|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1178 |
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: 1194.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 2 FLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFAGSDSRKRLNLAEVT 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 82 LTLDNDDHFLP-IDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSI 160
Cdd:TIGR02168 81 LVFDNSDGLLPgADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 161 FEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGK 240
Cdd:TIGR02168 161 FEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 241 WSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQ 320
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 321 LEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKE---KQQALSLHNENVEEKIEQLKSDYFELLNSQASIRN 397
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 398 ELQLLDDQMSQSAVTLQRLADNNEKHLQERHdiSARKAACETEFARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNESALY 477
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 478 QAYQYVQQARSKKDMLETMQGDFSGFYQGVKEVLKAKERLGGIRGAVLELISTEQKYETAIEIALGASAQHVVTDDEQSA 557
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 558 RKAIQYLKQNSFGRATFLPLSVIRDRQLQSRDAETAARHSSFLGVASELVTFDPAYRSVIQNLLGTVLITEDLKGANELA 637
Cdd:TIGR02168 559 KKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 638 KLLGHRYRIVTLEGDVVNPGGSMTGGAVKKkNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADL 717
Cdd:TIGR02168 639 KKLRPGYRIVTLDGDLVRPGGVITGGSAKT-NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 718 RETGEGLRlkqQDVKGQLYELQVAEKNINTHLELYDQEKSALSESDEERKVRKRKLEE---ELSAVSEKMKQLEEDIDRL 794
Cdd:TIGR02168 718 RKELEELS---RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQL 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 795 TKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEA 874
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 875 AKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFE 954
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 955 GAKEKYQ-LETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRF 1033
Cdd:TIGR02168 955 EAEALENkIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1034 NDTFVQIRSHFDQVFRSLFGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPF 1113
Cdd:TIGR02168 1035 KDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPF 1114
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162902455 1114 CVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSKVISVKL 1178
Cdd:TIGR02168 1115 CILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1186 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 876.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFAGSDSRKRLNLAEV 80
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 81 TLTLDNDDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSI 160
Cdd:COG1196 81 SLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 161 FEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGK 240
Cdd:COG1196 161 IEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 241 WSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQ 320
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 321 LEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQ 400
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 401 LLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEIHSQVGAYRDMQT---KYEQKKRQYEKNESALY 477
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAlleLLAELLEEAALLEAALA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 478 QAYQYVQQARSKKDMLETMQGDFSGFYQGVKEvLKAKERLGGIRGAVLELISTEQKYETAIEIALGASAQHVVTDDEQSA 557
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 558 RKAIQYLKQNSFGRATFLPLSVIRDRQLQSRDAETAARHSSFLGVASELVTFDPAYRSVIQNLLGTVLITEDLKGANELA 637
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 638 KLLGHRYRIVTLEGDVVNPGGSMTGGAVKKKNnsllgrsreledvtkrlaemeektalleqevktlkhsiqdmekkladl 717
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELL------------------------------------------------ 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 718 retgeglrlkqqdvkgqlyelqvaekninthlelydqeksalsesdEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQ 797
Cdd:COG1196 672 ----------------------------------------------AALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 798 KQTQSSTKESLSNELTElkiaaakkeqackgeednlarlkkeltetelalkeakedlsfltsemssstsgeekleeaakh 877
Cdd:COG1196 706 ERELAEAEEERLEEELE--------------------------------------------------------------- 722
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 878 klndktktielialrrdqriklqhgldtyerelkemkrlykqkttllkdEEVKLGRMEVELDNLLQYLREEYSLSFEGAK 957
Cdd:COG1196 723 -------------------------------------------------EEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 958 EKYQLETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRFNDTF 1037
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETF 833
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1038 VQIRSHFDQVFRSLFGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLD 1117
Cdd:COG1196 834 DAVNENFQELFPRLFGGGEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLD 913
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162902455 1118 EVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSKVISVKLEETKEFVQ 1186
Cdd:COG1196 914 EVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEELAE 982
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-1172 |
