|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1200 |
0e+00 |
|
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: 926.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 3 YVKRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLPDLVNNTfKGNRGSSEASVS 82
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNG-KNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 83 VTFELHDGenlsepganhngngngaKISKEWTVTRRLKVTKGGNYSSnYYINGETATVTELHEQLNELRIYPEGYNIVLQ 162
Cdd:TIGR02169 80 VTFKNDDG-----------------KFPDELEVVRRLKVTDDGKYSY-YYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 163 GDVTRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKYQALRQQVQ 242
Cdd:TIGR02169 142 GDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 243 EKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQLAVAAQLATQKA 322
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 323 QRDQLQ-------QRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSfhntqtlpQLEAAVQTSQQQLEQLRHQA 395
Cdd:TIGR02169 302 EIASLErsiaekeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD--------KLTEEYAELKEELEDLRAEL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 396 QAIASASEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEAL 475
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 476 TSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEA-ASQAQQEVQGTYATKVILQSDLPGVCGLVAQLGQV 554
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAqARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSV 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 555 EPQYQLALEIAAGGRLGFLVVEDDGVAAAGIEILKQAKAGRATFLPLNKIRPPkGQNPNLSYAHGYIDLAVNLIDGDRRY 634
Cdd:TIGR02169 534 GERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDE-RRDLSILSEDGVIGFAVDLVEFDPKY 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 635 ADIFAFIFGNTIVFDTLVNARNHLGKHRIVTLEGDLLEASGAMSGGSRNQRSGLRFGTmvsEDTAEVKQLRQRLQDIQQV 714
Cdd:TIGR02169 613 EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSR---SEPAELQRLRERLEGLKRE 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 715 QGRNEELLLERTVRSRQLTQQLMEMRQQQREAQLHGEQTERDIARLSQQQTQINQQQINQQQKLAELQQNLALLQQSLPP 794
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 795 LEQQLASAQQQLTALETSQTHQQWQTIQIQIRTVEAEYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQD 874
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 875 LTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQLNQLRSQQQeqqwqweKLQTNQQEYQENLTQL 954
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE-------ELEAQIEKKRKRLSEL 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 955 QTQLEALEQDLPDPWPEIPLLQDRDEANLDFANILEELERSirngQKRLEAMEPVNMLALQEYEKTEARLGELSEKLQTI 1034
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRV----EEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1035 AGERTELLLRIENFTTLRRRSFQDAFDAVNKNFQIIFAELSDGDGYLQLDDAEDPFNGGLNLVAHPKGKPVRRLSSMSGG 1114
Cdd:TIGR02169 999 EEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGG 1078
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1115 EKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVSLRRPMIEAAERTIGVTQARGAHTQ 1194
Cdd:TIGR02169 1079 EKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQ 1158
|
....*.
gi 81670625 1195 VLGIKL 1200
Cdd:TIGR02169 1159 VFGLKL 1164
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1194 |
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: 666.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 3 YVKRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLPDLVNntFKGNRGSSEASVS 82
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 83 VTFELHDGEnlsepganhngngngAKISKEWTVTRRLKVTKGgnySSNYYINGETATVTELHEQLNELRIYPEGYNIVLQ 162
Cdd:pfam02463 79 ITFDNEDHE---------------LPIDKEEVSIRRRVYRGG---DSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 163 GDVTRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKYQALRQQVQ 242
Cdd:pfam02463 141 GGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 243 EKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQLAVAAQLATQKA 322
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 323 QRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASAS 402
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 403 EAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEALTSQIQTL 482
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 483 ASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQGTYATKVILQSDLPGVCGLVAQLGQVEPQYQLAL 562
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 563 EIAAGGRLGFLVVEDDGVAAAGIEILKQAKAGRATFLPLNKIRPPKGQNPNLSYAHGYIDLAVNLIDGDRRyadifafif 642
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA--------- 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 643 gnTIVFDTLVNARNHLGKHRIVTLEGDLLEASGAMSGGSRNQRSGLRFGTMVSEDTAEVKQLRQRLQDIQQVQGRNEELL 722
Cdd:pfam02463 612 --TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 723 LERTVRSRQLTQQLMEMRQQQREAQLHGEQTERDIARLSQQQTQINQQQINQQQKLAELQQNLALLQQSLPPLEQQLASA 802
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 803 QQQLTALETSQTHQQWQTIQIQIRTVEAEYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQE 882
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 883 QLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQLNQLRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLEALE 962
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEI 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 963 QDLPDPWPEIPLLQDRDEANLDFANILEELERSIRNGQKRLEAMEPVNMLALQEYEKTEARLGELSEKLQTIAGERTELL 1042
Cdd:pfam02463 930 LLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1043 LRIENFTTLRRRSFQDAFDAVNKNFQIIFAELSDGDGYLQLDDAEDPFNGGLNLVAHPKGKPVRRLSSMSGGEKSLTALS 1122
Cdd:pfam02463 1010 AIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALA 1089
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81670625 1123 FIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVSLRRPMIEAAERTIGVTQARGAHTQ 1194
Cdd:pfam02463 1090 LIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-1200 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 613.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 2 VYVKRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLPDLVNNTFKGNRGSSEASV 81
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 82 SVTFELHDGENLSEpganhngngngakiSKEWTVTRRLkvtkGGNYSSNYYINGETATVTELHEQLNELRIYPEGYNIVL 161
Cdd:COG1196 81 SLTFDNSDGTLPID--------------YDEVTITRRL----YRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 162 QGDVTRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKYQALRQQV 241
Cdd:COG1196 143 QGMIDRIIEAKPEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 242 QEKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQLAVAaQLATQK 321
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-ELARLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 322 AQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSfhntqtlpQLEAAVQTSQQQLEQLRHQAQAIASA 401
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE--------EAEEELEEAEAELAEAEEALLEAEAE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 402 SEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAEL--------TPLLTKVSVELEEKQFAQGQFNFQGE 473
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLeeeleeleEALAELEEEEEEEEEALEEAAEEEAE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 474 ALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQGTYATKviLQSDLPGVCGLVAQLGQ 553
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL--LLAGLRGLAGAVAVLIG 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 554 VEPQYQLALEIAAGGRLGFLVVEDDGVAAAGIEILKQAKAGRATFLPLNKIRPPKGQNPNLsyAHGYIDLAVNLIDGDRR 633
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL--ARGAIGAAVDLVASDLR 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 634 YADIFAFIFGNTIVFDTLVNARNHLGKHRIVTLEGDLLEASGAMSGGSRNQRSGLRFGTmvsedtaevkqlrqrlqdiqq 713
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR--------------------- 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 714 vqgRNEELLLERTVRSRQLTQQLMEMRQQQREAqlhgeqterdiarlsqqqtqinqqqinqqqklaelqqnlallqqslp 793
Cdd:COG1196 669 ---ELLAALLEAEAELEELAERLAEEELELEEA----------------------------------------------- 698
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 794 pleqqlasaqqqltaletsqthqqwqtiqiqirtveaeyqrqlqalrqgedhlkdlqnssqrlEEKIAQAQEKIAQHQAQ 873
Cdd:COG1196 699 ---------------------------------------------------------------LLAEEEEERELAEAEEE 715
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 874 DLTLAQEQEQLKialaemngaiqtteaqlaklseklgstkqerdrletqlnqlrsqqqeqqwqweklqtnQQEYQENLTQ 953
Cdd:COG1196 716 RLEEELEEEALE----------------------------------------------------------EQLEAEREEL 737
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 954 LQTQLEALEQDLPDPWPEIPLLQDRdeanldfanilEELERSIRNGQKRLEAMEPVNMLALQEYEKTEARLGELSEKLQT 1033
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDL-----------EELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQRED 806
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1034 IAGERTELLLRIENFTTLRRRSFQDAFDAVNKNFQIIFAELSDG-DGYLQLDDAEDPFNGGLNLVAHPKGKPVRRLSSMS 1112
Cdd:COG1196 807 LEEARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLFGGgEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLS 886
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1113 GGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVSLRRPMIEAAERTIGVTQARGAH 1192
Cdd:COG1196 887 GGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYGVTMQEPGV 966
|
....*...
gi 81670625 1193 TQVLGIKL 1200
Cdd:COG1196 967 SRVVSVDL 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-1200 |
7.44e-150 |
|
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: 481.09 E-value: 7.44e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 3 YVKRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLPDLVNNTFKGNRGSSEASVS 82
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 83 VTFELHDGenlsepganhngnGNGAKISKEWTVTRRLKvtKGGnySSNYYINGETATVTELHEQLNELRIYPEGYNIVLQ 162
Cdd:TIGR02168 81 LVFDNSDG-------------LLPGADYSEISITRRLY--RDG--ESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 163 GDVTRIITMNSKERREIIDELAGVAEF-------DRKIVKTKETLTEVQDreercqiIATELERTLERLAADRQKAEKYQ 235
Cdd:TIGR02168 144 GKISEIIEAKPEERRAIFEEAAGISKYkerrketERKLERTRENLDRLED-------ILNELERQLKSLERQAEKAERYK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 236 ALRQQVQEKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTEL----EKLNAQVKALGE--EE 309
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleEEIEELQKELYAlaNE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 310 QLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSfhntqtlpQLEAAVQTSQQQLE 389
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE--------SLEAELEELEAELE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 390 QLRHQAQAIASASEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVsveleEKQFAQGQFN 469
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA-----ELKELQAELE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 470 FQGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQGTYATKVIL---QSDLPGVCG 546
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALlknQSGLSGILG 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 547 LVAQLGQVEPQYQLALEIAAGGRLGFLVVEDDGVAAAGIEILKQAKAGRATFLPLNKIRPPKGQNPNLSYAH---GYIDL 623
Cdd:TIGR02168 524 VLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKnieGFLGV 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 624 AVNLIDGDRRYADIFAFIFGNTIVFDTLVNARNHLGK----HRIVTLEGDLLEASGAMSGGSRNQRSGL--------RFG 691
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgYRIVTLDGDLVRPGGVITGGSAKTNSSIlerrreieELE 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 692 TMVSEDTAEVKQLRQRLQDIQQVQGRNEELLLERTVRSRQLTQQLMEMRQQQREAQLHGEQTERDIARLSQQQTQINQQQ 771
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 772 INQQQKLAELQQNLALLQQSLPPLEQQLASAQQQLTALETSQThqqwqTIQIQIRTVEAEYQRQLQALRQGEDHLKDLQN 851
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD-----ELRAELTLLNEEAANLRERLESLERRIAATER 838
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 852 SSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQLNQLRSQQQ 931
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 932 EQQWQWEKLQTNQQEYQENLTQLQTQLEALEQDLPDPWPEIPLLQDRDEanldfanilEELERSIRNGQKRLEAMEPVNM 1011
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE---------EEARRRLKRLENKIKELGPVNL 989
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1012 LALQEYEKTEARLGELSEKLQTIAGERTELLLRIENFTTLRRRSFQDAFDAVNKNFQIIFAELSDGD-GYLQLDDAEDPF 1090
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGeAELRLTDPEDLL 1069
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1091 NGGLNLVAHPKGKPVRRLSSMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVS 1170
Cdd:TIGR02168 1070 EAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
|
1210 1220 1230
....*....|....*....|....*....|
gi 81670625 1171 LRRPMIEAAERTIGVTQARGAHTQVLGIKL 1200
Cdd:TIGR02168 1150 HNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1101-1193 |
2.63e-48 |
|
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: 170.72 E-value: 2.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1101 KGKPVRRLSSMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVSLRRPMIEAAE 1180
Cdd:cd03278 104 PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
90
....*....|....
gi 81670625 1181 RTIGVTQA-RGAHT 1193
Cdd:cd03278 184 RLYGVTMQeSGVSK 197
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
5-174 |
2.63e-38 |
|
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: 141.83 E-value: 2.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 5 KRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLPDLVNNTFKGNRGSSEASVSVT 84
Cdd:cd03278 2 KKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 85 FELHDGEnlsepganhngngngakiskewtvtrrlkvtkggnyssnyyingetatvtelheqlnelriypegYNIVLQGD 164
Cdd:cd03278 82 FDNSDGR-----------------------------------------------------------------YSIISQGD 96
|
170
....*....|
gi 81670625 165 VTRIITMNSK 174
Cdd:cd03278 97 VSEIIEAPGK 106
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
542-655 |
8.71e-37 |
|
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: 134.67 E-value: 8.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 542 PGVCGLVAQLGQVEPQYQLALEIAAGGRLGFLVVEDDGVAAAGIEILKQAKAGRATFLPLNKIRPPKGQNPNLSYAH--- 618
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAGSKLREALlpe 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 81670625 619 -GYIDLAVNLIDGDRRYADIFAFIFGNTIVFDTLVNAR 655
Cdd:smart00968 81 pGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETAR 118
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
541-656 |
9.44e-28 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 108.89 E-value: 9.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 541 LPGVCGLVAQLGQVEPQYQLALEIAAGGRLGFLVVEDDGVAAAGIEILKQAKAGRATFLPLNKIRPPKgqNPNLSYAHGY 620
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRP--RRPGADLKGG 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 81670625 621 IDLAVNLIDGDRRYADIFAFIFGNTIVFDTLVNARN 656
Cdd:pfam06470 79 AGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALE 114
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
5-185 |
4.72e-25 |
|
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: 105.35 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 5 KRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKgMRAERLPDLVNNTFKGNRGSSEASVSVT 84
Cdd:cd03275 2 KRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSH-LRSKNLKDLIYRARVGKPDSNSAYVTAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 85 FELHDGEnlsepganhngngngakiskEWTVTRRlkVTKGGnysSNYYINGETATVTELHEQLNELRIYPEGYN-IVLQG 163
Cdd:cd03275 81 YEDDDGE--------------------EKTFRRI--ITGGS---SSYRINGKVVSLKEYNEELEKINILVKARNfLVFQG 135
|
170 180
....*....|....*....|....
gi 81670625 164 DVTRIITMN--SKERREiIDELAG 185
Cdd:cd03275 136 DVESIASKNppGKRFRD-MDNLSG 158
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1100-1185 |
1.65e-22 |
|
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: 98.03 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1100 PKGKPVRRLSSMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQA-QQAQFIVVSLRRPMIEA 1178
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEFFSK 224
|
....*..
gi 81670625 1179 AERTIGV 1185
Cdd:cd03275 225 ADALVGV 231
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1100-1185 |
1.89e-22 |
|
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: 96.98 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1100 PKgKPVRRLSSMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVSLRRPMIEAA 1179
Cdd:cd03274 118 PK-KSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELA 196
|
....*.
gi 81670625 1180 ERTIGV 1185
Cdd:cd03274 197 DRLVGI 202
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1111-1193 |
3.03e-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: 92.37 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1111 MSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQA-QQAQFIVVSLRRPMIEAAERTIGVTQAR 1189
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAkHTSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 81670625 1190 GAHT 1193
Cdd:cd03239 175 GVST 178
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
3-185 |
1.39e-20 |
|
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: 92.36 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 3 YVKRIELSHFKSFGGTTAI-PFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLPDLVNNtfKGNRGSSEASV 81
Cdd:cd03273 2 HIKEIILDGFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYK--RGQAGITKASV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 82 SVTFelhdgeNLSEPGANHNGNGNGAKIskewTVTRrlKVTKGGnySSNYYINGETATVTELHE-----QLNelRIYPeg 156
Cdd:cd03273 80 TIVF------DNSDKSQSPIGFENYPEI----TVTR--QIVLGG--TNKYLINGHRAQQQRVQDlfqsvQLN--VNNP-- 141
|
170 180
....*....|....*....|....*....
gi 81670625 157 YNIVLQGDVTRIITMNSKErREIIDELAG 185
Cdd:cd03273 142 HFLIMQGRITKVLNMGGVW-KESLTELSG 169
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1101-1187 |
3.57e-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: 88.09 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1101 KGKPVRRLSSMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVSLRRPMIEAAE 1180
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVAD 228
|
....*..
