|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1180 |
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: 1157.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 2 FLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSRKRLNLAEVT 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 82 LTLDNDDHFLP-IDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSI 160
Cdd:TIGR02168 81 LVFDNSDGLLPgADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 161 FGEAAGVLKYKTRKEKAGNKLFETQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPLTAYDIEELHGK 240
Cdd:TIGR02168 161 FEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 241 WSTLKEKVQMAKEEELAESSAISPKEAKIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQ 320
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 321 LEEAIVQFQQKETVLTRRAFEAEAVFETLQAEVKQLRAQVKE---KQHALSLHNENVEEKIEQLKSDYFELLNSQASIRN 397
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 398 ELQLLDDQMSQSAVTLQRLADNNEKHLQERHdiSARKAACKTEFARFEQEIHSQVGAYRDMQTKYEQKKRQYEKNESPLY 477
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 478 QAYQYVQQARSKKDMLDTMQGDFSGFYQGVKEVLKAKDRLGGIRGAVLELISTEQKYETAIEIAVGASPQHVVTDDEQSA 557
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 558 RKAIQYLKQNSFGRATFLPLSVIRDRQLsKPLRGNSGPAFIISFGVASELVTFDPAYRSVIQNLLGNRSDYRGLKGgANE 637
Cdd:TIGR02168 559 KKAIAFLKQNELGRVTFLPLDSIKGTEI-QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDN-ALE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 638 LAKLLGHRYRIVTLEGDVVNPGGSMTGGSVKKkNNSLLGRTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLA 717
Cdd:TIGR02168 637 LAKKLRPGYRIVTLDGDLVRPGGVITGGSAKT-NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 718 DLRETGEGLRvkqQDVKGQLYEPQFAEKNINTHLELYDQEKSALSESDEERKVRKRKLEE---ELSAVSEKMKQLEEDID 794
Cdd:TIGR02168 716 QLRKELEELS---RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 795 RLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLE 874
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 875 EAAKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLS 954
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 955 FEGAKEKYQ-LETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTK 1033
Cdd:TIGR02168 953 LEEAEALENkIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1034 RFNDTFVQIRSHFDQVFRSLFGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPV 1113
Cdd:TIGR02168 1033 RFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPA 1112
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237015 1114 PFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSKVISVKL 1180
Cdd:TIGR02168 1113 PFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1188 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 852.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSRKRLNLAEV 80
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 81 TLTLDNDDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSI 160
Cdd:COG1196 81 SLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 161 FGEAAGVLKYKTRKEKAGNKLFETQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPLTAYDIEELHGK 240
Cdd:COG1196 161 IEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 241 WSTLKEKVQMAKEEELAESSAISPKEAKIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQ 320
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 321 LEEAIVQFQQKETVLTRRAFEAEAVFETLQAEVKQLRAQVKEKQHALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQ 400
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 401 LLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACKTEFARFEQEIHSQVGAYRDMQT---KYEQKKRQYEKNESPLY 477
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAlleLLAELLEEAALLEAALA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 478 QAYQYVQQARSKKDMLDTMQGDFSGFYQGVKEvLKAKDRLGGIRGAVLELISTEQKYETAIEIAVGASPQHVVTDDEQSA 557
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 558 RKAIQYLKQNSFGRATFLPLSVIRDRQLSKPL--RGNSGPAFIisfGVASELVTFDPAYRSVIQNLLGNRSDYRGLkGGA 635
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAAlaRGAIGAAVD---LVASDLREADARYYVLGDTLLGRTLVAARL-EAA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 636 NELAKLLGHRYRIVTLEGDVVNPGGSMTGGSVKKKNnsllgrtrelgdvtkrlaemeektslleqevqtlkhsiqdmekk 715
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL-------------------------------------------- 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 716 ladlretgeglrvkqqdvkgqlyepqfaekninthlelydqeksalsesdEERKVRKRKLEEELSAVSEKMKQLEEDIDR 795
Cdd:COG1196 672 --------------------------------------------------AALLEAEAELEELAERLAEEELELEEALLA 701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 796 LTKQKQTQSSTKESLSNELTElkiaaakkeqackgeednlarlkkeltetelalkeakedlsfltsemssstsgeeklee 875
Cdd:COG1196 702 EEEEERELAEAEEERLEEELE----------------------------------------------------------- 722
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 876 aakhklndktktielialrrdqriklqhgldtyerelkemkrlykqkttllkdEEVKLGRMEVELDNLLQYLREEYSLSF 955
Cdd:COG1196 723 -----------------------------------------------------EEALEEQLEAEREELLEELLEEEELLE 749
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 956 EGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRF 1035
Cdd:COG1196 750 EEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERF 829
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1036 NDTFVQIRSHFDQVFRSLFGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPF 1115
Cdd:COG1196 830 LETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPF 909
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237015 1116 CVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSKVISVKLEETKEFVQ 1188
Cdd:COG1196 910 CVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEELAE 982
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-1174 |
0e+00 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 674.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 2 FLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFagSDSRKRLNLAEVT 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 82 LTLDNDDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSIF 161
Cdd:pfam02463 79 ITFDNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 162 GEAAGVLKYKTRKEKAGNKLFETQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPLTAYDIEELHGKW 241
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 242 STLKEKVQMAKEEELAESSAISPKEAKIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQL 321
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 322 EEAIVQFQQKETVLTRRAFEAEAVFETLQAEVKQLRAQVKEKQHALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQL 401
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 402 LDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACKTEFARFEQEIHSQVGAYRDMQTKYEQKKRQYEKNESPLYQAYQ 481
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 482 YVQQARSKKDMLDTMQGDFSGFYQGVKEVLKAKDRLGGIRGAVLELISTEQKYETAIEIAVGASPQHVVTDDEQSARKAI 561
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 562 QYLKQNSFGRATFLPLSVIRDRQLSKPLRGNSgpafiisfgvASELVTFDPAYRSVIQNLLGNRSDYRGLKGGANELAKL 641
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLP----------LKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 642 LGHRYRIVTLEGDVVNPGGSMTGGSVKKKNNSLLGRTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRE 721
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 722 TGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQ 801
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 802 TQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKL 881
Cdd:pfam02463 789 EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 882 NDKTKTIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEK 961
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 962 YQLETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRFNDTFVQ 1041
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS 1028
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1042 IRSHFDQVFRSLFGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEV 1121
Cdd:pfam02463 1029 INKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEI 1108
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|...
gi 1237015 1122 EAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSK 1174
Cdd:pfam02463 1109 DAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1180 |
2.41e-144 |
|
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: 465.70 E-value: 2.41e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 2 FLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSRKrLNLAEVT 81
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQS-GNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 82 LTLDNDDHFLPIDFhEVSVTRRVYRSG-ESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSI 160
Cdd:TIGR02169 80 VTFKNDDGKFPDEL-EVVRRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 161 FGEAAGVLKYKTRKEKAGNKLFETQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPLTAYDIEELHGK 240
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 241 WSTLKEKVQmAKEEELAESSA-ISPKEAKIEGTRDKIQALDESVDEL-QQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQ 318
Cdd:TIGR02169 239 KEAIERQLA-SLEEELEKLTEeISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 319 EQLEEAIVQFQQKETVLTRRAFEAEAVFETLQAEVKQLRAQVKEKQHALslhnENVEEKIEQLKSDYFELLNSQASIRNE 398
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEFAETRDELKDYREK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 399 LQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACKTEFARFEQEIHSQVGAYRDMQTKYEQKKRQYEKNESPLY- 477
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYd 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 478 --QAYQYVQQARSKK----DMLDTMQG---DFSGFYQGVKEVLkaKDRLGGIRGAVLELISTEQKYETAIEIAVGASPQH 548
Cdd:TIGR02169 474 lkEEYDRVEKELSKLqrelAEAEAQARaseERVRGGRAVEEVL--KASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNN 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 549 VVTDDEQSARKAIQYLKQNSFGRATFLPLSVIRDRQlsKPLRGNSGPAFIisfGVASELVTFDPAYRSVIQNLLGNRSDY 628
Cdd:TIGR02169 552 VVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDER--RDLSILSEDGVI---GFAVDLVEFDPKYEPAFKYVFGDTLVV 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 629 RGLkgganELAKLLGHRYRIVTLEGDVVNPGGSMTGGSVKKKNNSLLGRT---------RELGDVTKRLAEMEEKTSLLE 699
Cdd:TIGR02169 627 EDI-----EAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSepaelqrlrERLEGLKRELSSLQSELRRIE 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 700 QEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLyepqfaeKNINTHLELYDQEKSALSESDEERKVRKRKLEEEL 779
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL-------EELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 780 SAVSEKMKQLEEDIDR-LTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEdlSF 858
Cdd:TIGR02169 775 HKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK--SI 852
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 859 LTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDqRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEV 938
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 939 ELDNLLQYLREEYSLSFEgakekyqlETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKN 1018
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIPEE--------ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1019 TLFQVIEEMDEEMTKRFNDTFVQIRSHFDQVFRSLfGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERAL 1098
Cdd:TIGR02169 1004 AILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSL 1082
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1099 TAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSKVISV 1178
Cdd:TIGR02169 1083 TALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQVFGL 1162
|
..
gi 1237015 1179 KL 1180
Cdd:TIGR02169 1163 KL 1164
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1057-1174 |
1.15e-61 |
|
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: 208.86 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1057 GRAELRLT-DPNDLLHS----G-VEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANV 1130
Cdd:cd03278 74 NFAEVTLTfDNSDGRYSiisqGdVSEIIEAPGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANV 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1237015 1131 FRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSK 1174
Cdd:cd03278 154 ERFARLLKEFSKETQFIVITHRKGTMEAADRLYGVTMQESGVSK 197
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-153 |
9.28e-51 |
|
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: 177.66 E-value: 9.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSRKRLNLAEVTL 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237015 83 TLDNDDHFlpidfhevsvtrrvyrsgeseflinnqpcrlkdiidlfmdsglgkeaFSIISQGKVEEILSSK 153
Cdd:cd03278 81 TFDNSDGR-----------------------------------------------YSIISQGDVSEIIEAP 104
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
518-624 |
1.83e-30 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 116.56 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 518 GGIRGAVLELISTEQKYETAIEIAVGASPQHVVTDDEQSARKAIQYLKQNSFGRATFLPLSVIRDRQLS---KPLRGNSG 594
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAgskLREALLPE 80
|
90 100 110
....*....|....*....|....*....|
gi 1237015 595 PAFIisfGVASELVTFDPAYRSVIQNLLGN 624
Cdd:smart00968 81 PGFV---GPAIDLVEYDPELRPALEYLLGN 107
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1074-1180 |
1.19e-27 |
|
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: 113.05 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1074 VEIIAQ--PPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSS-DTQFIVIT 1150
Cdd:cd03275 137 VESIASknPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVIS 216
|
90 100 110
....*....|....*....|....*....|.
gi 1237015 1151 HRKGTMEEADVLYGVTM-QESGVSKVISVKL 1180
Cdd:cd03275 217 LKEEFFSKADALVGVYRdQECNSSKVLTLDL 247
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
519-624 |
9.60e-27 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 105.81 E-value: 9.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 519 GIRGAVLELISTEQKYETAIEIAVGASPQHVVTDDEQSARKAIQYLKQNSFGRATFLPLSVIRDRQLskplrgNSGPAFI 598
Cdd:pfam06470 3 GVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPR------RPGADLK 76
|
90 100
....*....|....*....|....*.
gi 1237015 599 ISFGVASELVTFDPAYRSVIQNLLGN 624
Cdd:pfam06470 77 GGAGPLLDLVEYDDEYRKALRYLLGN 102
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1090-1174 |
1.60e-23 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 98.92 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1090 LLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYS-SDTQFIVITHRKGTMEEADVLYGVTMQ 1168
Cdd:cd03239 94 ILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAkHTSQFIVITLKKEMFENADKLIGVLFV 173
|
....*.
gi 1237015 1169 EsGVSK 1174
Cdd:cd03239 174 H-GVST 178
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1069-1165 |
1.18e-19 |
|
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: 88.89 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1069 LLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIV 1148
Cdd:cd03274 106 ILQGEVEQIAQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIV 185
|
90
....*....|....*..
gi 1237015 1149 ITHRKGTMEEADVLYGV 1165
Cdd:cd03274 186 ISLRNNMFELADRLVGI 202
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-158 |
1.70e-19 |
|
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: 89.17 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSArSLRGGKMEDIIFAGSDSRKRLNLAEVTL 82
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSS-HLRSKNLKDLIYRARVGKPDSNSAYVTA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 83 TLDNDDhflpidfHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEA--FsIISQGKVEEILSSKAEDRR 158
Cdd:cd03275 80 VYEDDD-------GEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKArnF-LVFQGDVESIASKNPPGKR 149
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-151 |
1.83e-19 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 89.28 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAERISV-DFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFA-GSDSRKRlnlA 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKrGQAGITK---A 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237015 79 EVTLTLDNDD-HFLPIDFH---EVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGL--GKEAFsIISQGKVEEILS 151
Cdd:cd03273 78 SVTIVFDNSDkSQSPIGFEnypEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLnvNNPHF-LIMQGRITKVLN 155
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1091-1174 |
9.52e-18 |
|
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: 81.64 E-value: 9.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1091 LSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYS-SDTQFIVITHRKGTMEEADVLYGVTMQE 1169
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIKKVI 157
|
....*
gi 1237015 1170 SGVSK 1174
Cdd:cd03227 158 TGVYK 162
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1086-1175 |
2.81e-16 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 80.03 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1086 QNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGV 1165
Cdd:cd03273 162 ESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRT 241
|
90
....*....|
gi 1237015 1166 TMQEsGVSKV 1175
Cdd:cd03273 242 RFVD-GTSTV 250
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1086-1166 |
4.50e-16 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 79.23 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1086 QNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGV 1165
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
.
