|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1114 |
0e+00 |
|
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: 761.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 2 RLKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENMTDVIFNGSVNRTAHARASVE 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 82 LVFDNPHNRVPGefGRFTEISVRREVLRDGTNHYQINGQKCRRKDVTDLFLGTGLGPRSYAIIEQGTVSRLVESRPADLK 161
Cdd:TIGR02168 81 LVFDNSDGLLPG--ADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 162 LFMEEAAGVSRYKERRRETEQRIRHTQENLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRSRAARAELIGSELWALE 241
Cdd:TIGR02168 159 AIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 242 TRLGEAKSELAQVEQALAALDAKRTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDLQART 321
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 322 QALGERITSRKAQLSSQQEQLTEGVLRSELEEARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQT 401
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 402 RARLGGLHEL--QAKTRLARLK--LEDERSGPIGAEDADLQPTLDTLGGELELGRAAAEELAAQLAQAIEEHEALKLAHS 477
Cdd:TIGR02168 399 NNEIERLEARleRLEDRRERLQqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 478 QQQGLLRELEARLTTLDQILGEQME------------------GATLADRLQVVPEWAQALDKVLGRWLTATPADECNPA 539
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGfsegvkallknqsglsgiLGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 540 LDG------------------LWIGPALPA-----------VAGTLASLISGDH-----VPAFLNAIWLADNREEALARQ 585
Cdd:TIGR02168 559 KKAiaflkqnelgrvtflpldSIKGTEIQGndreilkniegFLGVAKDLVKFDPklrkaLSYLLGGVLVVDDLDNALELA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 586 PTLLAGESVLTPAGDWLGPNWAdIGQGAALGTMALLG---ERERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELS 662
Cdd:TIGR02168 639 KKLRPGYRIVTLDGDLVRPGGV-ITGGSAKTNSSILErrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 663 QRTLRGQEQKWQQLREAWSLQQGQRQERLLRFGQLGEELIRLDKEQAEEAQR-------LAETEQQLALEEARLAELQEQ 735
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaeeeLAEAEAEIEELEAQIEQLKEE 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 736 GEPLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAP 815
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 816 LLAEQRNLEALQLACHQRLAELERQLSELDQARSADHKQLVVLQEKLATLRLERERNLTRRQGLHEQFEELGVRLVDLDQ 895
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 896 A--VLIAADRGKLRQEIQTLETQVEALGAINLAALEEYEEAKTRATYLENQCQDLEQALETLSQAIKRIDKETQIRFRDT 973
Cdd:TIGR02168 958 AleNKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDT 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 974 FDKVNEDLKSLFPKVFGGGSAWLELT-SDDLLEAGVSIMARPPGKKNATIALLSGGEKALTALALVFAIFRLNPAPFCLL 1052
Cdd:TIGR02168 1038 FDQVNENFQRVFPKLFGGGEAELRLTdPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCIL 1117
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267170 1053 DEVDAPLDEVNVGRFCSLVKEMSSTVQFVYISHNKVSMEMAEQLVGVTMQEPGVSRIVSVDI 1114
Cdd:TIGR02168 1118 DEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1123 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 716.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1 MRLKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENMTDVIFNGSVNRTAHARASV 80
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 81 ELVFDNPHNRVPGEFgrfTEISVRREVLRDGTNHYQINGQKCRRKDVTDLFLGTGLGPRSYAIIEQGTVSRLVESRPADL 160
Cdd:COG1196 81 SLTFDNSDGTLPIDY---DEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 161 KLFMEEAAGVSRYKERRRETEQRIRHTQENLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRSRAARAELIGSELWAL 240
Cdd:COG1196 158 RAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLREL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 241 ETRLGEAKSELAQVEQALAALDAKRTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDLQAR 320
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 321 TQALGERITSRKAQLSSQQEQLTEGVLRSELEEARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQ 400
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 401 TRARLGGLHELQAKTRLARLKLEDERSgpigAEDADLQPTLDTLGGELELGRAAAEELAAQLAQAIEEHEALKLAHSQQQ 480
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 481 GLLRELEARLTTLDQILGEQMEGATLADRLQVVPEWAQALDKVlgrwltatpadecnpaldglwigPALPAVAGTLASLI 560
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL-----------------------AGLRGLAGAVAVLI 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 561 SGDHVPAFLNAIWLADNREEALARqptllagesvltpagdwlgpNWADIGQGAALGTMALLGERERLHTDQRAAADALAQ 640
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNIVVE--------------------DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 641 LSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAWSLQQGQRQERLLRFGQLGEELIRLDKEQAEEAQRLAETEQ 720
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 721 QLALEEARLAELQEQgeplsealqaaqdlvgrcERAQEEARGRREQQqatcqrlqlelgnlrqlialgeeelarlelela 800
Cdd:COG1196 671 LAALLEAEAELEELA------------------ERLAEEELELEEAL--------------------------------- 699
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 801 glknpeneaipdlapllaeqrnlealqlachQRLAELERQLSELDQARsadhkqlvvLQEKLATLRLERERNLTRRQGLH 880
Cdd:COG1196 700 -------------------------------LAEEEEERELAEAEEER---------LEEELEEEALEEQLEAEREELLE 739
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 881 EQFEELGVRLVDLDQAVLIAADRGKLRQEIQTLETQVEALGAINLAALEEYEEAKTRATYLENQCQDLEQALETLSQAIK 960
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 961 RIDKETQIRFRDTFDKVNEDLKSLFPKVFGGGSAWLELT-SDDLLEAGVSIMARPPGKKNATIALLSGGEKALTALALVF 1039
Cdd:COG1196 820 EIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLTdPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLF 899
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1040 AIFRLNPAPFCLLDEVDAPLDEVNVGRFCSLVKEMSSTVQFVYISHNKVSMEMAEQLVGVTMQEPGVSRIVSVDIGEAVA 1119
Cdd:COG1196 900 AIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEE 979
|
....
gi 2051267170 1120 LAEQ 1123
Cdd:COG1196 980 LAEA 983
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1107 |
3.63e-108 |
|
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: 365.83 E-value: 3.63e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 3 LKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENMTDVIFNGSVNRTAHAraSVEL 82
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSA--EVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 83 VFDNPHNRVPGEFgrfTEISVRREVLRDGTNHYQINGQKCRRKDVTDLFLGTGLGPRSYAIIEQGTVSRLVESRPADLKL 162
Cdd:pfam02463 80 TFDNEDHELPIDK---EEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 163 FMEEAAGVSRYKERRRETEQRIRHTQENLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRSRAARAELIGSELWALET 242
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 243 RLGEAKSELAQVEQALAALDAKRTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDL----- 317
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDdeekl 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 318 ---QARTQALGERITSRKAQLSSQQEQLTEGVLRSELEEARLEQCEQLLTE---QQEARLRASEQLEQTRQQQQQWQQQV 391
Cdd:pfam02463 317 kesEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKleqLEEELLAKKKLESERLSSAAKLKEEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 392 TRLQGELNQTRARLGGLHELQAKTRLARLKLEDERSGPIGAEDADLQPTLDTLGGELELGRAAAEELAAQLAQAIEEHEA 471
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 472 LKLAHSQQQGLLRELEARLTTLDQILGEQMEGATLADRLQVVPE-------------WAQALDKVLGRWLTATPADECNP 538
Cdd:pfam02463 477 TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggriisahgrlgdLGVAVENYKVAISTAVIVEVSAT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 539 ALDGLWIGPALPAVAGTLASLISGDHVPAFLNAIWLADNREEALARQPTLLAGESVLTPAGDWLGPNW------------ 606
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVvegilkdteltk 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 607 -------------ADIGQGAALGTMALLGERERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKW 673
Cdd:pfam02463 637 lkesakakesglrKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 674 QQ--------LREAWSLQQGQRQERLLRFGQLGEEL--IRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEAL 743
Cdd:pfam02463 717 LEaeelladrVQEAQDKINEELKLLKQKIDEEEEEEekSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 744 QAAQDLvgrcERAQEEARGRREQQQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAPLLAE---- 819
Cdd:pfam02463 797 KAQEEE----LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELlqel 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 820 -QRNLEALQLACHQRLAELERQLSELDQARSADHKQLVVLQEKLATLRLERERNLTRRQGLHEQFEELgvRLVDLDQAVL 898
Cdd:pfam02463 873 lLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL--LLEEADEKEK 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 899 IAADRGKLRQEIQTLETQVEALGAINLAALEEYEEAKTRATYLENQCQDLEQALETLSQAIKRIDKETQIRFRDTFDKVN 978
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 979 EDLKSLFPKVFGGGSAWLELT-SDDLLEAGVSIMARPPGKKNATIALLSGGEKALTALALVFAIFRLNPAPFCLLDEVDA 1057
Cdd:pfam02463 1031 KGWNKVFFYLELGGSAELRLEdPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDA 1110
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1058 PLDEVNVGRFCSLVKEMSSTVQFVYISHNKVSMEMAEQLVGVTMQEPGVS 1107
Cdd:pfam02463 1111 ALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVS 1160
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1113 |
2.65e-98 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 338.20 E-value: 2.65e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 3 LKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENMTDVIFNGSVNRTAHaRASVEL 82
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQSGN-EAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 83 VFDNPHNRVPGEFgrftEISVRREVLRDG-TNHYQINGQKCRRKDVTDLFLGTGLGPRSYAIIEQGTVSRLVESRPADLK 161
Cdd:TIGR02169 81 TFKNDDGKFPDEL----EVVRRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 162 LFMEEAAGVSRYKERRRETEQRIRHTQENLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRSRAARAELIGSELWALE 241
Cdd:TIGR02169 157 KIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 242 TRLGEAKSELAQVEQALAALDAKRTADEGRHVTLSVARQEAQA--------EQANRQQQIFLGGQAIARLEQQQLHQSEL 313
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 314 GRDLQARTQALGERITSRKAQLSSQQEQLTE-GVLRSELEE--ARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQ 390
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEeRKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 391 VTRLQGELNQTRARLGGLHElQAKTRLARLKLEDERsgpIGAEDADLQPTLDTLGGELELGRAAAEELAAQLAQAIEEHE 470
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQ-RLSEELADLNAAIAG---IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 471 ALKLAHSQ----QQGLLRELEARLTTLDQILGEQMEGA---------------TLADRLQVVPEWAQALDKVLGRWLTAT 531
Cdd:TIGR02169 473 DLKEEYDRvekeLSKLQRELAEAEAQARASEERVRGGRaveevlkasiqgvhgTVAQLGSVGERYATAIEVAAGNRLNNV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 532 ------PADECNPALDGLWIGPA--LP----AVAGTLASLISGDHV-----------PAFLNAIW-------LADNREEA 581
Cdd:TIGR02169 553 vveddaVAKEAIELLKRRKAGRAtfLPlnkmRDERRDLSILSEDGVigfavdlvefdPKYEPAFKyvfgdtlVVEDIEAA 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 582 LArqptLLAGESVLTPAGDWLGPNWADIG-----QGAALGTMALLGERERLHTDQRAAADALAQLSGQLAAADERRTRIV 656
Cdd:TIGR02169 633 RR----LMGKYRMVTLEGELFEKSGAMTGgsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 657 NAQELSQRTLRGQEQKWQQLREAWSLQQGQRQERLLRFGQLGEELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEqg 736
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA-- 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 737 EPLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAPL 816
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 817 LAEQRNLEAlqlachqRLAELERQLSELDQARSADHKQLVVLQEKLATLRLERERN-------LTRRQGLHEQFEELGVR 889
Cdd:TIGR02169 867 EEELEELEA-------ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrlselKAKLEALEEELSEIEDP 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 890 LVDLDQAVLIAADRGKLRQEIQTLETQVEALGAINLAALEEYEEAKTRATYLENQCQDLEQALETLSQAIKRIDKETQIR 969
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 970 FRDTFDKVNEDLKSLFPKVfGGGSAWLELTS-DDLLEAGVSIMARPPGKKNATIALLSGGEKALTALALVFAIFRLNPAP 1048
Cdd:TIGR02169 1020 FMEAFEAINENFNEIFAEL-SGGTGELILENpDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSP 1098
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267170 1049 FCLLDEVDAPLDEVNVGRFCSLVKEMSSTVQFVYISHNKVSMEMAEQLVGVTMQEPGVSRIVSVD 1113
Cdd:TIGR02169 1099 FYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQVFGLK 1163
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1015-1108 |
2.48e-56 |
|
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: 193.45 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1015 PGKKNATIALLSGGEKALTALALVFAIFRLNPAPFCLLDEVDAPLDEVNVGRFCSLVKEMSSTVQFVYISHNKVSMEMAE 1094
Cdd:cd03278 104 PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
90
....*....|....