gi 81670625 1181 RTIGVTQ 1187
Cdd:cd03272 229 KFYGVKF 235
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
5-224 |
1.56e-18 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 85.45 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 5 KRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERlpDLVnntfkgNRGSSEASVSVT 84
Cdd:COG0419 3 LRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRS--DLI------NVGSEEASVELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 85 FELHDgenlsepganhngngngakisKEWTVTRRlkvtkggnyssnyyingetatvtelheqlnelriypegynivlQGD 164
Cdd:COG0419 75 FEHGG---------------------KRYRIERR-------------------------------------------QGE 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 165 VTRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERL 224
Cdd:COG0419 91 FAEFLEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQL 150
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1108-1181 |
6.46e-17 |
|
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: 81.96 E-value: 6.46e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81670625 1108 LSSMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVSLRRPMIEAAER 1181
Cdd:cd03273 164 LTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANV 237
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
4-95 |
1.51e-16 |
|
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: 79.65 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIELSHFKSFGGTTAI-PFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKgMRAERLPDLVNNTfKGNRGSSEASVS 82
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIgPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASK-MRQKKLSDLIHNS-AGHPNLDSCSVE 80
|
90
....*....|....
gi 81670625 83 VTF-ELHDGENLSE 95
Cdd:cd03274 81 VHFqEIIDKPLLKS 94
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1108-1186 |
1.56e-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: 75.47 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1108 LSSMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQ-AQFIVVSLRRPMIEAAERTIGVT 1186
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
4-86 |
6.40e-15 |
|
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: 73.88 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLPDlvnNTFKGNRGSSEASVSV 83
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFL---AGGGVKAGINSASVEI 77
|
...
gi 81670625 84 TFE 86
Cdd:cd03239 78 TFD 80
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
4-518 |
7.04e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIELSHFKSFGgTTAIPFLPGFTVVSGPNGSGKSNILDALLFclGLATSKGMrAERLPDLVNNtfkgnrGSSEASVSV 83
Cdd:PRK02224 3 FDRVRLENFKCYA-DADLRLEDGVTVIHGVNGSGKSSLLEACFF--ALYGSKAL-DDTLDDVITI------GAEEAEIEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 84 TFElHDGenlsepganhngngngakisKEWTVTRRLKVTKGGNYSSNYYINGETATV---TELHEQLNE-LRIYPEGY-- 157
Cdd:PRK02224 73 WFE-HAG--------------------GEYHIERRVRLSGDRATTAKCVLETPEGTIdgaRDVREEVTElLRMDAEAFvn 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 158 -NIVLQGDVTRIITMNSKERREIIDELAgvaefdrkivktkeTLTEVQDREERCQIIATELERTLerlaadRQKAEKYQA 236
Cdd:PRK02224 132 cAYVRQGEVNKLINATPSDRQDMIDDLL--------------QLGKLEEYRERASDARLGVERVL------SDQRGSLDQ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 237 LRQQVQEKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQALD----------QRSQAIQTQQTELEKLNAQVKAlG 306
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDeadevleeheERREELETLEAEIEDLRETIAE-T 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 307 EEEQLAVAAQLATQKAQRDQLQQRYND-------GDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSFHNTQTLPQLEA 379
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDllaeaglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 380 AvQTSQQQLEQLRHQAQAIASASEAWVQEQTQLSRTVNQLQDELIPQRS-------QLAQLEERQQQLLTNLAELTPLLT 452
Cdd:PRK02224 351 A-DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELREERDELREREA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 453 KVSVELEEKQ---------FAQGQFNFQGEALT------------SQIQTLASDLAQLEQERSLLQETQTRlLKEQQEKQ 511
Cdd:PRK02224 430 ELEATLRTARerveeaealLEAGKCPECGQPVEgsphvetieedrERVEELEAELEDLEEEVEEVEERLER-AEDLVEAE 508
|
....*..
gi 81670625 512 RQLDKLE 518
Cdd:PRK02224 509 DRIERLE 515
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
172-506 |
1.40e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.68 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 172 NSKERREIIDElagVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKY-----QALRQQ--VQEK 244
Cdd:COG3096 276 HANERRELSER---ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHlnlvqTALRQQekIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 245 QGWAKVIQYKAVEQQ--RQKLWGQLERDREQSQQI--------------QQALD-QRSQAIQTQQTeleklnaqVKALGE 307
Cdd:COG3096 353 QEDLEELTERLEEQEevVEEAAEQLAEAEARLEAAeeevdslksqladyQQALDvQQTRAIQYQQA--------VQALEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 308 EEQL---------AVAAQLATQKAQRDQ-------LQQRYNDGDRQITNHQ---QQVGQIQAEISQSQ-----QQFL--H 361
Cdd:COG3096 425 ARALcglpdltpeNAEDYLAAFRAKEQQateevleLEQKLSVADAARRQFEkayELVCKIAGEVERSQawqtaRELLrrY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 362 IQQEksfHNTQTLPQLEAAVQTSQQQLEQLR-----------HQAQAIASASE------AWVQEQTQLSRTVNQLQDELI 424
Cdd:COG3096 505 RSQQ---ALAQRLQQLRAQLAELEQRLRQQQnaerlleefcqRIGQQLDAAEEleellaELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 425 PQRSQLAQLEERQQQL-------LTNLAELTPLLTKVSVELEEKQfaqgqfnfqgeALTSQIQTLASDLAQLEQERSLLQ 497
Cdd:COG3096 582 ELRQQLEQLRARIKELaarapawLAAQDALERLREQSGEALADSQ-----------EVTAAMQQLLEREREATVERDELA 650
|
....*....
gi 81670625 498 ETQTRLLKE 506
Cdd:COG3096 651 ARKQALESQ 659
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
172-506 |
1.63e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.30 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 172 NSKERREIIDElagVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKYQ-----ALRQQVQEKQG 246
Cdd:PRK04863 277 HANERRVHLEE---ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtALRQQEKIERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 247 WAKV--IQYKAVEQQ--RQKLWGQLERDREQSQQI--------------QQALD-QRSQAIQTQQ--TELEKLNAQV--- 302
Cdd:PRK04863 354 QADLeeLEERLEEQNevVEEADEQQEENEARAEAAeeevdelksqladyQQALDvQQTRAIQYQQavQALERAKQLCglp 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 303 -----KALGEEEQLAVAAQLATQkaQRDQLQQRYNDGD---RQITNHQQQVGQIQAEISQSQ--QQF--LHIQQEKSFHN 370
Cdd:PRK04863 434 dltadNAEDWLEEFQAKEQEATE--ELLSLEQKLSVAQaahSQFEQAYQLVRKIAGEVSRSEawDVAreLLRRLREQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 371 TQTLPQLEAAVQT------SQQQLEQLRHQAQAIASAS-------EAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQ 437
Cdd:PRK04863 512 AEQLQQLRMRLSEleqrlrQQQRAERLLAEFCKRLGKNlddedelEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81670625 438 QQLLTNLAELTP--LLTKVSVELEEKQFAQGQFNfqGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKE 506
Cdd:PRK04863 592 QARIQRLAARAPawLAAQDALARLREQSGEEFED--SQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-183 |
4.05e-12 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 69.03 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 3 YVKRIELSHFKSFGgTTAIPFLPGFTVVSGPNGSGKSNILDALLFclgLATSKGMRAERLPDLVnntfkgNRGSSEASVS 82
Cdd:COG1195 1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYL---LATGRSFRTARDAELI------RFGADGFRVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 83 VTFELHDGEnlsepganhngngngakiskewtvtRRLKVTKGGNYSSNYYINGETA-TVTELHEQLNELRIYPEGYNIVL 161
Cdd:COG1195 71 AEVERDGRE-------------------------VRLGLGLSRGGKKRVRINGKPVrRLSDLAGLLPVVLFSPEDLRLVK 125
|
170 180
....*....|....*....|..
gi 81670625 162 QGdvtriitmnSKERREIIDEL 183
Cdd:COG1195 126 GG---------PSERRRFLDRL 138
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-208 |
2.50e-11 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 64.05 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 7 IELSHFKSFGGTTaIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLpDLVNNTFK-GNRGSSEASVSVTF 85
Cdd:pfam13476 1 LTIENFRSFRDQT-IDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGG-GFVKGDIRiGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 86 ELHDGENlsepganhngngnGAKISKEWTVTRRLKVTKGGNYSSNYYINGETATVTELHEQLNELRIYpegYNIVLQGDV 165
Cdd:pfam13476 79 ENNDGRY-------------TYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPL---LVFLGQERE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 81670625 166 TRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREE 208
Cdd:pfam13476 143 EEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELE 185
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
2-185 |
7.67e-11 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 65.18 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 2 VYVKRIELSHFKSFGgTTAIPFLPGFTVVSGPNGSGKSNILDALLFclgLATSKGMRAERLPDLVnntfkgNRGSSEASV 81
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYL---LAPGRSHRTARDKELI------RFGAEAAVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 82 SVTFELHDGEnlsepganhngngngakiskewtvtRRLKVTKGGNYSSNYYINGETA-TVTELHEQLNELRIYPEGYNIV 160
Cdd:PRK00064 71 HGRVEKGGRE-------------------------LPLGLEIDKKGGRKVRINGEPQrKLAELAGLLNVVLFTPEDLRLV 125
|
170 180
....*....|....*....|....*
gi 81670625 161 LQGdvtriitmnSKERREIIDELAG 185
Cdd:PRK00064 126 KGG---------PSERRRFLDRLLF 141
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-93 |
1.35e-10 |
|
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: 62.24 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLF-CLGLATSKGMRAERLPDLVnntfkgNRGSSEASVS 82
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYaLTGELPPNSKGGAHDPKLI------REGEVRAQVK 74
|
90
....*....|.
gi 81670625 83 VTFELHDGENL 93
Cdd:cd03240 75 LAFENANGKKY 85
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6-563 |
2.09e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 65.38 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 6 RIELSHFKSFGGTTAIPF--LPGFTVVSGPNGSGKSNILDALlfCLGLATSKGMRAErlpDLVNNTFKGNRGSSEASVSV 83
Cdd:TIGR00618 5 RLTLKNFGSYKGTHTIDFtaLGPIFLICGKTGAGKTTLLDAI--TYALYGKLPRRSE---VIRSLNSLYAAPSEAAFAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 84 TFELhdgeNLSEPGANHNGNGNGAKISKEWTVTRRLKVTKGGNYSSNYYINgETATVTELHEQLNelriYPEGYNIVL-- 161
Cdd:TIGR00618 80 EFSL----GTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKS-ETEEVIHDLLKLD----YKTFTRVVLlp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 162 QGDVTRIITMNSKERREIIDELAGVAEFDRKIVKTKEtltevQDREERCQIIATELERTLERLAADRQKAEKYQalRQQV 241
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFA-----KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHE--RKQV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 242 QEKQgwakVIQYKAVEQQRQKLWGQLERDREQsqqiQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQlavAAQLATQK 321
Cdd:TIGR00618 224 LEKE----LKHLREALQQTQQSHAYLTQKREA----QEEQLKKQQLLKQLRARIEELRAQEAVLEETQE---RINRARKA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 322 AQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKsfhntQTLPQLEAAVQTSQQQLEQLRHQAQAIASA 401
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ-----SSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 402 SEAWVQEQTQLSRTVNQLQD-ELIPQRSQLA-----QLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEAL 475
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQkTTLTQKLQSLckeldILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 476 --TSQIQTLASDLAQ-----LEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQGT---YATKVILQSDLPGVC 545
Cdd:TIGR00618 448 tcTAQCEKLEKIHLQesaqsLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihPNPARQDIDNPGPLT 527
|
570
....*....|....*...
gi 81670625 546 GLVAQLGQVEPQYQLALE 563
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEE 545
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
4-185 |
4.53e-10 |
|
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: 61.51 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIELSHFKSFGGTTAI-PFLPGFTVVSGPNGSGKSNILDALLFCLGLATSkGMRAERLPDLVNNtfkgNRGSSEASVS 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIePFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYT-HLREEQRQALLHE----GSGPSVMSAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 83 VTFELHDGEN-LSEPGAnhngngngakiskewTVTRRLKVtkgGNYSSNYYINGETATVTELHEQLNEL---RIYPegYN 158
Cdd:cd03272 76 VEIIFDNSDNrFPIDKE---------------EVRLRRTI---GLKKDEYFLDKKNVTKNDVMNLLESAgfsRSNP--YY 135
|
170 180
....*....|....*....|....*..
gi 81670625 159 IVLQGDVTRIITMNSKERREiIDELAG 185
Cdd:cd03272 136 IVPQGKINSLTNMKQDEQQE-MQQLSG 161
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-432 |
4.99e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 216 ELERTLERLAADRQKAEKYQALRQQVQEKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTEL 295
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 296 EKLNAQVKALGeeeqlavAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEkSFHNTQTLP 375
Cdd:COG4913 326 DELEAQIRGNG-------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE-AAALLEALE 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 81670625 376 QLEAAVQTSQQQLEQLRHQAQAiasASEAWVQEQTQLSRTVNQLQDELIPQRSQLAQ 432
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRR---ELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
191-528 |
5.44e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 191 RKIVKTKETLTEVQDREERCQIIATELERTLERLA-ADRQKAEKYQALRQQVQEKQGWAKVIQYKAVEQQRQKLWGQLER 269
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEeLEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 270 DREQSQQIQQALDQrsqaIQTQQTELEKLNAQVKALGEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQ 349
Cdd:COG4717 151 LEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 350 AEISQSQQQFLHIQQEKSFHNTQTLPQLEAAV---QTSQQQLEQLRHQAQAIASASEAWVQEQTQLSRTVNQLQDELIPQ 426
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALlalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 427 RSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQfnfQGEALTSQIQTLASDLAQLEQE---RSLLQETQTRL 503
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE---ELQELLREAEELEEELQLEELEqeiAALLAEAGVED 383
|
330 340
....*....|....*....|....*
gi 81670625 504 LKEQQEKQRQLDKLEAASQAQQEVQ 528
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELE 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-526 |
8.90e-10 |
|
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: 62.09 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 285 SQAIQTQQTELEKLNAQVKALgEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQ 364
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAEL-EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 365 EKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASAseawVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNL 444
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA----VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 445 AELTPLLTkvsvELEEKQfaqgqfnfqgEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQ 524
Cdd:COG4942 174 AELEALLA----ELEEER----------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
..