gi 1237015 1166 T 1166
Cdd:cd03272 234 K 234
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-226 |
1.15e-15 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 76.97 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARslRGGKMEDIIFAGSDSrkrlnlAEVTL 82
Cdd:COG0419 2 LLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINVGSEE------ASVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 83 TLDNDDhflpidfHEVSVTRRvyrsgeseflinnqpcrlkdiidlfmdsglgkeafsiisQGKVEEILSSKAEDRRSIFG 162
Cdd:COG0419 74 EFEHGG-------KRYRIERR---------------------------------------QGEFAEFLEAKPSERKEALK 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237015 163 EAAGVLKYKTRKEkagnklfetqdnlnRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVE 226
Cdd:COG0419 108 RLLGLEIYEELKE--------------RLKELEEALESALEELAELQKLKQEILAQLSGLDPIE 157
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-92 |
6.70e-15 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 73.88 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDiifAGSDSRKRLNLAEVTL 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFL---AGGGVKAGINSASVEI 77
|
90
....*....|
gi 1237015 83 TLDNDDHFLP 92
Cdd:cd03239 78 TFDKSYFLVL 87
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-160 |
7.93e-15 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 75.37 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFAERISVD-FVKGVTAVVGPNGSGKSNITDAIRWVLGGQSArSLRGGKMEDIIFAGSDSrkRLNLAEVT 81
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEpFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYT-HLREEQRQALLHEGSGP--SVMSAYVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 82 LTLDNDDHFLPIDFHEVSVtRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKE-AFSIISQGKVEEILSSKAEDRRSI 160
Cdd:cd03272 78 IIFDNSDNRFPIDKEEVRL-RRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSnPYYIVPQGKINSLTNMKQDEQQEM 156
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-435 |
1.19e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAErISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSlrgGKMEDIIFAGSDSrkrlnlAEV 80
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALD---DTLDDVITIGAEE------AEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 81 TLTLDNDDHflpiDFHevsVTRRVYRSGESeflINNQPCRLKD---IID------------LFMDSglgkEAF---SIIS 142
Cdd:PRK02224 71 ELWFEHAGG----EYH---IERRVRLSGDR---ATTAKCVLETpegTIDgardvreevtelLRMDA----EAFvncAYVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 143 QGKVEEILSSKAEDRRSIFGEAAGVLKYKTRKEKAGnklfetqDNLNRVGDILHELEGQVEPLK--IQASIAKDYLEKKK 220
Cdd:PRK02224 137 QGEVNKLINATPSDRQDMIDDLLQLGKLEEYRERAS-------DARLGVERVLSDQRGSLDQLKaqIEEKEEKDLHERLN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 221 ELEHVEIPLTAyDIEELHGKWSTLKEKVQMAKE---------EELAE-SSAISPKEAKIEGTRDKIQALDESVDELQQVL 290
Cdd:PRK02224 210 GLESELAELDE-EIERYEEQREQARETRDEADEvleeheerrEELETlEAEIEDLRETIAETEREREELAEEVRDLRERL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 291 LVTSEELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQ--KETVLTRRAFEAEAvfETLQAEVKQLRAQVKEKQHAls 368
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrlEECRVAAQAHNEEA--ESLREDADDLEERAEELREE-- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237015 369 lhNENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKA 435
Cdd:PRK02224 365 --AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-88 |
1.92e-13 |
|
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: 70.33 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGK-MEDIIFAGSdsrkrlNLAEVT 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAhDPKLIREGE------VRAQVK 74
|
....*..
gi 1237015 82 LTLDNDD 88
Cdd:cd03240 75 LAFENAN 81
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-856 |
2.79e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 272 TRDKIQALDESVDELQQvllvTSEELEKLEGRKEVLKDrkknAVQNQEQLEEAIVQFQQKETVLTR-RAFEAEAVFETLQ 350
Cdd:COG4913 223 TFEAADALVEHFDDLER----AHEALEDAREQIELLEP----IRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 351 AEVKQLRAQVKEKQHALslhnENVEEKIEQLKSDYFELLNSQASirNELQLLDDqmsqsavtLQRLADNNEKHLQERHDI 430
Cdd:COG4913 295 AELEELRAELARLEAEL----ERLEARLDALREELDELEAQIRG--NGGDRLEQ--------LEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 431 SAR-KAACKT----------EFARFEQEIHSQVGAYRDMQTKYEQKKRQYEKNESPLYQAYQyvqQARSKKDMLDTMQGD 499
Cdd:COG4913 361 RARlEALLAAlglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR---ELEAEIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 500 FSGFYQGVKEVLKAKdrLGGIRGAV------LELISTEQKYETAIEIAVGASPQHVVTDDEQSARkAIQYLKQNSF-GRA 572
Cdd:COG4913 438 IPARLLALRDALAEA--LGLDEAELpfvgelIEVRPEEERWRGAIERVLGGFALTLLVPPEHYAA-ALRWVNRLHLrGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 573 TFLPLSVIRDRQLSKPLRGNSgpafiisfgVASELVTFDPAYRSVIQNLLGNRSDYRGlkggANELAKLLGHRYRIvTLE 652
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDS---------LAGKLDFKPHPFRAWLEAELGRRFDYVC----VDSPEELRRHPRAI-TRA 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 653 GDVvnpggSMTGGSVKKKNNSLLGRTRELG-DVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLREtgeglrvkQQ 731
Cdd:COG4913 581 GQV-----KGNGTRHEKDDRRRIRSRYVLGfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQE--------RR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 732 DVKGQLYEPQFAEKNINTHLELYD---QEKSALSESD----------EERKVRKRKLEEELSAVSEKMKQLEEDIDRLTK 798
Cdd:COG4913 648 EALQRLAEYSWDEIDVASAEREIAeleAELERLDASSddlaaleeqlEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 799 QKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDL 856
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-128 |
7.25e-12 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 68.26 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 2 FLKRLDVIGFKSFAErISVDFVKGVTAVVGPNGSGKSNITDAIrWVLGgqSARSLRGGKMEDIIFAGSDSrkrlnlAEVT 81
Cdd:COG1195 1 RLKRLSLTNFRNYES-LELEFSPGINVLVGPNGQGKTNLLEAI-YLLA--TGRSFRTARDAELIRFGADG------FRVR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1237015 82 LTLDNDDHflpidFHEVSVTRRvyRSGESEFLINNQPC-RLKDIIDLF 128
Cdd:COG1195 71 AEVERDGR-----EVRLGLGLS--RGGKKRVRINGKPVrRLSDLAGLL 111
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-57 |
1.81e-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: 67.33 E-value: 1.81e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1237015 1 MFLKRLDVIGFKSFaERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLR 57
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFD 56
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
679-1180 |
7.95e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLREtgegLRVKQQDVKGQLYEpqfaeknINTHLELYDQEK 758
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEE-------LEERHELYEEAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 759 SALSESDEERKVRK----RKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAK----------- 823
Cdd:PRK03918 369 AKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltee 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 824 -KEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSST-------------SGEEKLEEAAKHKLNDKTKTIE 889
Cdd:PRK03918 449 hRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaeqlkELEEKLKKYNLEELEKKAEEYE 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 890 LIalrRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKdeevKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQ------ 963
Cdd:PRK03918 529 KL---KEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKelepfy 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 964 ----------------------LETDPEEARKRVKLIKLAIEELGT-----VNLGSIDEFERVNERYKFLSEQ------- 1009
Cdd:PRK03918 602 neylelkdaekelereekelkkLEEELDKAFEELAETEKRLEELRKeleelEKKYSEEEYEELREEYLELSRElaglrae 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1010 ----KEDLTEAKNTLFQVIEEMDEEMTKRFNDTFVQIRSHFDQVFRSLFGGGRAELRL--------------TDPNDLLH 1071
Cdd:PRK03918 682 leelEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKEralskvgeiaseifEELTEGKY 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1072 SGVEIIAQPPGKKL--------QNLNLLSGGERALTAIA--LLFSILKVRPVPFCVLDEVEAALDEANVFRF----AQYL 1137
Cdd:PRK03918 762 SGVRVKAEENKVKLfvvyqgkeRPLTFLSGGERIALGLAfrLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYL 841
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1237015 1138 KKYSsdtQFIVITHRKGTMEEADVLYGVTMqESGVSKVISVKL 1180
Cdd:PRK03918 842 RKIP---QVIIVSHDEELKDAADYVIRVSL-EGGVSKVEVVSL 880
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-84 |
1.62e-10 |
|
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: 61.93 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAERISVD-FVKGVTAVVGPNGSGKSNITDAIRWVLGGQsARSLRGGKMEDIIFAgSDSRKRLNLAE 79
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGpFHKSFSAIVGPNGSGKSNVIDSMLFVFGFR-ASKMRQKKLSDLIHN-SAGHPNLDSCS 78
|
....*
gi 1237015 80 VTLTL 84
Cdd:cd03274 79 VEVHF 83
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-876 |
1.69e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVL--------------GGQSARSLRG---GKMED 63
Cdd:COG4913 1 FRLQRLQLINWGTFDGVHTIDFDGRGTLLTGDNGSGKSTLLDAIQTLLvpakrprfnkaandAGKSDRTLLSyvrGKYGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 64 IifAGSDSRKRLNLAE------VTLTLDNDD---HFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLfmDSGLG 134
Cdd:COG4913 81 E--RDEAGTRPVYLRPgdtwsaIAATFANDGsgqTVTLAQVFWLKGDASSLGDVKRFFVIADGPLDLEDFEEF--AHGFD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 135 KEAFSIISQGKVEEILSSK---AEDRRSIFG---EAAGVLKYKTrkeKAGNKLfetqDNLN-----------RVGDILHE 197
Cdd:COG4913 157 IRALKARLKKQGVEFFDSFsayLARLRRRLGigsEKALRLLHKT---QSFKPI----GDLDdfvreymleepDTFEAADA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 198 LEGQVEPLKiqaSIAKDYLEKKKELEHVEipltayDIEELHGKWSTLKEKVQMAKEEELAessaispkeAKIEGTRDKIQ 277
Cdd:COG4913 230 LVEHFDDLE---RAHEALEDAREQIELLE------PIRELAERYAAARERLAELEYLRAA---------LRLWFAQRRLE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 278 ALDESVDELQqvllvtsEELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQKETvltrrafeaeavfETLQAEVKQLR 357
Cdd:COG4913 292 LLEAELEELR-------AELARLEAELERLEARLDALREELDELEAQIRGNGGDRL-------------EQLEREIERLE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 358 AQVKEKQHALslhnENVEEKIEQLKsdyfellnsqASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAAC 437
Cdd:COG4913 352 RELEERERRR----ARLEALLAALG----------LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 438 KTEFARFEQEIHSqvgayrdmqtkYEQKKRQYEknesplyqayQYVQQARskkDMLdtmqgdfsgfyqgvkevlkaKDRL 517
Cdd:COG4913 418 RRELRELEAEIAS-----------LERRKSNIP----------ARLLALR---DAL--------------------AEAL 453
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 518 GGIRGAV------LELISTEQKYETAIEIAVGASPQHVVTDDEQSARkAIQYLKQNSF-GRATFLPLSVIRDRQLSKPLR 590
Cdd:COG4913 454 GLDEAELpfvgelIEVRPEEERWRGAIERVLGGFALTLLVPPEHYAA-ALRWVNRLHLrGRLVYERVRTGLPDPERPRLD 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 591 GNSgpafiisfgVASELVTFDPAYRSVIQNLLGNRSDYRglkgGANELAKLLGHRYRIvTLEGDVvnpggSMTGGSVKKK 670
Cdd:COG4913 533 PDS---------LAGKLDFKPHPFRAWLEAELGRRFDYV----CVDSPEELRRHPRAI-TRAGQV-----KGNGTRHEKD 593
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 671 NNSLLGRTRELG-DVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLREtgeglrvkQQDVKGQLYEPQFAEKNINT 749
Cdd:COG4913 594 DRRRIRSRYVLGfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQE--------RREALQRLAEYSWDEIDVAS 665
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 750 HLELYD---QEKSALSESDEERkvrkRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELK-IAAAKKE 825
Cdd:COG4913 666 AEREIAeleAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdRLEAAED 741
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 1237015 826 QACKGEEDNLARLKKELTETELALKEAKEdlsfLTSEMSSSTSGEEKLEEA 876
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELREN----LEERIDALRARLNRAEEE 788
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-94 |
5.33e-10 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 62.48 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFaERISVDFVKGVTAVVGPNGSGKSNITDAIrWVLGgqSARSLRGGKMEDIIFAGSDSrkrlnlAEV 80
Cdd:PRK00064 1 MYLTRLSLTDFRNY-EELDLELSPGVNVLVGENGQGKTNLLEAI-YLLA--PGRSHRTARDKELIRFGAEA------AVI 70
|
90
....*....|....
gi 1237015 81 TLTLDNDDHFLPID 94
Cdd:PRK00064 71 HGRVEKGGRELPLG 84
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
10-59 |
1.44e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 58.14 E-value: 1.44e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1237015 10 GFKSFAERISVDFVKG-VTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGG 59
Cdd:cd03227 6 RFPSYFVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS 56
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-88 |
1.81e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 61.10 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFAErISVDFvKGVTAVVGPNGSGKSNITDAIR---WVLGG--QSARSLRGGkMEDIIFAGSDSRKRlnL 77
Cdd:COG4637 2 ITRIRIKNFKSLRD-LELPL-GPLTVLIGANGSGKSNLLDALRflsDAARGglQDALARRGG-LEELLWRGPRTITE--P 76
|
90
....*....|.