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: 662.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 2 FLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFagSDSRKRLNLAEVT 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 82 LTLDNDDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSIF 161
Cdd:pfam02463 79 ITFDNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 162 EEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGKW 241
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 242 STLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQL 321
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 322 EEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQL 401
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 402 LDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNESALYQAYQ 481
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 482 YVQQARSKKDMLETMQGDFSGFYQGVKEVLKAKERLGGIRGAVLELISTEQKYETAIEIALGASAQHVVTDDEQSARKAI 561
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 562 QYLKQNSFGRATFLPLSVIRDRQLQSRDAETAARHSSFLGVASELVtfdpayrsVIQNLLGTVLITEDLKGANELAKLLG 641
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN--------LAQLDKATLEADEDDKRAKVVEGILK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 642 HRYRIVTLEGDVVNPGGSMTGGAVKKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETG 721
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 722 EGLRLKQQDVKGQLYELQVAEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQ 801
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 802 SSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLND 881
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 882 KTKTIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQ 961
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 962 LETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRFNDTFVQIR 1041
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1042 SHFDQVFRSLFGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEA 1121
Cdd:pfam02463 1031 KGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDA 1110
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 1122 ALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSK 1172
Cdd:pfam02463 1111 ALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1178 |
2.61e-147 |
|
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: 473.79 E-value: 2.61e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 2 FLKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFAGSDSRKrLNLAEVT 81
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQS-GNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 82 LTLDNDDHFLPIDFhEVSVTRRVYRSG-ESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSI 160
Cdd:TIGR02169 80 VTFKNDDGKFPDEL-EVVRRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 161 FEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGK 240
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 241 WSTLKEKVQmAKEEELAESSA-ISAKEAKIEDTRDKIQALDESVDEL-QQVLLVTSEELEKLEGRKEVLKERKKNAVQNQ 318
Cdd:TIGR02169 239 KEAIERQLA-SLEEELEKLTEeISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 319 EQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALslhnENVEEKIEQLKSDYFELLNSQASIRNE 398
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEFAETRDELKDYREK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 399 LQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACET--------------EFARIEQEIHSQVGAYRDMQTKYEQ 464
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkineleeekedkalEIKKQEWKLEQLAADLSKYEQELYD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 465 KKRQYEKNESALYQAYQYVQQARSKKDMLETMQGDFSgfyqGVKEVLKAkeRLGGIRGAVLELISTEQKYETAIEIALGA 544
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR----AVEEVLKA--SIQGVHGTVAQLGSVGERYATAIEVAAGN 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 545 SAQHVVTDDEQSARKAIQYLKQNSFGRATFLPLSVIRDRQLQSRdaetAARHSSFLGVASELVTFDPAYRSVIQNLLGTV 624
Cdd:TIGR02169 548 RLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLS----ILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDT 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 625 LITEDLkganELAKLLGHRYRIVTLEGDVVNPGGSMTGGAVKKKNNSLLGRS---------RELEDVTKRLAEMEEKTAL 695
Cdd:TIGR02169 624 LVVEDI----EAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSepaelqrlrERLEGLKRELSSLQSELRR 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 696 LEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLELYDQEKSALSESDEERKVRKRKLEE 775
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 776 ELSAVseKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLS 855
Cdd:TIGR02169 780 ALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 856 FLTSEMssstsgEEKLEEAAKHKLNDKTKTIELIALRRDqRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRME 935
Cdd:TIGR02169 858 NLNGKK------EELEEELEELEAALRDLESRLGDLKKE-RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 936 VELDNLLQYLREEYSLSFEgakekyqlETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAK 1015
Cdd:TIGR02169 931 EELSEIEDPKGEDEEIPEE--------ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1016 NTLFQVIEEMDEEMTKRFNDTFVQIRSHFDQVFRSLfGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGERA 1095
Cdd:TIGR02169 1003 KAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKS 1081
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1096 LTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSKVIS 1175
Cdd:TIGR02169 1082 LTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQVFG 1161
|
...