gi 81670625 525 QE 526
Cdd:COG4942 240 AE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
270-1010 |
1.07e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 270 DREQSQQIQQALDQRSQAIQTQQtELEKLNAQVKALGE-----EEQLAVAAQLATQKAQRDQL-----QQRYNDGDRQIT 339
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHE-ALEDAREQIELLEPirelaERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 340 NHQQQVGQIQAEISQsqqqflhiqqeksfhntqtlpqLEAAVQTSQQQLEQLRHQAQAIASaseawvqeqtqlsRTVNQL 419
Cdd:COG4913 299 ELRAELARLEAELER----------------------LEARLDALREELDELEAQIRGNGG-------------DRLEQL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 420 QDELIPQRSQLAQLEERQQQLLTNLAELtplltKVSVELEEKQFAqgqfnfqgealtSQIQTLASDLAQLEQERSLLQET 499
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAAL-----GLPLPASAEEFA------------ALRAEAAALLEALEEELEALEEA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 500 QTRLLKEQQEKQRQLDKLEAASQAQQEVQGTYATKV------------ILQSDLPGVCGLVaQLGQVEPQYQLALEIAAG 567
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLlalrdalaealgLDEAELPFVGELI-EVRPEEERWRGAIERVLG 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 568 GrLGF-LVVEDDGVAAAgIEILKQAK-AGRATFLPLnKIRPPKGQNPNL---SYAHgYIDLAVNLIDG--DRRYADIFAF 640
Cdd:COG4913 486 G-FALtLLVPPEHYAAA-LRWVNRLHlRGRLVYERV-RTGLPDPERPRLdpdSLAG-KLDFKPHPFRAwlEAELGRRFDY 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 641 IfgntIVfDTLVNARNHlgkHRIVTLEGdLLEASGAM--SGGSRNQRSGLRFGtmvSEDTAEVKQLRQRLQDIQQVQGRN 718
Cdd:COG4913 562 V----CV-DSPEELRRH---PRAITRAG-QVKGNGTRheKDDRRRIRSRYVLG---FDNRAKLAALEAELAELEEELAEA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 719 EELLlertvrsRQLTQQLMEMRQQQREAQLHGEQTERDIarlsqqqtqinqqqinqqqklaelqqnlallqqSLPPLEQQ 798
Cdd:COG4913 630 EERL-------EALEAELDALQERREALQRLAEYSWDEI---------------------------------DVASAERE 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 799 LASAQQQLTALETSQthqqwqtiqIQIRTVEAEYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQ-DLTL 877
Cdd:COG4913 670 IAELEAELERLDASS---------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRlEAAE 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 878 AQEQEQLKIALAEMNGAIQTTEAQ---LAKLSEKLGSTKQERDRLETQLNQLRSQ-QQEQQWQWEKLQTN---QQEYQEN 950
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVErelRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADlesLPEYLAL 820
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81670625 951 LTQLQTQ-LEALEQDLPDpwpeipLLQDRDEAnlDFANILEELERSIRNGQKRleaMEPVN 1010
Cdd:COG4913 821 LDRLEEDgLPEYEERFKE------LLNENSIE--FVADLLSKLRRAIREIKER---IDPLN 870
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
258-525 |
1.80e-09 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 62.24 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 258 QQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEE--EQLAVA---AQLATQKAQRDQLQQRYN 332
Cdd:PRK11281 66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlSTLSLRqleSRLAQTLDQLQNAQNDLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 333 DGDRQITNHQQQVGQIQAEISQSQQQflhiqqeksfhnTQTLPQLEAAVQTSQqqlEQLRHQAQAIASASEAWVQEQTQL 412
Cdd:PRK11281 146 EYNSQLVSLQTQPERAQAALYANSQR------------LQQIRNLLKGGKVGG---KALRPSQRVLLQAEQALLNAQNDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 413 SRTV----NQLQDELIPQRSQLAqleERQQQLLTNLAELTPLLTKVSVELEEKQFAQgqfnFQGEALTSQIQT---LASD 485
Cdd:PRK11281 211 QRKSlegnTQLQDLLQKQRDYLT---ARIQRLEHQLQLLQEAINSKRLTLSEKTVQE----AQSQDEAARIQAnplVAQE 283
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 81670625 486 LA---QLEQErsLLQETQtRLLKEQQEKQRQLDKLEAASQAQQ 525
Cdd:PRK11281 284 LEinlQLSQR--LLKATE-KLNTLTQQNLRVKNWLDRLTQSER 323
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-85 |
2.09e-09 |
|
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: 57.75 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 6 RIELSHFKSFGGTTAIPFLPG-FTVVSGPNGSGKSNILDALLFCLGLATSKGMRAErlpdlvnntfKGNRGSSEASVSVT 84
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS----------GVKAGCIVAAVSAE 70
|
.
gi 81670625 85 F 85
Cdd:cd03227 71 L 71
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
292-525 |
3.60e-09 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 61.47 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 292 QTELEKLN------AQVKALGE--EEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLhiq 363
Cdd:PRK11281 42 QAQLDALNkqklleAEDKLVQQdlEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 364 qeksfhNTQTLPQLEAAVQTSQQQLEQLR-----------------HQAQAIASASEAWVQEQTQLSRTVNQLQDELIPQ 426
Cdd:PRK11281 119 ------STLSLRQLESRLAQTLDQLQNAQndlaeynsqlvslqtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 427 RSQLAQLE--------ERQQQLLTNLAELTPLLTKvsveleekqfaqgqfnfQGEALTSQIQtlasdlaQLEQERSLLQE 498
Cdd:PRK11281 193 QRVLLQAEqallnaqnDLQRKSLEGNTQLQDLLQK-----------------QRDYLTARIQ-------RLEHQLQLLQE 248
|
250 260
....*....|....*....|....*...
gi 81670625 499 T-QTRLLKEQQEKQRQLDKLEAASQAQQ 525
Cdd:PRK11281 249 AiNSKRLTLSEKTVQEAQSQDEAARIQA 276
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
206-525 |
3.68e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.51 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 206 REERCQIIATELERTLERLA---ADRQKAEK-YQALRQQV-QEKQGW-----AKVIQykAVEQQRQKLWGQLERDREQSQ 275
Cdd:COG3096 783 REKRLEELRAERDELAEQYAkasFDVQKLQRlHQAFSQFVgGHLAVAfapdpEAELA--ALRQRRSELERELAQHRAQEQ 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 276 QIQQALDQrsqaIQTQQTELEKLNAQVKALGEEEqlaVAAQLATQKAQRDQLQQryndGDRQITNHQQQVGQIQAEISQS 355
Cdd:COG3096 861 QLRQQLDQ----LKEQLQLLNKLLPQANLLADET---LADRLEELREELDAAQE----AQAFIQQHGKALAQLEPLVAVL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 356 QQqflhiqqeksfhNTQTLPQLEAAVQTSQQQLEQLRHQAQAIA---------SASEAwVQEQTQLSRTVNQLQDELIPQ 426
Cdd:COG3096 930 QS------------DPEQFEQLQADYLQAKEQQRRLKQQIFALSevvqrrphfSYEDA-VGLLGENSDLNEKLRARLEQA 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 427 RSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKE 506
Cdd:COG3096 997 EEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRSRRS 1076
|
330
....*....|....*....
gi 81670625 507 QQEKQRQLDKLEAASQAQQ 525
Cdd:COG3096 1077 QLEKQLTRCEAEMDSLQKR 1095
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
217-440 |
5.46e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.42 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 217 LERTLERLAADRQKAEKY-----QALRQQVQEKQgwAKVIQYKA------VEQQRQKLWGQLERDREQSQQIQQALDQRS 285
Cdd:COG3206 162 LEQNLELRREEARKALEFleeqlPELRKELEEAE--AALEEFRQknglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 286 QAIQTQQTELEKLNAQVKALGEEEQL-AVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHiqq 364
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA--- 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 365 eksfhntqtlpQLEAAVQTSQQQLEQLRHQAQAIasasEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQL 440
Cdd:COG3206 317 -----------SLEAELEALQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-50 |
1.19e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 58.48 E-value: 1.19e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 81670625 3 YVKRIELSHFKSFGGTTaIPFLPGFTVVSGPNGSGKSNILDALLFCLG 50
Cdd:COG3593 2 KLEKIKIKNFRSIKDLS-IELSDDLTVLVGENNSGKSSILEALRLLLG 48
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
224-467 |
1.28e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 224 LAADRQKAEKYQALRQQVQEkqgwakviQYKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVK 303
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQ--------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 304 ALGEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITN---HQQQVGQIqAEISQSQQQFLHIQQEKSFHNTQTLPQLEAA 380
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 381 VQTSQQQLEQLRHQAQAIASASEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEE 460
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
....*..
gi 81670625 461 KQFAQGQ 467
Cdd:COG4942 246 AGFAALK 252
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
21-181 |
1.31e-08 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 57.60 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 21 IPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGM-RAerlpdlvnntfkgnrGSSEASVSVTFELHDGENLSEpgan 99
Cdd:cd03241 17 LDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLiRS---------------GAEKAVVEGVFDISDEEEAKA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 100 hnGNGNGAKISKEWTVTRRLKVTKGgnySSNYYINGETATVTELHEQLNELriypegynIVLQGDVTRIITMNSKERREI 179
Cdd:cd03241 78 --LLLELGIEDDDDLIIRREISRKG---RSRYFINGQSVTLKLLRELGSLL--------VDIHGQHDHQNLLNPERQLDL 144
|
..
gi 81670625 180 ID 181
Cdd:cd03241 145 LD 146
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
197-439 |
1.40e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.58 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 197 KETLTEVQDREERcqiiATELERTLE-RL----AADRQKAEKYQALRQQVQEkqgwakVIQYKAVEQQRQklwgQLERDR 271
Cdd:COG3096 440 EDYLAAFRAKEQQ----ATEEVLELEqKLsvadAARRQFEKAYELVCKIAGE------VERSQAWQTARE----LLRRYR 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 272 EQsqqiqQALDQRSQAIQTQQTELEKLNAQVKALgEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAE 351
Cdd:COG3096 506 SQ-----QALAQRLQQLRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 352 ISQSQQQFLHIQQEKsfhntQTLPQLEAAVQTSQQQLEQLRHQ-AQAIASASE--AWVQEQTQLSRTVNQLQDELIPQRS 428
Cdd:COG3096 580 RSELRQQLEQLRARI-----KELAARAPAWLAAQDALERLREQsGEALADSQEvtAAMQQLLEREREATVERDELAARKQ 654
|
250
....*....|.
gi 81670625 429 QLAQLEERQQQ 439
Cdd:COG3096 655 ALESQIERLSQ 665
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
5-94 |
2.43e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 57.63 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 5 KRIELSHFKSFGGTTaIPfLPGFTVVSGPNGSGKSNILDALLFcLGLATSKGMRAE-----RLPDLVnnTFKGNRGSSEA 79
Cdd:COG4637 3 TRIRIKNFKSLRDLE-LP-LGPLTVLIGANGSGKSNLLDALRF-LSDAARGGLQDAlarrgGLEELL--WRGPRTITEPI 77
|
90
....*....|....*
gi 81670625 80 SVSVTFELHDGENLS 94
Cdd:COG4637 78 RLELEFAEEDERDLR 92
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-527 |
2.65e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 311 LAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQflhiqqeksfhntqtLPQLEAAVQTSQQQLEQ 390
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ---------------LAALERRIAALARRIRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 391 LRHQAQAIAsaseawvQEQTQLSRTVNQLQDELIPQRSQLAQLEeRQQQLLTNLAELTPLLTKVSVELEEKQFAQgqFNF 470
Cdd:COG4942 74 LEQELAALE-------AELAELEKEIAELRAELEAQKEELAELL-RALYRLGRQPPLALLLSPEDFLDAVRRLQY--LKY 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 81670625 471 QGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEV 527
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1099-1170 |
4.69e-08 |
|
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: 54.53 E-value: 4.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 1099 HPKGKPVRRLSSMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGAN----VEKLSKMVRKQaQQAQFIVVS 1170
Cdd:cd03276 98 TSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNrkisTDLLVKEAKKQ-PGRQFIFIT 172
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
21-391 |
6.04e-08 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 57.01 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 21 IPFLPGFTVVSGPNGSGKSNILDALLFCLglatskGMRAErlPDLVNNtfkgnrGSSEASVSVTFELHDGENLSEpganh 100
Cdd:COG0497 18 LEFGPGLTVLTGETGAGKSILLDALGLLL------GGRAD--ASLVRH------GADKAEVEAVFDLSDDPPLAA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 101 NGNGNGAKISKEWTVTRRlKVTKGGNysSNYYINGETATVTELhEQLNELRIypegyNIVLQGDVTRIitMNSKERREII 180
Cdd:COG0497 79 WLEENGLDLDDGELILRR-EISADGR--SRAFINGRPVTLSQL-RELGELLV-----DIHGQHEHQSL--LDPDAQRELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 181 DELAGvaefdrkivkTKETLTEVQDREERCQiiatELERTLERLAAD-RQKAEKYQALRQQVQEKQGWA-KVIQYKAVEQ 258
Cdd:COG0497 148 DAFAG----------LEELLEEYREAYRAWR----ALKKELEELRADeAERARELDLLRFQLEELEAAAlQPGEEEELEE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 259 QRQKLwGQLERDREQSQQIQQALDQRSQAIQTQ----QTELEKLNAQVKALGE--------------------------- 307
Cdd:COG0497 214 ERRRL-SNAEKLREALQEALEALSGGEGGALDLlgqaLRALERLAEYDPSLAElaerlesalieleeaaselrryldsle 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 308 ---------EEQLAVAAQLAtQK---------AQRDQLQQRYNdgdrQITNHQQQVGQIQAEISQSQQQFLHIQQEKSFH 369
Cdd:COG0497 293 fdperleevEERLALLRRLA-RKygvtveellAYAEELRAELA----ELENSDERLEELEAELAEAEAELLEAAEKLSAA 367
|
410 420
....*....|....*....|..
gi 81670625 370 NTQTLPQLEAAVqtsQQQLEQL 391
Cdd:COG0497 368 RKKAAKKLEKAV---TAELADL 386
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
4-86 |
6.34e-08 |
|
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: 54.14 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIEL------SHFKsfggttaIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERLPDLVNNtfkgnrGSS 77
Cdd:cd03276 1 IESITLknfmchRHLQ-------IEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKD------GES 67
|
....*....
gi 81670625 78 EASVSVTFE 86
Cdd:cd03276 68 SAKITVTLK 76
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
4-490 |
8.04e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIELSHFKSFGgTTAIPFLPGFTVVSGPNGSGKSNILDALLFCLGLATskgmRAERLPDLVNntfKGNRgsseaSVSV 83
Cdd:PRK01156 3 IKRIRLKNFLSHD-DSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIK---KGKN-----NLEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 84 TFELHDGENLsepganhngngngakiskewTVTRRLKVTKGGNYSSNYYINGETATVTELHEQLN---ELRIYPEGYNIV 160
Cdd:PRK01156 70 ELEFRIGGHV--------------------YQIRRSIERRGKGSRREAYIKKDGSIIAEGFDDTTkyiEKNILGISKDVF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 161 L------QGDVTRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAA-DRQKAEK 233
Cdd:PRK01156 130 LnsifvgQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENiKKQIADD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 234 YQALRQQVQEKQgwAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQaLDQRSQAIQTQQTELEKLNAQVKALgEEEQLAV 313
Cdd:PRK01156 210 EKSHSITLKEIE--RLSIEYNNAMDDYNNLKSALNELSSLEDMKNR-YESEIKTAESDLSMELEKNNYYKEL-EERHMKI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 314 AAQLATqkAQRDQLQQRYNDgDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSFHNTqtlpqleaaVQTSQQQLEQLRH 393
Cdd:PRK01156 286 INDPVY--KNRNYINDYFKY-KNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYND---------YIKKKSRYDDLNN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 394 QAQAIASASEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGE 473
Cdd:PRK01156 354 QILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIR 433
|
490
....*....|....*..