gi 1237015 78 AEVTLTLDNDD 88
Cdd:COG4637 77 IRLELEFAEED 87
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
3-911 |
2.36e-09 |
|
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: 61.99 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFA----ERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARslrGGKMEDIIFAGSDSRKRLNLA 78
Cdd:TIGR00606 3 FLKMSILGVRSFGiedkDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPP---GTKGNTFVHDPKVAQETDVRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 79 EVTLtldnddHFLPIDFHEVSVTRRVYRS--------GESEFLINNQPCRLKDI-------IDLFMDSGLG--------- 134
Cdd:TIGR00606 80 QIRL------QFRDVNGEECAVVRSMVCTqktkktefKTLEGVITRYKHGEKVSlsskcaeIDREMISHLGvskavlnnv 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 135 ----------------------KEAFSIISQGKVEEILSSKAEDRRSIFGEAAGVLKY-KTRKEKAG---NKLFETQDNL 188
Cdd:TIGR00606 154 ifchqedsnwplsegkalkqkfDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYlKQYKEKACeirDQITSKEAQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 189 NRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPL--TAYDIEELHGKWSTLKEKVQMAKEEELAE-----SSA 261
Cdd:TIGR00606 234 ESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALksRKKQMEKDNSELELKMEKVFQGTDEQLNDlyhnhQRT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 262 ISPKEAKIEGTRDKIQALDESVDELQQvllvTSEELEKLEGRKEVLKDRKKNAV--------QNQEQLE------EAIVQ 327
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQ----EKTELLVEQGRLQLQADRHQEHIrardsliqSLATRLEldgferGPFSE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 328 FQQKETV-LTRRAFEAEAVF------------ETLQAEVKQLRAQVKEKQHALSLHNENVEEKIEQLKSDYFELLNSQAS 394
Cdd:TIGR00606 390 RQIKNFHtLVIERQEDEAKTaaqlcadlqskeRLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 395 IRNELQLlDDQMSQSAVTLQRLADNN--------EKHLQ-ERHDISARKAACKTEFARFEQEIHSQVGAY---RDMQTKY 462
Cdd:TIGR00606 470 SDRILEL-DQELRKAERELSKAEKNSltetlkkeVKSLQnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmltKDKMDKD 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 463 EQKKRQYEKNESPLYQAYQYVQQARSKKDMLDTMQGDFSGFYQGV----KEVLKAKDRLGGIRGAVLELISTEQKYETAI 538
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLaklnKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 539 EIAVGASpqhvvtDDEQSARKAIQYLKQNSFGRATFLPLSVIRDRQLSKPLRGNSG--PAFIISFGVASELVTFDpayrS 616
Cdd:TIGR00606 629 FDVCGSQ------DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccPVCQRVFQTEAELQEFI----S 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 617 VIQNLLgnRSDYRGLKGGANELAKLLGHRYRIVTLegdvvnpggsmtggsvkkknnsLLGRTRELGDVTKRLAEMEEKTS 696
Cdd:TIGR00606 699 DLQSKL--RLAPDKLKSTESELKKKEKRRDEMLGL----------------------APGRQSIIDLKEKEIPELRNKLQ 754
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 697 LLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVkGQLYEPQFAEKNINTHlelYDQEKSALSESDEERKVRK-RKL 775
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERK---IAQQAAKLQGSDLDRTVQQvNQE 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 776 EEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKED 855
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ 910
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237015 856 LSFLTS-------EMSSSTSGEEKLEEAAKHKLND-KTKTIELIALRRDQRIKLQHGLDTYERE 911
Cdd:TIGR00606 911 DSPLETflekdqqEKEELISSKETSNKKAQDKVNDiKEKVKNIHGYMKDIENKIQDGKDDYLKQ 974
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
683-1030 |
4.87e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 683 DVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQEKSAL- 761
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLe 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 762 -SESDEERKVRKRK-----LEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNL 835
Cdd:TIGR04523 391 sQINDLESKIQNQEklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 836 ARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEaakhKLNDKTKTIELIALRRDqriKLQHGLDTYERELKEM 915
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE----KVKDLTKKISSLKEKIE---KLESEKKEKESKISDL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 916 KRLYKQKTTLLKDEEVKlgRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEarKRVKLIKlAIEELGTVNLGSIDE 995
Cdd:TIGR04523 544 EDELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK--EKKDLIK-EIEEKEKKISSLEKE 618
|
330 340 350
....*....|....*....|....*....|....*
gi 1237015 996 FERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEE 1030
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
677-1037 |
8.53e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 677 RTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKgqlyepqfaeknintHLELYDQ 756
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---------------ELKEKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 757 EKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLS---NELTELKIAAAKKEQAcKGEED 833
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKeleKRLEELEERHELYEEA-KAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 834 NLARLKKELT------------ETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAkhklnDKTKTIELIALRRDQRIKL 901
Cdd:PRK03918 373 ELERLKKRLTgltpeklekeleELEKAKEEIEEEISKITARIGELKKEIKELKKAI-----EELKKAKGKCPVCGRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 902 QHGLDTYERELKEMKRLYKQKTTlLKDEEVKLGRMEVELDNLLQYLREEYSL--------SFEGAKEKYQLETDPEEARK 973
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKE-IEEKERKLRKELRELEKVLKKESELIKLkelaeqlkELEEKLKKYNLEELEKKAEE 526
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237015 974 RVKLIKLAIEELGTVnLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRFND 1037
Cdd:PRK03918 527 YEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-864 |
9.45e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAERIsVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSrkrlnlAEV 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSV-VEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSG------TEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 81 TLTLDNDDHFLPIDFHEVSVTRRVYRSGESEFLINNQpcrlKDIIDlFMDSGLGKEAFS---IISQGKVEEILSSKaEDR 157
Cdd:PRK03918 74 ELKFEKNGRKYRIVRSFNRGESYLKYLDGSEVLEEGD----SSVRE-WVERLIPYHVFLnaiYIRQGEIDAILESD-ESR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 158 RSIFGEAAGVLKYktrkEKAGNKLFETQDNLNRVGDILHELegqvepLKIQASIAKDYLEKKKELEHV--EIPLTAYDIE 235
Cdd:PRK03918 148 EKVVRQILGLDDY----ENAYKNLGEVIKEIKRRIERLEKF------IKRTENIEELIKEKEKELEEVlrEINEISSELP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 236 ELHGKWSTLKEKVQmaKEEELAESsaISPKEAKIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAv 315
Cdd:PRK03918 218 ELREELEKLEKEVK--ELEELKEE--IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 316 QNQEQLEEAIVQFQQKEtvltrraFEAEAVFETLQAEVKQLRAQVKEKqhalslhnENVEEKIEQLKSDYFELLNSQASI 395
Cdd:PRK03918 293 EEYIKLSEFYEEYLDEL-------REIEKRLSRLEEEINGIEERIKEL--------EEKEERLEELKKKLKELEKRLEEL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 396 RNELQLLDDqmsqsavtLQRLADNNEKHLQERHDISARKAACKTEFARFEQEihsqvgAYRDMQTKYEQKKRQYEKNESP 475
Cdd:PRK03918 358 EERHELYEE--------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKE------EIEEEISKITARIGELKKEIKE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 476 LYQAYQYVQQARSKKDMldtmqgdfsgfyqgVKEVLKAKDRLGGIRGAVLELISTEQKYETAIEIavgaspqhvvtddEQ 555
Cdd:PRK03918 424 LKKAIEELKKAKGKCPV--------------CGRELTEEHRKELLEEYTAELKRIEKELKEIEEK-------------ER 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 556 SARKAIQYLKQNSFGRATFLPLSVIRD--RQLSKPLRGNSgpafiisfgvASELVTFDPAYRSVIQNLLGNRSDYRGLKg 633
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEqlKELEEKLKKYN----------LEELEKKAEEYEKLKEKLIKLKGEIKSLK- 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 634 gaNELAKLLGHRYRIVTLEGDVvnpggsmtgGSVKKKNNSLLGRTRELGdvTKRLAEMEEKTSLLEQ------EVQTLKH 707
Cdd:PRK03918 546 --KELEKLEELKKKLAELEKKL---------DELEEELAELLKELEELG--FESVEELEERLKELEPfyneylELKDAEK 612
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 708 SIQDMEKKLADLRETGEGLRVKQQDVKGQLYEpqfAEKNINTHLELYDQEKSalsesdEERKVRKRKLEEELSAVSEKMK 787
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEE---LRKELEELEKKYSEEEY------EELREEYLELSRELAGLRAELE 683
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 788 QLEedidrltKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEED------NLARLKKELTETelALKEAKEDLSFLTS 861
Cdd:PRK03918 684 ELE-------KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERveelreKVKKYKALLKER--ALSKVGEIASEIFE 754
|
...
gi 1237015 862 EMS 864
Cdd:PRK03918 755 ELT 757
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-189 |
1.36e-08 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 55.97 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 6 LDVIGFKSFaERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGK--MEDIIFAGSDSRKRLNLAEVTLT 83
Cdd:pfam13476 1 LTIENFRSF-RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGggFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 84 LDNDDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSIFGE 163
Cdd:pfam13476 80 NNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELEK 159
|
170 180
....*....|....*....|....*.
gi 1237015 164 AAGVLKYKTRKEKAGNKLFETQDNLN 189
Cdd:pfam13476 160 ALEEKEDEKKLLEKLLQLKEKKKELE 185
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1089-1163 |
1.86e-08 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). 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: 213195 [Multi-domain] Cd Length: 171 Bit Score: 55.08 E-value: 1.86e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237015 1089 NLLSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLY 1163
Cdd:cd03228 95 NILSGGQRQRIAIARAL----LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
602-1179 |
2.68e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 602 GVASELVTFDPAYRSvIQNLLGNRSDYRGLKGGANELAKLlghryrIVTLEGDVVNPGGSMTG-GSVKKKNNSLLGRTRE 680
Cdd:PRK01156 316 NIDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQ------ILELEGYEMDYNSYLKSiESLKKKIEEYSKNIER 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 681 LGDVTKRLAEMEEKT-SLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVK-------GQLYEP----QFAEKNIN 748
Cdd:PRK01156 389 MSAFISEILKIQEIDpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSrnmemlnGQSVCPvcgtTLGEEKSN 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 749 THLELYDQEKSALSEsdeerkvRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTK----ESLSNELTELKIaaakK 824
Cdd:PRK01156 469 HIINHYNEKKSRLEE-------KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEynkiESARADLEDIKI----K 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 825 EQACKGEEDNLARLKKELTETELALKEAK-EDLSFLTSEMSS-STSGEEKLEEAAKHKLNDKTKTIELIALRRDQrikLQ 902
Cdd:PRK01156 538 INELKDKHDKYEEIKNRYKSLKLEDLDSKrTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPD---DK 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 903 HGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAK---EKYQLETDPEEARKRVKLIK 979
Cdd:PRK01156 615 SYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAK 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 980 LAIEELGT---VNLGSIDEFE-RVNERYKFLsEQKEDLTEAKNTLFQVIEEMDEemtkrfNDTFVQIRSHFDQVFRSLFG 1055
Cdd:PRK01156 695 ANRARLEStieILRTRINELSdRINDINETL-ESMKKIKKAIGDLKRLREAFDK------SGVPAMIRKSASQAMTSLTR 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1056 GGRAELRLtDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKV--RPVPFCVLDEVEAALDE---ANV 1130
Cdd:PRK01156 768 KYLFEFNL-DFDDIDVDQDFNITVSRGGMVEGIDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPTAFLDEdrrTNL 846
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1237015 1131 FRFAQYLKKYSSDT-QFIVITHRKGTMEEADVLYGVTmQESGVSKVISVK 1179
Cdd:PRK01156 847 KDIIEYSLKDSSDIpQVIMISHHRELLSVADVAYEVK-KSSGSSKVIPLR 895
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
679-1157 |
3.70e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLE--QEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQ 756
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 757 EK-SALSESDEERKV---RKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSsTKESLSNELTELKIAAA---------- 822
Cdd:COG4717 189 ATeEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAAllallglggs 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 823 -----------------------------KKEQACKGEEDNLARLKKELTETELalKEAKEDLSFLTSEMSSSTSGEEKL 873
Cdd:COG4717 268 llsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEEL--EELLAALGLPPDLSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 874 EEAAK---HKLNDKTKTIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREe 950
Cdd:COG4717 346 IEELQellREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 951 ysLSFEGAKEKYQ--------LETDPEEARKRVKLIKLAIEELGTVnlgsiDEFERVNERYKFLSEQKEDLTEAKNTLfQ 1022
Cdd:COG4717 425 --LDEEELEEELEeleeeleeLEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAAL-K 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1023 VIEEMDEEMTKRFNDTFV-QIRSHFDQVFRSLFGGGRAELRLTDpndllhsGVEIIAQPPGKKLQNLNLLSGGERALTAI 1101
Cdd:COG4717 497 LALELLEEAREEYREERLpPVLERASEYFSRLTDGRYRLIRIDE-------DLSLKVDTEDGRTRPVEELSRGTREQLYL 569
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1237015 1102 ALLFSI---LKVRPVPFcVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTME 1157
Cdd:COG4717 570 ALRLALaelLAGEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVE 627
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-54 |
3.83e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 56.16 E-value: 3.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1237015 1 MFLKRLDVIGFKSFaERISVDF--VKGVTAVVGPNGSGKSNITDAIRWVLGGQSAR 54
Cdd:COG3950 1 MRIKSLTIENFRGF-EDLEIDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLSR 55
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-473 |
5.20e-08 |
|
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: 57.67 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAERISVDF--VKGVTAVVGPNGSGKSNITDAIRWVLGGQSARslrggKMEDIIFAGSDSRKRLNLA 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFtaLGPIFLICGKTGAGKTTLLDAITYALYGKLPR-----RSEVIRSLNSLYAAPSEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 79 EVTLTLDNDdhFLPIDFHEVSVTRRVYRSGESEF-LINNQPCRLKDIID---------LFMDSGLGKEAFS---IISQGK 145
Cdd:TIGR00618 76 FAELEFSLG--TKIYRVHRTLRCTRSHRKTEQPEqLYLEQKKGRGRILAakkseteevIHDLLKLDYKTFTrvvLLPQGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 146 VEEILSSKAEDRRSIFGEAAGVLKYKTRKekagnklfetqdnlNRVGDILHELEGQVEPLKIQASIAKDYLEKK------ 219
Cdd:TIGR00618 154 FAQFLKAKSKEKKELLMNLFPLDQYTQLA--------------LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpdtyhe 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 220 ------KELEHVEIPLTAYDI--EELHGKWSTLKEKVQMAKE--EELAESSAISPKEAKIEGTRDKIQ---------ALD 280
Cdd:TIGR00618 220 rkqvleKELKHLREALQQTQQshAYLTQKREAQEEQLKKQQLlkQLRARIEELRAQEAVLEETQERINrarkaaplaAHI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 281 ESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQketvltrrAFEAEAVFEtLQAEVKQLRAQV 360
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT--------LHSQEIHIR-DAHEVATSIREI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 361 KEKQHALSLHNENVEEKIEQLKsdyfELLNSQASIRNELQLLDDQM-----SQSAVTLQRLADNNEKHLQERHDISARKA 435
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLT----QKLQSLCKELDILQREQATIdtrtsAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
490 500 510
....*....|....*....|....*....|....*....
