN----ELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 507 E-LRGQQTEHETeIKDLTQLLEKErSILDDIklslkDKTKNISAeIIRHEKELepwdlqLQEKESQIQLAESELSLLEET 585
Cdd:COG3883 90 ErARALYRSGGS-VSYLDVLLGSE-SFSDFL-----DRLSALSK-IADADADL------LEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 586 QAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSK 665
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
....*.
gi 29427672 666 AQNKSK 671
Cdd:COG3883 236 AAAAAA 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
399-633 |
3.96e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 399 KLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRIsscSSKEKTLVLERRELEGTRVSLEERTK 478
Cdd:pfam01576 16 KVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARL---AARKQELEEILHELESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 479 NLVSKMEKAEKTLKSTKHSISEAE------------------------NMLE------------------ELRGQQTEHE 516
Cdd:pfam01576 93 QLQNEKKKMQQHIQDLEEQLDEEEaarqklqlekvtteakikkleediLLLEdqnsklskerklleerisEFTSNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 517 TEIKDLTQLLEKERSILDDIKLSLKDKTKN-ISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLL---EETQAKLKKN 592
Cdd:pfam01576 173 EKAKSLSKLKNKHEAMISDLEERLKKEEKGrQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAkkeEELQAALARL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 29427672 593 VETLEEKILAKKTHKqELQDLILDLKKKLNSLKDERSQGEK 633
Cdd:pfam01576 253 EEETAQKNNALKKIR-ELEAQISELQEDLESERAARNKAEK 292
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
159-352 |
5.22e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 45.56 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 159 LVLENFKSYAGKQVvgPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLIHKSEAFPSL--QSCSVAVHF 236
Cdd:pfam13476 1 LTIENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEgkGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 237 QYVIDESSGTSRIDEEkpglIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLIlQGEVENIAQMKPKAE 316
Cdd:pfam13476 79 ENNDGRYTYAIERSRE----LSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLG-QEREEEFERKEKKER 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 29427672 317 KESDDGLLEYLEDIIGTANYKPLIEERMGQIENLNE 352
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
183-616 |
6.87e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 183 VVGPNGSGKSNVIDSMLFV-FG--FRanKMRQDRLSDLIHKSEafpslqsCSVAVHFQYVIDEssgtsrideekpgLIIT 259
Cdd:PHA02562 32 ITGKNGAGKSTMLEALTFAlFGkpFR--DIKKGQLINSINKKD-------LLVELWFEYGEKE-------------YYIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 260 RkAFKNNSSKYYINEK---ESSYTEVTkllknegidldhkrflilQGEVENIAQMKPKAEKESDdglleyledIIGTANY 336
Cdd:PHA02562 90 R-GIKPNVFEIYCNGKlldESASSKDF------------------QKYFEQMLGMNYKSFKQIV---------VLGTAGY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 337 KPLIE----ERMGQIENLNEVC----LEKENRFEIvdREKNSlesgketalEFLEKEKQLTLLRSKLFQFKLLQSNSKla 408
Cdd:PHA02562 142 VPFMQlsapARRKLVEDLLDISvlseMDKLNKDKI--RELNQ---------QIQTLDMKIDHIQQQIKTYNKNIEEQR-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 409 stlekiSSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSS--KEKTLVLERRELEGTRVSLEERTKNLVSKMEK 486
Cdd:PHA02562 209 ------KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMdiEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 487 AEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDI------KLSLKDKTKNISAEIIRHEKELEP 560
Cdd:PHA02562 283 KGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFneqskkLLELKNKISTNKQSLITLVDKAKK 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 29427672 561 WDLQLQEKESQIQLAESELSLLeetQAKLKKNVETLEEKILaKKTHKQELQDLILD 616
Cdd:PHA02562 363 VKAAIEELQAEFVDNAEELAKL---QDELDKIVKTKSELVK-EKYHRGIVTDLLKD 414
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1285-1382 |
7.24e-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: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1285 ITMGGNAELELVDSL------DPFSEgvtFSVMPPKK---SWRNITNL--------SGGEKTLSSLALVFALHKYKPTPL 1347
Cdd:cd03277 75 IELYGNPGNIQVDNLcqflpqDRVGE---FAKLSPIEllvKFREGEQLqeldphhqSGGERSVSTMLYLLSLQELTRCPF 151
|
90 100 110
....*....|....*....|....*....|....*...