gi 81670625 474 ALTSQIQTLASDLAQLE 490
Cdd:PRK01156 434 ALRENLDELSRNMEMLN 450
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
309-528 |
1.12e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 309 EQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSF--------HNTQTLPQLEAA 380
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdlseeakLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 381 VQTSQQQLEQLRHQAQAIASASEAWVQEQTQL--SRTVNQLQDELIPQRSQLAQLEERQ-------QQLLTNLAELTPLL 451
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQL 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81670625 452 tkvsveLEEKQFAQGQFNFQGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQ 528
Cdd:COG3206 308 ------QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
221-429 |
1.12e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 221 LERLAADRQKAE-KYQALRQQVQEKQGWAKVIQykaveqQRQKLWGQLERDREQSQQIQQALDQRsQAIQTQQTELEKLN 299
Cdd:COG4913 612 LAALEAELAELEeELAEAEERLEALEAELDALQ------ERREALQRLAEYSWDEIDVASAEREI-AELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 300 AQVKALgeeeqlavAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQqeksfhntqtlpqlEA 379
Cdd:COG4913 685 DDLAAL--------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE--------------DL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 81670625 380 AVQTSQQQLEQLRHQA---QAIASASEAWVQEQTQLSRTVNQLQDELIPQRSQ 429
Cdd:COG4913 743 ARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-518 |
1.26e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIELSHFKSFGgTTAIPFLPGFTVVSGPNGSGKSNILDALLfcLGLATSKGMraeRLPDLVNNTFKgNRGSSEASVSV 83
Cdd:PRK03918 3 IEELKIKNFRSHK-SSVVEFDDGINLIIGQNGSGKSSILEAIL--VGLYWGHGS---KPKGLKKDDFT-RIGGSGTEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 84 TFElHDGenlsepganhngngngakisKEWTVTRrlKVTKGGNYSSNYYINGETAT----VTELHEqlnelRIYPegYNI 159
Cdd:PRK03918 76 KFE-KNG--------------------RKYRIVR--SFNRGESYLKYLDGSEVLEEgdssVREWVE-----RLIP--YHV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 160 VL------QGDVTRIITmnSKERRE-IIDELAGV--------------AEFDRKIVKTKETLTEVQDREERCQIIATELE 218
Cdd:PRK03918 126 FLnaiyirQGEIDAILE--SDESREkVVRQILGLddyenayknlgeviKEIKRRIERLEKFIKRTENIEELIKEKEKELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 219 RTLERL----AADRQKAEKYQALRQQVQEKQGWAKVIQYKavEQQRQKLWGQLERDREQSQQIQqaldqrsQAIQTQQTE 294
Cdd:PRK03918 204 EVLREIneisSELPELREELEKLEKEVKELEELKEEIEEL--EKELESLEGSKRKLEEKIRELE-------ERIEELKKE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 295 LEKLNAQVKALGEEEQlaVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQ-EKSFHNTQT 373
Cdd:PRK03918 275 IEELEEKVKELKELKE--KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElKKKLKELEK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 374 -LPQLEAAVQTSQ---QQLEQLRHQAQAIASAS-EAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELT 448
Cdd:PRK03918 353 rLEELEERHELYEeakAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 449 PLLTKVSV---ELEEKQfaqgqfnfQGEAL---TSQIQTLASDLAQLEQERSLLQETQTRLLKEqQEKQRQLDKLE 518
Cdd:PRK03918 433 KAKGKCPVcgrELTEEH--------RKELLeeyTAELKRIEKELKEIEEKERKLRKELRELEKV-LKKESELIKLK 499
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
264-525 |
1.92e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.61 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 264 WGQLERD-REQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQLAVAA-QLATQKAQR--DQLQQRYNDGDRQIT 339
Cdd:pfam12128 595 WAASEEElRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlKNARLDLRRlfDEKQSEKDKKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 340 NHQQQVGQIQAEISQSQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRhqAQAIASASEAWVQEQTQLSRTVNQL 419
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGAL--DAQLALLKAAIAARRSGAKAELKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 420 QDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVEleeKQFAQGQFNFQGEALTSQIQTLASDLAQLEQERSLLQET 499
Cdd:pfam12128 753 ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR---RQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQ 829
|
250 260
....*....|....*....|....*.
gi 81670625 500 QTRLLKEQQEKQRQLDKLEAASQAQQ 525
Cdd:pfam12128 830 LARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
208-563 |
2.87e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.19 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 208 ERCQIIATELERTLER--------LAADRQKAEKYQALRQQVQEKQGWAKVIQYKAVEQQRQKLWG-----------QLE 268
Cdd:PRK10246 297 ERIQEQSAALAHTRQQieevntrlQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNnelagwraqfsQQT 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 269 RDREQSQQIQQALDQRSQaiqtqqtELEKLNAQVKALGEEEqlaVAAQLATQKAQRdQLQQRYNDGDRQITNHQQQVGQI 348
Cdd:PRK10246 377 SDREQLRQWQQQLTHAEQ-------KLNALPAITLTLTADE---VAAALAQHAEQR-PLRQRLVALHGQIVPQQKRLAQL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 349 QAEISQSQQQFLHIQQ------------EKSFHNTQTLPQLEAAVQTsqqqLEQLRHQAQA------IASASEAWVQEQT 410
Cdd:PRK10246 446 QVAIQNVTQEQTQRNAalnemrqrykekTQQLADVKTICEQEARIKD----LEAQRAQLQAgqpcplCGSTSHPAVEAYQ 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 411 QLSRTVNQLqdelipqrsQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEALTSQIQTLASDLAQLE 490
Cdd:PRK10246 522 ALEPGVNQS---------RLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITL 592
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81670625 491 QerslLQETQTRLLKEQQEKQRQLDKLeaaSQAQqevqgtyatkvILQSDLPGVCGLVAQLGQVEPQYQLALE 563
Cdd:PRK10246 593 Q----PQDDIQPWLDAQEEHERQLRLL---SQRH-----------ELQGQIAAHNQQIIQYQQQIEQRQQQLL 647
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
232-441 |
4.10e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 232 EKYQALRQQVQEKQGWAKVIQYKAVEQQRQKLwGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQL 311
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 312 A-VAAQLATQKAQRDQLQQRYNDGDRQITNHQQQvgqiQAEISQSQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQ 390
Cdd:COG4717 128 LpLYQELEALEAELAELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 81670625 391 LRHQAQAIASASEAWVQEQTQLSRTVNQLQDELIPQRsQLAQLEERQQQLL 441
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLL 253
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
285-440 |
4.64e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 53.43 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 285 SQAIQTQQTELEKLNAQVKALGE------------EEQLA-VAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAE 351
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADllslerqgnqdlQDSVAnLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 352 ISQSQQQflhiqqeksfhNTQTLPQLEAAvqtsQQQLEQLRHQAQAIASA---SEAWVQEQTqlsrtvNQLQDelIPQRS 428
Cdd:PRK09039 125 LDSEKQV-----------SARALAQVELL----NQQIAALRRQLAALEAAldaSEKRDRESQ------AKIAD--LGRRL 181
|
170
....*....|..
gi 81670625 429 QLAqLEERQQQL 440
Cdd:PRK09039 182 NVA-LAQRVQEL 192
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
154-467 |
5.25e-07 |
|
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: 53.81 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 154 PEGYNIVLQGDVTRIITMNSKErreiiDELAGVAEFDRKIVKTK--ETLTEVQDREERCQIIATELERTLERLAADRQKA 231
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTS-----DKLEKLVEQNTDLRLEKlgENAESSKRLNENANNLIKQFENTKEKIAEYTKSI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 232 EKYQALRQQVQEKQGWAKVIQY----KAVEQQRQKLWGQLERDREQSQQIQQALDQR------SQAIQTQQTELEKLNAQ 301
Cdd:COG5185 306 DIKKATESLEEQLAAAEAEQELeeskRETETGIQNLTAEIEQGQESLTENLEAIKEEienivgEVELSKSSEELDSFKDT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 302 VKALGEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSFHNTqtlpqlEAAV 381
Cdd:COG5185 386 IESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMR------EADE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 382 QTSQQQLEQLRHQAQAIASASEAWVQEQTQLSRTVNQLQDELipqRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEK 461
Cdd:COG5185 460 ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYA 536
|
....*.
gi 81670625 462 QFAQGQ 467
Cdd:COG5185 537 HILALE 542
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
844-1065 |
5.42e-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: 53.23 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 844 DHLKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQL 923
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 924 N--------QLRSQQQEQQWQWEKLQTNQQE----------YQENLTQLQTQLEALEQDLPDpwpeiplLQDRDEANLDF 985
Cdd:COG4942 100 EaqkeelaeLLRALYRLGRQPPLALLLSPEDfldavrrlqyLKYLAPARREQAEELRADLAE-------LAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 986 ANILEELERSIRNGQKRLEAMEPVNMLALQEYEKTEARLGELSEKLQTIAGERTELLLRIENFTTLRRRSFQDAFDAVNK 1065
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
829-1016 |
5.80e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 829 EAEYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGA-IQTTEAQLAKLSE 907
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 908 KLGSTKQERDRLETQLNQLRSQQQEQQWQwekLQTNQQEYQENLTQLQTQLEALEQDLPDpwpeipLLQDRDEANLDFAN 987
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAE------AEAALRDLRRELRE 423
|
170 180
....*....|....*....|....*....
gi 81670625 988 ILEELErSIRNGQKRLeamePVNMLALQE 1016
Cdd:COG4913 424 LEAEIA-SLERRKSNI----PARLLALRD 447
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
138-518 |
6.22e-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: 53.87 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 138 ATVTELHEQLNELRIYPEGYNIVLQGDVTRIITMNSKERREIIDELagvaefDRKIVKTKETLTEVQDREErcQIIATEL 217
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEI------QNQISQNNKIISQLNEQIS--QLKKELT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 218 ERTLERLAADRQKAEKYQALRQQVQEKQGWAKVIQykAVEQQRQKLWGQLERDREQSQQIQQ---ALDQRSQAIQTQQTE 294
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK--NLESQINDLESKIQNQEKLNQQKDEqikKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 295 L----EKLNAQVKALgEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSfhn 370
Cdd:TIGR04523 431 LketiIKNNSEIKDL-TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK--- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 371 tqtlpQLEAAVQTSQQQLEQLRHQAQAIASaseawvqEQTQLSRTVNQLQDELIPQRSQL--AQLEERQQQLLTNLAELT 448
Cdd:TIGR04523 507 -----ELEEKVKDLTKKISSLKEKIEKLES-------EKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 449 PLLTKVSVELEEKQFAQGQFNFQGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLE 518
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
213-522 |
6.54e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.90 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 213 IATELERTLERLA---ADRQKAEKYQ-----------ALRQQVQEKQGWAKVIQ----YKAVEQQRQKLWGQLerdREQS 274
Cdd:PRK10929 46 IVEALQSALNWLEerkGSLERAKQYQqvidnfpklsaELRQQLNNERDEPRSVPpnmsTDALEQEILQVSSQL---LEKS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 275 QQIQQALDqRSQAIQ-------TQQTELEKLNAQVK-----------ALGEEEQLAVAAQLATQKAQRDQLQQRyndgdr 336
Cdd:PRK10929 123 RQAQQEQD-RAREISdslsqlpQQQTEARRQLNEIErrlqtlgtpntPLAQAQLTALQAESAALKALVDELELA------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 337 QIT-NHQQQVGQIQAEISQSQQQFL--HIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASAseawVQEQTQLS 413
Cdd:PRK10929 196 QLSaNNRQELARLRSELAKKRSQQLdaYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQ----FKINRELS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 414 RTVNQLQ---DELIPQRSQLAQLEERQQQLLTNLAELTPLLtkvsveleekqfaqGQFNFQGEALTSQI---------QT 481
Cdd:PRK10929 272 QALNQQAqrmDLIASQQRQAASQTLQVRQALNTLREQSQWL--------------GVSNALGEALRAQVarlpempkpQQ 337
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 81670625 482 LASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQ 522
Cdd:PRK10929 338 LDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQN 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-551 |
7.20e-07 |
|
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: 53.97 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 121 VTKGGNYSSNYYINGETATVTELHEQ---LNELRIYPEgYNIVLQGDvTRIITMNSKERRE-IIDELA-GVAEFDRKIVK 195
Cdd:pfam15921 19 ITSNRGSSSPFFVSSIRGTIIENTSStgtFTQIPIFPK-YEVELDSP-RKIIAYPGKEHIErVLEEYShQVKDLQRRLNE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 196 TKEtLTEVQDREERCQII--ATEL-ERTLERLA-AD--RQKAEKYQALRQQVQEKqgwakVIQYKAVEQQRQKLWGQLER 269
Cdd:pfam15921 97 SNE-LHEKQKFYLRQSVIdlQTKLqEMQMERDAmADirRRESQSQEDLRNQLQNT-----VHELEAAKCLKEDMLEDSNT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 270 DREQSQQIQQALDQRSQAIQTQQTELEKlnAQVKALGEEEQLAVAAQLATQKAQRDQLQQRyndgDRQITNHQQQV---- 345
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFEE--ASGKKIYEHDSMSTMHFRSLGSAISKILREL----DTEISYLKGRIfpve 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 346 GQIQAEISQSQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEAwVQEQ------------TQLS 413
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEI-IQEQarnqnsmymrqlSDLE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 414 RTVNQLQDELI-PQRSQLAQLEERQQQLLTNLAELTPLLTkvsvelEEKQFAQGQFNfqgeaLTSQIQTLASDLAQLEQE 492
Cdd:pfam15921 324 STVSQLRSELReAKRMYEDKIEELEKQLVLANSELTEART------ERDQFSQESGN-----LDDQLQKLLADLHKREKE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81670625 493 RSLLQETQTRLL--------------KEQQEKQRQLDKLEAASQA-QQEVQGTYATKVIL----QSDLPGVCGLVAQL 551
Cdd:pfam15921 393 LSLEKEQNKRLWdrdtgnsitidhlrRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAiqgkNESLEKVSSLTAQL 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
5-528 |
8.77e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 5 KRIELSHFKSFGGTTaIPFLPGFTVVSGPNGSGKSNILDALLfclglatskGMRAERLPDLVNNTFKGNRGSSEAsvsvt 84
Cdd:COG4717 4 KELEIYGFGKFRDRT-IEFSPGLNVIYGPNEAGKSTLLAFIR---------AMLLERLEKEADELFKPQGRKPEL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 85 felhdgeNLSEPGANHNGNGNGAKISKEWTVTRRlkvtkggnyssnyYINGETATVTELHEQLNELRIYPEGYNIVLQgd 164
Cdd:COG4717 69 -------NLKELKELEEELKEAEEKEEEYAELQE-------------ELEELEEELEELEAELEELREELEKLEKLLQ-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 165 VTRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAAD-----RQKAEKYQALRQ 239
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteeelQDLAEELEELQQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 240 QVQEKQGWAKVIQYK--AVEQQRQKLWGQLERDREQsQQIQQAldQRSQAIQTQQTELEKLNAQVKALGEE--EQLAVAA 315
Cdd:COG4717 207 RLAELEEELEEAQEEleELEEELEQLENELEAAALE-ERLKEA--RLLLLIAAALLALLGLGGSLLSLILTiaGVLFLVL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 316 QLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQA 395
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 396 QaiasaseaWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEkqfaqgqfnfqgEAL 475
Cdd:COG4717 364 Q--------LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEE------------LLE 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 476 TSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLE---AASQAQQEVQ 528
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedgELAELLQELE 479
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
206-526 |
9.25e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 206 REERCQIIATELERTLER---LAADRQKAEK-YQALRQQVQEKQG----WAKVIQYKAVEQQRQKLWGQLERDREQSQQI 277
Cdd:PRK04863 784 REKRIEQLRAEREELAERyatLSFDVQKLQRlHQAFSRFIGSHLAvafeADPEAELRQLNRRRVELERALADHESQEQQQ 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 278 QQALDQRSQAIQTqqteLEKLNAQVKALGEEeqlAVAAQLATQKAQRDQLQQryndGDRQITNHQQQVGQIQAEISQSQQ 357
Cdd:PRK04863 864 RSQLEQAKEGLSA----LNRLLPRLNLLADE---TLADRVEEIREQLDEAEE----AKRFVQQHGNALAQLEPIVSVLQS 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 358 qflhiqqeksfhNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASE-----AWVQEQTQLSRT---VNQLQDELIPQRSQ 429
Cdd:PRK04863 933 ------------DPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfSYEDAAEMLAKNsdlNEKLRQRLEQAEQE 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 430 LA----QLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQG--------EALTSQIQTLASDLAQLEQERSLLQ 497
Cdd:PRK04863 1001 RTrareQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsgaeERARARRDELHARLSANRSRRNQLE 1080
|
330 340
....*....|....*....|....*....