gi 1237015 436 ACKTEFARFEQEIHSQVGAYR-DMQTKYEQKKRQYEKNE 473
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQIHLQE 485
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
5-83 |
1.23e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 53.43 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 5 RLDVIGFKSFAERISVDFVK----GVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSrkrlnlAEV 80
Cdd:cd03279 5 KLELKNFGPFREEQVIDFTGldnnGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDT------AEV 78
|
...
gi 1237015 81 TLT 83
Cdd:cd03279 79 SFT 81
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
681-1020 |
1.46e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 681 LGDVTKRLAEM----EEKTSLLEQEVQ---TLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLEl 753
Cdd:pfam15921 383 LADLHKREKELslekEQNKRLWDRDTGnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 754 ydqEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQA---CKG 830
Cdd:pfam15921 462 ---KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQElqhLKN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 831 EEDNLARLKKELTETELALKEAKEDLSFLTSEMssstsgEEKLEEAAKHKLNDKTKTIElialrrdqRIKLQHGLDTYER 910
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKVIEILRQQI------ENMTQLVGQHGRTAGAMQVE--------KAQLEKEINDRRL 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 911 ELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNL 990
Cdd:pfam15921 605 ELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684
|
330 340 350
....*....|....*....|....*....|.
gi 1237015 991 GSIDEFERVNERYKF-LSEQKEDLTEAKNTL 1020
Cdd:pfam15921 685 NKSEEMETTTNKLKMqLKSAQSELEQTRNTL 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-385 |
1.49e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 182 FETQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPLTAYDIEELhgKWSTLKEKVQmAKEEELAEssa 261
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--DVASAEREIA-ELEAELER--- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 262 ispkeakIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQKETVLTRraFE 341
Cdd:COG4913 680 -------LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--AL 750
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1237015 342 AEAVFETLQAE--VKQLRAQVKEKQHALSLHNENVEEKIEQLKSDY 385
Cdd:COG4913 751 LEERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
679-878 |
2.39e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLE------ 752
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEaqkeel 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 753 -----------LYDQEKSALSESDEERKVRKRKLEEELS-AVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIA 820
Cdd:COG4942 107 aellralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 821 AAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAK 878
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-241 |
4.45e-07 |
|
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: 53.16 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 26 VTAVVGPNGSGKSNITDAIRWVL-------------------GGQSARSLRGGKMEDIIFAGSDSRKRLNLAEVTLTLDN 86
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLAdfdalvigltdersrnggiGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 87 DDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDI-IDLFMDSGLGKEAFSIISQGKVEEILSSkAEDRRSIFGEAA 165
Cdd:pfam13304 81 EDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELrLGLDVEERIELSLSELSDLISGLLLLSI-ISPLSFLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237015 166 GVLKYKTRKEKAGNKLFETQDnlnrVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPLTAYDIEELHGKW 241
Cdd:pfam13304 160 GLLLEDWAVLDLAADLALFPD----LKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGE 231
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
16-86 |
4.64e-07 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 51.44 E-value: 4.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237015 16 ERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSrkrlnlAEVTLTLDN 86
Cdd:cd03276 13 RHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESS------AKITVTLKN 77
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
683-1078 |
7.65e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 683 DVTKRLAEMEEKTSLLEQEVQTLKHSiqDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQEKSalS 762
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA--K 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 763 ESDEERKVRKRKLEEELSAVSEKMKQLE----EDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARL 838
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADElkkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 839 KKELTETELALKEAKEDLSflTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELKEMKRL 918
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 919 YKQKTTLLKDEEvKLGRMEVE---LDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELgtvnlgSIDE 995
Cdd:PTZ00121 1681 KKAEEDEKKAAE-ALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA------KKDE 1753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 996 FERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRFNDTFVQIRSHFDQVFRSLFGGGRAELRLTDPNDLLHSGVE 1075
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
...
gi 1237015 1076 IIA 1078
Cdd:PTZ00121 1834 EVA 1836
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-130 |
8.35e-07 |
|
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: 51.82 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVigfKSFA--ERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQ-SARSLRGGKMEDII---FAGSdsrkrlN 76
Cdd:cd03241 1 LLELSI---KNFAliEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRaSADLIRSGAEKAVVegvFDIS------D 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1237015 77 LAEVTLTLDNDDhflPIDFHEVSVTRRVYRSGESEFLINNQPC---RLKDIIDLFMD 130
Cdd:cd03241 72 EEEAKALLLELG---IEDDDDLIIRREISRKGRSRYFINGQSVtlkLLRELGSLLVD 125
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1091-1159 |
8.80e-07 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 49.94 E-value: 8.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1091 LSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSD-TQFIVITHRKGTMEEA 1159
Cdd:cd00267 81 LSGGQRQRVALARAL----LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELA 146
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
679-1165 |
1.57e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEpqfAEKNINTHLELYDQ-- 756
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT---ARERVEEAEALLEAgk 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 757 --------EKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTkESLSNELTELKIAAAKKEQAC 828
Cdd:PRK02224 454 cpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRI-ERLEERREDLEELIAERRETI 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 829 KGEEDNLARLKKELTETELALKEAKEDLSFLTSEmssstsGEEKLEEAAkhKLNDKTKTielIALRRDQRIKLQHGLDTY 908
Cdd:PRK02224 533 EEKRERAEELRERAAELEAEAEEKREAAAEAEEE------AEEAREEVA--ELNSKLAE---LKERIESLERIRTLLAAI 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 909 ERELKEMKRLYKQKTTLLKDEEVKLGRMEvELDNLLQYLREEYSLS-FEGAKEK------YQLETDPEEARKRVKLIKLA 981
Cdd:PRK02224 602 ADAEDEIERLREKREALAELNDERRERLA-EKRERKRELEAEFDEArIEEAREDkeraeeYLEQVEEKLDELREERDDLQ 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 982 iEELGTVNlGSIDEFERVNERYKFLSEQKEDLteakNTLFQVIEEMDEemtkrfndTFVQIRSHFDQvfRSLfggGRAEL 1061
Cdd:PRK02224 681 -AEIGAVE-NELEELEELRERREALENRVEAL----EALYDEAEELES--------MYGDLRAELRQ--RNV---ETLER 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1062 RLTDPNDLL-----HSGVEI-------IAQPPGKKLqNLNLLSGGERAL------TAIALLFS--ILKVRPVPFCVLDEV 1121
Cdd:PRK02224 742 MLNETFDLVyqndaYSHIELdgeyeltVYQKDGEPL-EPEQLSGGERALfnlslrCAIYRLLAegIEGDAPLPPLILDEP 820
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1237015 1122 EAALDEANVFRFAQyLKKYSSD---TQFIVITHRKGTMEEADVLYGV 1165
Cdd:PRK02224 821 TVFLDSGHVSQLVD-LVESMRRlgvEQIVVVSHDDELVGAADDLVRV 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
233-448 |
2.60e-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: 51.30 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 233 DIEELHGKWSTLKEKVQMAKEEELAESSAISPKEAKIEGTRDKIQALDESVDELQQVLLVTSEELEKLE----GRKEVLK 308
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaeleAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 309 DRKKNAVQNQEQLEEAIVQFQQKETVLTRRAFEAEAVFETLQAEVKQLRAQVKEkqhalslhnenVEEKIEQLKSDYFEL 388
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-----------LAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 389 LNSQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACKTEFARFEQEI 448
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-450 |
3.11e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAERiSVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSarslRGGKMEDIIfagsdsRKRLNLAEV 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDS-EIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMI------KKGKNNLEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 81 TLTLDNDDHFLPIdfhEVSVTRRVYR-SGESEFLINNQPCR--LKDIIDLFMDSGLG--KEAF--SIIS-QGKVEEILSS 152
Cdd:PRK01156 70 ELEFRIGGHVYQI---RRSIERRGKGsRREAYIKKDGSIIAegFDDTTKYIEKNILGisKDVFlnSIFVgQGEMDSLISG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 153 KAEDRRSIFGEAAGVlkyktrkekagNKLFETQDNLNRVGDILhelegqveplkiQASIAK-DYLEKKKELEHVEIPLTA 231
Cdd:PRK01156 147 DPAQRKKILDEILEI-----------NSLERNYDKLKDVIDML------------RAEISNiDYLEEKLKSSNLELENIK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 232 YDIEELHGKWS-TLKEKVQMAKEEELAESSAISPKEA--KIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLK 308
Cdd:PRK01156 204 KQIADDEKSHSiTLKEIERLSIEYNNAMDDYNNLKSAlnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHM 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 309 DRKKNAVQNQEqlEEAIVQFQQKETVLTRRafeaeAVFETLQAEVKQLRAQVKEKQHALSLHNENVEEK----------- 377
Cdd:PRK01156 284 KIINDPVYKNR--NYINDYFKYKNDIENKK-----QILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKsryddlnnqil 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 378 -IEQLKSDYFELLNSQAS----IRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACKTEFARFEQEIHS 450
Cdd:PRK01156 357 eLEGYEMDYNSYLKSIESlkkkIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRA 434
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
3-468 |
3.27e-06 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 51.28 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVI-GFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIrwvlggqsaRSLRGGKMEDIIfagsdsrkrlnLAEVT 81
Cdd:COG4694 2 ITKIKKLkNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRIL---------RSLELGDTSSEV-----------IAEFE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 82 LTLDNDDHFLPIdfhevsvtrRVYRsgeSEFlINNQPCRLKDIIDLFMDSGLGKEAFSIISQ--GKVEEILSSKAEDRRS 159
Cdd:COG4694 62 IEAGGSAPNPSV---------RVFN---RDF-VEENLRSGEEIKGIFTLGEENIELEEEIEEleKEIEDLKKELDKLEKE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 160 IFGEAAGVLKYKTRKEKAGNKLFETQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPLTAYDIEELHG 239
Cdd:COG4694 129 LKEAKKALEKLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 240 KWST----LKEKVQMAKEEELAESSAISPKEAKIEGTRDKIQALDESVDEL-QQVLlvTSEELEKLEGR-KEVLKDRKKN 313
Cdd:COG4694 209 LLSEaetlLEKSAVSSAIEELAALIQNPGNSDWVEQGLAYHKEEEDDTCPFcQQEL--AAERIEALEAYfDDEYEKLLAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 314 AVQNQEQLEEAIVQFQQKETVLTRRAFEA-----EAVFETLQAEVKQLRAQVKEKQHALSLH-NENVEEKIEQLKSDYFE 387
Cdd:COG4694 287 LKDLLEELESAINALSALLLEILRTLLPSakedlKAALEALNALLETLLAALEEKIANPSTSiDLDDQELLDELNDLIAA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 388 LlnsQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQErhDISARKAACKTEFARFeQEIHSQVGAYRDMQTKYEQKKR 467
Cdd:COG4694 367 L---NALIEEHNAKIANLKAEKEEARKKLEAHELAELKE--DLSRYKAEVEELIEEL-KTIKALKKALEDLKTEISELEA 440
|
.