gi 2051267170 1095 QLVGVTMQEPGVSR 1108
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 ... |
3-156 |
2.41e-46 |
|
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: 164.95 E-value: 2.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 3 LKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENMTDVIFNGSVNRTAHARASVEL 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267170 83 VFDNPHNRvpgefgrfteisvrrevlrdgtnhyqingqkcrrkdvtdlflgtglgprsYAIIEQGTVSRLVESR 156
Cdd:cd03278 81 TFDNSDGR--------------------------------------------------YSIISQGDVSEIIEAP 104
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-136 |
2.80e-24 |
|
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: 103.15 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1 MRLKLIKLAGFKSFVEPTRIE-LNADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENMTDVIF-NGSVNRTahaRA 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISgFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYkRGQAGIT---KA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 79 SVELVFDN--PHNRVPGeFGRFTEISVRREVLRDGTNHYQINGQKCRRKDVTDLFLGTGL 136
Cdd:cd03273 78 SVTIVFDNsdKSQSPIG-FENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQL 136
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1024-1108 |
4.25e-24 |
|
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: 100.46 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1024 LLSGGEKALTALALVFAIFRLNPAPFCLLDEVDAPLDEVNVGRFCSLVKEMS-STVQFVYISHNKVSMEMAEQLVGVTMQ 1102
Cdd:cd03239 94 ILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAkHTSQFIVITLKKEMFENADKLIGVLFV 173
|
....*.
gi 2051267170 1103 EpGVSR 1108
Cdd:cd03239 174 H-GVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1011-1113 |
4.22e-23 |
|
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: 99.57 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1011 MARPPGKKNATIALLSGGEKALTALALVFAIFRLNPAPFCLLDEVDAPLDEVNVGRFCSLVKEMSS-TVQFVYISHNKVS 1089
Cdd:cd03275 142 SKNPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEF 221
|
90 100
....*....|....*....|....*
gi 2051267170 1090 MEMAEQLVGVTM-QEPGVSRIVSVD 1113
Cdd:cd03275 222 FSKADALVGVYRdQECNSSKVLTLD 246
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-120 |
1.51e-18 |
|
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: 86.47 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 3 LKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSArHLRGENMTDVIFNGSVNRTAHARASVEL 82
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSS-HLRSKNLKDLIYRARVGKPDSNSAYVTA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 2051267170 83 VFDnphnrvpgefGRFTEISVRREVLRDGTNHYQINGQ 120
Cdd:cd03275 80 VYE----------DDDGEEKTFRRIITGGSSSYRINGK 107
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1003-1099 |
1.84e-17 |
|
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: 82.34 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1003 LLEAGVSIMARPPGKKNATIALLSGGEKALTALALVFAIFRLNPAPFCLLDEVDAPLDEVNVGRFCSLVKEMSSTVQFVY 1082
Cdd:cd03274 106 ILQGEVEQIAQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIV 185
|
90
....*....|....*..
gi 2051267170 1083 ISHNKVSMEMAEQLVGV 1099
Cdd:cd03274 186 ISLRNNMFELADRLVGI 202
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-152 |
1.45e-16 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 80.38 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 3 LKLIKLAGFKSFVEPTRIE-LNADMTAVVGPNGCGKSNVIDAVRWVLGESSArHLRGENMTDVIFNGSVNRTAHarASVE 81
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEpFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYT-HLREEQRQALLHEGSGPSVMS--AYVE 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267170 82 LVFDNPHNRVPGEFGrftEISVRREV-LRDgtNHYQINGQKCRRKDVTDLFLGTGLGpRS--YAIIEQGTVSRL 152
Cdd:cd03272 78 IIFDNSDNRFPIDKE---EVRLRRTIgLKK--DEYFLDKKNVTKNDVMNLLESAGFS-RSnpYYIVPQGKINSL 145
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1025-1107 |
7.41e-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: 73.16 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1025 LSGGEKALTALALVFAIFRLNPAPFCLLDEVDAPLDEVNVGRFCSLVKEMS-STVQFVYISHNKVSMEMAEQLVGVTMQE 1103
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIKKVI 157
|
....
gi 2051267170 1104 PGVS 1107
Cdd:cd03227 158 TGVY 161
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-98 |
4.29e-14 |
|
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: 71.57 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 3 LKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENmtdVIFNGSVNRTAHARASVEL 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSL---LFLAGGGVKAGINSASVEI 77
|
90
....*....|....*..
gi 2051267170 83 VFDNPHNRVP-GEFGRF 98
Cdd:cd03239 78 TFDKSYFLVLqGKVEQI 94
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1021-1109 |
4.98e-14 |
|
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: 73.06 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1021 TIALLSGGEKALTALALVFAIFRLNPAPFCLLDEVDAPLDEVNVGRFCSLVKEMSSTVQFVYISHNKVSMEMAEQLVGVT 1100
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
....*....
gi 2051267170 1101 mQEPGVSRI 1109
Cdd:cd03272 235 -FRNKVSTI 242
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-224 |
3.27e-12 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 66.37 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 6 IKLAGFKSFvEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARhlRGENMTDVIFNGSVN--RTAHARASVELV 83
Cdd:pfam13476 1 LTIENFRSF-RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSR--LKRKSGGGFVKGDIRigLEGKGKAYVEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 84 FDNPHNRvpgefgRFTEISVRREVLRDGTNHYQ-INGQKCRRKDvtdlflgtglgprsyaiiEQGTVSRLVESRPADLKL 162
Cdd:pfam13476 78 FENNDGR------YTYAIERSRELSKKKGKTKKkEILEILEIDE------------------LQQFISELLKSDKIILPL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267170 163 FMEEAAGVSRYKErRRETEQRIRHTQENLERLGDIRgelgSRLDHLKAQAETAERYKQLKSR 224
Cdd:pfam13476 134 LVFLGQEREEEFE-RKEKKERLEELEKALEEKEDEK----KLLEKLLQLKEKKKELEELKEE 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-419 |
8.15e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.94 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 177 RRETEQRIRHTQENLERLGDIRGEL---GSRLDHLKAQAETAERYKQLKSRSRAARAELIGSELWALETRLGEAKSELAQ 253
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALedaREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 254 VEQALAALDAKRTADEGRHVTLSVARQEAQAEQANrqqqifLGGQAIARLEQQqlhqselgrdLQARTQALGERITSRkA 333
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRG------NGGDRLEQLERE----------IERLERELEERERRR-A 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 334 QLSSQQEQLTEGVLRSELE-EARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQTRARLGGL--HE 410
Cdd:COG4913 363 RLEALLAALGLPLPASAEEfAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpaRL 442
|
....*....
gi 2051267170 411 LQAKTRLAR 419
Cdd:COG4913 443 LALRDALAE 451
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-87 |
1.00e-11 |
|
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: 67.72 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1 MRLKLIKLAGFKSFvEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENmtdviFNGSvNRTAHARASV 80
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEED-----FYLG-DDPDLPEIEI 73
|
....*..