gi 1162902455 1176 VKL 1178
Cdd:TIGR02169 1162 LKL 1164
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1055-1172 |
1.08e-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: 1.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1055 GRAELRLT-DPNDLLHS----G-VEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANV 1128
Cdd:cd03278 74 NFAEVTLTfDNSDGRYSiisqGdVSEIIEAPGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANV 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1162902455 1129 FRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGVTMQESGVSK 1172
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 |
7.71e-52 |
|
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: 180.74 E-value: 7.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFAGSDSRKRLNLAEVTL 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 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 ... |
518-636 |
6.11e-39 |
|
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: 140.83 E-value: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 518 GGIRGAVLELISTEQKYETAIEIALGASAQHVVTDDEQSARKAIQYLKQNSFGRATFLPLSVIRDRQL-QSRDAETAARH 596
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPaGSKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1162902455 597 SSFLGVASELVTFDPAYRSVIQNLLGTVLITEDLKGANEL 636
Cdd:smart00968 81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
519-637 |
8.91e-33 |
|
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: 123.14 E-value: 8.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 519 GIRGAVLELISTEQKYETAIEIALGASAQHVVTDDEQSARKAIQYLKQNSFGRATFLPLSVIRDRQLQSrdaetAARHSS 598
Cdd:pfam06470 3 GVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRP-----GADLKG 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1162902455 599 FLGVASELVTFDPAYRSVIQNLLGTVLITEDLKGANELA 637
Cdd:pfam06470 78 GAGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1072-1178 |
1.11e-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: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1072 VEIIAQ--PPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSS-DTQFIVIT 1148
Cdd:cd03275 137 VESIASknPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVIS 216
|
90 100 110
....*....|....*....|....*....|.
gi 1162902455 1149 HRKGTMEEADVLYGVTM-QESGVSKVISVKL 1178
Cdd:cd03275 217 LKEEFFSKADALVGVYRdQECNSSKVLTLDL 247
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1088-1172 |
1.49e-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: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1088 LLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYS-SDTQFIVITHRKGTMEEADVLYGVTMQ 1166
Cdd:cd03239 94 ILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAkHTSQFIVITLKKEMFENADKLIGVLFV 173
|
....*.
gi 1162902455 1167 EsGVSK 1172
Cdd:cd03239 174 H-GVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-158 |
1.08e-20 |
|
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: 92.64 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSArSLRGGKMEDIIFAGSDSRKRLNLAEVTL 82
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSS-HLRSKNLKDLIYRARVGKPDSNSAYVTA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162902455 83 TLDNDDhflpidfHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEA--FsIISQGKVEEILSSKAEDRR 158
Cdd:cd03275 80 VYEDDD-------GEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKArnF-LVFQGDVESIASKNPPGKR 149
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1067-1163 |
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 1162902455 1067 LLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIV 1146
Cdd:cd03274 106 ILQGEVEQIAQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIV 185
|
90
....*....|....*..
gi 1162902455 1147 ITHRKGTMEEADVLYGV 1163
Cdd:cd03274 186 ISLRNNMFELADRLVGI 202
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-151 |
1.18e-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: 89.66 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFAERISV-DFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFA-GSDSRKRlnlA 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKrGQAGITK---A 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162902455 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 ... |
1089-1172 |
1.01e-17 |
|
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: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1089 LSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYS-SDTQFIVITHRKGTMEEADVLYGVTMQE 1167
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIKKVI 157
|
....*
gi 1162902455 1168 SGVSK 1172
Cdd:cd03227 158 TGVYK 162
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1084-1173 |
2.26e-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: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1084 QNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGV 1163
Cdd:cd03273 162 ESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRT 241
|
90
....*....|
gi 1162902455 1164 TMQEsGVSKV 1173
Cdd:cd03273 242 RFVD-GTSTV 250
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1084-1164 |
5.23e-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: 78.84 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1084 QNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLYGV 1163
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
.
gi 1162902455 1164 T 1164
Cdd:cd03272 234 K 234
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-160 |
2.11e-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: 77.30 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVIGFKSFAERISVD-FVKGVTAVVGPNGSGKSNITDAIRWVLGEQSArSLRGGKMEDIIFAGSDSrkRLNLAEVT 81
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEpFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYT-HLREEQRQALLHEGSGP--SVMSAYVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 82 LTLDNDDHFLPIDFHEVSVtRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKE-AFSIISQGKVEEILSSKAEDRRSI 160
Cdd:cd03272 78 IIFDNSDNRFPIDKEEVRL-RRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSnPYYIVPQGKINSLTNMKQDEQQEM 156
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-200 |
8.13e-15 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 74.66 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARslRGGKMEDIIFAGSDSrkrlnlAEVTL 82
Cdd:COG0419 2 LLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINVGSEE------ASVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 83 TLDNDDhflpidfHEVSVTRRvyrsgeseflinnqpcrlkdiidlfmdsglgkeafsiisQGKVEEILSSKAEDRRSIFE 162
Cdd:COG0419 74 EFEHGG-------KRYRIERR---------------------------------------QGEFAEFLEAKPSERKEALK 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1162902455 163 EAAGVLKY-------KTRKKKAENKLFETQDNLNRVEDILHELEG 200
Cdd:COG0419 108 RLLGLEIYeelkerlKELEEALESALEELAELQKLKQEILAQLSG 152
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-92 |
1.71e-14 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 72.73 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDiifAGSDSRKRLNLAEVTL 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFL---AGGGVKAGINSASVEI 77
|
90
....*....|
gi 1162902455 83 TLDNDDHFLP 92
Cdd:cd03239 78 TFDKSYFLVL 87
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-88 |
2.94e-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: 69.94 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVIGFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIRWVL-GEQSARSLRGGKMEDIIFAGSdsrkrlNLAEVT 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGE------VRAQVK 74
|
....*..