gi 1237015 468 Q 468
Cdd:COG4694 441 E 441
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-87 |
3.40e-06 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 49.99 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVIGFKSFAErISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGqsaRSLRGGKMEDIIFAGSDSrkrlnlAEVTL 82
Cdd:cd03242 1 LKSLELRNFRNYAE-LELEFEPGVTVLVGENAQGKTNLLEAISLLATG---KSHRTSRDKELIRWGAEE------AKISA 70
|
....*
gi 1237015 83 TLDND 87
Cdd:cd03242 71 VLERQ 75
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
745-1034 |
4.35e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 745 KNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMK---QLEEDIDRLTKQKQTQSSTKEslsnELTELKIAA 821
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEELKE----EIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 822 AKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLtsemssstsgeEKLEEAAKhklndktKTIELIALRRDQRIKL 901
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----------KELKEKAE-------EYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 902 QH---GLDTYERELKEMKRlykqkttLLKDEEVKLGRMEvELDNLLQYLREEYSlSFEGAKEKYQletdpeearkRVKLI 978
Cdd:PRK03918 310 REiekRLSRLEEEINGIEE-------RIKELEEKEERLE-ELKKKLKELEKRLE-ELEERHELYE----------EAKAK 370
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1237015 979 KLAIEELGTVNlgSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKR 1034
Cdd:PRK03918 371 KEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
682-1033 |
7.86e-06 |
|
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: 49.89 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 682 GDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKgqlyepqfaekniNTHLELyDQEKSAL 761
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS-------------ASSEEL-SEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 762 SESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTK-------------------QKQTQSSTKE--SLSNELTELKIA 820
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErakkagaqrkeeeaerkqlQAKLQQTEEElrSLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 821 AAKKEQACKGEEDNLARLKKELTET---ELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQ 897
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 898 RIKLQHGLDTYERELKEMK-RLYKQKTTLLKDEE---VKLGRMEVELDNLLQYLREEYSlsfegAKEKYQLETDPEEARK 973
Cdd:pfam07888 281 AAQLTLQLADASLALREGRaRWAQERETLQQSAEadkDRIEKLSAELQRLEERLQEERM-----EREKLEVELGREKDCN 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 974 RVKLIKlaieelgtvnlgSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTK 1033
Cdd:pfam07888 356 RVQLSE------------SRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET 403
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
679-914 |
8.88e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLyepqFAEKNINTHLElydQEK 758
Cdd:pfam19220 69 RELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL----AAETEQNRALE---EEN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 759 SALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLArl 838
Cdd:pfam19220 142 KALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLA-- 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237015 839 kKELTETELALKEAKEDLSFLTSEMSSSTSgeeKLEEA-AKHKLNDKtktieLIALRRDQRIKLQHGLDTYERELKE 914
Cdd:pfam19220 220 -AEQAERERAEAQLEEAVEAHRAERASLRM---KLEALtARAAATEQ-----LLAEARNQLRDRDEAIRAAERRLKE 287
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
256-471 |
9.31e-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: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 256 LAESSAISPKEAKIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQKETVL 335
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 336 TRRafeaeavFETLQAEV-KQLRAQVKEKQH---ALSLHNENVEEKIEQLKsdYFELLNSQ-----ASIRNELQLLDDQM 406
Cdd:COG4942 96 RAE-------LEAQKEELaELLRALYRLGRQpplALLLSPEDFLDAVRRLQ--YLKYLAPArreqaEELRADLAELAALR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237015 407 SQSAVTLQRLADNNEKHLQERHDISARKAACKTEFARFEQEIHSQVGAYRDMQTKYEQKKRQYEK 471
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1091-1152 |
1.04e-05 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 47.97 E-value: 1.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237015 1091 LSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHR 1152
Cdd:cd03245 141 LSGGQRQAVALARAL----LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHR 198
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
731-904 |
1.83e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 731 QDVKGQLYEPQFAEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKE-- 808
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 809 SLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTI 888
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
170
....*....|....*.
gi 1237015 889 ELIALRRDQRIKLQHG 904
Cdd:COG1579 173 PPELLALYERIRKRKN 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
677-1029 |
2.56e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 677 RTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEpqFAEKNIntHLELYDQ 756
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE--IEELEK--ELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 757 EKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEdIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLA 836
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 837 RL---KKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELK 913
Cdd:PRK03918 332 ELeekEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 914 EMKRLYKQKTTLLK--------------------DEEVKLGRME---VELDNLLQYLREEYSLSFEGAKEKYQLETDPEE 970
Cdd:PRK03918 412 ARIGELKKEIKELKkaieelkkakgkcpvcgrelTEEHRKELLEeytAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237015 971 ARKRVKLIKLA------IEELGTVNLGSID----EFERVNERY-------KFLSEQKEDLTEAKNTLFQVIEEMDE 1029
Cdd:PRK03918 492 ESELIKLKELAeqlkelEEKLKKYNLEELEkkaeEYEKLKEKLiklkgeiKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
3-48 |
2.80e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.97 E-value: 2.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1237015 3 LKRLDVIGFKSF-AERISVDfVKGVTAVVGPNGSGKSNITDAIRWVL 48
Cdd:pfam13555 1 LTRLQLINWGTFdGHTIPID-PRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-86 |
3.98e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 47.35 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 2 FLKRLDVIGFKSFAERISVDFVKG------VTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSRKRL 75
Cdd:COG1106 1 MLISFSIENFRSFKDELTLSMVASglrllrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEP 80
|
90
....*....|.
gi 1237015 76 NLAEVTLTLDN 86
Cdd:COG1106 81 SEFEILFLLDG 91
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-417 |
5.77e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 251 AKEEELAESSAISPKEAKIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKDR----KKNAVQNQEQLEEAIV 326
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 327 QFQQKETVLT---------------RRAFEAEAVFETLQA---EVKQLRAQVKEKQHALSLHNENVEEKIEQLKSDYFEL 388
Cdd:COG3883 94 ALYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180
....*....|....*....|....*....
gi 1237015 389 LNSQASIRNELQLLDDQMSQSAVTLQRLA 417
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1091-1160 |
6.33e-05 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 46.90 E-value: 6.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1091 LSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEAD 1160
Cdd:TIGR02857 459 LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1091-1163 |
7.94e-05 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 46.75 E-value: 7.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237015 1091 LSGGERalTAIALLFSILKvRPvPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLY 1163
Cdd:COG2274 612 LSGGQR--QRLAIARALLR-NP-RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII 680
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
681-859 |
9.04e-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: 46.71 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 681 LGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQEKSA 760
Cdd:pfam01576 421 LSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 761 LSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKK 840
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
170
....*....|....*....
gi 1237015 841 ELTETELALKEAKEDLSFL 859
Cdd:pfam01576 581 ELDDLLVDLDHQRQLVSNL 599
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-57 |
9.65e-05 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 46.19 E-value: 9.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 1 MFLKRLDVIGFKSFaERISVDFVKGVTAVVGPNGSGKSNITDAIrWVLG-GQSARSLR 57
Cdd:TIGR00611 1 MYLSRLELTDFRNY-DAVDLELSPGVNVIVGPNGQGKTNLLEAI-YYLAlGRSHRTSR 56
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1086-1152 |
9.65e-05 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 44.77 E-value: 9.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 1086 QNLNLLSGGERALTAIAllfSILKVRPvPFCVLDEVEAALDEANVFRFAQYLKKYSSD-TQFIVITHR 1152
Cdd:cd03225 130 RSPFTLSGGQKQRVAIA---GVLAMDP-DILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHD 193
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
193-909 |
1.32e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 193 DILHELEGQVEPLKIQASIAKDYLEKKK-ELEHVEIPLTAYDiEELHGKWSTLKEkVQMAKEEELAESSAISPKEAKIEG 271
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNtQIEQLRKMMLSHE-GVLQEIRSILVD-FEEASGKKIYEHDSMSTMHFRSLG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 272 TrdkiqALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAV-----QNQEQLEEAIVQFQQKETVLTRRAFEAEAVF 346
Cdd:pfam15921 220 S-----AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIelllqQHQDRIEQLISEHEVEITGLTEKASSARSQA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 347 ETLQAEVKQLRAQVKEKQHALSLHNENVEEKIEQLKSdyfELLNSQASIRNELQLLDDQ--MSQSAVTLQRladnnekhl 424
Cdd:pfam15921 295 NSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRS---ELREAKRMYEDKIEELEKQlvLANSELTEAR--------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 425 QERHDISARKAACKTEFARFEQEIHSQvgaYRDMQTKYEQKKRQYEKN----------ESPLYQAYQYVQQARSkkdMLD 494
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKLLADLHKR---EKELSLEKEQNKRLWDRDtgnsitidhlRRELDDRNMEVQRLEA---LLK 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 495 TMQGDFSG-------FYQGVKEVLKAKDRLGGIRGAVLELISTEQKYETAIEIAVGASPQHV--VTDDEQSARKAIQylk 565
Cdd:pfam15921 437 AMKSECQGqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVsdLTASLQEKERAIE--- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 566 qnsfgrATFLPLSVIRDR---QLSKPLRGNSGPAFIISFGVASELVTFDPAYRSVIQNLLGNRSDyrglkgganELAKLL 642
Cdd:pfam15921 514 ------ATNAEITKLRSRvdlKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE---------NMTQLV 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 643 GHRYRivtlegdvvnpggsmTGGSVKKKNNSLlgrTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRET 722
Cdd:pfam15921 579 GQHGR---------------TAGAMQVEKAQL---EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNA 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 723 GEGLRVKQQDVKGQ----LYEPQFAEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMkqleedidrltk 798
Cdd:pfam15921 641 GSERLRAVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL------------ 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 799 qKQTQSSTKESLSNELTELKIAAAKKEQ--ACKGEEDNLAR----LKKELTETELALKEAKEDLSFLTSEMSS------S 866
Cdd:pfam15921 709 -EQTRNTLKSMEGSDGHAMKVAMGMQKQitAKRGQIDALQSkiqfLEEAMTNANKEKHFLKEEKNKLSQELSTvateknK 787
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 867 TSGEEKLEEAAKHKLNDKTKTIEL--------------IALRRDQ---RIKLQHGLDTYE 909
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEValdkaslqfaecqdIIQRQEQesvRLKLQHTLDVKE 847
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
686-1027 |
1.38e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 686 KRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGqlyepqfaekNINTHLELYDQEKSALSE-- 763
Cdd:pfam01576 264 KKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLD----------TTAAQQELRSKREQEVTElk 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 764 --SDEERKVRKRKLEE-------ELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDN 834
Cdd:pfam01576 334 kaLEEETRSHEAQLQEmrqkhtqALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 835 LARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEaakhklndktktielialrrdQRIKLQHGLDTYERELKE 914
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG---------------------KNIKLSKDVSSLESQLQD 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 915 MKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNLGSID 994
Cdd:pfam01576 473 TQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR 552
|
330 340 350
....*....|....*....|....*....|...
gi 1237015 995 EFERVNERYKFLSEQKEDLTEAKNTLFQVIEEM 1027
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
687-982 |
1.41e-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: 46.12 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 687 RLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQEKSALSESDE 766
Cdd:TIGR00618 294 PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 767 ERKVRK--RKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSStkESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTE 844
Cdd:TIGR00618 374 QHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDT--RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 845 TELALKEAkedlsfLTSEMSSSTSgEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQhgldtyERELKEMKRLYKQKTT 924
Cdd:TIGR00618 452 QCEKLEKI------HLQESAQSLK-EREQQLQTKEQIHLQETRKKAVVLARLLELQEE------PCPLCGSCIHPNPARQ 518
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1237015 925 LLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEA-RKRVKLIKLAI 982
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMqEIQQSFSILTQ 577
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
678-915 |
1.42e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 678 TRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLrvkQQDvkgqlyepqfaekNINTHLELYDQE 757
Cdd:pfam10174 379 AGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSL---QTD-------------SSNTDTALTTLE 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 758 KsALSESD-------EERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKG 830
Cdd:pfam10174 443 E-ALSEKEriierlkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 831 EEDNLARLKKELTETELALKEAKEdlsfltSEMSSSTSGEekleeaakhkLNDKTKTIEL-IALRRDQRIKLQHGLDTYE 909
Cdd:pfam10174 522 LEIAVEQKKEECSKLENQLKKAHN------AEEAVRTNPE----------INDRIRLLEQeVARYKEESGKAQAEVERLL 585
|
....*.