gi 29427672 1348 YVMDEIDAALDFRNVSIVANYIKE---RTKNAQFIVIS 1382
Cdd:cd03277 152 RVVDEINQGMDPTNERKVFDMLVEtacKEGTSQYFLIT 189
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
340-628 |
7.36e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 340 IEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETALEFLEKEKQ-LTLLRSKLfqfKLLQSNSKLASTLE---KIS 415
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRErEAELEATL---RTARERVEEAEALLeagKCP 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 416 SSNKDLEDEKM--KFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVlERRELEGTRVSLEERTKNLVSKMEKAEKTlks 493
Cdd:PRK02224 456 ECGQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRET--- 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 494 tkhsISEAENMLEELRGQQTEHETE-------------------------------IKDLTQLLEKERSILDDIK----- 537
Cdd:PRK02224 532 ----IEEKRERAEELRERAAELEAEaeekreaaaeaeeeaeeareevaelnsklaeLKERIESLERIRTLLAAIAdaede 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 538 -LSLKDKTKNIsAEIIRHEKElepwdlQLQEKESQIQLAESEL--SLLEETQAKLKKNVETLE---EKILAKKTHKQELQ 611
Cdd:PRK02224 608 iERLREKREAL-AELNDERRE------RLAEKRERKRELEAEFdeARIEEAREDKERAEEYLEqveEKLDELREERDDLQ 680
|
330 340
....*....|....*....|
gi 29427672 612 DLILDLK---KKLNSLKDER 628
Cdd:PRK02224 681 AEIGAVEnelEELEELRERR 700
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
156-222 |
1.01e-04 |
|
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: 44.91 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29427672 156 INELVLENFKSYAGKQVVgPFHTSFSAVVGPNGSGKSNVIDSMLFV-FG-FRANKMRQDRLSDLIHKSE 222
Cdd:cd03240 1 IDKLSIRNIRSFHERSEI-EFFSPLTLIVGQNGAGKTTIIEALKYAlTGeLPPNSKGGAHDPKLIREGE 68
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
155-224 |
1.15e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 45.92 E-value: 1.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29427672 155 FINELVLENFKSYAGKQVvgPFHTSFSAVVGPNGSGKSNVIDSM-LFVFG--FRANkmrqdRLSDLIHKSEAF 224
Cdd:COG1195 1 RLKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEAIyLLATGrsFRTA-----RDAELIRFGADG 66
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
456-675 |
1.43e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 456 EKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKS--TKHSISEAE-------NMLEELRGQQTEHETEIKDLTQLL 526
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSeeaklllQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 527 EKERSILDDIKLSLKDKTKN-----ISAEIIRHEKELEPWDLQLQEKESQIQLAESEL-SLLEETQAKLKKNVETLEEKI 600
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSpviqqLRAQLAELEAELAELSARYTPNHPDVIALRAQIaALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29427672 601 LAKKTHKQELQDLILDLKKKLNSLKD---ERSQGEKNFTSAhlklkemQKVLNAHRQRAMEARSSLSKAQNKSKVLTA 675
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPEleaELRRLEREVEVA-------RELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
357-1143 |
1.44e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 357 KENRFEIVDREkNSLESGKETALEFLEKEKQLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVD 436
Cdd:TIGR00606 258 EHNLSKIMKLD-NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 437 EIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERtknlvSKMEKAEKTLKSTKhsisEAENMLE-ELRGQQTEH 515
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATR-----LELDGFERGPFSER----QIKNFHTlVIERQEDEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 516 ETEIKDLTQLLEKERSI---LDDIKLSLKDKTKNISAEIIRHEKELEpwdlQLQEKESQIQLAESELSLLEETQAKLKKN 592
Cdd:TIGR00606 408 KTAAQLCADLQSKERLKqeqADEIRDEKKGLGRTIELKKEILEKKQE----ELKFVIKELQQLEGSSDRILELDQELRKA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 593 VETLEekilakkthKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKV 672
Cdd:TIGR00606 484 ERELS---------KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 673 ltalsRLQKSGRINGFHGRLGDLGVIDDSFdvaistacprlddvvvdtvecaqhcidylrkNKLGYARFILLDRLRQFNL 752
Cdd:TIGR00606 555 -----KSRHSDELTSLLGYFPNKKQLEDWL-------------------------------HSKSKEINQTRDRLAKLNK 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 753 QPISTPENVPRLFDLVKPKNPKFSNafysvLRDTLVAQNLKQANNVAYGKKRFRVVTVDGKLIDISGTMSGGGNHVakgl 832
Cdd:TIGR00606 599 ELASLEQNKNHINNELESKEEQLSS-----YEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFI---- 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 833 mklgTNQSDKVDDYTP--EEVDKIERELSE----RENNFRVASDTVHEMEEELKKLrdhEPDLESQISKAEMEadslASE 906
Cdd:TIGR00606 670 ----TQLTDENQSCCPvcQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKK---EKRRDEMLGLAPGR----QSI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 907 LTLAEQQVKEAEMAYVKAVSDKAQLNVVMKNLERLRGEYNDLQSETKTKKEKIKGLQDEIMKIGGIKLQMQNSKVESVCQ 986
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 987 KLDILVAKLKKVKSASKKsggdvvKFQKLLQNSERDVELSSDElkviEEQLKHTKlalaendTNMNETLNLKVELKEQSE 1066
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQH------ELDTVVSKIELNRKLIQDQ----QEQIQHLK-------SKTNELKSEKLQIGTNLQ 881
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29427672 1067 QLKEQMEDMEESINEFKSIEIEMKNKLEKLNSLLTYIKSEITQQEKGLNElsirdvTHTLGMLDDNKMDSVKEDVKN 1143
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS------KETSNKKAQDKVNDIKEKVKN 952
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
346-553 |
1.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 346 QIENLNEVclekENRFEIVDREKNSLESGKETALEFLEKEKQLTL---LRSKLFQFKLLQSNSKLASTLEKISSSNKDLE 422
Cdd:COG4913 233 HFDDLERA----HEALEDAREQIELLEPIRELAERYAAARERLAEleyLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 423 DEKMKFQESLK----KVDEIKAQRKEIK-DRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHS 497
Cdd:COG4913 309 AELERLEARLDalreELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29427672 498 ISEAENMLEELRGQQTEHETEIKD-LTQLLEKERSILDDIKlSLKDKTKNISAEIIR 553
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAaLRDLRRELRELEAEIA-SLERRKSNIPARLLA 444
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
397-587 |
1.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 397 QFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRIsscsSKEKTLVLERRELEGTRVSLEER 476
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----AEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 477 TKN----------------LVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQL---LEKERSILDDIK 537
Cdd:COG3883 98 SGGsvsyldvllgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALkaeLEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29427672 538 LSLKDKTKNISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQA 587
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
472-687 |
1.95e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 472 SLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDiklsLKDKTKNISAEI 551
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE----RREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 552 IRHEKELEPWDLQLQEKE-----SQI----QLAESELSLLEETQAkLKKNVETLEEKILAKKthkQELQDLILDLKKKLN 622