gi 2051267170 81 ELVFDNP 87
Cdd:COG3593 74 ELTFGSL 80
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-208 |
1.36e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 65.03 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 2 RLKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARhlRGENMTDVIFNGSVnrtahaRASVE 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINVGSE------EASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 82 LVFDNphnrvpgefgrfteisvrrevlrdGTNHYQINgqkcRRkdvtdlflgtglgprsyaiieQGTVSRLVESRPADLK 161
Cdd:COG0419 73 LEFEH------------------------GGKRYRIE----RR---------------------QGEFAEFLEAKPSERK 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2051267170 162 LFMEEAAGVSRYKERR---RETEQRIRHTQENLERLGDIRGELGSRLDHL 208
Cdd:COG0419 104 EALKRLLGLEIYEELKerlKELEEALESALEELAELQKLKQEILAQLSGL 153
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
630-877 |
4.60e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 630 DQRAAADALAQLSGQLAAADERRTRIVNAQElSQRTLRGQEQKWQQLREAWSLQQGQRQER-LLRFGQLGEELIRLDKEQ 708
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDARE-QIELLEPIRELAERYAAARERLAELEYLRaALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 709 AEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQ-DLVGRCERAQEEARGRREQQQATCQRLQLELGNLrqlial 787
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAL------ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 788 geeelarlelelaGLKNPENEAIpdlapllaeqrnLEALQLACHQRLAELERQLSELDQARSADHKQLVVLQEKLATLRL 867
Cdd:COG4913 372 -------------GLPLPASAEE------------FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
250
....*....|
gi 2051267170 868 ERERnLTRRQ 877
Cdd:COG4913 427 EIAS-LERRK 435
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-84 |
8.55e-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: 59.54 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 3 LKLIKLAGFKSFVEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVL-GESSARHLRGENMTDVIFNGSVnrtahaRASVE 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGEV------RAQVK 74
|
...
gi 2051267170 82 LVF 84
Cdd:cd03240 75 LAF 77
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-924 |
5.17e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 60.75 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1 MRLKLIKLAGFKSFVEPTRIELNAD--MTAVVGPNGCGKSNVIDAVRWVLgessARHLRGENMTDVIFNG-SVNRTAHAR 77
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALgpIFLICGKTGAGKTTLLDAITYAL----YGKLPRRSEVIRSLNSlYAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 78 ASVELVFDNPHNRVPG-----EFGRFTEISVRREVLRDGTNHYQINGQKCRRKDVTDLFLGTGLGP-RSYAIIEQGTVSR 151
Cdd:TIGR00618 77 AELEFSLGTKIYRVHRtlrctRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTfTRVVLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 152 LVESRPADLKLFMEEAAGVSRYKERRRETEqrirhtqenlerlgDIRGELGSRLDHLKAQAETAERYKQLKSRSRAARAE 231
Cdd:TIGR00618 157 FLKAKSKEKKELLMNLFPLDQYTQLALMEF--------------AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 232 LIGSELWALETRLGEAKSELAQVEQALAALDAK-----------RTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAI 300
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqllkqlrARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 301 ARLEQQ-QLHQSELGRDLQARTQALGERITSRKAQLSSQQEQLTEGVLRSELEEARLEqceqllTEQQEARLRASEQLEQ 379
Cdd:TIGR00618 303 TQIEQQaQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA------HEVATSIREISCQQHT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 380 TRQQQQQWQQQVTRLQGELNQTRARLGGLHELQAKTRlarlkledersgPIGAEDADLQPTLDTLGGELELGRAAAEELA 459
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATID------------TRTSAFRDLQGQLAHAKKQQELQQRYAELCA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 460 AQLAQAIEEHEALKLAHSQQQGLLRELEARLTTLDQILgeQMEGATLADRLQVVPEWAQALDKVLGRWLTATPAdecnpA 539
Cdd:TIGR00618 445 AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH--LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPA-----R 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 540 LDGLWIGPALPAVAGTLASLISGDHVPAFLNAIWLAD-NREEALARQPTLLAGEsvltpagdwlgpnwadigqgaalgTM 618
Cdd:TIGR00618 518 QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSErKQRASLKEQMQEIQQS------------------------FS 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 619 ALLGERERLHTDQRAAADALAQLSGQLAAADERRTRIvnaQELSQRTLRGQEQKWQQLREAWSLQQGQRQERLLRFGQLG 698
Cdd:TIGR00618 574 ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML---ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 699 EELIRLDKEQAEEAqrLAETEQQLALEEARLAELQ------EQGEPLSEALQAAQDLVGRCERAQEEARGRREQQQ---- 768
Cdd:TIGR00618 651 LQLTLTQERVREHA--LSIRVLPKELLASRQLALQkmqsekEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEnass 728
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 769 ATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAPLLAEQRNLEALQLACHQRLAELERQLSELDqar 848
Cdd:TIGR00618 729 SLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLE--- 805
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 849 sADHKQlvVLQEKLATLRLERERNLTRRQGLHEQFEELGVRLVDLDQAVLIAADRGK----LRQEIQTLETQVEALGAIN 924
Cdd:TIGR00618 806 -AEIGQ--EIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKqlaqLTQEQAKIIQLSDKLNGIN 882
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1025-1085 |
1.06e-08 |
|
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: 57.31 E-value: 1.06e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267170 1025 LSGGEKALTALALVFAIFRLNPAPFCLLDEVDAPLD---EVNVGRfcsLVKEMSSTVQFVYISH 1085
Cdd:cd03273 167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDlshTQNIGR---MIKTHFKGSQFIVVSL 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
726-972 |
3.68e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 726 EARLAELQEQGEPLSEALQAAQDLvgrceRAQEEARGRREQQQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNP 805
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDA-----REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 806 ENEAipDLAPLLAEQRNLEALQLACHQRLAELERQLseldqaRSADHKQLVVLQEKLATLRLERERNLTRRQGLHEQFEE 885
Cdd:COG4913 299 ELRA--ELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 886 LGVRLVDLDQAVLiaadrgKLRQEIQTLETQVEALGAinlAALEEYEEAKTRATYLENQCQDLEQALETLSQAIKRIDKE 965
Cdd:COG4913 371 LGLPLPASAEEFA------ALRAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
....*..
gi 2051267170 966 tQIRFRD 972
Cdd:COG4913 442 -LLALRD 447
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
6-84 |
4.51e-08 |
|
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: 54.99 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 6 IKLAGFKSFVEPTRI-ELNADMTAVVGPNGCGKSNVIDAVRWVLGeSSARHLRGENMTDVIFNGSvNRTAHARASVELVF 84
Cdd:cd03274 6 LVLENFKSYAGEQVIgPFHKSFSAIVGPNGSGKSNVIDSMLFVFG-FRASKMRQKKLSDLIHNSA-GHPNLDSCSVEVHF 83
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-90 |
7.71e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 55.71 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 2 RLKLIKLAGFKSFVEpTRIELnADMTAVVGPNGCGKSNVIDAVRWV-------LGESSARhlRGEnMTDVIFNGSVNRTA 74
Cdd:COG4637 1 MITRIRIKNFKSLRD-LELPL-GPLTVLIGANGSGKSNLLDALRFLsdaarggLQDALAR--RGG-LEELLWRGPRTITE 75
|
90
....*....|....*.
gi 2051267170 75 HARasVELVFDNPHNR 90
Cdd:COG4637 76 PIR--LELEFAEEDER 89
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
707-1099 |
8.89e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 707 EQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVgRCERAQEEARGRREqqqatcqrlqlelgNLRQLIA 786
Cdd:PRK02224 462 EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERRE--------------DLEELIA 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 787 LGEEELARLELELAGLKNPENEAIPDLAPLLAEQRNLEALQLACHQRLAELERQLSELDQARSADHKqLVVLQEKLATLR 866
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 867 LERERNLTRRQGLHEQFEELGVRLVDLDQ------AVLIAADRGKLRQEIQTLETQVE------------------ALGA 922
Cdd:PRK02224 606 DEIERLREKREALAELNDERRERLAEKRErkreleAEFDEARIEEAREDKERAEEYLEqveekldelreerddlqaEIGA 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 923 INlAALEEYEEAKTRATYLENQCQDLE---QALETLSQAIKRIDKETQIRFRDTFDKVnedLKSLFPKVFGGGS-AWLEL 998
Cdd:PRK02224 686 VE-NELEELEELRERREALENRVEALEalyDEAEELESMYGDLRAELRQRNVETLERM---LNETFDLVYQNDAySHIEL 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 999 TSDDLLEAGvsimarppgKKNATI---ALLSGGEKALTALALVFAIFRL--------NPAPFCLLDEVDAPLDEVNVGRF 1067
Cdd:PRK02224 762 DGEYELTVY---------QKDGEPlepEQLSGGERALFNLSLRCAIYRLlaegiegdAPLPPLILDEPTVFLDSGHVSQL 832
|
410 420 430
....*....|....*....|....*....|....
gi 2051267170 1068 CSLVKEMSS--TVQFVYISHNKVSMEMAEQLVGV 1099
Cdd:PRK02224 833 VDLVESMRRlgVEQIVVVSHDDELVGAADDLVRV 866
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
225-786 |
1.06e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 56.42 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 225 SRAARAELIGSELWALETRLGEAKSELAQVEQALAAL---------DAKRTADEGRHVTL---SVARQEAQAEQANRQQQ 292
Cdd:COG3321 804 TGLVRQCLAAAGDAVVLPSLRRGEDELAQLLTALAQLwvagvpvdwSALYPGRGRRRVPLptyPFQREDAAAALLAAALA 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 293 IFLGGQAIARLEQQQLHQSELGRDLQARTQALGERITSRKAQLSSQQEQLTEGVLRSELEEARLEQCEQLLTEQQEARLR 372
Cdd:COG3321 884 AALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGA 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 373 ASEQLEQTRQQQQQWQQQVTRLQGELNQTRARLGGLHELQAKTRLARLKLEDERSGPIGAEDADLQPTLDTLGGELELGR 452
Cdd:COG3321 964 LLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAA 1043
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 453 AAAEELAAQLAQAIEEHEALKLAHSQQQGLLRELE---ARLTTLDQILGEQMEGATLADRLQVVPEWAQALDKVLGRWLT 529
Cdd:COG3321 1044 AAAALAALAAAAAAAAALALALAALLLLAALAELAlaaAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAA 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 530 ATPADECNPALDGLWIGPALPAVAGTLASLISGDHVPAFLNAIWLADNREEALARQPTLLAGESVLTPAGDWLGPNWADI 609
Cdd:COG3321 1124 LLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAA 1203
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 610 GQGAALGTMALLGERERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAWSLQQGQRQE 689
Cdd:COG3321 1204 LLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAA 1283
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 690 RLLRFGQLGEELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQQQA 769
Cdd:COG3321 1284 ALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAAL 1363
|
570
....*....|....*..