gi 1162902455 82 LTLDNDD 88
Cdd:cd03240 75 LAFENAN 81
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
271-854 |
7.35e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 271 DTRDKIQALDESVDELQQvllvTSEELEKLEGRKEVLKErkknAVQNQEQLEEAIVQFQQKETVL--------KEELSKQ 342
Cdd:COG4913 222 DTFEAADALVEHFDDLER----AHEALEDAREQIELLEP----IRELAERYAAARERLAELEYLRaalrlwfaQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 343 EAVFETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSDYFELLnsqASIRNELQLLDDQMSQsavtLQRLADNNEK 422
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL---EQLEREIERLERELEE----RERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 423 HLQerhDISARKAACETEFARIEQEIHSQVGAYRDMQTKYEQkkrQYEKNESALYQAYQYVQQARSKKDMLETMQGDFSG 502
Cdd:COG4913 367 LLA---ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 503 FYQGVKEVLKakERLGGIRGAV------LELISTEQKYETAIEIALGASAQHVVTDDEQSARkAIQYLKQNSFGRAtflp 576
Cdd:COG4913 441 RLLALRDALA--EALGLDEAELpfvgelIEVRPEEERWRGAIERVLGGFALTLLVPPEHYAA-ALRWVNRLHLRGR---- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 577 lsvIRDRQLQSRDAETAARHSSFLGVASELVTFDPAYRSVIQNLLGTvliTEDLKGANELAKLLGHRYRIvTLEGDVvnp 656
Cdd:COG4913 514 ---LVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGR---RFDYVCVDSPEELRRHPRAI-TRAGQV--- 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 657 ggSMTGGAVKKKNNSLLGRSREL-EDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQ------ 729
Cdd:COG4913 584 --KGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdei 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 730 DVKGQLYELQVAEKNInTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLS 809
Cdd:COG4913 662 DVASAEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1162902455 810 NELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDL 854
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-128 |
1.21e-11 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 67.49 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 2 FLKRLDVIGFKSFAErISVDFVKGVTAVVGPNGSGKSNITDAIrWVLGeqSARSLRGGKMEDIIFAGSDSrkrlnlAEVT 81
Cdd:COG1195 1 RLKRLSLTNFRNYES-LELEFSPGINVLVGPNGQGKTNLLEAI-YLLA--TGRSFRTARDAELIRFGADG------FRVR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1162902455 82 LTLDNDDHflpidFHEVSVTRRvyRSGESEFLINNQPC-RLKDIIDLF 128
Cdd:COG1195 71 AEVERDGR-----EVRLGLGLS--RGGKKRVRINGKPVrRLSDLAGLL 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-448 |
1.59e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFAErISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSlrgGKMEDIIFAGSDSrkrlnlAEV 80
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALD---DTLDDVITIGAEE------AEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 81 TLTLDNDDHflpiDFHevsVTRRVYRSGESeflINNQPCRLKD---IID------------LFMDSglgkEAF---SIIS 142
Cdd:PRK02224 71 ELWFEHAGG----EYH---IERRVRLSGDR---ATTAKCVLETpegTIDgardvreevtelLRMDA----EAFvncAYVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 143 QGKVEEILSSKAEDRRSIFEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKiqasiAKDYLEKKKEL 222
Cdd:PRK02224 137 QGEVNKLINATPSDRQDMIDDLLQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE-----EKDLHERLNGL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 223 EHvEIALTAYDIEELHGKWSTLKEKVQMAKE--EELAES-SAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEK 299
Cdd:PRK02224 212 ES-ELAELDEEIERYEEQREQARETRDEADEvlEEHEERrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 300 LEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKE-KQQALSLHNE--NVEE 376
Cdd:PRK02224 291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDlEERAEELREEaaELES 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162902455 377 KIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEI 448
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-57 |
3.89e-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: 66.18 E-value: 3.89e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 1 MFLKRLDVIGFKSFaERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLR 57
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFD 56
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
267-925 |
9.04e-11 |
|
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: 66.53 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 267 AKIEDTRDKIQALDEsvdELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAVF 346