Cdd:COG3883 96 YRSGGSVSYLDVLLGSESfsdflDRLsalsKIADADADLLEELKA-DKAELEAKKAELEAKL---AELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29427672 623 SLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKVLTALSRLQKSGRING 687
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1010-1382 |
2.45e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1010 VKFQKLLQNSERDVELSS--DELKVIEEQLKHTKLALAENDTNMNETLNLKV-ELKEQSEQLKEQMEDMEESINEFKSIE 1086
Cdd:PRK03918 483 RELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEIKSLKKELEKLEELKKKLAELE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1087 IEMKNKLEKLNSLLTYIKseitqqEKGLNelSIRDVTHTLGMLDD--NKMDSVKEDVKNNQELDQEYRSCETQ-DESEIK 1163
Cdd:PRK03918 563 KKLDELEEELAELLKELE------ELGFE--SVEELEERLKELEPfyNEYLELKDAEKELEREEKELKKLEEElDKAFEE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1164 DAETSCDnyhpmnIDETSDEVSRGIPRLSEDELRELDVELIEsKINELSYYVEEtnvdigvLEEYARRLAEFKRRKLDLN 1243
Cdd:PRK03918 635 LAETEKR------LEELRKELEELEKKYSEEEYEELREEYLE-LSRELAGLRAE-------LEELEKRREEIKKTLEKLK 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1244 NAVQKRDEVKEQLGILKK---------KRFDEFMA-----GFNIISMTLKEMYQMITMGGNAELELVDSldpfSEGVTFS 1309
Cdd:PRK03918 701 EELEEREKAKKELEKLEKalerveelrEKVKKYKAllkerALSKVGEIASEIFEELTEGKYSGVRVKAE----ENKVKLF 776
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29427672 1310 VMPPKKSwRNITNLSGGEKTLSSLALVFALHKYK--PTPLYVMDEIDAALD----FRNVSIVANYIKertKNAQFIVIS 1382
Cdd:PRK03918 777 VVYQGKE-RPLTFLSGGERIALGLAFRLALSLYLagNIPLLILDEPTPFLDeerrRKLVDIMERYLR---KIPQVIIVS 851
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
327-676 |
2.51e-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: 45.48 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 327 LEDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETALEFLEKE-------------------KQ 387
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEihdleiqltaiktseehylKE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 388 LTLLRSKLFQFKLlqSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDE----IKAQRKEIKDRISSCSSKEKTLvleR 463
Cdd:pfam05483 473 VEDLKTELEKEKL--KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEdiinCKKQEERMLKQIENLEEKEMNL---R 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 464 RELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELrgqqtehETEIKDLTQLLEKERSILDDIKLSLKDK 543
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL-------ENKCNNLKKQIENKNKNIEELHQENKAL 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 544 TKNISAEiirhEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLns 623
Cdd:pfam05483 621 KKKGSAE----NKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEI-- 694
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29427672 624 lkDERSQGeknftsahlKLKEMQKVLNAHRQ---RAMEARSS-----LSKAQNKSKVLTAL 676
Cdd:pfam05483 695 --DKRCQH---------KIAEMVALMEKHKHqydKIIEERDSelglyKNKEQEQSSAKAAL 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1098 |
2.52e-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: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 868 ASDTVHEMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEMAYVKAvsdKAQLNVVMKNLERLRGEYND 947
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL---EQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 948 LQSETKTKKEKIKGLQDEIMKIG---GIKLQMQNSKVESVCQKLDILvaklKKVKSASKKSGGDVVKFQKLLQNSERDVE 1024
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGrqpPLALLLSPEDFLDAVRRLQYL----KYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29427672 1025 LSSDELKVIEEQLKHTKLALAENDTNMNETLN-LKVELKEQSEQLKEQMEDMEESINEFKSIEIEMKNKLEKLNS 1098
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLArLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
498-945 |
2.61e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 498 ISEAENMLEELRGQQTEHETEIKDLTQLLEKERSilddiklsLKDKTKNISAEIIRHEKELEPWDLQLQEKEsqiqlAES 577
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEE--------LEAELEELREELEKLEKLLQLLPLYQELEA-----LEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 578 ELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSL----KDERSQGEKNFTSAHLKLKEMQKVLNAHR 653
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 654 QRAMEARSSLSKAQNKSKVLTALSRLQKSGRINGFHGRLGDLGVIDDSFDVAISTACPRLddvvvdTVECAQHCIDYLRK 733
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL------FLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 734 NKLGYARFILLDRLRQFNLQPISTPENVPRLFDLVkPKNPKFSNAFYSVLRDTLvaQNLKQANNVAygKKRFRVVTVDGK 813
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAAL-GLPPDLSPEELLELLDRI--EELQELLREA--EELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 814 LIDISGTMSGGGNHVAKGLMKLGTNQSDKVDDYtpEEVDKIERELSERENNFRVASDT----------------VHEMEE 877
Cdd:COG4717 369 EQEIAALLAEAGVEDEEELRAALEQAEEYQELK--EELEELEEQLEELLGELEELLEAldeeeleeeleeleeeLEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 878 ELKKLRDHEPDLESQISkaEMEADSLASELtLAEQQVKEAEMAYV--KAVSDKAQLNVVMKNLERLRGEY 945
Cdd:COG4717 447 ELEELREELAELEAELE--QLEEDGELAEL-LQELEELKAELRELaeEWAALKLALELLEEAREEYREER 513
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1322-1390 |
3.53e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 43.28 E-value: 3.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1322 NLSGGEKTLSSLALVFALhkyKPTpLYVMDEIDAALDFRNVSIVANYIKE-RTKNAQFIVISLRNNMFEL 1390
Cdd:cd03217 104 GFSGGEKKRNEILQLLLL---EPD-LAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLLDY 169
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
154-219 |
3.96e-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: 44.27 E-value: 3.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29427672 154 LFINELVLENFKSYAgkQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDrlSDLIH 219
Cdd:TIGR00611 1 MYLSRLELTDFRNYD--AVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTSRD--KPLIR 62
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1256-1381 |
4.15e-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: 42.81 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1256 LGILKKKRFDEFMAGFNIISMTLKEMYQMITMGGNAeLELVDsLDPFSEgvtfsvmppkkswRNITNLSGGEKTLSSLAL 1335
Cdd:cd03214 46 AGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQA-LELLG-LAHLAD-------------RPFNELSGGERQRVLLAR 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 29427672 1336 VFAlhkyKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVI 1381
Cdd:cd03214 111 ALA----QEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVV 152
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
159-237 |
5.02e-04 |
|
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: 43.03 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 159 LVLENFKSYAGKQVV---GPFHTSFSAVVGPNGSGKSNVIDSMLF-VFGFRANKMRQDRLSDLIHKSEafpslQSCSVAV 234
Cdd:cd03279 6 LELKNFGPFREEQVIdftGLDNNGLFLICGPTGAGKSTILDAITYaLYGKTPRYGRQENLRSVFAPGE-----DTAEVSF 80
|
...