gi 2051267170 770 TCQRLQLELGNLRQLIA 786
Cdd:COG3321 1364 AAAAGAAAAAAALALAA 1380
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
615-1095 |
2.98e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 615 LGTMALLGERERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREawsLQQGQRQERLLRF 694
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 695 GQLGEELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEP------LSEALQAAQDLVGRCERAQEEAR------- 761
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaaleerLKEARLLLLIAAALLALLGLGGSllslilt 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 762 ----------------GRREQQQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAPLLAEQRNLEA 825
Cdd:COG4717 275 iagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 826 LQLACHQRL--AELERQLSELDQARSAD-----------HKQLVVLQEKLATL--RLERERNLTRRQGLHEQFEELGVRL 890
Cdd:COG4717 355 EAEELEEELqlEELEQEIAALLAEAGVEdeeelraaleqAEEYQELKEELEELeeQLEELLGELEELLEALDEEELEEEL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 891 VDLDQAV-LIAADRGKLRQEIQTLETQVEALGAINL--AALEEYEEAKTRATYLENQCQDLEQALETLSQAIKRIDKETQ 967
Cdd:COG4717 435 EELEEELeELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 968 irfrdtfDKVNEDLKSLFPKVFGGgsawleLTSDDLLEAGVSIMARPPGKKNATIALLSGGEKALTALALVFAIFRL--- 1044
Cdd:COG4717 515 -------PPVLERASEYFSRLTDG------RYRLIRIDEDLSLKVDTEDGRTRPVEELSRGTREQLYLALRLALAELlag 581
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2051267170 1045 NPAPFcLLDEVDAPLDEVNVGRFCSLVKEMSSTVQFVYISHNKVSMEMAEQ 1095
Cdd:COG4717 582 EPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVELFQE 631
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
623-783 |
5.78e-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: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 623 ERERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAWSLQQGQRQERLLR-FGQLGEEL 701
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEReIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 702 IRLDKEQAEEAQRLAETEQQLALEEARLAELQEQgepLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNL 781
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
..
gi 2051267170 782 RQ 783
Cdd:COG4913 432 ER 433
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-59 |
6.13e-07 |
|
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: 50.44 E-value: 6.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2051267170 6 IKLAGFKSFVEPTRIEL-NADMTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGE 59
Cdd:cd03227 2 IVLGRFPSYFVPNDVTFgEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS 56
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-54 |
3.97e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 50.00 E-value: 3.97e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267170 1 MRLKLIKLAGFKSFvEPTRIELNAD--MTAVVGPNGCGKSNVIDAVRWVLGESSAR 54
Cdd:COG3950 1 MRIKSLTIENFRGF-EDLEIDFDNPprLTVLVGENGSGKTTLLEAIALALSGLLSR 55
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
699-938 |
5.84e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 699 EELIRLDKEQAEEA-----QRLAETEQQLALEEARLAELQEQ--GEPLSEALQAAQDLVGRCERAQEEARGRREQQQATC 771
Cdd:COG3206 163 EQNLELRREEARKAlefleEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 772 QRLQLELGNLRQLIALGEeelarlelelaglknpENEAIPDLApllaeqrnlealqlachQRLAELERQLSELDQARSAD 851
Cdd:COG3206 243 AALRAQLGSGPDALPELL----------------QSPVIQQLR-----------------AQLAELEAELAELSARYTPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 852 HKQLVVLQEKLATLRLERERNLTR--------RQGLHEQFEELGVRLVDLDQAVLIAAdrgKLRQEIQTLETQVEALGAI 923
Cdd:COG3206 290 HPDVIALRAQIAALRAQLQQEAQRilasleaeLEALQAREASLQAQLAQLEARLAELP---ELEAELRRLEREVEVAREL 366
|
250
....*....|....*
gi 2051267170 924 NLAALEEYEEAKTRA 938
Cdd:COG3206 367 YESLLQRLEEARLAE 381
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-338 |
5.89e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 172 RYKERRRETEQRIRHTQENLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRSRA--------ARAELIGSELWALETR 243
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaeleaelERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 244 LGEAKSELAQVEQALAALDAKRTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDLQARTQA 323
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170
....*....|....*
gi 2051267170 324 LGERITSRKAQLSSQ 338
Cdd:COG4913 774 RIDALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
706-927 |
9.03e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 706 KEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNLRQLI 785
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 786 ALGEEELARLELELAGLKNPENEAI----PDLAPLLAEQRNLEALQLACHQRLAELERQLSELDQARSADHKQLVVLQEK 861
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267170 862 LATLRLERERNLTRRQGLHEQFEELGVRLVDLDQAVL-IAADRGKLRQEIQTLETQVEALGAINLAA 927
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAeLQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-52 |
9.78e-06 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 49.13 E-value: 9.78e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2051267170 1 MRLKLIKLAGFKSFvEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESS 52
Cdd:pfam13175 1 MKIKSIIIKNFRCL-KDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKE 51
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
251-715 |
1.03e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.58 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 251 LAQVEQALAALDAKRTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDLQARTQALGERITS 330
Cdd:COG4995 5 ALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 331 RKAQLSSQQEQLTEGVLRSELEEARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQTRARLGGLHE 410
Cdd:COG4995 85 LALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 411 LQAKTRLARLKLEDERSGPIGAEDADLQPTLDTLGGELELGRAAAEELAAQLAQAIEEHEALKLAHSQQQGLLRELEARL 490
Cdd:COG4995 165 LLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 491 TTLDQILGEQMEGATLADRLQVVPEWAQALDKVLGRWLTATPADECNPALDGLWIGPALPAVAGTLASLISGDHVPAFLN 570
Cdd:COG4995 245 AAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 571 AIWLADNREEALARQPTLLAGESVLTPAGDWLGPNWADIGQGAALGTMALLGERERLHTDQRAAADALAQLSGQLAAADE 650
Cdd:COG4995 325 LLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALA 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051267170 651 RRTRIVNAQELSQRTLRGQEQKWQQLREAWSLQQGQRQERLLRFGQLGEELIRLDKEQAEEAQRL 715
Cdd:COG4995 405 AAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQLLIAPIEAELPGIKRL 469
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
20-130 |
1.64e-05 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 47.97 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 20 IELNADMTAVVGPNGCGKSNVIDAVRWVLGESSarhlrgenMTDVIfngsvnRTAHARASVELVFDNPHN------RVPG 93
Cdd:cd03241 17 LDFEEGLTVLTGETGAGKSILLDALSLLLGGRA--------SADLI------RSGAEKAVVEGVFDISDEeeakalLLEL 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 2051267170 94 EFGRFTEISVRREVLRDGTNHYQINGQKCRRKDVTDL 130
Cdd:cd03241 83 GIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLREL 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
630-890 |
3.67e-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: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 630 DQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAWSLQQGQRQErllrfgqLGEELIRLDKEQA 709
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 710 EEAQRLAETEQQLAleeARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNLRQLIALGE 789
Cdd:COG4942 94 ELRAELEAQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 790 EELARLELELAGLKnpeneaipdlapllAEQRNLEALQLACHQRLAELERQLSELDQARSADHKQLVVLQEKLAtlRLER 869
Cdd:COG4942 171 AERAELEALLAELE--------------EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA--RLEA 234
|
250 260
....*....|....*....|.
gi 2051267170 870 ERNLTRRQGLHEQFEELGVRL 890
Cdd:COG4942 235 EAAAAAERTPAAGFAALKGKL 255
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-178 |
3.73e-05 |
|
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: 46.91 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 3 LKLIKLAGFKSFvEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVlgeSSARHLRGENMTDVIfngsvnRTAHARASVEL 82
Cdd:cd03242 1 LKSLELRNFRNY-AELELEFEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELI------RWGAEEAKISA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 83 VFDNPHNRVPGEFGRFTEisvrrevlrdGTNHYQINGQKCRRkdvTDLFLGtglgprsyaiieqgtVSRLVESRPADLKL 162
Cdd:cd03242 71 VLERQGGELALELTIRSG----------GGRKARLNGIKVRR---LSDLLG---------------VLNAVWFAPEDLEL 122
|
170
....*....|....*.
gi 2051267170 163 FMEEAAgvsrykERRR 178
Cdd:cd03242 123 VKGSPA------DRRR 132
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-84 |
3.82e-05 |
|
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: 46.11 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1 MRLKLIKLAGFKSFVEPTRIEL----NADMTAVVGPNGCGKSNVIDAVRWVL-GESSArhLRGENMTDVIFNgsvnrTAH 75
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYALyGKTPR--YGRQENLRSVFA-----PGE 73
|
....*....