Cdd:TIGR00618 187 AKKKSLHGKAELLTL---RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 347 EtLQAEVKQLRAQVKE------------KQQALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAVTLQ 414
Cdd:TIGR00618 264 Q-LRARIEELRAQEAVleetqerinrarKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 415 RLADNNEKHLQERHDisarkaACETEFARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNESALYQAYQYVQQARSKKDMLE 494
Cdd:TIGR00618 343 QRRLLQTLHSQEIHI------RDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 495 TMQGDFsgfyQGVKEVLKAKERLGGIRGAVLELISTEQKYETAIEIALGASAQHVVTDDEQSARKAIQYLKQNSfgRATF 574
Cdd:TIGR00618 417 SAFRDL----QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET--RKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 575 LPLSVIRDRQLQSRDAETAARHssfLGVASELVTFDPAYRSVIQNLLGTV--LITEDLKGANELAKLLGHRYRIVTLEGD 652
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIH---PNPARQDIDNPGPLTRRMQRGEQTYaqLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 653 VVNPGGSMTG--GAVKKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQD 730
Cdd:TIGR00618 568 IQQSFSILTQcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 731 VKGQLYELQVAEKNINTHLELYDQEKSALSESDEERKVRKRKLE-----EELSAVSEKMKQLEEDIDRLTKQKQTQSSTK 805
Cdd:TIGR00618 648 LHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQltywkEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 806 ESLSNELTELKIAAAK-------------KEQACKGEEDNLARLKKELTETELAlkEAKEDLSFLTSEMSSSTSG----E 868
Cdd:TIGR00618 728 SSLGSDLAAREDALNQslkelmhqartvlKARTEAHFNNNEEVTAALQTGAELS--HLAAEIQFFNRLREEDTHLlktlE 805
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 869 EKLEEAAKHKLNDKTKTIELIALRR---DQRIKLQHG-LDTYERELKEMKRLYKQKTTLLK 925
Cdd:TIGR00618 806 AEIGQEIPSDEDILNLQCETLVQEEeqfLSRLEEKSAtLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-84 |
1.25e-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: 62.31 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFAERISVD-FVKGVTAVVGPNGSGKSNITDAIRWVLGEQsARSLRGGKMEDIIFAgSDSRKRLNLAE 79
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGpFHKSFSAIVGPNGSGKSNVIDSMLFVFGFR-ASKMRQKKLSDLIHN-SAGHPNLDSCS 78
|
....*
gi 1162902455 80 VTLTL 84
Cdd:cd03274 79 VEVHF 83
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-1178 |
2.44e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 675 RSRELEDVTKRLAEMEEKTAL---LEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQD----------VKGQLYELQVA 741
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleekeerleeLKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 742 EKNINTHLELYDQEKSALSESDEERKVRK----RKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKI 817
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 818 AAAK------------KEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSST-------------SGEEKLE 872
Cdd:PRK03918 434 AKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaeqlkELEEKLK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 873 EAAKHKLNDKTKTIELIalrRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKdeevKLGRMEVELDNLLQYLREEYSLS 952
Cdd:PRK03918 514 KYNLEELEKKAEEYEKL---KEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFES 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 953 FEGAKEKYQ----------------------------LETDPEEARKRVKLIKLAIEELGT-----VNLGSIDEFERVNE 999
Cdd:PRK03918 587 VEELEERLKelepfyneylelkdaekelereekelkkLEEELDKAFEELAETEKRLEELRKeleelEKKYSEEEYEELRE 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1000 RYKFLSEQ-----------KEDLTEAKNTLFQVIEEMDEEMTKRFNDTFVQIRSHFDQVFRSLFGGGRAELRL------- 1061
Cdd:PRK03918 667 EYLELSRElaglraeleelEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKEralskvg 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1062 -------TDPNDLLHSGVEIIAQPPGKKL--------QNLNLLSGGERALTAIA--LLFSILKVRPVPFCVLDEVEAALD 1124
Cdd:PRK03918 747 eiaseifEELTEGKYSGVRVKAEENKVKLfvvyqgkeRPLTFLSGGERIALGLAfrLALSLYLAGNIPLLILDEPTPFLD 826
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1162902455 1125 EANVFRF----AQYLKKYSsdtQFIVITHRKGTMEEADVLYGVTMqESGVSKVISVKL 1178
Cdd:PRK03918 827 EERRRKLvdimERYLRKIP---QVIIVSHDEELKDAADYVIRVSL-EGGVSKVEVVSL 880
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-197 |
5.91e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 59.82 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 6 LDVIGFKSFaERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGK--MEDIIFAGSDSRKRLNLAEVTLT 83