gi 29427672 235 HFQ 237
Cdd:cd03279 81 TFQ 83
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
457-930 |
6.58e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 457 KTLVLERRELEgtrvsleERTKNLVSKMEkaekTLKSTKHSISEAE---NMLEELRGQQTEHETEIKDLtQLLEKERSIL 533
Cdd:COG4913 214 REYMLEEPDTF-------EAADALVEHFD----DLERAHEALEDAReqiELLEPIRELAERYAAARERL-AELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 534 DDIKLSLKDKTknISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLK-KNVETLEEKILAKKTHKQELQD 612
Cdd:COG4913 282 RLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 613 LILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAM----EARSSLSKAQNKSKVLTA-LSRLQKsgRING 687
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELEAeIASLER--RKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 688 FHGRLgdlgvidDSFDVAISTACPRLDD---VVVDTVECAQHCID-------YLRknklGYARFILLD--RLRQFNlqpi 755
Cdd:COG4913 438 IPARL-------LALRDALAEALGLDEAelpFVGELIEVRPEEERwrgaierVLG----GFALTLLVPpeHYAAAL---- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 756 stpENVPRL-------FDLVKPKNPKFSNAfySVLRDTLVAQnLKQANNVAYG------KKRFRVVTVD--------GKL 814
Cdd:COG4913 503 ---RWVNRLhlrgrlvYERVRTGLPDPERP--RLDPDSLAGK-LDFKPHPFRAwleaelGRRFDYVCVDspeelrrhPRA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 815 IDISGTMSGGGNHVAKGLMK-------LGTNQSDK-----------------------------------------VDDY 846
Cdd:COG4913 577 ITRAGQVKGNGTRHEKDDRRrirsryvLGFDNRAKlaaleaelaeleeelaeaeerlealeaeldalqerrealqrLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 847 TPEEVD--KIERELSEREN---NFRVASDTVHEMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEMAY 921
Cdd:COG4913 657 SWDEIDvaSAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
....*....
gi 29427672 922 VKAVSDKAQ 930
Cdd:COG4913 737 EAAEDLARL 745
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
375-675 |
7.20e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 375 KETALEFLEKEKqlTLLRSKLFQFKL-LQSNSKLASTLEKISSS-NKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSC 452
Cdd:pfam01576 564 KAAAYDKLEKTK--NRLQQELDDLLVdLDHQRQLVSNLEKKQKKfDQMLAEEKAISARYAEERDRAEAEAREKETRALSL 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 453 SSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEheteikdltqlLEKERSI 532
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEE-----------LEDELQA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 533 LDDIKLSLKdktKNISAEIIRHEKELEPWDLQLQEKESQI--QLAESELSLLEETQAKlkknvetlEEKILAKKTHKQEL 610
Cdd:pfam01576 711 TEDAKLRLE---VNMQALKAQFERDLQARDEQGEEKRRQLvkQVRELEAELEDERKQR--------AQAVAAKKKLELDL 779
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29427672 611 QdlilDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKVLTA 675
Cdd:pfam01576 780 K----ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA 840
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
325-628 |
7.41e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 325 EYLEDIIGTANYKPLIEERMGQ--IENLNEVCLEKEnrfeivdREKNSLESGKETALEFLEKEKQLTLLRsklfQFKLLQ 402
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQekFEKMEQERLRQE-------KEEKAREVERRRKLEEAEKARQAEMDR----QAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 403 SNSKLA----STLEKISSSNKDLEDEKMKFQE------SLKKVDEIKAQRKEIKDRIsscsskektlvleRRELEGTR-- 470
Cdd:pfam17380 338 EQERMAmereRELERIRQEERKRELERIRQEEiameisRMRELERLQMERQQKNERV-------------RQELEAARkv 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 471 -VSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTE----HETEIKDLTQLLEKERSILDDIKLSL-KDKT 544
Cdd:pfam17380 405 kILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMErvrlEEQERQQQVERLRQQEEERKRKKLELeKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 545 KNISAEIIRH---EKELEPWDLQLQEKESQIQLAESEL----SLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDL 617
Cdd:pfam17380 485 DRKRAEEQRRkilEKELEERKQAMIEEERKRKLLEKEMeerqKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
330
....*....|.
gi 29427672 618 KKKLNSLKDER 628
Cdd:pfam17380 565 RSRLEAMERER 575
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
356-671 |
7.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 356 EKENRFEIVDR----EKNSLESGKETALEFLEKEKQLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQES 431
Cdd:PTZ00121 1221 EDAKKAEAVKKaeeaKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 432 LKKVDEIKAQRKE------IKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENML 505
Cdd:PTZ00121 1301 KKKADEAKKKAEEakkadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 506 EELRgQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKnisAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEEt 585
Cdd:PTZ00121 1381 DAAK-KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK---ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE- 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 586 qaklKKNVETLEEKilAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSK 665
Cdd:PTZ00121 1456 ----AKKAEEAKKK--AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
....*.