gi 2051267170 76 ARASVELVF 84
Cdd:cd03279 74 DTAEVSFTF 82
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
188-448 |
6.21e-05 |
|
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: 47.25 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 188 QENLERLGDIRGELGsrLDHLkAQAETAERYKQLKsrsraARAELIGSELWALETRLGEAKSELAQVEQALAALdaKRTA 267
Cdd:COG3096 416 QQAVQALEKARALCG--LPDL-TPENAEDYLAAFR-----AKEQQATEEVLELEQKLSVADAARRQFEKAYELV--CKIA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 268 DEgrhVTLSVARQEAQA--EQANRQQQIflggqaIARLEQQQLHQSELGRDL--QARTQALGERITSRKAQLSSQQEQLT 343
Cdd:COG3096 486 GE---VERSQAWQTAREllRRYRSQQAL------AQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELE 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 344 EgvLRSELEeARLEQCEQLLTEQQEARlraseqleqtrqqqqqwqqqvTRLQGELNQTRARLGGLHE-----LQAKTRLA 418
Cdd:COG3096 557 E--LLAELE-AQLEELEEQAAEAVEQR---------------------SELRQQLEQLRARIKELAArapawLAAQDALE 612
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267170 419 RLK--------------------LEDER-----------------------SGPIGAEDADLQPTLDTLGGEL 448
Cdd:COG3096 613 RLReqsgealadsqevtaamqqlLEREReatverdelaarkqalesqierlSQPGGAEDPRLLALAERLGGVL 685
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
6-63 |
6.97e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 46.19 E-value: 6.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267170 6 IKLAGFKSFVEPTRIELNAD------MTAVVGPNGCGKSNVIDAVRWVLGESSARHLRGENMTD 63
Cdd:COG1106 5 FSIENFRSFKDELTLSMVASglrllrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVE 68
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
622-953 |
7.65e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 622 GERERLHTDQRAA--ADALAQLSGQLAAADERRTRIvnAQELSqrTLRGQEQKWQQLreawsLQQGQRQERLL--RFGQL 697
Cdd:pfam01576 424 SERQRAELAEKLSklQSELESVSSLLNEAEGKNIKL--SKDVS--SLESQLQDTQEL-----LQEETRQKLNLstRLRQL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 698 GEELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQ-- 775
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEkt 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 776 ------------LELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAPLLAEQRNLEALQLACHQRLAELERQLSE 843
Cdd:pfam01576 575 knrlqqelddllVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 844 LDQARS---ADHKQLVVLQEKLATLRLERERNltrRQGLHEQFEELGVRLVDLDQAvLIAADRGKLRQEI--QTLETQVE 918
Cdd:pfam01576 655 LERTNKqlrAEMEDLVSSKDDVGKNVHELERS---KRALEQQVEEMKTQLEELEDE-LQATEDAKLRLEVnmQALKAQFE 730
|
330 340 350
....*....|....*....|....*....|....*
gi 2051267170 919 AlgaiNLAALEEYEEAKTRAtyLENQCQDLEQALE 953
Cdd:pfam01576 731 R----DLQARDEQGEEKRRQ--LVKQVRELEAELE 759
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-178 |
7.98e-05 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 46.30 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1 MRLKLIKLAGFKSFvEPTRIELNADMTAVVGPNGCGKSNVIDAVrWVLgeSSARHLRGENMTDVIFNGSVNRTAHARASV 80
Cdd:PRK00064 1 MYLTRLSLTDFRNY-EELDLELSPGVNVLVGENGQGKTNLLEAI-YLL--APGRSHRTARDKELIRFGAEAAVIHGRVEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 81 ELVfdnphnrvpgefgrftEISVRREVLRDGTNHYQINGQKCRRkdvtdlflgtglgPRSYAIIeqgtvSRLVESRPADL 160
Cdd:PRK00064 77 GGR----------------ELPLGLEIDKKGGRKVRINGEPQRK-------------LAELAGL-----LNVVLFTPEDL 122
|
170
....*....|....*...
gi 2051267170 161 KLFMEEAAgvsrykERRR 178
Cdd:PRK00064 123 RLVKGGPS------ERRR 134
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1025-1097 |
8.25e-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: 8.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051267170 1025 LSGGEKALTALALVFAifrLNPaPFCLLDEVDAPLDEVNVGRFCSLVKEMSST-VQFVYISHNkvsMEMAEQLV 1097
Cdd:cd00267 81 LSGGQRQRVALARALL---LNP-DLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHD---PELAELAA 147
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
209-414 |
1.04e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 209 KAQAETAERYKQLKSRSRAARAEL--IGSELWALETRLGEAKSELAQVEQALAALDAKRTADEGRHVTLSVARQEAQAEQ 286
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELaaLKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 287 ANRQQQIFLGGQAIARLEQQQ----LHQSELGRDLQARTQALGERITSRKAQLSSQQEQLTEGVLRSELEEARLEQCEQL 362
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2051267170 363 LTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQTRARLGGLHELQAK 414
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
699-986 |
2.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 699 EELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEaRGRREQQQATCQRLQLEL 778
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR-LEELEERHELYEEAKAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 779 GNLRQLIALGEEELARLELEL-AGLKNPENEAIPDLAPLLAEQRNLEalqlachQRLAELERQLSELDQAR--------- 848
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELK-------KEIKELKKAIEELKKAKgkcpvcgre 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 849 -SADHKQlvvlqEKLATLRLERERNLTRRQGLHEQFEELGVRLVDLDQAVLIAADRGKLRQEIQTLETQVEALGAINLAA 927
Cdd:PRK03918 445 lTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 928 LE----EYEEAKTRATYLE----------NQCQDLEQALETLSQAIKRIDKE-----TQIRFR--DTFDKVNEDLKSLFP 986
Cdd:PRK03918 520 LEkkaeEYEKLKEKLIKLKgeikslkkelEKLEELKKKLAELEKKLDELEEElaellKELEELgfESVEELEERLKELEP 599
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
228-448 |
2.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 228 ARAELIGSELWALETRLGEAKSELAQVEQALAAL----------DAKRTADE--GRHVTLSVARQEAQA--------EQA 287
Cdd:PRK04863 449 AKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkiagevsrsEAWDVAREllRRLREQRHLAEQLQQlrmrlselEQR 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 288 NRQQQiflggQAIARLEQ--QQLHQSELGRD-LQARTQALGERITSRKAQLSSQQEQLTEgvLRSELEE-----ARLEQC 359
Cdd:PRK04863 529 LRQQQ-----RAERLLAEfcKRLGKNLDDEDeLEQLQEELEARLESLSESVSEARERRMA--LRQQLEQlqariQRLAAR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 360 EQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQTRarlggLHELQAKTRLARLKLEDER-SGPIGAEDADLQ 438
Cdd:PRK04863 602 APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELT-----VERDELAARKQALDEEIERlSQPGGSEDPRLN 676
|
250
....*....|
gi 2051267170 439 PTLDTLGGEL 448
Cdd:PRK04863 677 ALAERFGGVL 686
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
832-981 |
2.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 832 QRLAELERQLSELDQarsadhkQLVVLQEKLATLRLERERnLTRRQGLHEQFEELGVRLVDLDQAVL-IAADRGKLRQ-- 908
Cdd:COG4913 610 AKLAALEAELAELEE-------ELAEAEERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAEReIAELEAELERld 681
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267170 909 ----EIQTLETQVEALGAINLAALEEYEEAKTRATYLENQCQDLEQALETLSQAIKRIDKETQIRFRDTFDKVNEDL 981
Cdd:COG4913 682 assdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
697-843 |
2.50e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 697 LGEELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQL 776
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267170 777 ELGNLRQLIALGEEELARLELELAGLKnpenEAIPDLAPLL--AEQRNLEA----------LQLACHQRLAELERQLSE 843
Cdd:PRK09039 124 ELDSEKQVSARALAQVELLNQQIAALR----RQLAALEAALdaSEKRDRESqakiadlgrrLNVALAQRVQELNRYRSE 198
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-761 |
3.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 311 SELGRDLQARTQALGERITSRKAQLSSQQEQLTEgvLRSELEEARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQ 390
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKE--AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 391 VTRLQGELNQTRARLGGLhelqaKTRLARLKLEDERSGPIGAEDADLQPTLDTLGGEL-ELGRAAAEELAAQLAQAIEEH 469
Cdd:COG4717 127 LLPLYQELEALEAELAEL-----PERLEELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 470 EALKLAHSQQQGLLRELEARLTTLDQILgEQMEGATLADRLQVVPEWAQALDKVLGRWLTATPADECNPALDGLWIGPAL 549
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEEL-EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 550 PAVAGTLASLISGDHVPAFLNAI--------WLADNREEALARQPTLLAGESVLTPAGdwLGPNWADIGQGAALGTMALL 621
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEaeelqalpALEELEEEELEELLAALGLPPDLSPEE--LLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 622 GERERLHTDQRAAADALAQLSGqLAAADERRTRIVNAQELSQrtlrgQEQKWQQLREAWSLQQGQRQERLLRFG--QLGE 699
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAG-VEDEEELRAALEQAEEYQE-----LKEELEELEEQLEELLGELEELLEALDeeELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051267170 700 ELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEpLSEALQAAQDLVGRCERAQEEAR 761
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGE-LAELLQELEELKAELRELAEEWA 493
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
641-919 |
3.97e-04 |
|
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: 44.50 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 641 LSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAWslqQGQRQERLLRFGQLGEELIRLDKEQAE-EAQRLAETE 719
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEElEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 720 QQLALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEA----RGRREQQQATCQR--LQLELGNLRQLIALGEEELA 793
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREteleRMKERAKKAGAQRkeEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 794 RLELELAGLKNPENEAIPDLAPLLAEQRNLEALQLACHQRLAELERQLSELDQAR---SADHKQLVVLQEKLATLRLERE 870
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQerlNASERKVEGLGEELSSMAAQRD 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2051267170 871 RNLTRRQGLHEQFEELGVRLVDLDQAvlIAADRGKLRQEIQTLETQVEA 919
Cdd:pfam07888 269 RTQAELHQARLQAAQLTLQLADASLA--LREGRARWAQERETLQQSAEA 315
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
154-489 |
4.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 154 ESRPAD-LKLFMEEAAGVSRYKERRRETEQR---IRHTQENLERLGDIR-GELGSRLDHLKaQAETAERYKQLKSRSRAA 228
Cdd:PTZ00121 1468 EAKKADeAKKKAEEAKKADEAKKKAEEAKKKadeAKKAAEAKKKADEAKkAEEAKKADEAK-KAEEAKKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 229 RAEligselwalETRLGEaksELAQVEQALAALDAKRtADEGRHVTLSVARQEAQAEQAnRQQQIFLGGQAIARLEQQQL 308
Cdd:PTZ00121 1547 KAD---------ELKKAE---ELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEA 1612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 309 HQSElgrdlqartqalGERITSRKAQLSSQQEQLTEGVLRSELEEARleQCEQLLTEQQEARLRASEqLEQTRQQQQQWQ 388
Cdd:PTZ00121 1613 KKAE------------EAKIKAEELKKAEEEKKKVEQLKKKEAEEKK--KAEELKKAEEENKIKAAE-EAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 389 QQVTRLQGELNQTRARLGGLHELQAKTRLARLKLEDERSgpiGAEDADLQPTLDTLGGElELGRAAAEELAAQLAQAIEE 468
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK---KAEELKKAEEENKIKAE-EAKKEAEEDKKKAEEAKKDE 1753
|
330 340
....*....|....*....|.