gi 81670625 498 ETQTRLLKEQQEKQRQLDKLEAASQAQQE 526
Cdd:PRK04863 1081 KQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
195-527 |
9.96e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 195 KTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKYQALRQQVQE-KQGWAKVIQY-KAVEQQRQKLWGQLERDRE 272
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSeEDVYHQLTSERKQRASLKE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 273 QSQQIQQALDQRSQAIQTQQTELEKLN---AQVKALGEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQ 349
Cdd:TIGR00618 564 QMQEIQQSFSILTQCDNRSKEDIPNLQnitVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 350 AEISQSQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEAWVQEQTQL----------SRTVNQL 419
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLrelethieeyDREFNEI 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 420 QDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQ---------------GQFNFQGEALTSQIQTLAS 484
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEvtaalqtgaelshlaAEIQFFNRLREEDTHLLKT 803
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 81670625 485 DLAQLEQER-SLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEV 527
Cdd:TIGR00618 804 LEAEIGQEIpSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
4-86 |
1.97e-06 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 50.76 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 4 VKRIELSHFKSFGgTTAIPFLPGFTVVSGPNGSGKSNILDALLFclgLATSKGMRAERLPDLVnntfkgNRGSSEASVSV 83
Cdd:cd03242 1 LKSLELRNFRNYA-ELELEFEPGVTVLVGENAQGKTNLLEAISL---LATGKSHRTSRDKELI------RWGAEEAKISA 70
|
...
gi 81670625 84 TFE 86
Cdd:cd03242 71 VLE 73
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
28-447 |
2.01e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 28 TVVSGPNGSGKSNILDALLFCLglaTSKGMRAERLPDLVNNTFKgnrgsSEASVSVTFELHDgenlsepganhngngnga 107
Cdd:PHA02562 30 TLITGKNGAGKSTMLEALTFAL---FGKPFRDIKKGQLINSINK-----KDLLVELWFEYGE------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 108 kisKEWTVTRRLKVTKGGNYSSNYYINgETATVTELHEQLNE-LRI-YPEGYNIVLQGDVTRIITMNSK--ERREIIDEL 183
Cdd:PHA02562 84 ---KEYYIKRGIKPNVFEIYCNGKLLD-ESASSKDFQKYFEQmLGMnYKSFKQIVVLGTAGYVPFMQLSapARRKLVEDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 184 agvaeFDRKIVKTKETLTEVQDREERCQIiaTELERTLERLaadRQKAEKYQALRQQVQEKQGwakviqykaveQQRQKL 263
Cdd:PHA02562 160 -----LDISVLSEMDKLNKDKIRELNQQI--QTLDMKIDHI---QQQIKTYNKNIEEQRKKNG-----------ENIARK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 264 WGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEeqlavAAQLATQKAQRDQLQQRYNDGD------RQ 337
Cdd:PHA02562 219 QNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTA-----AAKIKSKIEQFQKVIKMYEKGGvcptctQQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 338 ITNHQQQVGQIQAEISQSQQQF----LHIQQEKSFHN-----TQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEawvqe 408
Cdd:PHA02562 294 ISEGPDRITKIKDKLKELQHSLekldTAIDELEEIMDefneqSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE----- 368
|
410 420 430
....*....|....*....|....*....|....*....
gi 81670625 409 qtqlsrtvnQLQDELIPQRSQLAQLEERQQQLLTNLAEL 447
Cdd:PHA02562 369 ---------ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
162-542 |
2.34e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 162 QGDVTRIITMNSKERREIIDELAGVAEFD----RKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQ---KAEKY 234
Cdd:PRK10246 155 QGQFAAFLNAKPKERAELLEELTGTEIYGqisaMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQvltDEEKQ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 235 QALRQQVqekqgwakviqykaveQQRQKLWgqLERDREqsqqIQQALDQRSQAIQTQQTELEKLNAQVKALgeeeqlava 314
Cdd:PRK10246 235 LLTAQQQ----------------QQQSLNW--LTRLDE----LQQEASRRQQALQQALAAEEKAQPQLAAL--------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 315 aQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQeksfHNTQTLPQLEAAVQTSQQQL---EQL 391
Cdd:PRK10246 284 -SLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRH----HAAKQSAELQAQQQSLNTWLaehDRF 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 392 RHQAQAIAsaseAWVQEQTQLSRTVNQLQDelipQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQfnfQ 471
Cdd:PRK10246 359 RQWNNELA----GWRAQFSQQTSDREQLRQ----WQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQ---R 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81670625 472 GEALTSQIQTLASDLAQLEQERSLLQETQTRL-----LKEQQ--EKQRQLDKLEAASQAQQEVQGTYATKVILQSDLP 542
Cdd:PRK10246 428 LVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRnaalnEMRQRykEKTQQLADVKTICEQEARIKDLEAQRAQLQAGQP 505
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-55 |
2.43e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 50.77 E-value: 2.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 81670625 3 YVKRIELSHFKSFGGTTaIPF--LPGFTVVSGPNGSGKSNILDALLFCLGLATSK 55
Cdd:COG3950 2 RIKSLTIENFRGFEDLE-IDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLSR 55
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
350-525 |
3.29e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 50.85 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 350 AEISQSQQQFLHIQQEksfhntqtLPQLEAAVQTSQQQ----LEQLRHQAQAIASASEAWVQEQTQLsrtvNQLQDELIP 425
Cdd:PRK11637 40 AHASDNRDQLKSIQQD--------IAAKEKSVRQQQQQraslLAQLKKQEEAISQASRKLRETQNTL----NQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 426 QRSQLAQLEERQQQLLTNLAE-------------LTPLLTkvSVELEEKQFAQGQFNFQGEALTSQIQTLASDLAQLEQE 492
Cdd:PRK11637 108 LNASIAKLEQQQAAQERLLAAqldaafrqgehtgLQLILS--GEESQRGERILAYFGYLNQARQETIAELKQTREELAAQ 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 81670625 493 RSLLQETQT---RLLKEQQEKQrqlDKLEAASQAQQ 525
Cdd:PRK11637 186 KAELEEKQSqqkTLLYEQQAQQ---QKLEQARNERK 218
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
6-90 |
3.61e-06 |
|
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: 49.19 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 6 RIELSHFKSFGGTTAIPF----LPGFTVVSGPNGSGKSNILDALLFCLglaTSKGMRAERLPDLVNNTfkgNRGSSEASV 81
Cdd:cd03279 5 KLELKNFGPFREEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYAL---YGKTPRYGRQENLRSVF---APGEDTAEV 78
|
....*....
gi 81670625 82 SVTFELHDG 90
Cdd:cd03279 79 SFTFQLGGK 87
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
4-49 |
4.98e-06 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 44.90 E-value: 4.98e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 81670625 4 VKRIELSHFKSFGGTTAIPFLPGFTVVSGPNGSGKSNILDALLFCL 49
Cdd:pfam13555 1 LTRLQLINWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
188-542 |
5.38e-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: 50.74 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 188 EFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKaekYQALRQQVQEKQGWAKVIQYKAVEQQRQKLWGQL 267
Cdd:TIGR00618 287 NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK---RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 268 ERDREQSQQIQQALDQRSQAIQTQQT---ELEKLNAQVKALGEEEQLAVAAQLATQKAQRDQL---------QQRYNDGD 335
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTtltQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahakkqqelQQRYAELC 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 336 RQITNHQQQVgQIQAEISQSQQQFLHIQQEKSFHNTQTL-------PQLEAAVQTSQQQLE-----QLRHQAQAIASAS- 402
Cdd:TIGR00618 444 AAAITCTAQC-EKLEKIHLQESAQSLKEREQQLQTKEQIhlqetrkKAVVLARLLELQEEPcplcgSCIHPNPARQDIDn 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 403 --------EAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEekqfaqgqfnfqgeA 474
Cdd:TIGR00618 523 pgpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP--------------N 588
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81670625 475 LTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQGTYATKVILQSDLP 542
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-426 |
1.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 183 LAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAAD--------RQKAEKYQALRQQVQEKQGWAKVIQYK 254
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspeelLELLDRIEELQELLREAEELEEELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 255 AVEQQRQKLWGQLE-RDREQSQQIQQALDQRsqaiQTQQTELEKLNAQVKAL-GEEEQLAVAAQLATQKAQRDQLQQRYN 332
Cdd:COG4717 367 ELEQEIAALLAEAGvEDEEELRAALEQAEEY----QELKEELEELEEQLEELlGELEELLEALDEEELEEELEELEEELE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 333 DGDRQITNHQQQVGQIQAEISQSQQQflhiqqeksfhntQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEAwvqeqtqL 412
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEED-------------GELAELLQELEELKAELRELAEEWAALKLALEL-------L 502
|
250
....*....|....
gi 81670625 413 SRTVNQLQDELIPQ 426
Cdd:COG4717 503 EEAREEYREERLPP 516
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
342-532 |
1.71e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 342 QQQVGQIQAEISQSQ-QQFLHIQQEKSFHNTQTLPQ----LEAAVQTSQQQLEQLRHQA---------QAIASASEAWVQ 407
Cdd:NF012221 1541 SQQADAVSKHAKQDDaAQNALADKERAEADRQRLEQekqqQLAAISGSQSQLESTDQNAletngqaqrDAILEESRAVTK 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 408 EQTQLSRTVNQLqdelipqRSQLAQLEERQQQLLTNLAEltPLLTKVSVELEE-KQFAQGQFNFQGEALTSQIQTLASDL 486
Cdd:NF012221 1621 ELTTLAQGLDAL-------DSQATYAGESGDQWRNPFAG--GLLDRVQEQLDDaKKISGKQLADAKQRHVDNQQKVKDAV 1691
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 81670625 487 AQ----LEQERSLLQETQTRLLKEQ-QEKQRQLDKLEAASQAQQEVQGTYA 532
Cdd:NF012221 1692 AKseagVAQGEQNQANAEQDIDDAKaDAEKRKDDALAKQNEAQQAESDANA 1742
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
225-324 |
2.16e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 225 AADRQKAEKYQAlRQQVQEKQgwakviQYKAVEQQRQKlwgQLERDREQSQQIQ-QALDQRSQAIQTQQTELE-----KL 298
Cdd:PRK09510 74 AKRAEEQRKKKE-QQQAEELQ------QKQAAEQERLK---QLEKERLAAQEQKkQAEEAAKQAALKQKQAEEaaakaAA 143
|
90 100
....*....|....*....|....*.
gi 81670625 299 NAQVKALGEEEQLAVAAQLATQKAQR 324
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKK 169
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
3-181 |
2.44e-05 |
|
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: 48.12 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 3 YVKRIELSHFKSFGGTTaIPFLPGFTVVSGPNGSGKSNILDALLFclgLATSKGMRAERLPDLVNNtfkgnrGSSEASVS 82
Cdd:TIGR00611 2 YLSRLELTDFRNYDAVD-LELSPGVNVIVGPNGQGKTNLLEAIYY---LALGRSHRTSRDKPLIRF------GAEAFVIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 83 VTFELHDGEnlsepganhngngngAKISKEWTVTRRLKVTKggnyssnyyING-ETATVTELHEQLNELRIYPEGYNIVl 161
Cdd:TIGR00611 72 GRVSKGDRE---------------VTIPLEGLLKKKGKKAK---------VNIdGQDKLSDLAGLLPMQLFAPEDLTLV- 126
|
170 180
....*....|....*....|
gi 81670625 162 QGDvtriitmnSKERREIID 181
Cdd:TIGR00611 127 KGS--------PKYRRRFLD 138
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
6-91 |
2.55e-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: 46.82 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 6 RIELSHFKSFGGTTAIPFlPGFTVVSGPNGSGKSNILDALlfCLGLA-TSKGM-RAERLPDLVNNtfkgnrGSSEASVSV 83
Cdd:cd03277 5 RIKLENFVTYDETEFRPG-PSLNMIIGPNGSGKSSIVCAI--CLGLGgKPKLLgRAKKVGEFVKR------GCDEGTIEI 75
|
....*...
gi 81670625 84 TFELHDGE 91
Cdd:cd03277 76 ELYGNPGN 83
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
5-62 |
2.83e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 47.73 E-value: 2.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81670625 5 KRIELSHFKSFGGTTAIPF------LPGFTVVSGPNGSGKSNILDALLFCLGLATSKGMRAERL 62
Cdd:COG1106 3 ISFSIENFRSFKDELTLSMvasglrLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKL 66
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1046 |
2.97e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 850 QNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQLNQLRsq 929
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 930 qqeqqwqwEKLQTNQQEYQENLTQLQTQleaLEQDLPDPW--PEIPLLQDRDEANLD-FANILEELERSIRNGQKRLEAM 1006
Cdd:COG4942 97 --------AELEAQKEELAELLRALYRL---GRQPPLALLlsPEDFLDAVRRLQYLKyLAPARREQAEELRADLAELAAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 81670625 1007 EPVNMLALQEYEKTEARLGELSEKLQTIAGERTELLLRIE 1046
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
324-537 |
3.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 324 RDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEksfhnTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASE 403
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-----QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 404 AWVQEQtqlsrtvnqlqdELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEALT----SQI 479
Cdd:COG4717 127 LLPLYQ------------ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 81670625 480 QTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQGTYATKVIL 537
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
829-1008 |
3.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 829 EAEYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQ------- 901
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 902 -----------LAKLSEKLGSTKQERDRLETQLNQLRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLEALEQDLPDPWP 970
Cdd:COG4942 127 spedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
170 180 190
....*....|....*....|....*....|....*...
gi 81670625 971 EIPLLQDRDEANLDFANILEELERSIRNGQKRLEAMEP 1008
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-351 |
4.95e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 174 KERREIIDELAgvaEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQkaekYQALRQQVQE-KQGWAKViq 252
Cdd:COG4913 617 AELAELEEELA---EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE----IAELEAELERlDASSDDL-- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 253 yKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQLAVAAQLATQKAQ--------- 323
Cdd:COG4913 688 -AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgdavere 766
|
170 180
....*....|....*....|....*....
gi 81670625 324 -RDQLQQRYNDGDRQITNHQQQVGQIQAE 351
Cdd:COG4913 767 lRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
854-1046 |
5.29e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 854 QRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQLNQLRsqqqeq 933
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 934 qwqweklqtNQQEYQenltQLQTQLEALEQDlpdpwpeiplLQDRDEANLDFANILEELERSIRNGQKRLEAMEPvnmlA 1013
Cdd:COG1579 87 ---------NNKEYE----ALQKEIESLKRR----------ISDLEDEILELMERIEELEEELAELEAELAELEA----E 139
|
170 180 190
....*....|....*....|....*....|....