gi 29427672 666 AQNKSK 671
Cdd:PTZ00121 1530 AEEAKK 1535
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
488-697 |
8.15e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 488 EKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKL----SLKDKTKNISAEIIRHEK------- 556
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLladeTLADRVEEIREQLDEAEEakrfvqq 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 557 ------ELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEkILAKKTHkqelqdlildlkkklnsLKDERSQ 630
Cdd:PRK04863 916 hgnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTE-VVQRRAH-----------------FSYEDAA 977
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29427672 631 GEKNFTSA-HLKLKEMQKVLNAHRQRAMEA-RSSLSKAQNKSKVLTAL--SRLQKSGRINGFHGRLGDLGV 697
Cdd:PRK04863 978 EMLAKNSDlNEKLRQRLEQAEQERTRAREQlRQAQAQLAQYNQVLASLksSYDAKRQMLQELKQELQDLGV 1048
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
419-646 |
1.31e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 419 KDLEDEKMKFQEslkkvDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSI 498
Cdd:PHA02562 190 IDHIQQQIKTYN-----KNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 499 SEAENMLEELRGQQTEHE--TEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIRHEkelepwdlQLQEKESQIQLAE 576
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAID--------ELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 577 SELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSqgEKNFTSAHLKLKEMQ 646
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD--KIVKTKSELVKEKYH 404
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
485-666 |
1.32e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 485 EKAEKTLKSTKHSIseaENMLEELRGQQTEHETEIKDLTQL----------LEKERSILDDIKLSLKDKTKNISAEII-- 552
Cdd:PRK00409 505 EEAKKLIGEDKEKL---NELIASLEELERELEQKAEEAEALlkeaeklkeeLEEKKEKLQEEEDKLLEEAEKEAQQAIke 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 553 -RHEKELEPWDLQLQEKESQIQLAESElslLEETQAKLKKNVETLEEKILAKKTHKQEL--------------------- 610
Cdd:PRK00409 582 aKKEADEIIKELRQLQKGGYASVKAHE---LIEARKRLNKANEKKEKKKKKQKEKQEELkvgdevkylslgqkgevlsip 658
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29427672 611 -------QDLILDLKKKLNSLkdERSQGEKNF-----TSAHLKLKEMQKVLNAHRQRAMEARSSLSKA 666
Cdd:PRK00409 659 ddkeaivQAGIMKMKVPLSDL--EKIQKPKKKkkkkpKTVKPKPRTVSLELDLRGMRYEEALERLDKY 724
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
505-680 |
1.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 505 LEELRGQQTEHETEIKDLTQLLEK---ERSILDDIKLSLKDKTKNISAEIirhekELEPWDLQLQEKESQIQLAE---SE 578
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEAleaELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDassDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 579 LSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLkemqkvLNAHRQRAME 658
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL------LEERFAAALG 760
|
170 180
....*....|....*....|..
gi 29427672 659 ARSSLSKAQNKSKVLTALSRLQ 680
Cdd:COG4913 761 DAVERELRENLEERIDALRARL 782
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
505-622 |
1.44e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 505 LEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEI---IRHEKELEPWDLQLQEK-ESQIQLAESELS 580
Cdd:smart00787 142 LEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELrqlKQLEDELEDCDPTELDRaKEKLKKLLQEIM 221
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 29427672 581 LLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLN 622
Cdd:smart00787 222 IKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
464-658 |
1.63e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 464 RELEGTRVSLEERtknlvskmEKAEKTLKSTKHSISEAENMLEELRgQQTEHETE----------IKDL--------TQL 525
Cdd:PRK10929 48 EALQSALNWLEER--------KGSLERAKQYQQVIDNFPKLSAELR-QQLNNERDeprsvppnmsTDALeqeilqvsSQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 526 LEKERSILDDiklslKDKTKNISAEIIRHEKELEPWDLQLQEKESQIQ--------LAESELSLLEETQAKLKKNVETLE 597
Cdd:PRK10929 119 LEKSRQAQQE-----QDRAREISDSLSQLPQQQTEARRQLNEIERRLQtlgtpntpLAQAQLTALQAESAALKALVDELE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29427672 598 EKILAKkTHKQELQDLILDLKKKLNSLKDersqgeknftsahLKLKEMQKVLNAHRQRAME 658
Cdd:PRK10929 194 LAQLSA-NNRQELARLRSELAKKRSQQLD-------------AYLQALRNQLNSQRQREAE 240
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
419-673 |
1.87e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 419 KDLEDEKMKFQESLKKVDEIKAQ----RKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSt 494
Cdd:pfam01576 836 KNLEAELLQLQEDLAASERARRQaqqeRDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRK- 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 495 khSISEAENMLEELRGQQTeheteikdLTQLLEKERSILDdiklslkdktknisaeiiRHEKELEpwdLQLQEKESQIql 574
Cdd:pfam01576 915 --STLQVEQLTTELAAERS--------TSQKSESARQQLE------------------RQNKELK---AKLQEMEGTV-- 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 575 aeselslleetQAKLKKNVETLEEKILAkkthkqelqdlildLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQ 654
Cdd:pfam01576 962 -----------KSKFKSSIAALEAKIAQ--------------LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERR 1016
|
250
....*....|....*....
gi 29427672 655 RAMEARSSLSKAQNKSKVL 673
Cdd:pfam01576 1017 HADQYKDQAEKGNSRMKQL 1035
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
462-634 |
1.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 462 ERRELEGTRVSLEERTKNLvskmEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIK--DLTQLLEKERSILDDIKLS 539
Cdd:COG4717 72 ELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 540 LKDKTKNIsAEIIRHEKELEPWDLQLQEKESQIQLAESELSLleETQAKLKKNVETLEEKILAKKTHKQELQDL---ILD 616
Cdd:COG4717 148 LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEELQQRLAELEEELEEAqeeLEE 224
|
170
....*....|....*...