gi 2051267170 469 HEALKLAHSQQQGLLRELEAR 489
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIR 1774
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
527-903 |
4.97e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 44.24 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 527 WLTATPADECNPALDGLWIGPALPAVAGTLASLISGDHVPAFLNAIWLADNREEALARQPTLLAGESVLTPAGDWLGPNW 606
Cdd:COG3903 555 WFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAA 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 607 ADIGQGAALGTMALLGERERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAWSLQQGQ 686
Cdd:COG3903 635 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAA 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 687 RQERLLRFGQLGEELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQ 766
Cdd:COG3903 715 AAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAA 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 767 QQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAiPDLAPLLAEQRNLEALQLACHQRLAELERQLSELDQ 846
Cdd:COG3903 795 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAA-AAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAA 873
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2051267170 847 ARSADHKQLVVLQEKLATLRLERERNLTRRQGLHEQFEELGVRLVDLDQAVLIAADR 903
Cdd:COG3903 874 AAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAA 930
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
623-968 |
5.04e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 623 ERERLHTDQRAAADALAQLSGQLAAADERRTRivnAQELSQrtLRGQEQKWQQLREAWSLQQGQ--RQERLLRFGQLGEE 700
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKK---QQLLKQ--LRARIEELRAQEAVLEETQERinRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 701 LIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVGRCE---RAQEEARGRREQqqaTCQRLQLE 777
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIhirDAHEVATSIREI---SCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 778 lGNLRQLiALGEEELARLELELAGLKNPENEAIPDLAPLLAEQRNLEALQLACHqrlAELERQLSELDQARSADHKQLVV 857
Cdd:TIGR00618 379 -QHIHTL-QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK---KQQELQQRYAELCAAAITCTAQC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 858 LQEKLATLRlerernlTRRQGLHEQFEELGVRLVDLDQAVLIAADRGKLRQEIQTLETQVE-----------------AL 920
Cdd:TIGR00618 454 EKLEKIHLQ-------ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCgscihpnparqdidnpgPL 526
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2051267170 921 GAINLAALEEYEEAKTRATYLENQCQDLEQALETLSQAIKRIDKETQI 968
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-264 |
5.29e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1 MRLKLIKLAGFKSFvEPTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSarhlRGENMTDVIFNGSVNrtaharASV 80
Cdd:PRK01156 1 MIIKRIRLKNFLSH-DDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNN------LEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 81 ELVFdnphnRVPGEFGRfteisVRREVLRDGTN-----HYQINGQKCRR--KDVTDLFLGTGLGP-----RSYAIIEQGT 148
Cdd:PRK01156 70 ELEF-----RIGGHVYQ-----IRRSIERRGKGsrreaYIKKDGSIIAEgfDDTTKYIEKNILGIskdvfLNSIFVGQGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 149 VSRLVESRPADLKLFMEEAAGVSRYKERRRETEQRIRHTQENLERLGDIRGELGSR---LDHLKAQAETAERYKQLKSRS 225
Cdd:PRK01156 140 MDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSnleLENIKKQIADDEKSHSITLKE 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2051267170 226 RAARAELIGS-------------ELWALETRLGEAKSELAQVEQALAALDAK 264
Cdd:PRK01156 220 IERLSIEYNNamddynnlksalnELSSLEDMKNRYESEIKTAESDLSMELEK 271
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-499 |
5.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1 MRLKLIKLAGFKSFVEpTRIELNADMTAVVGPNGCGKSNVIDAVRWVLGESSARhlrGENMTDVIFNGSVNrtaharASV 80
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKAL---DDTLDDVITIGAEE------AEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 81 ELVFDNP------HNRVPGEFGRfteISVRREVLRDGTNhyQINGQKCRRKDVTDLFLGTGLGPRSYAIIEQGTVSRLVE 154
Cdd:PRK02224 71 ELWFEHAggeyhiERRVRLSGDR---ATTAKCVLETPEG--TIDGARDVREEVTELLRMDAEAFVNCAYVRQGEVNKLIN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 155 SRPADLKLFMEEAAGVSRYKE-RRRETEQRIRhtqenlerLGDIRGELGSRLDHLKAQAETAERyKQLKSRsraaraeli 233
Cdd:PRK02224 146 ATPSDRQDMIDDLLQLGKLEEyRERASDARLG--------VERVLSDQRGSLDQLKAQIEEKEE-KDLHER--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 234 gseLWALETRLGEAKSELAQVEqalaalDAKRTADEGRHvtlsvARQEAQAEQANRQQQIFLGGQAIARLeQQQLHQSEL 313
Cdd:PRK02224 208 ---LNGLESELAELDEEIERYE------EQREQARETRD-----EADEVLEEHEERREELETLEAEIEDL-RETIAETER 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 314 GRDlqartqALGERITSRKAQLSSQQEQLTEGVLRSELEEARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTR 393
Cdd:PRK02224 273 ERE------ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 394 LQGELNQTRARLGGLHE----LQAKTRLARLKLEDERSgpigaedadlqpTLDTLGGELELGRAAAEELAAQLAQAIEEH 469
Cdd:PRK02224 347 LREDADDLEERAEELREeaaeLESELEEAREAVEDRRE------------EIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
490 500 510
....*....|....*....|....*....|
gi 2051267170 470 EALKLAHSQQQGLLRELEARLTTLDQILGE 499
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEE 444
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-421 |
5.53e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 174 KERRRETEQRIRHTQENLERLGDIRGELGSRLDHLKAQ-AETAERYKQLKSRSRAARAEL--IGSELWALETRLGEAKSE 250
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAELaeLEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 251 LAQVEQALAALdakrtadeGRHVTLSVARQEAQAEQANRQQQIFlggQAIARLEQQQLhqselgRDLQARTQALgeriTS 330
Cdd:COG4942 106 LAELLRALYRL--------GRQPPLALLLSPEDFLDAVRRLQYL---KYLAPARREQA------EELRADLAEL----AA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 331 RKAQLSSQQEQLTEgvLRSELEEARLEQcEQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQTRARLGGLHE 410
Cdd:COG4942 165 LRAELEAERAELEA--LLAELEEERAAL-EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|.
gi 2051267170 411 LQAKTRLARLK 421
Cdd:COG4942 242 RTPAAGFAALK 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
604-941 |
5.55e-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: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 604 PNWADIGQgaalgtmALLGERERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLR-EAWSL 682
Cdd:pfam12128 593 PEWAASEE-------ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFdEKQSE 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 683 QQGQRQERLLRFGQLGEELIRLDKE--QAEEAQRLAETEQQLALEEARLaELQEQGEPLSEALQAAQDLVGRCERAQEEA 760
Cdd:pfam12128 666 KDKKNKALAERKDSANERLNSLEAQlkQLDKKHQAWLEEQKEQKREART-EKQAYWQVVEGALDAQLALLKAAIAARRSG 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 761 RGRR----EQQQAT-----------CQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAPLLAE-QRNLE 824
Cdd:pfam12128 745 AKAElkalETWYKRdlaslgvdpdvIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNiERAIS 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 825 ALQLACHQRLAELERQLSELDQARSADHKQLVVLQEKLATLRLERER--NLTRRQGLHEQFEELGVRLVDLDQAVLI-AA 901
Cdd:pfam12128 825 ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlaTLKEDANSEQAQGSIGERLAQLEDLKLKrDY 904
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2051267170 902 DRGKLRQEIQTLETQVEALGAINLAalEEYEEAKTRATYL 941
Cdd:pfam12128 905 LSESVKKYVEHFKNVIADHSGSGLA--ETWESLREEDHYQ 942
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-786 |
6.24e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 619 ALLGERERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAWSLQQGQRQERL------- 691
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 692 -----------------LRFGQLGEELIRLDKEQAEE----AQRLAETEQQLALEEARL----AELQEQGEPLSEALQAA 746
Cdd:COG4942 118 rqpplalllspedfldaVRRLQYLKYLAPARREQAEElradLAELAALRAELEAERAELeallAELEEERAALEALKAER 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2051267170 747 QDLVGRCERAQEEARGRREQQQATCQRLQLELGNLRQLIA 786
Cdd:COG4942 198 QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
621-878 |
6.48e-04 |
|
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: 43.73 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 621 LGERERLHTDQRAAADALAQLSGQLAAADERRTRIVnaQELSQRTLRGQEQKWQQLREAWSLQQGQRQERLLRfGQLGEE 700
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQR--RELESRVAELKEELRQSREKHEELEEKYKELSASS-EELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 701 LIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGN 780
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 781 LRQLIALGEEELARLELELAGLKNPENEA---IPDLAPLLAEQRNLEALQLACHQRLAELERQLSELDQARSADHKQL-- 855
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELhq 276
|
250 260
....*....|....*....|...
gi 2051267170 856 VVLQEKLATLRLErERNLTRRQG 878
Cdd:pfam07888 277 ARLQAAQLTLQLA-DASLALREG 298
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-341 |
7.89e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 170 VSRYKERRRETEQRIRHTQENLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRSRAARAELIGSELWALETRL----- 244
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylky 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 245 --GEAKSELAQVEQALAALDAKRTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDLQARTQ 322
Cdd:COG4942 144 laPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
170
....*....|....*....