Cdd:pfam13476 1 LTIENFRSF-RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGggFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 84 LDNDDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSIFEE 163
Cdd:pfam13476 80 NNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELEK 159
|
170 180 190
....*....|....*....|....*....|....
gi 1162902455 164 AagvLKYKTRKKKAENKLFETQDNLNRVEDILHE 197
Cdd:pfam13476 160 A---LEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-94 |
7.53e-10 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 62.10 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFaERISVDFVKGVTAVVGPNGSGKSNITDAIrWVLGeqSARSLRGGKMEDIIFAGSDSrkrlnlAEV 80
Cdd:PRK00064 1 MYLTRLSLTDFRNY-EELDLELSPGVNVLVGENGQGKTNLLEAI-YLLA--PGRSHRTARDKELIRFGAEA------AVI 70
|
90
....*....|....
gi 1162902455 81 TLTLDNDDHFLPID 94
Cdd:PRK00064 71 HGRVEKGGRELPLG 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
677-876 |
3.90e-09 |
|
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: 60.16 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 677 RELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLE------ 750
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEaqkeel 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 751 -----------LYDQEKSALSESDEERKVRKRKLEEELS-AVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIA 818
Cdd:COG4942 107 aellralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1162902455 819 AAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAK 876
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-88 |
4.34e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 59.94 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVIGFKSFAErISVDFvKGVTAVVGPNGSGKSNITDAIRWvLGE------QSARSLRGGkMEDIIFAGSDSRKRln 76
Cdd:COG4637 2 ITRIRIKNFKSLRD-LELPL-GPLTVLIGANGSGKSNLLDALRF-LSDaargglQDALARRGG-LEELLWRGPRTITE-- 75
|
90
....*....|..
gi 1162902455 77 LAEVTLTLDNDD 88
Cdd:COG4637 76 PIRLELEFAEED 87
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
10-59 |
5.98e-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: 56.21 E-value: 5.98e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 10 GFKSFAERISVDFVKG-VTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGG 59
Cdd:cd03227 6 RFPSYFVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS 56
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-1035 |
1.19e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 675 RSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKgqlyELQVAEKNINTHLELYDQ 754
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 755 EKSALSESdeerKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQtqssTKESLSNELTELKIAAAKKEQAcKGEEDNLA 834
Cdd:PRK03918 305 YLDELREI----EKRLSRLEEEINGIEERIKELEEKEERLEELKK----KLKELEKRLEELEERHELYEEA-KAKKEELE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 835 RLKKELT------------ETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAkhklnDKTKTIELIALRRDQRIKLQHG 902
Cdd:PRK03918 376 RLKKRLTgltpeklekeleELEKAKEEIEEEISKITARIGELKKEIKELKKAI-----EELKKAKGKCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 903 LDTYERELKEMKRLYKQKTTlLKDEEVKLGRMEVELDNLLQYLREEYSL--------SFEGAKEKYQLETDPEEARKRVK 974
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKE-IEEKERKLRKELRELEKVLKKESELIKLkelaeqlkELEEKLKKYNLEELEKKAEEYEK 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 975 LIKLAIEELGTVnLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRFND 1035
Cdd:PRK03918 530 LKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-872 |
1.26e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFAERIsVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFAGSDSrkrlnlAEV 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSV-VEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSG------TEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 81 TLTLDNDDHFLPIDFHEVSVTRRVYRSGESEFLINNQpcrlKDIIDlFMDSGLGKEAFS---IISQGKVEEILSSKaEDR 157
Cdd:PRK03918 74 ELKFEKNGRKYRIVRSFNRGESYLKYLDGSEVLEEGD----SSVRE-WVERLIPYHVFLnaiYIRQGEIDAILESD-ESR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 158 RSIFEEAAGVLKYKtrkkKAENKLFETQDNLNRVEDILHELegqvepLKIQASIAKDYLEKKKELEHV--EIALTAYDIE 235
Cdd:PRK03918 148 EKVVRQILGLDDYE----NAYKNLGEVIKEIKRRIERLEKF------IKRTENIEELIKEKEKELEEVlrEINEISSELP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 236 ELHGKWSTLKEKVQmaKEEELAESsaISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAv 315