gi 29427672 617 LKKKLNSLKDERSQGEKN 634
Cdd:COG4717 225 LEEELEQLENELEAAALE 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
272-627 |
1.99e-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: 42.79 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 272 INEKESSYTEVTKLLKNEGIDLDHKRFLIlqGEVENIAQMKPKAEKESDDgLLEYLEDIIGtanykpLIEERMGQIENL- 350
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKIL--AEDEKLLDEKKQFEKIAEE-LKGKEQELIF------LLQAREKEIHDLe 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 351 ---NEVCLEKENRFEIVDREKNSLESGKETALEFLEKEKQLTLLRSKLFQfKLLQSNSKLASTLEKISSSNK-------- 419
Cdd:pfam05483 457 iqlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ-EASDMTLELKKHQEDIINCKKqeermlkq 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 420 --DLEDEKMKFQESLKKV-DEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNL----------VSKMEK 486
Cdd:pfam05483 536 ieNLEEKEMNLRDELESVrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLkkqienknknIEELHQ 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 487 AEKTLKSTKHSISEAENMLE------ELRGQQTEHE-TEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIRHEKELe 559
Cdd:pfam05483 616 ENKALKKKGSAENKQLNAYEikvnklELELASAKQKfEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEI- 694
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29427672 560 pwDLQLQEKESQIqlaeseLSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDE 627
Cdd:pfam05483 695 --DKRCQHKIAEM------VALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAE 754
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
358-645 |
1.99e-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: 42.57 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 358 ENRFEIVDREKNSLESGKETALEFLEKEKQltllRSKLFQFKLLQSNSKLAStlekisssnkDLEDEKMKFQESLKKVDE 437
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKE----RYKRDREQWERQRRELES----------RVAELKEELRQSREKHEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 438 IKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKhsiSEAENMLEELRGQQTEHET 517
Cdd:pfam07888 99 LEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK---ERAKKAGAQRKEEEAERKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 518 EIKDLTQLLEKERSILDDIKlslkdKTKNISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLleetqakLKKNVETLE 597
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQ-----ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEA-------LLEELRSLQ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 29427672 598 EKiLAKKTHKQELqdlildLKKKLNSLKDERSQGEKNFTSAHLKLKEM 645
Cdd:pfam07888 244 ER-LNASERKVEG------LGEELSSMAAQRDRTQAELHQARLQAAQL 284
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
312-651 |
2.11e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 312 KPKAEKESDDGLLEYLEDIIGTANYKPLIEERMGQIENlnEVCLEKENRFEIVDREKNSLESGKETALEFLEKEKQLTLL 391
Cdd:COG5185 111 NYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIAD--IEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 392 RSKLFQFKLLQ------SNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRisscSSKEKTLVLERRE 465
Cdd:COG5185 189 LKGISELKKAEpsgtvnSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQT----SDKLEKLVEQNTD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 466 LEGTRVS-LEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQtehetEIKDLTQLLEKERSILDDIKLSLKdKT 544
Cdd:COG5185 265 LRLEKLGeNAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATE-----SLEEQLAAAEAEQELEESKRETET-GI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 545 KNISAEIIRHEKELEPWDLQLQEKESQIqLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILD-LKKKLNS 623
Cdd:COG5185 339 QNLTAEIEQGQESLTENLEAIKEEIENI-VGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKA 417
|
330 340
....*....|....*....|....*...
gi 29427672 624 LKDERSQGEKNFTSAHLKLKEMQKVLNA 651
Cdd:COG5185 418 ADRQIEELQRQIEQATSSNEEVSKLLNE 445
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
466-681 |
2.22e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 466 LEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKD-KT 544
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEaEG 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 545 KNI--SAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLN 622
Cdd:pfam01576 455 KNIklSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29427672 623 SLKDERSQGEKNftsahlkLKEMQKVLNAHRQRAMEarsslsKAQNKSKVLTALSRLQK 681
Cdd:pfam01576 535 EDAGTLEALEEG-------KKRLQRELEALTQQLEE------KAAAYDKLEKTKNRLQQ 580
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
155-242 |
2.39e-03 |
|
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: 41.91 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 155 FINELVLENFKSYAGKQVvgPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANkmRQDRLSDLIHKSEafPSLQSCSVAV 234
Cdd:COG3593 2 KLEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPSSS--RKFDEEDFYLGDD--PDLPEIEIEL 75
|
....*...
gi 29427672 235 HFQYVIDE 242
Cdd:COG3593 76 TFGSLLSR 83
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
399-598 |
2.42e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.24 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 399 KLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTK 478
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 479 NLVSKMEKAEKTLKSTKHSisEAENMLEELRG-----QQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIR 553
Cdd:pfam06008 107 TLGENDFALPSSDLSRMLA--EAQRMLGEIRSrdfgtQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29427672 554 HEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEE 598
Cdd:pfam06008 185 YEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSE 229
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1015-1341 |
2.55e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1015 LLQNSERDVELSSDELKviEEQLKHTKLALAENDTNMNETLNLKVELKEQSEQLKEQMEDMEESINEFKSIEIEM---KN 1091
Cdd:TIGR00618 655 LTQERVREHALSIRVLP--KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASsslGS 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1092 KLEKLNSLLTY-IKSEITQQEKGLNELSIRDVTHTLGMLDDNKMDSVKEDVKNNQELDQEYRSCETQdesEIKDAETSCD 1170
Cdd:TIGR00618 733 DLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH---LLKTLEAEIG 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1171 NYHPMNIDEtsdevsrgipRLSEDELRELDVELIESKINELSYYVEETNVDIGVLEEYARRLAEFKRRKLDLNNAVQKRD 1250
Cdd:TIGR00618 810 QEIPSDEDI----------LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1251 EVKEQLGILKKKRFDEFMAGFNIISMTLKEMYQMITMGGNAELELVDSLDPFSEgVTFSVMPPKKSWRNITNLSGGEKTL 1330
Cdd:TIGR00618 880 GINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQGL-ALLVADAYTGSVRPSATLSGGETFL 958
|
330
....*....|.