gi 2051267170 323 ALGERITSRKAQLSSQQEQ 341
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
622-955 |
8.20e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 622 GERERLHTDQRAAADALAQLSGQLAAADERRTRIVN---AQELSQRTLRGQEQKWQQLREAWSLQQGQRQERLLRFGQLG 698
Cdd:PRK02224 220 EEIERYEEQREQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 699 EELIRLDKEQAEEAQRLAETEQQLA-----LEEARLAeLQEQGEPLSEALQAAQDLVGRCERAQEEA----------RGR 763
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELEDRDEelrdrLEECRVA-AQAHNEEAESLREDADDLEERAEELREEAaeleseleeaREA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 764 REQQQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAPLLAEQRNL-------EALQLA------- 829
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTArerveeaEALLEAgkcpecg 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 830 --------------CHQRLAELERQLSELDQARSADHKQLVVLqEKLATLRLERERNLTRRQGLHEQFEelgvrlvdlDQ 895
Cdd:PRK02224 459 qpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIA---------ER 528
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267170 896 AVLIAADRGK---LRQEIQTLETQVEALGAINLAALEEYEEAKTRATYLENQCQDLEQALETL 955
Cdd:PRK02224 529 RETIEEKRERaeeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1022-1108 |
9.56e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1022 IALLSGGEKALTALALVFAIFRL--NPAPFCLLDEVDAPLDEVNV-GRFCSLVKEMSSTV--QFVYISHNKVSMEMAEQL 1096
Cdd:cd03240 113 RGRCSGGEKVLASLIIRLALAETfgSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKnfQLIVITHDEELVDAADHI 192
|
90
....*....|..
gi 2051267170 1097 VGVTMQEPGVSR 1108
Cdd:cd03240 193 YRVEKDGRQKSR 204
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
619-958 |
9.69e-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: 43.40 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 619 ALLGERERLHTDQRAA---ADALAQLSGQ-------LAAADERRTRIVNAQELSQRTLRGQEQkWQQLREAWSLQQGQRQ 688
Cdd:COG3096 293 ELFGARRQLAEEQYRLvemARELEELSAResdleqdYQAASDHLNLVQTALRQQEKIERYQED-LEELTERLEEQEEVVE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 689 ERLLRFGQLGEELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQgeplSEALQAAQDLVGRCERAQEEARGRREQQQ 768
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQA----VQALEKARALCGLPDLTPENAEDYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 769 ATCQRLQLELGNLRQLIALGEEELARLELELAGLKN-----PENEAIPDLAPLLAEQRNLEALQlachQRLAELERQLSE 843
Cdd:COG3096 448 AKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYRSQQALA----QRLQQLRAQLAE 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 844 LDQARSADHKqlvvLQEKLATLRLERERNLTRRQGLHEQFEELGVRLVDL-DQAVLIAADRGKLRQEIQTLETQVEALGA 922
Cdd:COG3096 524 LEQRLRQQQN----AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELeEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051267170 923 INLAALEeyeeAKTRATYLENQC-----------------------------------QDLEQALETLSQA 958
Cdd:COG3096 600 RAPAWLA----AQDALERLREQSgealadsqevtaamqqllerereatverdelaarkQALESQIERLSQP 666
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
625-862 |
1.07e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 625 ERLHTDQRAAADALAQLSGQLAAADERRTRIVNAQELSQRTLRG--QEQKWQQLREAwsLQQGQRQERLL-RFGQLGEEL 701
Cdd:COG3096 444 AAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEveRSQAWQTAREL--LRRYRSQQALAqRLQQLRAQL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 702 IRLDK--EQAEEAQRLAE-----TEQQLALE---EARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQ----- 766
Cdd:COG3096 522 AELEQrlRQQQNAERLLEefcqrIGQQLDAAeelEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaara 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 767 -----QQATCQRLQLELG----NLRQLIALgeeelarlelelaglknpeneaipdLAPLLAEQRNLEALQLACHQRLAEL 837
Cdd:COG3096 602 pawlaAQDALERLREQSGealaDSQEVTAA-------------------------MQQLLEREREATVERDELAARKQAL 656
|
250 260
....*....|....*....|....*
gi 2051267170 838 ERQLSELDQARSADHKQLVVLQEKL 862
Cdd:COG3096 657 ESQIERLSQPGGAEDPRLLALAERL 681
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
174-374 |
1.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 174 KERRRETEQRIRHTQENLERLGDIRGELGS--------------RLDHLKAQAETAERYKQLKSRSRAARAELigSELWA 239
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiklsefYEEYLDELREIEKRLSRLEEEINGIEERI--KELEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 240 LETRLGEAKSELAQVEQALAALdakrtadEGRHVTLSVARQ-EAQAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDLq 318
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEEL-------EERHELYEEAKAkKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI- 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2051267170 319 artqalgERITSRKAQLSSQQEQLTEGVlrSELEEARLE--QCEQLLTEQQEARLRAS 374
Cdd:PRK03918 408 -------SKITARIGELKKEIKELKKAI--EELKKAKGKcpVCGRELTEEHRKELLEE 456
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1025-1099 |
1.48e-03 |
|
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: 41.04 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 1025 LSGGEKALTALALVFAIFRLNPAPFCLLDEVDAPLDEVNvgRFCS---LVKEMSSTV--QFVYISHNKVSMEMAEQLVGV 1099
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN--RKIStdlLVKEAKKQPgrQFIFITPQDISGLASSDDVKV 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-426 |
2.19e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 232 LIGSELWALETRLGEAKSELAQVEQALAALDAKRTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAIARLEQQ----Q 307
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaelE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 308 LHQSELGRDLQARTQALGERItsRKAQLSSQQEQLTEGVLRSELEEA-RLEQCEQLLTEQQEARLRAseqleqtrqqQQQ 386
Cdd:COG4942 90 KEIAELRAELEAQKEELAELL--RALYRLGRQPPLALLLSPEDFLDAvRRLQYLKYLAPARREQAEE----------LRA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2051267170 387 WQQQVTRLQGELNQTRARLGGLHELQAKTRLARLKLEDER 426
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
633-751 |
2.20e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.15 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 633 AAADALAQLSGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAwslQQGQRQerllRFGQLGEELIRLDKEQAEEA 712
Cdd:COG5283 18 SAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQS---LQRLRQ----ALDQAGIDTRQLSAAQRRLR 90
|
90 100 110
....*....|....*....|....*....|....*....
gi 2051267170 713 QRLAETEQQLALEEARLAELQEQGEPLSEALQAAQDLVG 751
Cdd:COG5283 91 SSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRLAG 129
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
105-528 |
2.90e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 41.88 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 105 REVLRDGTNHYQINGQKCRRKDVTDLFLGTGLGPRSYAIIEQGTVSRLVESRPADLKLFMEEAAGVSRYKERRRETEQRI 184
Cdd:COG4995 40 LLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALALALAAAALAALALLAALLALAAAA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 185 RHTQENLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRSRAARAELIGSELWALETRLGEAKSELAQVEQALAALDAK 264
Cdd:COG4995 120 ALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLALLLAALAAALAAAAAALA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 265 RTADEGRHVTLSVARQEAQAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDLQARTQALGERITSRKAQLSSQQEQLTE 344
Cdd:COG4995 200 LLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 345 GVLRSELEEARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQTRARLGGLHELQAKTRLARLKLED 424
Cdd:COG4995 280 AALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAAL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 425 ERSGPIGAEDADLQPTLDTLGGELELGRAAAEELAAQLAQAIEEHEALKLAHSQQQGLLRELEARLTTLDQILGEQMEGA 504
Cdd:COG4995 360 ALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYI 439
|
410 420
....*....|....*....|....
gi 2051267170 505 TLADRLQVVPEWAQALDKVLGRWL 528
Cdd:COG4995 440 ILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
688-871 |
2.95e-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: 41.25 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 688 QERLLRFGQL---GEELIRLDKEQAEEAqrLAETEQQLALEEARLAELQ---EQGEPLSEALQAAQDLVGRCERAQEEAR 761
Cdd:pfam00529 32 TRVLVKEGDRvkaGDVLFQLDPTDYQAA--LDSAEAQLAKAQAQVARLQaelDRLQALESELAISRQDYDGATAQLRAAQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 762 GRREQQQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEaipdlapLLAEQRNLEALQLACHQRLAElerQL 841
Cdd:pfam00529 110 AAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQAN-------LLATVAQLDQIYVQITQSAAE---NQ 179
|
170 180 190
....*....|....*....|....*....|
gi 2051267170 842 SELDQARSADHKQLVVLQEKLATLRLERER 871
Cdd:pfam00529 180 AEVRSELSGAQLQIAEAEAELKLAKLDLER 209
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
402-802 |
3.18e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.54 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 402 RARLGGLHELQAKTRLARLKLEDERSGPIGAEDADLQPTLDTLGGELELGRAAAEELAAQLAQAIEEHEALKLAHSQQQG 481
Cdd:COG3903 515 LAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 482 LLRELEARLTTLDQILGEQMEGATLADRLQVVPEWAQALDKVLGRWLTATPADECNPALDGLWIGPALPAVAGTLASLIS 561
Cdd:COG3903 595 ARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAA 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 562 GDHVPAFLNAIWLADNREEALARQPTLLAGESVLTPAGDWLGPNWADIGQGAALGTMALLGERERLHTDQRAAADALAQL 641
Cdd:COG3903 675 AAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAA 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 642 SGQLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREAWSLQQGQRQERLLRFGQLGEELIRLDKEQAEEAQRLAETEQQ 721
Cdd:COG3903 755 AAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAAL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 722 LALEEARLAELQEQGEPLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNLRQLIALGEEELARLELELAG 801
Cdd:COG3903 835 AAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAA 914
|
.