gi 1237015 910 RELKEM 915
Cdd:pfam10174 586 GILREV 591
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-285 |
1.50e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 45.67 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAErISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSRKRLNLAEV 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKD-TEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNIFEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 81 TLTLDN---DDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDL--FMDSGLGKEAFSIISQGKVEEILSSKAE 155
Cdd:pfam13175 80 ISFSIDieiDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKadLLLELKISDLKKYLKQFKIYIYNNYYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 156 DRRSIF--GEAAGVLKYKTRKEKAGNKLFE-TQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHveipltay 232
Cdd:pfam13175 160 EKKNVFdkKSKYELPSLKEEFLNSEKEEIKvDKEDLKKLINELEKSINYHENVLENLQIKKLLISADRNASD-------- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1237015 233 diEELHGKWSTLKEKVQMAKEEELAESSAIspkEAKIEGTRDKIQALDESVDE 285
Cdd:pfam13175 232 --EDSEKINSLLGALKQRIFEEALQEELEL---TEKLKETQNKLKEIDKTLAE 279
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
937-1151 |
1.50e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.07 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 937 EVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVN-ERYKFLSEQKEDLTE 1015
Cdd:pfam13304 92 TLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLlLDEGLLLEDWAVLDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1016 AKNTLFQvieemDEEMTKRFNDTfvqirSHFDQVFRSLFGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGE 1095
Cdd:pfam13304 172 AADLALF-----PDLKELLQRLV-----RGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGT 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 1096 -RALTAIALLFSILKVRPVpfCVLDEVEAALDEANVFRFAQYLKKYSS-DTQFIVITH 1151
Cdd:pfam13304 242 kRLLALLAALLSALPKGGL--LLIDEPESGLHPKLLRRLLELLKELSRnGAQLILTTH 297
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1089-1160 |
1.58e-04 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 44.38 E-value: 1.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237015 1089 NLLSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEAD 1160
Cdd:cd03248 149 SQLSGGQKQRVAIARAL----IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERAD 216
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1082-1150 |
1.58e-04 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 44.12 E-value: 1.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237015 1082 GKKLQNLN--LLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEAN---VFRFAQYLKKYSSDTQFIVIT 1150
Cdd:cd03277 116 GEQLQELDphHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNerkVFDMLVETACKEGTSQYFLIT 189
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1082-1150 |
1.74e-04 |
|
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: 44.13 E-value: 1.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237015 1082 GKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANvFRFAQYL----KKYSSDTQFIVIT 1150
Cdd:cd03276 101 KAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN-RKISTDLlvkeAKKQPGRQFIFIT 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1091-1153 |
1.76e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 43.30 E-value: 1.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237015 1091 LSGGERALTAIALLFsILKVRpvpFCVLDEVEAALDEANVFRFAQYLKKYSsdTQFIVITHRK 1153
Cdd:cd03223 92 LSGGEQQRLAFARLL-LHKPK---FVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRP 148
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1091-1159 |
2.09e-04 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 44.25 E-value: 2.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1091 LSGGERALTAIAllfSILKVRPvPFCVLDEVEAALDEANVFRFAQYLKKY-SSDTQFIVITHRkgtMEEA 1159
Cdd:COG1122 135 LSGGQKQRVAIA---GVLAMEP-EVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHD---LDLV 197
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
18-385 |
2.52e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 18 ISVDFVK-GVTAVVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMediifAGSDSRKRLnLAEVTLTLDNDDHFlpidfh 96
Cdd:PHA02562 20 IEIQLDKvKKTLITGKNGAGKSTMLEALTFALFGKPFRDIKKGQL-----INSINKKDL-LVELWFEYGEKEYY------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 97 evsVTR-------RVYRSGEsefLINnQPCRLKDIIDLFMDS-GLGKEAFSII----SQGKVEeILSSKAEDRR------ 158
Cdd:PHA02562 88 ---IKRgikpnvfEIYCNGK---LLD-ESASSKDFQKYFEQMlGMNYKSFKQIvvlgTAGYVP-FMQLSAPARRklvedl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 159 ---SIFGEAAGVLKYKTR------------KEKAGNKLFETQDNLNRV----GDILHELEGQVEPLKIQA-SIAKDYLEK 218
Cdd:PHA02562 160 ldiSVLSEMDKLNKDKIRelnqqiqtldmkIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDELVEEAkTIKAEIEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 219 KKELEHVEIPLTAY--DIEELHGKWSTLKEKV-QMAKEEELAESSAISPKEAK-IEGTRDKIQALDESVDELQQvllvts 294
Cdd:PHA02562 240 TDELLNLVMDIEDPsaALNKLNTAAAKIKSKIeQFQKVIKMYEKGGVCPTCTQqISEGPDRITKIKDKLKELQH------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 295 eELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQKETVLTRRAFEAEAVfetlQAEVKQLRAQVKEKQHALSLHNENV 374
Cdd:PHA02562 314 -SLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV----KAAIEELQAEFVDNAEELAKLQDEL 388
|
410
....*....|.
gi 1237015 375 EEKIEQlKSDY 385
Cdd:PHA02562 389 DKIVKT-KSEL 398
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-457 |
2.75e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1 MFLKRLDVIGFKSFAERiSVDFVKGVTAVVGPNGSGKSNITDAIRWVLggqsARSLRggKMEDIIFAGSDSRKRLNLAEv 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDR-TIEFSPGLNVIYGPNEAGKSTLLAFIRAML----LERLE--KEADELFKPQGRKPELNLKE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 81 tltldnddhflpidFHEVSVTRRVYRSGESEFlinnqpcrlkdiidlfmdSGLGKEAFSIISQGKVEEILSSKAEDRRSI 160
Cdd:COG4717 73 --------------LKELEEELKEAEEKEEEY------------------AELQEELEELEEELEELEAELEELREELEK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 161 FGEAAGVLKYKTRKEKAGNKLFETQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIPLTAYDIEELHGK 240
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 241 WSTLKEKVQMAKEEELAESSAISPKEAKIEGTRDKIQALD--ESVDELQQVLLVTSE--ELEKLEGRKEVLKDRKKNAVQ 316
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 317 NQEQLEEAIVQFQQKETVLTRRAFEAEAVFETLQA-EVKQLRAQVKEKQHALSLHNENVEEKIEQLKsDYFELLNSQASI 395
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEEL 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237015 396 RNELQLLDDQMSQSAVtLQRLADNNEKHLQERHDISARKAACKTEFARFEQEIHSQVGAYRD 457
Cdd:COG4717 360 EEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEE 420
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1089-1152 |
2.79e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 2.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237015 1089 NLLSGGERALTAIA-LLFSilkvRPvPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHR 1152
Cdd:COG4178 484 QVLSLGEQQRLAFArLLLH----KP-DWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
241-407 |
3.11e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 241 WSTLKEKVQMAKEEE-LAES-SAISPKEAKIEGTRDKIQALDESVDELQQVL---LVTSEELEKL----EGRKEVLKDRK 311
Cdd:PRK04863 495 WDVARELLRRLREQRhLAEQlQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknLDDEDELEQLqeelEARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 312 KNAVQNQEQLEEAIVQFQQKETVLTRRA---FEAEAVFETLQ----------AEVKQLRAQVKEKQHALSLHNENVEEKI 378
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLReqsgeefedsQDVTEYMQQLLERERELTVERDELAARK 654
|
170 180
....*....|....*....|....*....
gi 1237015 379 EQLKSDYFELLNSQASIRNELQLLDDQMS 407
Cdd:PRK04863 655 QALDEEIERLSQPGGSEDPRLNALAERFG 683
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
665-925 |
3.28e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 665 GSVKKKNNSLLGRTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRetgegLRVKQQDVKGQLYEPQFAE 744
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE-----SEKKEKESKISDLEDELNK 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 745 KNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKK 824
Cdd:TIGR04523 550 DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 825 EQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQHG 904
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKL 709
|
250 260
....*....|....*....|.
gi 1237015 905 LDTYERELKEMKRLYKQKTTL 925
Cdd:TIGR04523 710 EEKYKEIEKELKKLDEFSKEL 730
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
176-359 |
3.63e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 176 KAGNKLFETQDNLNRVGDILHELEGQVEPLKIQASIAK---DYLEKKKELEHVEIPLTAYDIEElhgkwSTLKEKVQMAK 252
Cdd:COG3206 202 RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEarlAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 253 EEELAESSAISPKEAKIEGTRDKIQALDESVD-ELQQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQk 331
Cdd:COG3206 277 AELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR- 355
|
170 180
....*....|....*....|....*...
gi 1237015 332 etvLTRRAFEAEAVFETLQAEVKQLRAQ 359
Cdd:COG3206 356 ---LEREVEVARELYESLLQRLEEARLA 380
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
687-916 |
4.18e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 687 RLAEMEEKTSLLEQEVQTLKHSI-------QDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQEKS 759
Cdd:pfam10174 241 KISSLERNIRDLEDEVQMLKTNGllhtedrEEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 760 -------ALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEE 832
Cdd:pfam10174 321 dckqhieVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 833 DNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAakhkLNDKTKTIEliALR----RDQRIKLQHgLDTY 908
Cdd:pfam10174 401 KKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEA----LSEKERIIE--RLKeqreREDRERLEE-LESL 473
|
....*...
gi 1237015 909 ERELKEMK 916
Cdd:pfam10174 474 KKENKDLK 481
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
669-1053 |
4.54e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 669 KKNNSllgrTRELGDVTKRL-AEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNI 747
Cdd:pfam05483 148 KENNA----TRHLCNLLKETcARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 748 NTHLE------LYDQEKSA------LSESD----------EERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQ-KQTQS 804
Cdd:pfam05483 224 IQHLEeeykkeINDKEKQVsllliqITEKEnkmkdltfllEESRDKANQLEEKTKLQDENLKELIEKKDHLTKElEDIKM 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 805 STKESLSNELT---ELKIAAAKKEQACKGEEDNLARLKKeltetelalkeAKEDLSFLTSEMSSSTSGEEKLEEAAKHKL 881
Cdd:pfam05483 304 SLQRSMSTQKAleeDLQIATKTICQLTEEKEAQMEELNK-----------AKAAHSFVVTEFEATTCSLEELLRTEQQRL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 882 NDKTKTIELIALRRDQRI----KLQHGLDTYERELKEMKRLYKQKTTLLkDEEVKLGRMEVELDNLLQylrEEYSLSFEG 957
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSseleEMTKFKNNKEVELEELKKILAEDEKLL-DEKKQFEKIAEELKGKEQ---ELIFLLQAR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 958 AKEKYQLE-------TDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLT-EAKNTLFQVI--EEM 1027
Cdd:pfam05483 449 EKEIHDLEiqltaikTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTlELKKHQEDIIncKKQ 528
|
410 420
....*....|....*....|....*....
gi 1237015 1028 DEEMTKR---FNDTFVQIRSHFDQVFRSL 1053
Cdd:pfam05483 529 EERMLKQienLEEKEMNLRDELESVREEF 557
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
788-1042 |
4.92e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 788 QLEEDIDRLTKQKQTQSSTKESLSNELTELKIAaakkeqackgeednLARLKKELTETELALKEAKEDLSFLTSEMSSST 867
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGE--------------LEKASREETFARTALKNARLDLRRLFDEKQSEK 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 868 SGEEKLEEAAKHKLNDKTKTI--ELIALRRDQRIKLQHGLDTYeRELKEMKRLYKQktTLLKDEEVKLGRMEVELDNL-L 944
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLeaQLKQLDKKHQAWLEEQKEQK-REARTEKQAYWQ--VVEGALDAQLALLKAAIAARrS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 945 QYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELG--TVNLGSIDEFER-VNERYkflSEQKEDLTEAKNTLF 1021
Cdd:pfam12128 744 GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIEriAVRRQEVLRYFDwYQETW---LQRRPRLATQLSNIE 820
|
250 260
....*....|....*....|.
gi 1237015 1022 QVIEEMDEEMTKRFNDTFVQI 1042
Cdd:pfam12128 821 RAISELQQQLARLIADTKLRR 841
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1085-1174 |
6.41e-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: 42.21 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1085 LQNLNLLSGGERALTAIALLFSILKVRPV--PFCVLDEVEAALDEANV-FRFAQYLKKYSSDT--QFIVITHRKGTMEEA 1159
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERKSQKnfQLIVITHDEELVDAA 189
|
90
....*....|....*
gi 1237015 1160 DVLYGVTMQESGVSK 1174
Cdd:cd03240 190 DHIYRVEKDGRQKSR 204
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
679-1039 |
6.53e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQE- 757
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSi 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 758 KSALSESDEERKVRKRKlEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTElkiaaakKEQACKGEEDNLAR 837
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSK-EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE-------KESKISDLEDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 838 LKKELTETEL--ALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQriklqhgLDTYERELKEM 915
Cdd:TIGR04523 550 DDFELKKENLekEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK-------ISSLEKELEKA 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 916 KRLYKQKTTLLKDEEVKLGRMEVELDNL---LQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNLGS 992
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLKQEVKQIketIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIR 702
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1237015 993 IDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDeemtKRFNDTF 1039
Cdd:TIGR04523 703 IKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFN----KKFDDAF 745
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
687-856 |
6.96e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 687 RLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLREtgeglrvkqqdvkgqlyepqfAEKNINTHLELYDQEKSALSESDE 766
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA---------------------RLEAAKTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 767 ERKVRKRKLEEELSAVSEkmkqlEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETE 846
Cdd:COG1579 70 EVEARIKKYEEQLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
170
....*....|
gi 1237015 847 LALKEAKEDL 856
Cdd:COG1579 145 AELDEELAEL 154
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-446 |
8.04e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 150 LSSKAEDRRsifgEAAGVLKykTRKEKAGNKLFETQDNLNRVGDILHELEGQVEPLKIQASIAKDYLEKKKElehveipl 229
Cdd:PRK02224 354 LEERAEELR----EEAAELE--SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 230 tayDIEELHGKWSTLKEKVQMAkEEELAESSAI---------------SPKEAKIEGTRDKIQALDESVDELQQVL---- 290
Cdd:PRK02224 420 ---ERDELREREAELEATLRTA-RERVEEAEALleagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVeeve 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 291 --LVTSEELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQKETVLTRRAFEAEAVFETLQAEVKQLRAQVKEKQHALS 368
Cdd:PRK02224 496 erLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 369 LHNEN---VEEKIEQLKsDYFELLNSQASIRNELQLLDDQMSQsavtLQRLADNNEKHLQERHDisaRKAACKTEF--AR 443
Cdd:PRK02224 576 ELNSKlaeLKERIESLE-RIRTLLAAIADAEDEIERLREKREA----LAELNDERRERLAEKRE---RKRELEAEFdeAR 647
|
...
gi 1237015 444 FEQ 446
Cdd:PRK02224 648 IEE 650
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
262-446 |
8.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 262 ISPKEAK---IEGTRD--KIQALDESVDELQQvllvtseELEKLEGRkevlkdrkknaVQNQEQLEEAIVQFQQK----- 331
Cdd:PRK04863 489 VSRSEAWdvaRELLRRlrEQRHLAEQLQQLRM-------RLSELEQR-----------LRQQQRAERLLAEFCKRlgknl 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 332 --ETVLTRRAFEAEAVFETLQAEVKQLRAQVKEKQHALslhnENVEEKIEQLKSDYFELLNSQASI-RNELQLLDDQMSQ 408
Cdd:PRK04863 551 ddEDELEQLQEELEARLESLSESVSEARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALaRLREQSGEEFEDS 626
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1237015 409 SAVT--LQRLADNNEKHLQERHDISARKAACKTEFARFEQ 446
Cdd:PRK04863 627 QDVTeyMQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
265-450 |
8.66e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 265 KEAKIEGTRDkiqaLDESVDELQqvllvtsEELEKLEGRKEVLKDRKKNAVQNQEQLEeaivQFQQKETVLTRRAFEAEA 344
Cdd:TIGR01612 1471 KIKKDNATND----HDFNINELK-------EHIDKSKGCKDEADKNAKAIEKNKELFE----QYKKDVTELLNKYSALAI 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 345 V--FETLQAEVKQLRAQVKEKQHALSLHNENVEEKIEQLKSDYFELLNSQASirnelqllDDQMSQSAVTLQRLADNNEK 422
Cdd:TIGR01612 1536 KnkFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAK--------NDKSNKAAIDIQLSLENFEN 1607
|
170 180
....*....|....*....|....*...