gi 29427672 1331 SSLALVFALHK 1341
Cdd:TIGR00618 959 ASLSLALALAD 969
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
267-620 |
3.04e-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: 42.02 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 267 SSKYYINEKESSYTEVTK-LLKNEGIDlDHKRFLILQGEveniaqmkpKAEKESDDGLLE---YLEDIIgtaNYKPLIEE 342
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKeKLKNIELT-AHCDKLLLENK---------ELTQEASDMTLElkkHQEDII---NCKKQEER 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 343 RMGQIENLNEVCLEKENRFEIVDRE------------KNSLESGKETALEFLEKEKQLTLLRSKLFQFKLLQSNSklAST 410
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEfiqkgdevkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK--NKN 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 411 LEKISSSNKDLEDEKMKFQESLKkVDEIKAQRKEIKdrISSCSSK-EKTLVLERRELEGTRVSLEertkNLVSKMEKAek 489
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLN-AYEIKVNKLELE--LASAKQKfEEIIDNYQKEIEDKKISEE----KLLEEVEKA-- 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 490 tlkstKHSISEAENMLEELrGQQTEHEteIKDLTQLLEKERSILDDIklslkdktknisaeIIRHEKELEPWDLQLQEKE 569
Cdd:pfam05483 681 -----KAIADEAVKLQKEI-DKRCQHK--IAEMVALMEKHKHQYDKI--------------IEERDSELGLYKNKEQEQS 738
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 29427672 570 SQIQLAESELSLLEETQAKLKKNVETLEEKilaKKTHKQELQDLILDLKKK 620
Cdd:pfam05483 739 SAKAALEIELSNIKAELLSLKKQLEIEKEE---KEKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
564-686 |
3.28e-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: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 564 QLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKnftsahlKLK 643
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-------ELE 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 29427672 644 EMQKVLnAHRQRAMEARSSLSKAQ---NKSKVLTALSRLQKSGRIN 686
Cdd:COG4942 101 AQKEEL-AELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLA 145
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
412-553 |
3.98e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 412 EKISSSNKDLEDEKMKF-QESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKT 490
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29427672 491 lkstkhsISEAENMLEELRGQQTEhetEIKDltQLLEKersilddiklsLKDKTKNISAEIIR 553
Cdd:PRK12704 137 -------IEEQLQELERISGLTAE---EAKE--ILLEK-----------VEEEARHEAAVLIK 176
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
479-610 |
4.11e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 479 NLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDiklsLKDKTKnisaEIIRHEKEl 558
Cdd:COG1842 13 NINALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK----WEEKAR----LALEKGRE- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 29427672 559 epwDL------QLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQEL 610
Cdd:COG1842 84 ---DLarealeRKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL 138
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
362-600 |
4.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 362 EIVDREKNSLESGKETALEFLEK-EKQLTLLRSKLFQFKLLQSNS----KLASTLEKISssnkDLEDEKMKFQESLKKVD 436
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEAlEAELDALQERREALQRLAEYSwdeiDVASAEREIA----ELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 437 EIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKtlKSTKHSISEAENMLEELRGQQTEH- 515
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED--LARLELRALLEERFAAALGDAVERe 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 516 -----ETEIKDLTQLLEKERS----ILDDIKLSLKDKTKNISA------EIIRHEKELEpwDLQLQEKESQI--QLAESE 578
Cdd:COG4913 767 lrenlEERIDALRARLNRAEEelerAMRAFNREWPAETADLDAdleslpEYLALLDRLE--EDGLPEYEERFkeLLNENS 844
|
250 260
....*....|....*....|..
gi 29427672 579 LSLLEETQAKLKKNVETLEEKI 600
Cdd:COG4913 845 IEFVADLLSKLRRAIREIKERI 866
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
853-1281 |
4.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 853 KIERELSERENNFRVASDTVHEMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEMAYVKAVSDKAQLN 932
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 933 VVMKNLERLRGEYNDLQSETKTKKEKIKGLQDEIMKIGGIKlqmqnsKVESVCQKLDILVAKLKKVKSASKKSGGDVVKF 1012
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK------EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1013 QKLLQNSERDVELSSDELKVIEEQLKHTKLALAENDTNMnETLNLKVELKEQSEQLKEQM-----EDMEESINEFKSIEI 1087
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1088 EMKNKLEKLNSLLTYIKSEITQQEKGLNELSI---------RDVT--HTLGMLDD--NKMDSVKEDVKNNQELDQEYRSC 1154
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTeeHRKELLEEytAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 1155 ETQDESEIKDAETSCDNYhpmnidETSDEVsrgipRLSEDELRELDVELIESKINELSYYVEETNV---DIGVLEEYARR 1231
Cdd:PRK03918 482 LRELEKVLKKESELIKLK------ELAEQL-----KELEEKLKKYNLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEK 550
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 29427672 1232 LAEFKRRKLDLNNavqKRDEVKEQLGILKKKRFDEFMAGFNIISMTLKEM 1281
Cdd:PRK03918 551 LEELKKKLAELEK---KLDELEEELAELLKELEELGFESVEELEERLKEL 597
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
483-670 |
5.09e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 483 KMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDdiklslkdkTKNISAEIIRHEKELEpwD 562
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID---------VASAEREIAELEAELE--R 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 563 L-----QLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKIlakkthkQELQDLILDLKKKLNSLKDERSQGEKNFTS 637
Cdd:COG4913 680 LdassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL-------EQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190
....*....|....*....|....*....|...