gi 81670625 1014 LQEYEKT-EARLGELSEKLQTIAGERTELLLRIE 1046
Cdd:COG1579 140 LEEKKAElDEELAELEAELEELEAEREELAAKIP 173
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
216-447 |
5.45e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 47.68 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 216 ELERTLERLAADRQKAEKYQALRQQVQEKqgwakviqYKAVEQQRQklwgqlerdrEQSQQIQQALDQRSQaiQTQQTEL 295
Cdd:pfam13779 497 RLSEALERGASDEEIAKLMQELREALDDY--------MQALAEQAQ----------QNPQDLQQPDDPNAQ--EMTQQDL 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 296 EKLNAQVKALGEEEQLAVAAQLAtqkaqrDQLQQRYNDgdRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSFHNTQTLP 375
Cdd:pfam13779 557 QRMLDRIEELARSGRRAEAQQML------SQLQQMLEN--LQAGQPQQQQQQGQSEMQQAMDELGDLLREQQQLLDETFR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81670625 376 QLEAAVQTSQQQLEQLRHQAQaiasaseawvQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAEL 447
Cdd:pfam13779 629 QLQQQGGQQQGQPGQQGQQGQ----------GQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEEL 690
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
829-1054 |
6.38e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 829 EAEYQRQLQALRQGedhLKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEK 908
Cdd:PRK02224 323 DEELRDRLEECRVA---AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 909 LGSTKQERDRLETQLNQLRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLEA-----LEQDLPDPwPEIPLLQDRDEANL 983
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpeCGQPVEGS-PHVETIEEDRERVE 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81670625 984 DFANILEELERSIRNGQKRLEAMEpvnmlalqEYEKTEARLGELSEKLQT----IAGERTELLLRIENFTTLRRR 1054
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDleelIAERRETIEEKRERAEELRER 545
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
140-528 |
7.91e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 140 VTELHEQLNELRIYPEGYNIVLQGDVTRIITMNSKERreiidelagvaEFDRKIVKTKETLTEVQDREERCQiiaTELER 219
Cdd:pfam15921 383 LADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRR-----------ELDDRNMEVQRLEALLKAMKSECQ---GQMER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 220 TLERLAADRQKAEKYQALRQQVQEkqgwAKVIQYKAVEQQRQKLWgQLERDREQSQQIQQALDQRSQAIQTQQTELEKLN 299
Cdd:pfam15921 449 QMAAIQGKNESLEKVSSLTAQLES----TKEMLRKVVEELTAKKM-TLESSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 300 AQV-------KALGEEEQLAVAAQ-----LATQKAQRDQ----LQQRYNDGDRQITNHQQQVGQIQAEISQSQQQF---- 359
Cdd:pfam15921 524 SRVdlklqelQHLKNEGDHLRNVQteceaLKLQMAEKDKvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIndrr 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 360 LHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRhqaqaIASASEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEE---- 435
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLELEKVK-----LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyev 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 436 -------RQQQLLTNLAELTPLLTKVSVELEEKQFA------------------QGQFNF---QGEALTSQIQTLASDLA 487
Cdd:pfam15921 679 lkrnfrnKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmQKQITAkrgQIDALQSKIQFLEEAMT 758
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 81670625 488 QLEQERSLLQETQTRLLKE----QQEKQRQLDKLEAASQAQQEVQ 528
Cdd:pfam15921 759 NANKEKHFLKEEKNKLSQElstvATEKNKMAGELEVLRSQERRLK 803
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
281-519 |
8.29e-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: 46.94 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 281 LDQRSQAIQTQQTELEKLNAQVKALgeeeqlavaaqlatqKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFL 360
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQL---------------KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 361 HIQQEKSFHNTQtLPQLEAAVQTSQQQLEQLRHQAQA---------IASASEAWVQEQTQLSRTvNQLQDELipqRSQLA 431
Cdd:TIGR04523 271 EKQKELEQNNKK-IKELEKQLNQLKSEISDLNNQKEQdwnkelkseLKNQEKKLEEIQNQISQN-NKIISQL---NEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 432 QLEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQ 511
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
....*...
gi 81670625 512 RQLDKLEA 519
Cdd:TIGR04523 426 KEIERLKE 433
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
298-532 |
8.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 298 LNAQVKALGEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQflhiqqeksfhntqtLPQL 377
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---------------IDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 378 EAAVQTSQQQLEQLRHQAQAIASASeawvQEQTQLSRTVNQL-----QDELIPQRSQLAQLEERQQQLLTNLAELTPLLT 452
Cdd:COG3883 71 QAEIAEAEAEIEERREELGERARAL----YRSGGSVSYLDVLlgsesFSDFLDRLSALSKIADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 453 KVSVELEEKQfaqgqfnfqgEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQGTYA 532
Cdd:COG3883 147 AKKAELEAKL----------AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
701-923 |
8.43e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 701 VKQLRQRLQDIQQVQGRNEELLLertvrsrqltQQLMEMRQQQREAQLHGEQTERDIARLSQQQTQINQqqinqqqklae 780
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNL----------KELKELEEELKEAEEKEEEYAELQEELEELEEELEE----------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 781 lqqnlallqqslppLEQQLASAQQQLTALETSQTHQQWQTIQIQIRTVEAEYQRQLQALRQGEDHLKDLQNSSQRLEEKI 860
Cdd:COG4717 107 --------------LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81670625 861 AQAQEKIAQHQAQDLTLAQEQ-EQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQL 923
Cdd:COG4717 173 AELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1097-1179 |
9.46e-05 |
|
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: 44.16 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1097 VAHPKGKPVRRLSSM----SGGEKSLTALSFIFALQRyrpsPFYGFDEVDMFLDGANVEKLSKMVRKQAQQ-AQFIVVSL 1171
Cdd:cd00267 63 IAKLPLEELRRRIGYvpqlSGGQRQRVALARALLLNP----DLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTH 138
|
....*...
gi 81670625 1172 RRPMIEAA 1179
Cdd:cd00267 139 DPELAELA 146
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
827-1180 |
1.13e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 827 TVEAEYQRqLQALRQGEDHLKDLQNSSQRLEEKIAQA-------QEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTE 899
Cdd:PRK02224 493 EVEERLER-AEDLVEAEDRIERLEERREDLEELIAERretieekRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 900 AQLAKLSEKLGSTKQERDRLET------QLNQLRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLEALEQDLPDPWPEiP 973
Cdd:PRK02224 572 EEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE-E 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 974 LLQDRDEANLDFANI---LEELERSIRNGQKRLEAMEpvNMLA-LQEYEKTEARLGELSEKLQTIAGERTELL------- 1042
Cdd:PRK02224 651 AREDKERAEEYLEQVeekLDELREERDDLQAEIGAVE--NELEeLEELRERREALENRVEALEALYDEAEELEsmygdlr 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1043 --LRIENFTTLrRRSFQDAFDAVNKNfqiifaelsDGDGYLQLDDAedpfnggLNLVAHPKGKPVRRLSSMSGGEKSLTA 1120
Cdd:PRK02224 729 aeLRQRNVETL-ERMLNETFDLVYQN---------DAYSHIELDGE-------YELTVYQKDGEPLEPEQLSGGERALFN 791
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1121 LSFIFALQRY--------RPSPFYGFDEVDMFLDGANVEKLSKMVR--KQAQQAQFIVVSLRRPMIEAAE 1180
Cdd:PRK02224 792 LSLRCAIYRLlaegiegdAPLPPLILDEPTVFLDSGHVSQLVDLVEsmRRLGVEQIVVVSHDDELVGAAD 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
167-358 |
1.25e-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: 45.91 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 167 RIITMNSKERREIIDELAgvaEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKYQALRQQVQEKQG 246
Cdd:COG4942 41 KELAALKKEEKALLKQLA---ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 247 WAKVIQ-----------------YKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELeklnaqvkalgEEE 309
Cdd:COG4942 118 RQPPLAlllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL-----------EEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 81670625 310 QLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQ 358
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Activator_LAG-3 |
pfam11498 |
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ... |
200-370 |
1.48e-04 |
|
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.
Pssm-ID: 151935 [Multi-domain] Cd Length: 476 Bit Score: 45.72 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 200 LTEVQDREERCQIIATELERTLERLAADRQKAEKYQALRQQVQEKQGWAKVIQYKAVEQQRQklwgqlerDREQSQQIQQ 279
Cdd:pfam11498 284 LAELDAMEPEGETKKSPMEAGGDRMPQSAPPPAMNPQHIAQLAQQQNKMRLLQQQEMEMQRI--------EQQRQQQIMH 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 280 ALDQRSQAIQTQQTELEKLNAQVKALGEEEQLAVAAQLATQKAQRDQLQQRYN--DGDRQITNHQQQVGQIQAEISQSQQ 357
Cdd:pfam11498 356 QHQQQQQQEHQQQQMLLQQQQQMHQLQQHHQMNGGGQFATQAHQHAAYLQQMQhmRLQEQIQHQQQQAQHHQQAQQQHQQ 435
|
170
....*....|...
gi 81670625 358 QFLHIQQEKSFHN 370
Cdd:pfam11498 436 PAQHGQMGYGIPN 448
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
204-526 |
1.53e-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: 46.32 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 204 QDREERCQIIATELERTLERLAAD---RQKAEKYQALRQQVQEKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQA 280
Cdd:pfam01576 295 RDLGEELEALKTELEDTLDTTAAQqelRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKAN 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 281 LDQRSQAIQTQQTELE---KLNAQVKALGEEEQLAVAAQLAtqkaqrdQLQQRYNDGDRQITNHQQQVGQIQAEIsQSQQ 357
Cdd:pfam01576 375 LEKAKQALESENAELQaelRTLQQAKQDSEHKRKKLEGQLQ-------ELQARLSESERQRAELAEKLSKLQSEL-ESVS 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 358 QFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQaqaiasaseawvqeQTQLSRTVNQLQDELIPQRSQLAQLEERQ 437
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ--------------KLNLSTRLRQLEDERNSLQEQLEEEEEAK 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 438 QQLLTNLAELTPLLTKVSVELEEKqfaqgqfnfqgealtsqiqtlASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKL 517
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMKKKLEED---------------------AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
330
....*....|
gi 81670625 518 EAA-SQAQQE 526
Cdd:pfam01576 572 EKTkNRLQQE 581
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
258-518 |
1.56e-04 |
|
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: 46.17 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 258 QQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALgEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQ 337
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDL-KKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 338 ITNHQ----------QQVGQIQAEISQSQQQFLHIQQEKSfHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEAWVQ 407
Cdd:TIGR04523 196 LLKLElllsnlkkkiQKNKSLESQISELKKQNNQLKDNIE-KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 408 EQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNlaeltplltKVSVELEEKQFAQGQFNFQGEALTSQIQTLASDLA 487
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK---------ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
250 260 270
....*....|....*....|....*....|.
gi 81670625 488 QLEQERSLLQETQTRLLKEQQEKQRQLDKLE 518
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
259-525 |
1.70e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 259 QRQKLWGQLERDREQSQQIQQALDQRSQAIQTQqteLEKLNAQVKALGEEeqlavAAQLATQKAQRDQLQQRYNdgdrQI 338
Cdd:PRK10246 617 QRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTA---LAGYALTLPQEDEE-----ASWLATRQQEAQSWQQRQN----EL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 339 TNHQQQVGQI--------QAEISQSQQQFLHIQQEKSFHnTQTLpQLEAAVQTSQQQLEQLRHQAQAIASASEAWVQEQT 410
Cdd:PRK10246 685 TALQNRIQQLtplletlpQSDDLPHSEETVALDNWRQVH-EQCL-SLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASV 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 411 QLSRT--VNQLQDElipqrSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEKQfaqgQFNFQGEALTSQIQTLASDLAQ 488
Cdd:PRK10246 763 FDDQQafLAALLDE-----ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQ----QHRPDGLDLTVTVEQIQQELAQ 833
|
250 260 270
....*....|....*....|....*....|....*..
gi 81670625 489 LEQErslLQETQTRllkeQQEKQRQLDKLEAASQAQQ 525
Cdd:PRK10246 834 LAQQ---LRENTTR----QGEIRQQLKQDADNRQQQQ 863
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
834-1053 |
1.81e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 834 RQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQ-HQAQDLTLAQEQEqlkiaLAEMNGAIQTTEAQLAKLSEKLGST 912
Cdd:PRK03918 152 RQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtENIEELIKEKEKE-----LEEVLREINEISSELPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 913 KQERDRLEtqlnQLRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLEALE---QDLPDPWPEIPLLQDRDEANLDFANIL 989
Cdd:PRK03918 227 EKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81670625 990 EELERSIRNGQKRLEAMEpvNMLA-----LQEYEKTEARLGELSEKLQTIAGERTELLLRIENFTTLRR 1053
Cdd:PRK03918 303 EEYLDELREIEKRLSRLE--EEINgieerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA 369
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
831-998 |
1.95e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 831 EYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEkIAQHQAQDLTLAQEQEQLkiaLAEMNGAIQTTEAQLAKLSEKLG 910
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEE-FCQRIGQQLDAAEELEEL---LAELEAQLEELEEQAAEAVEQRS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 911 STKQERDRLETQLNQLRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLEALEQDLPDpwpEIPLLQDRDEAnldfANILE 990
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER---EREATVERDEL----AARKQ 654
|
....*...
gi 81670625 991 ELERSIRN 998
Cdd:COG3096 655 ALESQIER 662
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
698-923 |
2.59e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 698 TAEVKQLRQRLQDIQQVQGRNEELLLERTVRSRQLTQQLMEMRQQQREAQLHGEQTERDIARLSQQQTQINQQQINQQQK 777
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 778 LAELQQNLALLQQSlppleQQLASAQQQLTALETSQTHQQWQTIQIQIRTVEAEYQRQLQALRQgedHLKDLQNSSQRLE 857
Cdd:COG4942 99 LEAQKEELAELLRA-----LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA---DLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 858 EKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQL 923
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
829-958 |
2.64e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 829 EAEYQRQLQALRQGEDHLKDLQNSSQRLEekiaQAQEKIAQHQAQDltlaQEQEQLKIALAEMNGAIQTTEAQLAKLSEK 908
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLE----QTLALLDKIDRQK----EETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 909 LGSTKQER------DRLETQLNQlrsqqqeqqwqwekLQTNQQEYQENLTQLQTQL 958
Cdd:PRK11281 110 NDEETRETlstlslRQLESRLAQ--------------TLDQLQNAQNDLAEYNSQL 151
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
273-568 |
2.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 273 QSQQIQQALDQRSQAIQTQQTELEKLNAQVKALgEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEI 352
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEEL-NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 353 SQSQQQFLHIqqeksfhntqtlpqleaAVQTSQQQLEQLRHQAQAIASASEAwvqeQTQLSRTVNQLQDELipqRSQLAQ 432
Cdd:COG3883 96 YRSGGSVSYL-----------------DVLLGSESFSDFLDRLSALSKIADA----DADLLEELKADKAEL---EAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 433 LEERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQR 512
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 513 QLDKLEAASQAQQEVQGTYATKVILQSDLPGVCGLVAQLGQVEPQYQLALEIAAGG 568
Cdd:COG3883 232 AAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAG 287
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
3-45 |
3.09e-04 |
|
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: 44.51 E-value: 3.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 81670625 3 YVKRIELSHFKSFGGTTaIPFLPGFTVVSGPNGSGKSNILDAL 45
Cdd:pfam13175 2 KIKSIIIKNFRCLKDTE-IDLDEDLTVLIGKNNSGKSSILEAL 43
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
848-998 |
3.13e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 43.58 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 848 DLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQERDRLETQLNQLR 927
Cdd:pfam17078 21 QLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 928 SQQQEQQWQWEKLQTN-----------QQEYQENLTQLQTQLEALEQDLPDPWPEipLLQDRDEANLDFANILEELERSI 996
Cdd:pfam17078 101 ASETTLEAELERLQIQydalvdsqneyKDHYQQEINTLQESLEDLKLENEKQLEN--YQQRISSNDKDIDTKLDSYNNKF 178
|
..
gi 81670625 997 RN 998
Cdd:pfam17078 179 KN 180
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
384-455 |
3.18e-04 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 44.57 E-value: 3.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81670625 384 SQQQLEQLRHQAQAIASASEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVS 455
Cdd:COG2959 51 GWQQLQQQQAELAQLAQQLAALQQQAQELRALAQQLQELLQQLAARLAQLEQRLAELQQQLAALQQLLQSLS 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
188-499 |
3.20e-04 |
|
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: 45.01 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 188 EFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKyqalrqQVQ--EKQGWAKVIQYKAVEQQRQKLWG 265
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS------EIKdlTNQDSVKELIIKNLDNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 266 QLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEeqlavaaqLATQKAQRDQLQQRYNDGDRQITnhqqqv 345
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK--------VKDLTKKISSLKEKIEKLESEKK------ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 346 gQIQAEISQSQQQFLHIQQEKSFHNtqtlpqLEAAVQTSQQQLEQLRHqaqaiasaseawvqEQTQLSRTVNQLQDElip 425
Cdd:TIGR04523 535 -EKESKISDLEDELNKDDFELKKEN------LEKEIDEKNKEIEELKQ--------------TQKSLKKKQEEKQEL--- 590
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81670625 426 qrsqLAQLEERQQQLLTNLAELTPLLTKVSVELEEkqfaqgqFNFQGEALTSQIQTLASDLAQLEQERSLLQET 499
Cdd:TIGR04523 591 ----IDQKEKEKKDLIKEIEEKEKKISSLEKELEK-------AKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
252-528 |
3.27e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 252 QYKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQlavaaQLaTQKAQRDQLQQRY 331
Cdd:PRK10246 552 QLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHER-----QL-RLLSQRHELQGQI 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 332 NDGDRQITNHQQQVGQIQAEISQSQQQF-LHIQQEKSFHNTQTLPQLEAAV-QTSQQQLEQLRHQAQAIA-------SAS 402
Cdd:PRK10246 626 AAHNQQIIQYQQQIEQRQQQLLTALAGYaLTLPQEDEEASWLATRQQEAQSwQQRQNELTALQNRIQQLTplletlpQSD 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 403 EAWVQEQTQLSRTVNQLQDELIPQRSQLAQLeerQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQG-------EAL 475
Cdd:PRK10246 706 DLPHSEETVALDNWRQVHEQCLSLHSQLQTL---QQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAAlldeetlTQL 782
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 81670625 476 TSQIQTLASdlaQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQ 528
Cdd:PRK10246 783 EQLKQNLEN---QRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELA 832
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-53 |
3.27e-04 |
|
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: 44.30 E-value: 3.27e-04
10 20
....*....|....*....|....*..