Cdd:PRK03918 218 ELREELEKLEKEVK--ELEELKEE--IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 316 QNQEQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLraqvkekqqalslhnENVEEKIEQLKSDYFELLNSQASI 395
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL---------------EEKEERLEELKKKLKELEKRLEEL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 396 RNELQLLDDqmsqsavtLQRLADNNEKHLQERHDISARKAACETEFARIEQEihsqvgAYRDMQTKYEQKKRQYEKNESA 475
Cdd:PRK03918 358 EERHELYEE--------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKE------EIEEEISKITARIGELKKEIKE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 476 LYQAYQYVQQARSKKDMletmqgdfsgfyqgVKEVLKAKERLGGIRGAVLELISTEQKYETAIEIalgasaqhvvtddEQ 555
Cdd:PRK03918 424 LKKAIEELKKAKGKCPV--------------CGRELTEEHRKELLEEYTAELKRIEKELKEIEEK-------------ER 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 556 SARKAIQYLKQNSFGRATFLPLSVIRDrqlQSRDAEtaarhssflgvaSELVTFDpayrsviqnllgtvliTEDLKGANE 635
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAE---QLKELE------------EKLKKYN----------------LEELEKKAE 525
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 636 LAKLLghryrivtlegdvvnpggsmtggavKKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLA 715
Cdd:PRK03918 526 EYEKL-------------------------KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 716 DLRETGEglrlkqQDVKGQLYELqvaEKNINTHLELYDQEKSAlsesdEERKVRKRKLEEELSAVSEKMKQLEEDIDRLT 795
Cdd:PRK03918 581 ELGFESV------EELEERLKEL---EPFYNEYLELKDAEKEL-----EREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 796 KQ-----KQTQSSTKESLSNELTELkiaaakkeqackgeEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEK 870
Cdd:PRK03918 647 KEleeleKKYSEEEYEELREEYLEL--------------SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
..
gi 1162902455 871 LE 872
Cdd:PRK03918 713 LE 714
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
136-909 |
1.33e-08 |
|
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: 59.68 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 136 EAFSIISQGKVEEILSSKAEDRRSIFEEAAGVLKY-KTRKKKA---ENKLFETQDNLNRVEDILHELEGQVEPLKIQASI 211
Cdd:TIGR00606 177 EIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYlKQYKEKAceiRDQITSKEAQLESSREIVKSYENELDPLKNRLKE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 212 AKDYLEKKKELEHVEIAL--TAYDIEELHGKWSTLKEKVQMAKEEELAE-----SSAISAKEAKIEDTRDKIQALDESVD 284
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALksRKKQMEKDNSELELKMEKVFQGTDEQLNDlyhnhQRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 285 ELQQVLLVTSEELEKLEGRKEVLKE----RKKNAVQNQEQLE------------------EAIVQFQQKETVLKEELSKQ 342
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEhiraRDSLIQSLATRLEldgfergpfserqiknfhTLVIERQEDEAKTAAQLCAD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 343 EAVFETL-QAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQlLDDQMSQSAVTLQRLADNN- 420
Cdd:TIGR00606 417 LQSKERLkQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE-LDQELRKAERELSKAEKNSl 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 421 -------EKHLQ-ERHDISARKAACETEFARIEQEIHSQVGAY---RDMQTKYEQKKRQYEKNESALYQAYQYVQQARSK 489
Cdd:TIGR00606 496 tetlkkeVKSLQnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmltKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 490 KDMLETMQGDFSGFYQGV----KEVLKAKERLGGIRGAVLELISTEQKYETAIEIALGASAQHVVTDDEQsarkaiQYLK 565
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLaklnKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK------EEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 566 QNSFGRATFLPLSVIRDRQLQsrdaETAARHSSFLGVASELVTFDPAYRSVIQNLLGTVLITED-LKGANELAKLLGHRY 644
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFIT----QLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKKKEKRR 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 645 RIVTLEGDvvnpggsmtggavkkknnsllGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGL 724
Cdd:TIGR00606 726 DEMLGLAP---------------------GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 725 RLKQQDVkGQLYELQVAEKNINTHlelYDQEKSALSESDEERKVRK-RKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSS 803
Cdd:TIGR00606 785 KVCLTDV-TIMERFQMELKDVERK---IAQQAAKLQGSDLDRTVQQvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 804 TKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTS-------EMSSSTSGEEKLEEAAK 876
Cdd:TIGR00606 861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETflekdqqEKEELISSKETSNKKAQ 940
|
810 820 830
....*....|....*....|....*....|....