gi 29427672 638 AHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKS 670
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
155-286 |
5.21e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 40.91 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 155 FINELVLENFKSYAgkQVVGPFHTSFSAVVGPNGSGKSNVIDSmLFVF----GFRANkmrqdRLSDLIHKSEafpslQSC 230
Cdd:PRK00064 2 YLTRLSLTDFRNYE--ELDLELSPGVNVLVGENGQGKTNLLEA-IYLLapgrSHRTA-----RDKELIRFGA-----EAA 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 29427672 231 SVAVHFQYvideSSGTSRIdeekpGLIITRKAFKNNSskyyIN-EKESSYTEVTKLL 286
Cdd:PRK00064 69 VIHGRVEK----GGRELPL-----GLEIDKKGGRKVR----INgEPQRKLAELAGLL 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
424-672 |
5.92e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 424 EKMKFQESLKKVDEIKA---QRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTlKSTKHSISE 500
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKaeeAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-KIKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 501 AENMLEELRGQQTEHETEIKDLTQLL-EKERSILDDIKLSLKDKTKNISAEIIRHEKELEpwdlqlQEKESQIQLAESEL 579
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE------KKAAEALKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 580 SLLEEtqakLKKNVEtlEEKILAKKTHKQELQDLIL---------DLKKKLNSLKDErsQGEKNfTSAHLKLKEMQKVLN 650
Cdd:PTZ00121 1702 KKAEE----LKKKEA--EEKKKAEELKKAEEENKIKaeeakkeaeEDKKKAEEAKKD--EEEKK-KIAHLKKEEEKKAEE 1772
|
250 260
....*....|....*....|..
gi 29427672 651 AHRQRAMEARSSLSKAQNKSKV 672
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRM 1794
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
421-545 |
6.09e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 41.28 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 421 LEDEKMKFQESLKkvdEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKM-EKAEKTLKSTKhsiS 499
Cdd:COG1193 509 LGEESIDVEKLIE---ELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKArEEAEEILREAR---K 582
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 29427672 500 EAENMLEELRGQQTEHEtEIKDLTQLLEKERSILDDIKLSLKDKTK 545
Cdd:COG1193 583 EAEELIRELREAQAEEE-ELKEARKKLEELKQELEEKLEKPKKKAK 627
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1318-1382 |
7.67e-03 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 39.37 E-value: 7.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29427672 1318 RNITNLSGGEKTLSSLALVFALhkyKPtPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVIS 1382
Cdd:cd03225 130 RSPFTLSGGQKQRVAIAGVLAM---DP-DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIV 190
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
376-625 |
7.82e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 376 ETALEFLEK-EKQLTLLRSKLFQFKLLQSNSK--LASTLEKISSSNKDLEDEKMKFQEslkkvDEIKAQRKEIKDRISSC 452
Cdd:pfam06160 175 LEAREVLEKlEEETDALEELMEDIPPLYEELKteLPDQLEELKEGYREMEEEGYALEH-----LNVDKEIQQLEEQLEEN 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 453 SSKektlvLERRELEGTRV---SLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLtqlleKE 529
Cdd:pfam06160 250 LAL-----LENLELDEAEEaleEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERV-----QQ 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 530 RSILDDIKLSlkdKTKNISAEIIRHEKELEPWDLQLQEKE---SQIQL----AESELSLLEETQAKLKKNVETLEEKila 602
Cdd:pfam06160 320 SYTLNENELE---RVRGLEKQLEELEKRYDEIVERLEEKEvaySELQEeleeILEQLEEIEEEQEEFKESLQSLRKD--- 393
|
250 260
....*....|....*....|...
gi 29427672 603 kkthKQELQDLILDLKKKLNSLK 625
Cdd:pfam06160 394 ----ELEAREKLDEFKLELREIK 412
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
471-674 |
8.40e-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: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 471 VSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQlleKERSILDDIKLSlKDKTKNISAE 550
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQ---QIKDLNDKLKKN-KDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 551 IIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQ 630
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29427672 631 GEKNFTSAHLKLKEMQK---VLNAHRQRAMEARSSLSKAQNKSKVLT 674
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELllsNLKKKIQKNKSLESQISELKKQNNQLK 231
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
180-330 |
9.75e-03 |
|
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: 39.68 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 180 FSAVVGPNGSGKSNVIDSMLFVFGFRAN-KMRQDRLSDLIHKSEAFPSLQSCSVAVHFQYVIDESSGTSRidEEKPGLII 258
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALvIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGV--RYRYGLDL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29427672 259 TRKAFKNnsSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQMKPKAEKESDDGLLEYLEDI 330
Cdd:pfam13304 79 EREDVEE--KLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSII 148
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
400-672 |
9.90e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 400 LLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKdrisscsskeKTLvLERRELEGTRVS-LEERTK 478
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELR----------KSL-LANRFSFGPALDeLEKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 479 NLVSKMEKAEKTLKSTKHsiSEAENMLEELrgqqtehETEIKDLTQLLEKERSILDDIKLSLKDKTKNISA---EIIRHE 555
Cdd:PRK04778 176 NLEEEFSQFVELTESGDY--VEAREILDQL-------EEELAALEQIMEEIPELLKELQTELPDQLQELKAgyrELVEEG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29427672 556 KELEPWDL--QLQEKESQIQLAESELSLLE---------ETQAKLKKNVETLEEKILAKK---THKQELQDLILDLKKKL 621
Cdd:PRK04778 247 YHLDHLDIekEIQDLKEQIDENLALLEELDldeaeekneEIQERIDQLYDILEREVKARKyveKNSDTLPDFLEHAKEQN 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 29427672 622 NSLKDERSQGEKNFTSAHlKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKV 672
Cdd:PRK04778 327 KELKEEIDRVKQSYTLNE-SELESVRQLEKQLESLEKQYDEITERIAEQEI 376
|
|
| |