gi 81670625 27 FTVVSGPNGSGKSNILDALLFCLGLAT 53
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDA 27
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
826-1051 |
3.37e-04 |
|
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: 45.01 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 826 RTVEAEYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKL 905
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 906 SEKLGSTKQERDRLETQLNQLrsqQQEQQWQWEKLQTNQQEYQEN---LTQLQTQLEALEQDLPDPWPEIPLLQDRDEA- 981
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVL---SRSINKIKQNLEQKQKELKSKekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKl 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 982 -------------------NLDFANILEELERSIRNGQKRLEAMEpvnmlalQEYEKTEARLGELSEKLQTIAGERTELL 1042
Cdd:TIGR04523 530 esekkekeskisdledelnKDDFELKKENLEKEIDEKNKEIEELK-------QTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
....*....
gi 81670625 1043 LRIENFTTL 1051
Cdd:TIGR04523 603 KEIEEKEKK 611
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
188-516 |
3.66e-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: 45.04 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 188 EFDRKIVKTKET-LTEVQDREERCQIIAT---ELERTLERLAADRQKAEKYQALRQQVQEKQGWAKVIQYKAVEQQRQKL 263
Cdd:TIGR00606 234 ESSREIVKSYENeLDPLKNRLKEIEHNLSkimKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 264 WGQLERDREQSQQIQQALDQRSQAIQTQQTEL--EKLNAQVKALGEEEQLAVAAQLATQKAQRDQLQ--QRYNDGDRQIT 339
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQEKTELlvEQGRLQLQADRHQEHIRARDSLIQSLATRLELDgfERGPFSERQIK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 340 NHQQQVgqiqaeisqsqqqfLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEawvQEQTQLSRTVNQL 419
Cdd:TIGR00606 394 NFHTLV--------------IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE---LKKEILEKKQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 420 QDelipQRSQLAQLE-------ERQQQLLTNLAELTPLLTKVSVELEEKQFAQGQfNFQGEALTSqIQTLASDLAQLEQE 492
Cdd:TIGR00606 457 KF----VIKELQQLEgssdrilELDQELRKAERELSKAEKNSLTETLKKEVKSLQ-NEKADLDRK-LRKLDQEMEQLNHH 530
|
330 340
....*....|....*....|....
gi 81670625 493 RSLLQETQTrLLKEQQEKQRQLDK 516
Cdd:TIGR00606 531 TTTRTQMEM-LTKDKMDKDEQIRK 553
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
837-1055 |
4.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 837 QALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTKQER 916
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 917 DRLETQLNQLRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLEALEQDLPDPWPEIPLLQ------DRDEANLDFANILE 990
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqalSEAEAEQALDELLK 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81670625 991 ELERSIRNGQKRLEAMEPVNMLALQEYEKTEARLGELSEKLQTIAGERTELLLRIENFTTLRRRS 1055
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
833-1027 |
7.22e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 833 QRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQaQDLTLAQEQEQLKIALAEMngaiQTTEAQLAKLSEKLgst 912
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR-EELEKLEKLLQLLPLYQEL----EALEAELAELPERL--- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 913 kqerDRLETQLNQLRSqqqeqqwqwekLQTNQQEYQENLTQLQTQLEALEQDLPDPWPEI--PLLQDRDEANLDFANI-- 988
Cdd:COG4717 149 ----EELEERLEELRE-----------LEEELEELEAELAELQEELEELLEQLSLATEEElqDLAEELEELQQRLAELee 213
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 81670625 989 -LEELERSIRNGQKRLEAMEPvNMLALQEYEKTEARLGEL 1027
Cdd:COG4717 214 eLEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLL 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
175-494 |
7.79e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 175 ERREIIDELAGVAEFDRKIVKTKETLTEVQDREERcqiiaTELERTLERLAADRQKAEKYQALRQqvqekqgwakviqYK 254
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAREKQAA-----AEEQLVQANGELEKASREETFARTA-------------LK 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 255 AVEQQRQKLWGQLERDREQSQQiqqaldQRSQAIQTQQTELEKLNAQVKALGEEEQLAVAAQLATQKAQRDQLQQRYN-- 332
Cdd:pfam12128 650 NARLDLRRLFDEKQSEKDKKNK------ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvv 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 333 DGDRQItnhqqQVGQIQAEISQSQQQF-LHIQQ-EKSFHNT--------QTLPQLEAAVQTSQQQLEQLRHQAQAIAS-- 400
Cdd:pfam12128 724 EGALDA-----QLALLKAAIAARRSGAkAELKAlETWYKRDlaslgvdpDVIAKLKREIRTLERKIERIAVRRQEVLRyf 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 401 --ASEAWVQEQTQLSRTVNQLQDELIPQRSQLAQLEE----RQQQLLTNLAELTPLLTKVSVELEEKQFAQGQFNFQGEA 474
Cdd:pfam12128 799 dwYQETWLQRRPRLATQLSNIERAISELQQQLARLIAdtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED 878
|
330 340
....*....|....*....|..
gi 81670625 475 LTS-QIQ-TLASDLAQLEQERS 494
Cdd:pfam12128 879 ANSeQAQgSIGERLAQLEDLKL 900
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
828-968 |
8.59e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 828 VEAEYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQdLTLAQEQEQLKIALAEMNGA---IQTTEAQLAK 904
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEYEALQKEIESLkrrISDLEDEILE 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81670625 905 LSEKLGSTKQERDRLETQLNQLRSqqqEQQWQWEKLQTNQQEYQENLTQLQTQLEALEQDLPDP 968
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
134-522 |
9.36e-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: 43.57 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 134 NGETATVTELHEQLneLRIYPEGYNIVLQGDVTRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREERC--- 210
Cdd:pfam17380 261 NGQTMTENEFLNQL--LHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIyae 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 211 -QIIATELERTLERLAADRQKAEKYQALRQQVQEKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQalDQRSQAIQ 289
Cdd:pfam17380 339 qERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILE--EERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 290 TQQTELEKLNAQvkalgEEEQLAVAAQLATQKAQRDQLQQRYNDGDRqitnhQQQVGQIQAEISQSQQQFLHIQQEKSfh 369
Cdd:pfam17380 417 QQKVEMEQIRAE-----QEEARQREVRRLEEERAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELEKEKR-- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 370 ntqtlPQLEAAVQTSQQQLEQLRHQAQAIASASEAWVQEQTQLSRTVNQLQDElipQRSQLAQLEERQQQlltnlaeltp 449
Cdd:pfam17380 485 -----DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE---ERRREAEEERRKQQ---------- 546
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81670625 450 lltkvsvELEEKQFAQGQFNFQGEAltsqiqtlASDLAQLEQERSLLQETQtrllkeQQEKQRQldKLEAASQ 522
Cdd:pfam17380 547 -------EMEERRRIQEQMRKATEE--------RSRLEAMEREREMMRQIV------ESEKARA--EYEATTP 596
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
835-961 |
9.45e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 835 QLQALRQGEDHLKD-LQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTK 913
Cdd:pfam09787 48 ELEELRQERDLLREeIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLE 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81670625 914 QERDR-----------LETQLNQLRSQ---QQEQQWQWEKLQTNQQEYQENLTQLQTQLEAL 961
Cdd:pfam09787 128 EELRRskatlqsrikdREAEIEKLRNQltsKSQSSSSQSELENRLHQLTETLIQKQTMLEAL 189
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
164-465 |
1.00e-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: 43.42 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 164 DVTRIITMNSKERREIIDELAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKaekYQALRQQVQE 243
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVR---EHALSIRVLP 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 244 KQGWakviqykaveQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVkalgEEEQLAVAAQLATQKAQ 323
Cdd:TIGR00618 672 KELL----------ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF----NEIENASSSLGSDLAAR 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 324 RDQLQQryndgdrqitnhqqqvgqiqaEISQSQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQqLEQLRHQAQAIASASE 403
Cdd:TIGR00618 738 EDALNQ---------------------SLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE-LSHLAAEIQFFNRLRE 795
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81670625 404 AWVQEQTQLSRTVNQ-LQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEE-----KQFAQ 465
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQeIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKyeecsKQLAQ 863
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
168-525 |
1.42e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 168 IITMNSKERREIIDELAGV----AEFDRKIVKTKETLTEVQDREERCQIIATELErTLERLAADRQKAEKYQAlrQQVQE 243
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVnrdiQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVERKIA--QQAAK 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 244 KQGWAKVIQYKAVEQQRQKlwgqlerDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEqlavaAQLATQKAQ 323
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQE-------KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK-----LQIGTNLQR 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 324 RDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEK-----SFHNTQTLPQLEaaVQTSQQQLEQLRHQAQAI 398
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKeelisSKETSNKKAQDK--VNDIKEKVKNIHGYMKDI 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 399 asasEAWVQEQTQlsRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAE--------------LTPLLTKVSVELEEKQFA 464
Cdd:TIGR00606 961 ----ENKIQDGKD--DYLKQKETELNTVNAQLEECEKHQEKINEDMRLmrqdidtqkiqerwLQDNLTLRKRENELKEVE 1034
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81670625 465 QGQFNFQGEALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQ 525
Cdd:TIGR00606 1035 EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
852-965 |
1.66e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 852 SSQRLEEKIAQAQEKIAQHQAQdLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGS----------TKQERDRLET 921
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQ-LARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqalykkgavSQQELDEARA 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 81670625 922 QLNQLRSQQQEQQWQWEKLQtNQQEYQENLTQLQTQLEALEQDL 965
Cdd:COG1566 156 ALDAAQAQLEAAQAQLAQAQ-AGLREEEELAAAQAQVAQAEAAL 198
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
235-393 |
1.72e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 235 QALRQQVQEKQgwakviqyKAVEQQRQKLWGQLERDREQSQQIQQAldqrSQAIQTQQTELEKLNAQVKALG-------- 306
Cdd:PRK11637 50 KSIQQDIAAKE--------KSVRQQQQQRASLLAQLKKQEEAISQA----SRKLRETQNTLNQLNKQIDELNasiakleq 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 307 --EEEQLAVAAQL-------------------ATQKAQR----------------DQLQQRYNDGDRQITNHQQQVGQIQ 349
Cdd:PRK11637 118 qqAAQERLLAAQLdaafrqgehtglqlilsgeESQRGERilayfgylnqarqetiAELKQTREELAAQKAELEEKQSQQK 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 81670625 350 AEISQSQQQFLHIQQEKSfHNTQTLPQLEAAVQTSQQQLEQLRH 393
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARN-ERKKTLTGLESSLQKDQQQLSELRA 240
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
133-516 |
2.24e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 133 INGETATVTELHEQLNELRIYPEGYNIVLQGDVTRIITMNSKERrEIIDELAGVAEFDRKIVKTKETLTEVQDREErcqI 212
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER-TVSDLTASLQEKERAIEATNAEITKLRSRVD---L 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 213 IATELERTLERLAADRQKAEKYQALRQQVQEKQGWAKVIQyKAVEQQRQkLWGQLERD----REQSQQIQQALDQRSQAI 288
Cdd:pfam15921 529 KLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILR-QQIENMTQ-LVGQHGRTagamQVEKAQLEKEINDRRLEL 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 289 Q-------TQQTELEKLNAQVKALGEEEQLAVAAQLATQKAQRDQLQQRyNDGDRQITNHQQQVGQIQAEISQSQQQFlh 361
Cdd:pfam15921 607 QefkilkdKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQER-DQLLNEVKTSRNELNSLSEDYEVLKRNF-- 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 362 iqQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEAWVqeqtqlsRTVNQLQDELIPQRSQLAQLEERQQQLL 441
Cdd:pfam15921 684 --RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM-------KVAMGMQKQITAKRGQIDALQSKIQFLE 754
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81670625 442 TNLAELTplltkvsvelEEKQFAQGQFNfqgeALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDK 516
Cdd:pfam15921 755 EAMTNAN----------KEKHFLKEEKN----KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1096-1161 |
2.43e-03 |
|
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: 40.66 E-value: 2.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81670625 1096 LVAHPKGKPVRRLSS--MSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQA 1161
Cdd:cd03277 110 LVKFREGEQLQELDPhhQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETA 177
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
299-440 |
2.47e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 299 NAQVKA---LGEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNhQQQVGQIQAEISQSQQQFLHIQQEksFHNTQTLP 375
Cdd:COG1566 64 GDRVKKgqvLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRE--LERYQALY 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81670625 376 QLEAAvqtSQQQLEQLRHQAQAIASASEAWVQEQTQLSRTVNQLQDelipQRSQLAQLEERQQQL 440
Cdd:COG1566 141 KKGAV---SQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEE----LAAAQAQVAQAEAAL 198
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
235-448 |
2.56e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 235 QALRQQVQEKQgwAKVIQYKA-VEQQRQKLWGQLER----------------DREQSQQIQQALDQRSQAIQTQQTELEK 297
Cdd:PRK10246 619 HELQGQIAAHN--QQIIQYQQqIEQRQQQLLTALAGyaltlpqedeeaswlaTRQQEAQSWQQRQNELTALQNRIQQLTP 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 298 LNAQVKALGE-----------------EEQLAVAAQLATQKAQRDQLQQRYNDGDRQITnhqqqvGQIQAEISQSQQQFL 360
Cdd:PRK10246 697 LLETLPQSDDlphseetvaldnwrqvhEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFD------TALQASVFDDQQAFL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 361 hiqqeKSFHNTQTLPQLEAAVQTSQQQLEQL------------RHQAQAIASASEAWVQE--QTQLSRTVNQLQDELIPQ 426
Cdd:PRK10246 771 -----AALLDEETLTQLEQLKQNLENQRQQAqtlvtqtaqalaQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQ 845
|
250 260
....*....|....*....|....*...
gi 81670625 427 ---RSQLAQLEE-RQQQ--LLTNLAELT 448
Cdd:PRK10246 846 geiRQQLKQDADnRQQQqaLMQQIAQAT 873
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
5-47 |
2.78e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 41.11 E-value: 2.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 81670625 5 KRIELSHFKSFGGTTaIPFLPgFTVVSGPNGSGKSNILDALLF 47
Cdd:COG4938 2 KSISIKNFGPFKEAE-LELKP-LTLLIGPNGSGKSTLIQALLL 42
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
178-424 |
3.00e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.59 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 178 EIIDELAGVAEFDRKIVKTKETLTEVQD--REERCQIIATELERTLerlaadRQKAEKYQALRQQVQEKQgwakvIQYKA 255
Cdd:pfam15742 115 KLAQEKSRVADAEEKILELQQKLEHAHKvcLTDTCILEKKQLEERI------KEASENEAKLKQQYQEEQ-----QKRKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 256 VEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGE--------EEQLAVAAQlaTQKAQRDQL 327
Cdd:pfam15742 184 LDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEhlksnqelSEKLSSLQQ--EKEALQEEL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 328 QQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSfhntQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEAWVQ 407
Cdd:pfam15742 262 QQVLKQLDVHVRKYNEKHHHHKAKLRRAKDRLVHEVEQRD----ERIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLL 337
|
250
....*....|....*..
gi 81670625 408 EQTQLSRTVNQlQDELI 424
Cdd:pfam15742 338 EKRKLLEQLTE-QEELI 353
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
846-959 |
3.07e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.25 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 846 LKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEKLGSTkqerdrLETQLNQ 925
Cdd:TIGR04320 249 IPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQT------AQNNLAT 322
|
90 100 110
....*....|....*....|....*....|....
gi 81670625 926 LRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLE 959
Cdd:TIGR04320 323 AQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1096-1170 |
3.76e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 40.65 E-value: 3.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 1096 LVAHPKGKPVRRLS-SMSGGEKSLTALSFIFALQRYRPSPFYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVS 1170
Cdd:cd03241 155 LFSTNPGEPLKPLAkIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCIT 230
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
265-519 |
3.80e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 265 GQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKAlgEEEQLAVAAQlatqkaQRDQLQQRYNDGDRQITnhqqq 344
Cdd:PRK11637 40 AHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKK--QEEAISQASR------KLRETQNTLNQLNKQID----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 345 vgQIQAEISQSQQQflHIQQEKSFHNtqtlpQLEAAVQTSQQQLEQLrhqaqaIASASEAwvqeqtqlsrtvnqlqdeli 424
Cdd:PRK11637 107 --ELNASIAKLEQQ--QAAQERLLAA-----QLDAAFRQGEHTGLQL------ILSGEES-------------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 425 pQRSQLAQ-----LEERQQQLLTNLAELTPLLTKVSVELEEKQfaqgqfNFQGEALTSQIQtlasDLAQLEQERSLLQET 499
Cdd:PRK11637 152 -QRGERILayfgyLNQARQETIAELKQTREELAAQKAELEEKQ------SQQKTLLYEQQA----QQQKLEQARNERKKT 220
|
250 260
....*....|....*....|
gi 81670625 500 QTRLLKEQQEKQRQLDKLEA 519
Cdd:PRK11637 221 LTGLESSLQKDQQQLSELRA 240
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
270-358 |
4.06e-03 |
|
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.