gi 1237015 423 HLQERHDISARKAACKTEFARFEQEIHS 450
Cdd:TIGR01612 1608 KFLKISDIKKKINDCLKETESIEKKISS 1635
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1086-1160 |
9.43e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.47 E-value: 9.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237015 1086 QNLNLLSGGERALTAIA--LLfsilkvRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEAD 1160
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIAraLL------RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
680-877 |
9.52e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 680 ELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEpqfAEKNINTHLELYDQEKS 759
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---AEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 760 ALSESDEERKV---------------RKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKK 824
Cdd:COG3883 94 ALYRSGGSVSYldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1237015 825 EQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAA 877
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-68 |
9.59e-04 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 42.85 E-value: 9.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 1 MFLKRLDVIGFKSFAERiSVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGQsarsLRGGKMEDIIFAG 68
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPP-TLAFPPGVTAVVGENAAGKTNLLEAIYLALTGE----LPNGRLADLVRFG 63
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
650-1034 |
1.07e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 650 TLEGDVVNPGGSMTGGSVKKKNNSLLGRTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVK 729
Cdd:COG5185 172 LNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 730 QQDVKgqlyepQFAEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKEs 809
Cdd:COG5185 252 SDKLE------KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAE- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 810 lsNELTELKIAAAKKEQACKGEednlarLKKELTETELALKEAKEDLSFLTSEMSSSTSgEEKLEEAakhKLNDKTKTIE 889
Cdd:COG5185 325 --QELEESKRETETGIQNLTAE------IEQGQESLTENLEAIKEEIENIVGEVELSKS-SEELDSF---KDTIESTKES 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 890 LIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPE 969
Cdd:COG5185 393 LDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEI 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237015 970 EARKRVKLIKLAIEELGTVNlgSIDEFERVNERYKFLSEQKedLTEAKNTLFQVIEEMDEEMTKR 1034
Cdd:COG5185 473 NRSVRSKKEDLNEELTQIES--RVSTLKATLEKLRAKLERQ--LEGVRSKLDQVAESLKDFMRAR 533
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
767-925 |
1.16e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 42.03 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 767 ERKVRKRK-LEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDnlaRLKKELTET 845
Cdd:pfam17078 62 NRKERRLKdLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKD---HYQQEINTL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 846 ELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRI-----------KLQHGLDTYeRELKE 914
Cdd:pfam17078 139 QESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNKLltkldslaqllDLPSWLNLY-PESRN 217
|
170
....*....|.
gi 1237015 915 MKRLYKQKTTL 925
Cdd:pfam17078 218 KILEYAEKMEL 228
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
668-984 |
1.17e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 668 KKKNNSLLGRTRElgdvTKRLAEMEEKTS-LLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKN 746
Cdd:PTZ00121 1328 KKKADAAKKKAEE----AKKAAEAAKAEAeAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 747 INTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKEslSNELTELKIAAAKKEQ 826
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--AEEAKKADEAKKKAEE 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 827 ACKGEE--DNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAK----HKLNDKTKTIEliaLRRDQRIK 900
Cdd:PTZ00121 1482 AKKADEakKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADE---LKKAEELK 1558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 901 LQHGLDTYE--RELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLI 978
Cdd:PTZ00121 1559 KAEEKKKAEeaKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
....*.
gi 1237015 979 KLAIEE 984
Cdd:PTZ00121 1639 KKKEAE 1644
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
673-1034 |
1.22e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 673 SLLGRTRELGDVTKRLAEMEEKTSLLEQEVQTLkhsIQDMEKKLADLRETGEGLRVKQQDVKGQLyepqfaeKNINTHLE 752
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAEELKGKEQELIFL---LQAREKEIHDLEIQLTAIKTSEEHYLKEV-------EDLKTELE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 753 LYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELK--IAAAKKEQACKG 830
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRdeLESVREEFIQKG 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 831 E---------EDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEE---AAKHKLNDKTKTIELIALRRDQ- 897
Cdd:pfam05483 562 DevkckldksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkALKKKGSAENKQLNAYEIKVNKl 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 898 -------RIKLQHGLDTYERELkEMKRLYK-------QKTTLLKDEEVKLGRmevELDNLLQYLREEYSLSFEgaKEKYQ 963
Cdd:pfam05483 642 elelasaKQKFEEIIDNYQKEI-EDKKISEeklleevEKAKAIADEAVKLQK---EIDKRCQHKIAEMVALME--KHKHQ 715
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237015 964 LETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKR 1034
Cdd:pfam05483 716 YDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1024-1151 |
1.25e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.61 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 1024 IEEMDEEMTKRFNDTFVQIRSHFDQVFRSLFGGGRAELRLTDPNdllhsgveiiaqppGKKLQNLNLLSGGerALTAIAL 1103
Cdd:COG4637 206 LRETHPERFERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKG--------------LDRPFPARELSDG--TLRFLAL 269
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1237015 1104 LFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITH 1151
Cdd:COG4637 270 LAALLSPRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
679-1032 |
1.35e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLYEpqFAEKNINTHLELyDQEK 758
Cdd:pfam01576 370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE--LAEKLSKLQSEL-ESVS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 759 SALSESDEerkvRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLsneltelkiaaakkeqackgeEDNLARL 838
Cdd:pfam01576 447 SLLNEAEG----KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQL---------------------EDERNSL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 839 KKELTETELALKEAKEDLSFLTSEMSSStsgeekleeaaKHKLNDKTKTIELIalrRDQRIKLQHGLDTYERELKE---- 914
Cdd:pfam01576 502 QEQLEEEEEAKRNVERQLSTLQAQLSDM-----------KKKLEEDAGTLEAL---EEGKKRLQRELEALTQQLEEkaaa 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 915 MKRLYKQKTTL---LKDEEVKLGRMEVELDNLL-------QYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEE 984
Cdd:pfam01576 568 YDKLEKTKNRLqqeLDDLLVDLDHQRQLVSNLEkkqkkfdQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEE 647
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1237015 985 LgtvnLGSIDEFERVNERYKFLSEQ----KED-------LTEAKNTLFQVIEEMDEEMT 1032
Cdd:pfam01576 648 A----LEAKEELERTNKQLRAEMEDlvssKDDvgknvheLERSKRALEQQVEEMKTQLE 702
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
701-943 |
1.43e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 701 EVQTLKHsiqdMEKKLADLretgegLRVKQQDVKGQLYEPQFAEKNINTHLELYDQeksaLSESDEERKVRKRKLEEELS 780
Cdd:PHA02562 161 DISVLSE----MDKLNKDK------IRELNQQIQTLDMKIDHIQQQIKTYNKNIEE----QRKKNGENIARKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 781 avsEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKeqacKGEEDNLARLKKELTETELAlKEAKEDLSflt 860
Cdd:PHA02562 227 ---EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKI----KSKIEQFQKVIKMYEKGGVC-PTCTQQIS--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 861 semssstSGEEKLEEAaKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVEL 940
Cdd:PHA02562 296 -------EGPDRITKI-KDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI 367
|
...
gi 1237015 941 DNL 943
Cdd:PHA02562 368 EEL 370
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1091-1163 |
1.48e-03 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 42.83 E-value: 1.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237015 1091 LSGGERALTAIA--LLfsilkvRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLY 1163
Cdd:COG4987 472 LSGGERRRLALAraLL------RDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
763-985 |
1.70e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 763 ESDEERKVRKRKLEEELSAVSEKMKQLEEdidrLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKEL 842
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADE----AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 843 TETELALKEAKEDlsflTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELiaLRRDQRIKLQHGLDTYERELKEMKRLYKQK 922
Cdd:PTZ00121 1367 EAAEKKKEEAKKK----ADAAKKKAEEKKKADEAKKKAEEDKKKADEL--KKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237015 923 TTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEgAKEKYQLETDPEEARKRVKLIKLAIEEL 985
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE-AKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1089-1160 |
1.85e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 42.26 E-value: 1.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237015 1089 NLLSGGERALTAIALlfSILKVRPVpfCVLDEVEAALDEANVFRFAQYLKKYSSD-TQFIvITHRKGTMEEAD 1160
Cdd:PRK13657 470 RQLSGGERQRLAIAR--ALLKDPPI--LILDEATSALDVETEAKVKAALDELMKGrTTFI-IAHRLSTVRNAD 537
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
316-981 |
1.86e-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: 42.52 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 316 QNQEQLEEAIVQFQQketvLTRRAFEAEAVFETLQAEVKQLRAQVKEKqhaLSLHNENVEEKIEQLKSDYFELLNSQASI 395
Cdd:pfam12128 248 QEFNTLESAELRLSH----LHFGYKSDETLIASRQEERQETSAELNQL---LRTLDDQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 396 RNELQLLDDQMsqsavtLQRLADNNEKHLQERhdisARKAACKTEFARFEQEIHSQVGAYRDMQTKYEQKKRQY-EKNES 474
Cdd:pfam12128 321 RSELEALEDQH------GAFLDADIETAAADQ----EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 475 PLYQAYQYVQQARSKKDMLDTMQgdfSGFYQGVKEVLKAKdrlggIRGAVLELISTEQKYETAIEIAVGASPQHVVTDDE 554
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVA---EDDLQALESELREQ-----LEAGKLEFNEEEYRLKSRLGELKLRLNQATATPEL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 555 QSARKAIQYL---KQNSFGRATFLPLSVIRDRQLSKPLRGNSGPAFIISFGVASELVT--------FDPAYRSVIQNLLG 623
Cdd:pfam12128 463 LLQLENFDERierAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSaldelelqLFPQAGTLLHFLRK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 624 NRSDYRglKGGANELAKLLGHRYRIVTlEGDVVNPGGSMTGGSVKKKNNSLlgrtrelgDVTKRLA---EMEEKTSLLEQ 700
Cdd:pfam12128 543 EAPDWE--QSIGKVISPELLHRTDLDP-EVWDGSVGGELNLYGVKLDLKRI--------DVPEWAAseeELRERLDKAEE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 701 EVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLyepqfaEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELS 780
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANGELEKASREETFARTAL------KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 781 AVSEKMKQLEEDIDRLTKQKQTQSStkeslsneltELKIAAAKKEQACKGEEDN-LARLKKELTETELAlkeAKEDLSFL 859
Cdd:pfam12128 686 SLEAQLKQLDKKHQAWLEEQKEQKR----------EARTEKQAYWQVVEGALDAqLALLKAAIAARRSG---AKAELKAL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 860 TSEMSSSTSG---EEKLEEAAKHKLNDKTKTIELIALRRDQ----RIKLQHGLDTYERELKEMKRLYKQKTTLLKDEevk 932
Cdd:pfam12128 753 ETWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEvlryFDWYQETWLQRRPRLATQLSNIERAISELQQQ--- 829
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1237015 933 LGRMEVELDNLLQYLREEyslsfEGAKEKYQLETDPEEARKRVKLIKLA 981
Cdd:pfam12128 830 LARLIADTKLRRAKLEME-----RKASEKQQVRLSENLRGLRCEMSKLA 873
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
29-94 |
1.86e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 41.04 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237015 29 VVGPNGSGKSNITDAIRWVLGGQSARSLRGGKMEDIIFAGSDSRKrlnlAEVTL-------TLDNDDHFLPID 94
Cdd:cd03277 28 IIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGT----IEIELygnpgniQVDNLCQFLPQD 96
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
679-836 |
2.02e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKQQDVKGQLyepqfaeKNINTHLELydqek 758
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-------GNVRNNKEY----- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 759 SALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLA 836
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
709-1031 |
2.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 709 IQDMEKKLADLRETGEGLRVKQQDVKG---QLYEPQFAEKNINTHLELYDQEKSALsesdeERKVRKRKLEEELSAVSEK 785
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 786 MKQLEEDIDRLtkqkQTQSSTKESLSNELTELKIA-AAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMS 864
Cdd:COG4717 148 LEELEERLEEL----RELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 865 SSTSGEEKLE-EAAKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELKE---------------MKRLYKQKTTLLKD 928
Cdd:COG4717 224 ELEEELEQLEnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 929 -EEVKLGRMEVELDNL-LQYLREEYSLS-----------FEGAKEKYQLETDPEEARKRVKLIKLAIEE---LGTVNLGS 992
Cdd:COG4717 304 aEELQALPALEELEEEeLEELLAALGLPpdlspeellelLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVED 383
|
330 340 350
....*....|....*....|....*....|....*....
gi 1237015 993 IDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEM 1031
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
283-471 |
2.20e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 283 VDELQQVLLVTSEELEKLEGRK--EVLKDRKKNAVQNQEQLEEAIVQFQQKE--TVLTRRAFEAEAVFETLQAEVKQLRA 358
Cdd:COG3206 154 ANALAEAYLEQNLELRREEARKalEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 359 QVKEKQHALslhnENVEEKIEQLKSDYFELLNSQAsIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACK 438
Cdd:COG3206 234 ELAEAEARL----AALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190
....*....|....*....|....*....|...