gi 2051267170 802 L 802
Cdd:COG3903 915 A 915
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-236 |
3.27e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 26 MTAVVGPNGCGKSNVIDAVRWVLgeSSARHLRGENMTDVIFNGsvnrtaHARASVELVFDNPHNRVPGEFGRFTEISVRR 105
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLA--DFDALVIGLTDERSRNGG------IGGIPSLLNGIDPKEPIEFEISEFLEDGVRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 106 EV-LRDGTNHYQINGQKCRRKDVTDLFLGTGLGPRSYAIIEQGTVSRLVESRPADLKLFMEEAAGVSRYKERRRETEQRI 184
Cdd:pfam13304 73 RYgLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2051267170 185 RHTQeNLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRSRAARAELIGSE 236
Cdd:pfam13304 153 FLLL-LDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLG 203
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
179-411 |
3.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 179 ETEQRIRHTQENLERLGDIRGELGSRLDHLKAQAETAERYKQLKSRsRAARAELIGSELWALETRLGEAKSELAQVEQAL 258
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER-REDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 259 AALDAKRTADEGRHVTLSVARQEAqAEQANRQQQIFLGGQAIARLEQQQLHQSELGRDLQA---RTQALGERITSRKAQL 335
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEV-AELNSKLAELKERIESLERIRTLLAAIADAEDEIERlreKREALAELNDERRERL 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051267170 336 SSQQEQLTEgvLRSELEEARLEqceqlltEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQTRARLGGLHEL 411
Cdd:PRK02224 630 AEKRERKRE--LEAEFDEARIE-------EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
658-1064 |
4.01e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 658 AQELSQRTLRGQEQKWQQLREawslQQGQRQERLLRFGQLGEELIRLDKEQAEEAQRLAETEQQLALEEARLAELQEQGE 737
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQ----EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 738 PLSEALQAAQDLVGRCERAQEEArgrREQQQATCQRLQLELGNLRQLIALGEEELARLELELAGLKNPENEAIPDLAPLL 817
Cdd:TIGR00606 885 QFEEQLVELSTEVQSLIREIKDA---KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 818 AE-QRNLEALQLACHQRLAELERQLSELDQARSADHKQLVVLQEKLATLRLeRER----NLTRR---QGLHEQFEELGVR 889
Cdd:TIGR00606 962 NKiQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI-QERwlqdNLTLRkreNELKEVEEELKQH 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 890 LVDLDQAVLIaadrgKLRQEIQTLETQVEALG---AINLAALEEYEEAKT--RATYLENQCQDLEQ-------ALETLSQ 957
Cdd:TIGR00606 1041 LKEMGQMQVL-----QMKQEHQKLEENIDLIKrnhVLALGRQKGYEKEIKhfKKELREPQFRDAEEkyremmiVMRTTEL 1115
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 958 AIKRIDK------ETQIRFR-DTFDKVNEDLKSLFPKVFGGGS-AWLELTSDDLLEAGVSIMARppgKKNATIALLSG-- 1027
Cdd:TIGR00606 1116 VNKDLDIyyktldQAIMKFHsMKMEEINKIIRDLWRSTYRGQDiEYIEIRSDADENVSASDKRR---NYNYRVVMLKGdt 1192
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2051267170 1028 ----------GEKALTALALVFAIFRLnpapFCL------LDEVDAPLDEVNV 1064
Cdd:TIGR00606 1193 aldmrgrcsaGQKVLASLIIRLALAET----FCLncgiiaLDEPTTNLDRENI 1241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
172-374 |
4.16e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 172 RYKERRRETEQRIRH--TQENLERLGDIRGELGSRLDHLKAQAETAE-RYKQLKSRSRAARAELIGSELWALE----TRL 244
Cdd:COG3206 186 ELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRAQLGSGPDALPEllqsPVI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 245 GEAKSELAQVEQALAALDAKRTADegrhvtlSVARQEAQAEQANRQQQIFLGGQAIARLEQQQLhqselgRDLQARTQAL 324
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTPN-------HPDVIALRAQIAALRAQLQQEAQRILASLEAEL------EALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2051267170 325 GERITSRKAQLSSQQEQLTE-GVLRSELEEARlEQCEQLLTEQQEARLRAS 374
Cdd:COG3206 333 QAQLAQLEARLAELPELEAElRRLEREVEVAR-ELYESLLQRLEEARLAEA 382
|
|
| CynX |
COG2807 |
Cyanate permease [Inorganic ion transport and metabolism]; |
550-648 |
4.25e-03 |
|
Cyanate permease [Inorganic ion transport and metabolism];
Pssm-ID: 442057 [Multi-domain] Cd Length: 399 Bit Score: 41.01 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 550 PAVAGTLASLISGDHVPAFLNAIWLADnReeaLARQPTLLAGESVLT---PAGDWLGPNWAD--------IGQGAALGT- 617
Cdd:COG2807 249 AATAGLLLSLFQLAGIPGSLLVPLLAD-R---LGDRRPLLLLLGLLGlagLLGLLLAPGSLPwlwavllgLGQGGLFPLa 324
|
90 100 110
....*....|....*....|....*....|.
gi 2051267170 618 MALLGERERlHTDQRAAADALAQLSGQLAAA 648
Cdd:COG2807 325 LTLIGLRAR-TPAEAAALSGMAQSVGYLLAA 354
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
644-953 |
4.59e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 644 QLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREawslQQGQRQERLL---------RFGQLGEELIRLDKEQAEEAQR 714
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKA----QIEEKEEKDLherlnglesELAELDEEIERYEEQREQARET 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 715 LAETEQQLALEEARLAELQEqgepLSEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNLRqlialgeeelar 794
Cdd:PRK02224 236 RDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL------------ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 795 lelELAGLKNPENEAIpdlaplLAEQRNLEAlqlachqRLAELERQLSELDQARSADHKQLVVLQEKLATLRlerernlT 874
Cdd:PRK02224 300 ---AEAGLDDADAEAV------EARREELED-------RDEELRDRLEECRVAAQAHNEEAESLREDADDLE-------E 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 875 RRQGLHEQFEELGVRLVDLDQAVLIAADR-GKLRQEIQTLE-------TQVEALGAINLAALEEYEEAKTRATYLENQCQ 946
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEiEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLR 436
|
....*..
gi 2051267170 947 DLEQALE 953
Cdd:PRK02224 437 TARERVE 443
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
623-959 |
6.80e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 623 ERERLHTDQRAAADaLAQLSGQLAAADERRTRIVNAQElsqRTLRGQEQKWQQLREAWSLQQGQRQERLLRfgQLGEELI 702
Cdd:pfam12128 378 NRRRSKIKEQNNRD-IAGIKDKLAKIREARDRQLAVAE---DDLQALESELREQLEAGKLEFNEEEYRLKS--RLGELKL 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 703 RLDKEQAEEAQRLAETEQQLALEEARlaelqeqgeplsEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNLR 782
Cdd:pfam12128 452 RLNQATATPELLLQLENFDERIERAR------------EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 783 Q---------------LIALGEEELARLELELAGLKNPENEAIPDLAPLLAEQR------------NLEALQL-ACHQRL 834
Cdd:pfam12128 520 SaldelelqlfpqagtLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSvggelnlygvklDLKRIDVpEWAASE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 835 AELERQLSELDQARSADHKQLVVLQEKLATLRLERE---RNLTRRQGLHEQFEELGVRLVDLDQAV------LIAADRGK 905
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEkasREETFARTALKNARLDLRRLFDEKQSEkdkknkALAERKDS 679
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2051267170 906 LRQEIQTLETQVEALGAINLAALEEYEEAKTRATYLENQC-----QDLEQALETLSQAI 959
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAI 738
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
644-786 |
8.62e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.93 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 644 QLAAADERRTRIVNAQELSQRTLRGQEQKWQQLREawsLQQGQRQERLLRfgqlgeelirldkeQAEEAQRLAETEQQLA 723
Cdd:pfam15709 400 RQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQE---LQRKKQQEEAER--------------AEAEKQRQKELEMQLA 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051267170 724 LEEARLAELQEQgeplsEALQAAQDLVGRCERAQEEARGRREQQQATCQRLQLELGNLRQLIA 786
Cdd:pfam15709 463 EEQKRLMEMAEE-----ERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
171-271 |
8.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 171 SRYKERRRETEQRIRHTQENLERLGDIRG---ELGSRLDHLKAQAETAERYKQLKSRSRAARAELIGSELWALETRLGEA 247
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKklkELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
90 100
....*....|....*....|....
gi 2051267170 248 KSELAQVEQALAALDAKRTADEGR 271
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKE 420
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
250-654 |
9.80e-03 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 40.23 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 250 ELAQVEQALAALD--------AKRTADEGRHVTLSVARQEAQAEQANRQQqiflggQAIARLEQQQLHQSELGRDLQART 321
Cdd:COG1020 884 ELGEIEAALLQHPgvreavvvAREDAPGDKRLVAYVVPEAGAAAAAALLR------LALALLLPPYMVPAAVVLLLPLPL 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 322 QALGERITSRKAQLSSQQEQLTEGVLRSELEEARLEQCEQLLTEQQEARLRASEQLEQTRQQQQQWQQQVTRLQGELNQT 401
Cdd:COG1020 958 TGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLL 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 402 RARLGGLHELQAKTRLARLKLEDERSGPIGAEDADLQPTLDTLGGELELGRAAAEELAAQLAQAIEEHEALKLAHSQQQG 481
Cdd:COG1020 1038 LLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLAL 1117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 482 LLRELEARLTTLDQILGEQMEGATLADRLQVVPEWAQALDKVLGRWLTATPADECNPALDGLWIGPALPAVAGTLASLIS 561
Cdd:COG1020 1118 LLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLL 1197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051267170 562 GDHVPAFLNAIWLADNREEALARQPTLLAGESVLTPAGDWLGPNWADIGQGAALGTMALLGERERLHTDQRAAADALAQL 641
Cdd:COG1020 1198 LLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALA 1277
|
410
....*....|...
gi 2051267170 642 SGQLAAADERRTR 654
Cdd:COG1020 1278 LLLPALARARAAR 1290
|
|
| |