Pssm-ID: 468465 [Multi-domain] Cd Length: 230 Bit Score: 40.26 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 270 DREQSQQIQQALDQRSQAIQTQQTELEKLN--AQVKALGEEEQL---AVAAQlATQKAQRDQLQQRYNDGDRQITNHQQQ 344
Cdd:NF038305 106 STQALQQINQQAGQQETQLQQQLNQLQAQTspQQLNQLLKSEQKqgqALASG-QLPEEQKEQLQQFKSNPQALDKFLAQQ 184
|
90
....*....|....
gi 81670625 345 VGQIQAEISQSQQQ 358
Cdd:NF038305 185 LTQIRTQAEEAEKQ 198
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
222-970 |
4.97e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 222 ERLAADRQKAEKYQALRQQVQEkqgWAKVIQ-YKAVEQQRQKLWGqLERDREQSQQIQQALDQRSQAIQTQQTELEKLNA 300
Cdd:pfam12128 204 AILEDDGVVPPKSRLNRQQVEH---WIRDIQaIAGIMKIRPEFTK-LQQEFNTLESAELRLSHLHFGYKSDETLIASRQE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 301 QVKALGEEEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEisqsQQQFLHIQQEKSFHNTQTLPQLEAA 380
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQ----HGAFLDADIETAAADQEQLPSWQSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 381 VQTSQQQLEQLRHQAQAIASASEAWVQE-QTQLSRTVNQLQDELIPQRS----QLAQLEERQQQLLTNL-AELTPLLTKV 454
Cdd:pfam12128 356 LENLEERLKALTGKHQDVTAKYNRRRSKiKEQNNRDIAGIKDKLAKIREardrQLAVAEDDLQALESELrEQLEAGKLEF 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 455 SVELEEKQFAQGQFNFQGEALTSQIQTLaSDLAQLEQERSLLQETQTRLLKEQQEKQR-----------QLDKLEAASQA 523
Cdd:pfam12128 436 NEEEYRLKSRLGELKLRLNQATATPELL-LQLENFDERIERAREEQEAANAEVERLQSelrqarkrrdqASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 524 QQEVQGTYAtkvilqsdlpgvcglvaqlgqvepQYQLALEIAAGGRLGFLVVEDDGVAAAGIEILKQAKAGRATFLPLNK 603
Cdd:pfam12128 515 LEERQSALD------------------------ELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 604 IRPPKGQNpNLsyahGYIDLAVNLIDGDrRYADIFAFIFGNTIVFDTLVNARNHLGKH---RIVTLEGDLLEASGAMSGG 680
Cdd:pfam12128 571 DGSVGGEL-NL----YGVKLDLKRIDVP-EWAASEEELRERLDKAEEALQSAREKQAAaeeQLVQANGELEKASREETFA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 681 SRN-QRSGLRFGTMVSEDTAEVKQL-RQRLQDIQQVQGRNEELLLERTVRSRQLTQQLMEMRQQQREAqlhgeQTERDIA 758
Cdd:pfam12128 645 RTAlKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA-----RTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 759 RLSQQQTQINQQQINQQQKLAELQQNlallqqslppleqqlasaqqqltALETSQthqqwqtiqiqirtVEAEYQRQLQA 838
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRSGA-----------------------KAELKA--------------LETWYKRDLAS 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 839 LRQGEDHLKDLQNSSQRLEEKIAQA----QEKIAQHQAQDLTLAQEQEQLKIALAEMNGAIQTTEAQLAKLSEklgSTKQ 914
Cdd:pfam12128 763 LGVDPDVIAKLKREIRTLERKIERIavrrQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIA---DTKL 839
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 81670625 915 ERDRLETQLNQLRSQqqeqqwqweklqtnQQEYQENLTQLQTQLEALeQDLPDPWP 970
Cdd:pfam12128 840 RRAKLEMERKASEKQ--------------QVRLSENLRGLRCEMSKL-ATLKEDAN 880
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
186-519 |
5.11e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 186 VAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKYQALRQQ-VQEKQGWAKVIQYKAVEQQRQklw 264
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEArIRELEEDIKTLTQRVLERETE--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 265 gqLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQLAvAAQLATQKAQRDQLQQRYNDGDRQITNHQQQ 344
Cdd:pfam07888 152 --LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL-RNSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 345 VGQIQAEISQ--SQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQA----IASASEA-------WVQEQTQ 411
Cdd:pfam07888 229 EAENEALLEElrSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQltlqLADASLAlregrarWAQERET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 412 LSRTVNQLQDELIPQRSQLAQLEERQQQlltnlaeltplltkvsvELEEKQFAQGQFNFQGEALTSQIQTLASDLAQLEQ 491
Cdd:pfam07888 309 LQQSAEADKDRIEKLSAELQRLEERLQE-----------------ERMEREKLEVELGREKDCNRVQLSESRRELQELKA 371
|
330 340
....*....|....*....|....*...
gi 81670625 492 ERSLLQETQTRLLKEQQEKQRQLDKLEA 519
Cdd:pfam07888 372 SLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
248-394 |
5.81e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 248 AKVIQYKAVEQQRQKLWGQLERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKAlgeeeqlaVAAQLATQKAQRDQL 327
Cdd:pfam00529 58 AALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKA--------AQAQLAQAQIDLARR 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 328 QQRYNDGD---RQITNHQQQVGQIQAEISQSQQQFLHIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQ 394
Cdd:pfam00529 130 RVLAPIGGisrESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAE 199
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
268-529 |
6.17e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 40.01 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 268 ERDREQSQQIQQALDQRSQAIqtqQTELEKLNAQVKALGEEeqlavAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQ 347
Cdd:pfam04849 79 ERDLELAARIGQSLLKQNSVL---TERNEALEEQLGSAREE-----ILQLRHELSKKDDLLQIYSNDAEESETESSCSTP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 348 IQAEISQSqqqflhiqqekSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEAWVQEQTQLsrtVNQLQDELIPQR 427
Cdd:pfam04849 151 LRRNESFS-----------SLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL---MSDCVEQLSEAN 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 428 SQLAQLEE----RQQQLLTNLAELTPLLTKVsVELEEKqfaqgqfnfqgealtsqIQTLASDLAQLEQERSLLQETQTRL 503
Cdd:pfam04849 217 QQMAELSEelarKMEENLRQQEEITSLLAQI-VDLQHK-----------------CKELGIENEELQQHLQASKEAQRQL 278
|
250 260
....*....|....*....|....*..
gi 81670625 504 LKEQQE-KQRQLDKLEAASQAQQEVQG 529
Cdd:pfam04849 279 TSELQElQDRYAECLGMLHEAQEELKE 305
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1105-1170 |
6.74e-03 |
|
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: 39.13 E-value: 6.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81670625 1105 VRRLSSMSGGEKSLTALSFIFALQRYRPS--PFYGFDEVDMFLDGANVE-KLSKMVRKQAQQA--QFIVVS 1170
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIEeSLAEIIEERKSQKnfQLIVIT 180
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
213-526 |
6.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 213 IATELERTLERLAADRQkaEKYQALRQQVQEkqgwakviQYKAVEQQRqKLWGQLERDREQSQQIQQALD--QRSQAIQT 290
Cdd:PRK04863 277 HANERRVHLEEALELRR--ELYTSRRQLAAE--------QYRLVEMAR-ELAELNEAESDLEQDYQAASDhlNLVQTALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 291 QQTELEKLNAQVKALGE--EEQLAVAA----QLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQ--QFL-- 360
Cdd:PRK04863 346 QQEKIERYQADLEELEErlEEQNEVVEeadeQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQavQALer 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 361 --HIQQEKSFHNTQTLPQLEAAVQTSQQQLEQLRHQAQAIASASEAwVQEQTQLSRTVNQLQDELIPQRSQlaqleERQQ 438
Cdd:PRK04863 426 akQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAA-HSQFEQAYQLVRKIAGEVSRSEAW-----DVAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 439 QLLTNLAELtplltkvsveleekqfaqgqfnfqgEALTSQIQTLASDLAQLEQeRSLLQETQTRLLKEQQEKQRQldKLE 518
Cdd:PRK04863 500 ELLRRLREQ-------------------------RHLAEQLQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGK--NLD 551
|
....*...
gi 81670625 519 AASQAQQE 526
Cdd:PRK04863 552 DEDELEQL 559
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
308-486 |
7.09e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 308 EEQLAVAAQLATQKAQRDQLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQEKSfhntqtlpQLEAAVQTSQQQ 387
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK--------RLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 388 LEQLRHQAQAIASASE--AWVQEQTQLSRTVNQLQDELIPQRSQLAQLEERQQQLLTNLAELTPLLTKVSVELEEkqfAQ 465
Cdd:COG1579 75 IKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---EL 151
|
170 180
....*....|....*....|.
gi 81670625 466 GQFNFQGEALTSQIQTLASDL 486
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
831-1179 |
7.13e-03 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 40.49 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 831 EYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQ------EKIAQHQAQDLTLAQEQEQLKiALAEMNGAIQTTEAQLAK 904
Cdd:TIGR00634 162 AYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQfqleelEEADLQPGEDEALEAEQQRLS-NLEKLRELSQNALAALRG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 905 LSEKLGSTKQERDRlETQLNQLRSQQQEQQWQWEKLQTNQQEYQENLTQLQTQLEALEQDlPDPWPEIP-----LLQDRD 979
Cdd:TIGR00634 241 DVDVQEGSLLEGLG-EAQLALASVIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFD-PERLNEIEerlaqIKRLKR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 980 EANLDFANILEELERSirngQKRLEAMEPVNmlalQEYEKTEARLGELSEKLQTIAGERTelLLRIENFTTLRRRSFQD- 1058
Cdd:TIGR00634 319 KYGASVEEVLEYAEKI----KEELDQLDDSD----ESLEALEEEVDKLEEELDKAAVALS--LIRRKAAERLAKRVEQEl 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 1059 -AFDAVNKNFQIIFAELSDGDGYLQLddAEDPFNGGLNLVAHPKGKPVRRLS-SMSGGEKS--LTALSFIFALQRyrPSP 1134
Cdd:TIGR00634 389 kALAMEKAEFTVEIKTSLPSGAKARA--GAYGADQVEFLFSANTGEPVKPLAkVASGGELSrvMLALKVVLSSSA--AVT 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 81670625 1135 FYGFDEVDMFLDGANVEKLSKMVRKQAQQAQFIVVSlRRPMIEAA 1179
Cdd:TIGR00634 465 TLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVT-HLPQVAAH 508
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
204-325 |
7.26e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 204 QDREERCQIIATELER----TLERLAADRQKAEKYQAlRQQVQEKQGWAKVIQYKAVEQQRQKLWGQLERDREQSQQIQQ 279
Cdd:PRK09510 87 QQAEELQQKQAAEQERlkqlEKERLAAQEQKKQAEEA-AKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA 165
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 81670625 280 ALDQRSQAIQTQQTELE---KLNAQVKALGEEEQLAVAAQLATQKAQRD 325
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEakkKAEAEAAAKAAAEAKKKAEAEAKKKAAAE 214
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-561 |
7.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 177 REIIDELAGVAEFDRKIVKTKETLTEVQDREERCQIIATELERTLERLAADRQKAEKyQALRQQVQEKQgwakvIQYKAV 256
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL-ARLEAELERLE-----ARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 257 EQQRQKLWGQL-ERDREQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALG----------EEEQLAVAAQLATQKAQRD 325
Cdd:COG4913 322 REELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 326 QLQQRYNDGDRQITNHQQQVGQIQAEISQSQQQFLHIQQ----------------------------------------E 365
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPArllalrdalaealgldeaelpfvgelievrpeeerwrgaiE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 366 KSFHNT-QTL---PQLEAA------------------VQTSQQQLEQLRHQAQAIA-------SASEAWVQE-------- 408
Cdd:COG4913 482 RVLGGFaLTLlvpPEHYAAalrwvnrlhlrgrlvyerVRTGLPDPERPRLDPDSLAgkldfkpHPFRAWLEAelgrrfdy 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 409 --------------------QTQLSRTVNQLQDE-LIPQ--------RSQLAQLEERQQQLLTNLAELTPLLTKVSVELE 459
Cdd:COG4913 562 vcvdspeelrrhpraitragQVKGNGTRHEKDDRrRIRSryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 460 E--------KQFAQGQFNFQG-EALTSQIQTLASDLAQLEQERSLLQETQTRLLKEQQEKQRQLDKLEAASQAQQEVQGT 530
Cdd:COG4913 642 AlqerrealQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
490 500 510
....*....|....*....|....*....|.
gi 81670625 531 YATKVILQSDLPGVCGLVAQLGQVEPQYQLA 561
Cdd:COG4913 722 LEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
271-396 |
8.55e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.83 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 271 REQSQQIQQALDQRSQAIQTQQTELEKLNAQVKALGEEEQLAVA--------AQLATQKAQRDQLQQRYNDGDRQITNHQ 342
Cdd:COG3524 176 EDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALlqliatleGQLAELEAELAALRSYLSPNSPQVRQLR 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81670625 343 QQVGQIQAEISQSQQQFLHIQQEKSFHNT----QTLpQLEA-----AVQTSQQQLEQLRHQAQ 396
Cdd:COG3524 256 RRIAALEKQIAAERARLTGASGGDSLASLlaeyERL-ELERefaekAYTSALAALEQARIEAA 317
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
826-963 |
9.22e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81670625 826 RTVEAEYQRQLQALRQGEDHLKDLQNSSQRLEEKIAQAQEKIAQHQAQDLTLAQEQEQLKI---ALAEMNGAIQTTEAQL 902
Cdd:PRK04863 533 QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAriqRLAARAPAWLAAQDAL 612
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81670625 903 AKLSEKLGSTKQERDRLETQLNQLrsqqqeqQWQWEKLQTNQQEYQENLTQLQTQLEALEQ 963
Cdd:PRK04863 613 ARLREQSGEEFEDSQDVTEYMQQL-------LERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| |