gi 1237015 439 TEFARFEQEIHSQVGAYRDMQTKYEQKKRQYEK 471
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
675-917 |
2.22e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 675 LGRTRELGDVTK-RLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETgEGLRVKQQDVKGQL--------YEPQFAEK 745
Cdd:pfam17380 312 VERRRKLEEAEKaRQAEMDRQAAIYAEQERMAMERERELERIRQEERKR-ELERIRQEEIAMEIsrmrelerLQMERQQK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 746 NINTHLELYDQEKSALSESDEERKVRKRKLE------EELSAVSEKMKQLEEDIDR---------LTKQKQTQSSTKESL 810
Cdd:pfam17380 391 NERVRQELEAARKVKILEEERQRKIQQQKVEmeqiraEQEEARQREVRRLEEERARemervrleeQERQQQVERLRQQEE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 811 SNELTELKIAAAKKEQAcKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGeeKLEEAAKHKLNDKTKTIEL 890
Cdd:pfam17380 471 ERKRKKLELEKEKRDRK-RAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA--IYEEERRREAEEERRKQQE 547
|
250 260
....*....|....*....|....*...
gi 1237015 891 IALRRdqRIKLQHGLDTYER-ELKEMKR 917
Cdd:pfam17380 548 MEERR--RIQEQMRKATEERsRLEAMER 573
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
679-865 |
2.35e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 679 RELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLR------------------------------- 727
Cdd:pfam15905 94 KRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKakfsedgtqkkmsslsmelmklrnkleakmk 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 728 ---VKQQDVKGQLYEpqfAEKNINTHLELYDQEKSALSESDEERKVRKRKLE------EELSAVSEKMKQLEEDIDRLTK 798
Cdd:pfam15905 174 evmAKQEGMEGKLQV---TQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEklleyiTELSCVSEQVEKYKLDIAQLEE 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237015 799 QKQTQSSTKESLSNELTElkiaaaKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSS 865
Cdd:pfam15905 251 LLKEKNDEIESLKQSLEE------KEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEE 311
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
233-426 |
2.48e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 233 DIEELHGKWSTLKEKVQMAKEEELAESSAISPKEAKIEGTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKK 312
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 313 NAVQNQEQLEEAIVQFQQKETVLTRRAFEAEAVFETLQAEVKQLRAQVKEKQHALS-LHNENVEEKIEQLKSDYFELLNS 391
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQaLSEAEAEQALDELLKEANRNAEK 198
|
170 180 190
....*....|....*....|....*....|....*
gi 1237015 392 QASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQE 426
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
667-806 |
3.15e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 667 VKKKNNSLLGRTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEgLRVKQQDVKGQLYEPQFAEKN 746
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 747 INTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSST 806
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
677-875 |
3.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 677 RTRELGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRETGEGLRVKqqdvkgqlyepqfaekninthLELYDQ 756
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE---------------------AGLDDA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 757 EKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLA 836
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 1237015 837 RLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEE 875
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
276-430 |
4.21e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 276 IQALDESVDELQQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQKETVLTRRAfeaeavfetlQAEVKQ 355
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRA----------KEKLKK 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237015 356 LRAQVKEKQHALslhnENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSavtlqRLADNNE-KHLQERHDI 430
Cdd:smart00787 216 LLQEIMIKVKKL----EELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC-----RGFTFKEiEKLKEQLKL 282
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
3-130 |
4.52e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 3 LKRLDVigfKSFA--ERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGGqsarslRGGKmeDIIFAGSDSrkrlnlAEV 80
Cdd:COG0497 2 LTELSI---RNFAliDELELEFGPGLTVLTGETGAGKSILLDALGLLLGG------RADA--SLVRHGADK------AEV 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237015 81 TLTLDND----------DHFLPIDFHEVSVTRRVYRSGESEFLINNQPC---RLKDIIDLFMD 130
Cdd:COG0497 65 EAVFDLSddpplaawleENGLDLDDGELILRREISADGRSRAFINGRPVtlsQLRELGELLVD 127
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
681-975 |
5.08e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 681 LGDVTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLadlrETGEGLRVKQQdvkgqlYEPQFAEKNINTH----LELYDQ 756
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL----DEEEAARQKLQ------LEKVTTEAKIKKLeediLLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 757 ------EKSALSE---------SDEERKVR-----KRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTE 816
Cdd:pfam01576 147 nsklskERKLLEEriseftsnlAEEEEKAKslsklKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 817 LK--IAAAKKEQACKGEE--DNLARLKKELTETELALK---EAKEDLSFLTSEMSSSTSGEEKLE----------EAAKH 879
Cdd:pfam01576 227 LQaqIAELRAQLAKKEEElqAALARLEEETAQKNNALKkirELEAQISELQEDLESERAARNKAEkqrrdlgeelEALKT 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 880 KLNDKTKTI----ELIALRRDQRIKLQHGLD----TYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEY 951
Cdd:pfam01576 307 ELEDTLDTTaaqqELRSKREQEVTELKKALEeetrSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN 386
|
330 340
....*....|....*....|....
gi 1237015 952 SLSFEGAKEKYQLETDPEEARKRV 975
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKL 410
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
209-420 |
5.23e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 209 ASIAKDYLEKKKELEHVE---IPLTAYDIEELHGKWSTLKEKvQMAKEEELAESSAIS--PK-----EAKIEGTRDKIQA 278
Cdd:PRK10929 19 AATAPDEKQITQELEQAKaakTPAQAEIVEALQSALNWLEER-KGSLERAKQYQQVIDnfPKlsaelRQQLNNERDEPRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 279 LDE--SVDEL-QQVLLVTSEELEKleGRKevlkdrkknAVQNQEQLEE---AIVQFQQKETVlTRRAF------------ 340
Cdd:PRK10929 98 VPPnmSTDALeQEILQVSSQLLEK--SRQ---------AQQEQDRAREisdSLSQLPQQQTE-ARRQLneierrlqtlgt 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 341 ----EAEAVFETLQAEVKQLRAQVKEKQHA-LSLHN--ENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAV-T 412
Cdd:PRK10929 166 pntpLAQAQLTALQAESAALKALVDELELAqLSANNrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALeS 245
|
....*...
gi 1237015 413 LQRLADNN 420
Cdd:PRK10929 246 TELLAEQS 253
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
713-1036 |
5.88e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 713 EKKLADLRETGEGLRVKQQDVKGQLYEPQFAEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSE----KMKQ 788
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmKAEE 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 789 LEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKK--EQACKGEEDNLARLKKELTETELALKEAKedlsfltsEMSSS 866
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKkaEELKKAEEENKIKAAEEAKKAEEDKKKAE--------EAKKA 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 867 TSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQHgLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQY 946
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 947 LREEYSLSFEGAKEKYQL--ETDPEEARKRVKLIKLAIEELGTvNLGSIDEFERVNERYKFLSEQKED--LTEAKNTLFQ 1022
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFD-NFANIIEGGKEGNLVINDSKEMEDsaIKEVADSKNM 1841
|
330
....*....|....
gi 1237015 1023 VIEEMDEEMTKRFN 1036
Cdd:PTZ00121 1842 QLEEADAFEKHKFN 1855
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
786-985 |
5.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 786 MKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLtsemss 865
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 866 stsgeEKLEEAAKHklndktkTIELIALRRdQRIKLQHGLDTYERELKEMKRLYKQKTTLlkdeEVKLGRMEVELDNLLQ 945
Cdd:COG4717 122 -----EKLLQLLPL-------YQELEALEA-ELAELPERLEELEERLEELRELEEELEEL----EAELAELQEELEELLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1237015 946 YLREEYSLSFEGAKEKYQ-LETDPEEARKRVKLIKLAIEEL 985
Cdd:COG4717 185 QLSLATEEELQDLAEELEeLQQRLAELEEELEEAQEELEEL 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1091-1160 |
6.24e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 40.53 E-value: 6.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237015 1091 LSGGERALTAIA--LLF--SILkvrpvpfcVLDEVEAALD---EANVFrfaQYLKKYSSDTQFIVITHRKGTMEEAD 1160
Cdd:COG1132 477 LSGGQRQRIAIAraLLKdpPIL--------ILDEATSALDtetEALIQ---EALERLMKGRTTIVIAHRLSTIRNAD 542
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
684-844 |
6.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 684 VTKRLAEMEEKTSLLEQEVQTLKHSIQDMEKKLADLRE-------TGEG---------LRVKQQDVKGQLYEPQFAEKNI 747
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknglvdlSEEAklllqqlseLESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 748 NTHLELYDQEKSALSESDEERKVRKR--KLEEELSAVSEK-------MKQLEEDIDRLTKQKQTQssTKESLSNELTELK 818
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQE--AQRILASLEAELE 323
|
170 180
....*....|....*....|....*.
gi 1237015 819 IAAAKKEQAckgeEDNLARLKKELTE 844
Cdd:COG3206 324 ALQAREASL----QAQLAQLEARLAE 345
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
761-1048 |
6.48e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 761 LSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELT----ELKIAAAKKEQACKGEEDNLA 836
Cdd:pfam15921 94 LNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvhELEAAKCLKEDMLEDSNTQIE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 837 RLKKELTETELALKEAKEDLsfLTSEMSSSTSGEEKLEEAAKHKLNDKTkTIELIALRRDQRIKLQHG-LDTYERELKEM 915
Cdd:pfam15921 174 QLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMSTMHFRSLGS-AISKILRELDTEISYLKGrIFPVEDQLEAL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 916 KRLYKQKTTLLKDE-----EVKLGRMEVELDNLLQylrEEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVnl 990
Cdd:pfam15921 251 KSESQNKIELLLQQhqdriEQLISEHEVEITGLTE---KASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLEST-- 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1237015 991 gsidefervnerykfLSEQKEDLTEAKNTLFQVIEEMDEEMTKRfNDTFVQIRSHFDQ 1048
Cdd:pfam15921 326 ---------------VSQLRSELREAKRMYEDKIEELEKQLVLA-NSELTEARTERDQ 367
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
233-385 |
7.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 233 DIEELHGKWSTLKEKVQMAKEEELAESSAISPKEAKIEGTRDKIQAL-------DESVDELQQVLLVTS----------- 294
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESfsdfldrlsal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 295 --------EELEKLEGRKEVLKDRKKNAVQNQEQLEEAIVQFQQKETVLTRRAFEAEAVFETLQAEVKQLRAQVKEKQHA 366
Cdd:COG3883 125 skiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
170
....*....|....*....
gi 1237015 367 LSLHNENVEEKIEQLKSDY 385
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAA 223
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
257-491 |
7.14e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 257 AESSAISPKEAKIEGTRDKI--QALDESVDEL-QQVLLVTSEELEKLEGRKEVLKDRKKNAVQNQEQLEEA---IVQFQQ 330
Cdd:PRK11281 29 AASNGDLPTEADVQAQLDALnkQKLLEAEDKLvQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAqaeLEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 331 KETVLTRRAFEAEAVfETLQAEVKQLRAQVKEKQHALSLHN----------ENVE-------EKIEQLKSDYFELLNSQA 393
Cdd:PRK11281 109 DNDEETRETLSTLSL-RQLESRLAQTLDQLQNAQNDLAEYNsqlvslqtqpERAQaalyansQRLQQIRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 394 SIRN--------ELQLLDDQMSQSAvtlQRLADNNEKH--LQERHDISARKAacktefARFEQEIhsqvgayRDMQTKYE 463
Cdd:PRK11281 188 ALRPsqrvllqaEQALLNAQNDLQR---KSLEGNTQLQdlLQKQRDYLTARI------QRLEHQL-------QLLQEAIN 251
|
250 260
....*....|....*....|....*...
gi 1237015 464 QKKRQyeknesplyQAYQYVQQARSKKD 491
Cdd:PRK11281 252 SKRLT---------LSEKTVQEAQSQDE 270
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
775-1033 |
7.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 775 LEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKE 854
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 855 DLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLG 934
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 935 RMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLT 1014
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250
....*....|....*....
gi 1237015 1015 EAKNTLFQVIEEMDEEMTK 1033
Cdd:COG4372 269 VEKDTEEEELEIAALELEA 287
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
266-481 |
7.32e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 266 EAKIEGTRDKIQALDESVDELQQvllvtseELEKLEGRKEVLKdRKKNAVQNQEQLEEAIVQFQQketvLTRRAFEAEAV 345
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRK-------ELEEAEAALEEFR-QKNGLVDLSEEAKLLLQQLSE----LESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 346 FETLQAEVKQLRAQVKEKQHALSLHNENVEekIEQLKSDYFELlnsQASIRNELQLLDDQmSQSAVTLQRLADNNEKHLQ 425
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPV--IQQLRAQLAEL---EAELAELSARYTPN-HPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237015 426 ER-----HDISARKAACKTEFARFEQEIHSQVGAYRDM---QTKYEQKKRQYEKNESpLYQAYQ 481
Cdd:COG3206 309 QEaqrilASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARE-LYESLL 371
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
755-1032 |
9.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 755 DQEKSALSESDEERKVRKRK-LEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELkiaaakkeqacKGEED 833
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEH-----------EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 834 NLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLND---KTKTIELIALRRDQriklqhgLDTYER 910
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglDDADAEAVEARREE-------LEDRDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237015 911 ELKEMkrlykqkttlLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGtvnl 990
Cdd:PRK02224 325 ELRDR----------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE---- 390
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1237015 991 gsiDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMT 1032
Cdd:PRK02224 391 ---EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
|
| |