gi 1162902455 877 HKLND-KTKTIELIALRRDQRIKLQHGLDTYERE 909
Cdd:TIGR00606 941 DKVNDiKEKVKNIHGYMKDIENKIQDGKDDYLKQ 974
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1087-1161 |
1.99e-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: 1.99e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162902455 1087 NLLSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLY 1161
Cdd:cd03228 95 NILSGGQRQRIAIARAL----LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-385 |
2.73e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 182 FETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELhgKWSTLKEKVQmAKEEELAEssa 261
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--DVASAEREIA-ELEAELER--- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 262 isakeakIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSk 341
Cdd:COG4913 680 -------LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL- 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1162902455 342 qEAVFETLQAE--VKQLRAQVKEKQQALSLHNENVEEKIEQLKSDY 385
Cdd:COG4913 752 -EERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
256-476 |
3.78e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 256 LAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVL 335
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 336 KEELSKQEAVFEtlqaevKQLRAQVKEKQQ---ALSLHNENVEEKIEQLKsdYFELLNSQ-----ASIRNELQLLDDQMS 407
Cdd:COG4942 96 RAELEAQKEELA------ELLRALYRLGRQpplALLLSPEDFLDAVRRLQ--YLKYLAPArreqaEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162902455 408 QSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNESAL 476
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
3-446 |
4.96e-08 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 57.44 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVI-GFKSFAERISVDFVKGVTAVVGPNGSGKSNITDAIrwvlgeqsaRSLRGGKMEDIIfagsdsrkrlnLAEVT 81
Cdd:COG4694 2 ITKIKKLkNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRIL---------RSLELGDTSSEV-----------IAEFE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 82 LTLDNDDHFLPIdfhevsvtrRVYRsgeSEFlINNQPCRLKDIIDLFMDSGLGKEAFSIISQ--GKVEEILSSKAEDRRS 159
Cdd:COG4694 62 IEAGGSAPNPSV---------RVFN---RDF-VEENLRSGEEIKGIFTLGEENIELEEEIEEleKEIEDLKKELDKLEKE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 160 IFEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHG 239
Cdd:COG4694 129 LKEAKKALEKLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 240 KWST----LKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDEL-QQVLlvTSEELEKLEGR-KEVLKERKKN 313
Cdd:COG4694 209 LLSEaetlLEKSAVSSAIEELAALIQNPGNSDWVEQGLAYHKEEEDDTCPFcQQEL--AAERIEALEAYfDDEYEKLLAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 314 AVQNQEQLEEAI-----VQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEK-------------------QQALSL 369
Cdd:COG4694 287 LKDLLEELESAInalsaLLLEILRTLLPSAKEDLKAALEALNALLETLLAALEEKianpstsidlddqelldelNDLIAA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 370 HNENVEE---KIEQLKSDYFELLNS-QASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIE 445
Cdd:COG4694 367 LNALIEEhnaKIANLKAEKEEARKKlEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSSVD 446
|
.
gi 1162902455 446 Q 446
Cdd:COG4694 447 E 447
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-450 |
7.03e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFAERiSVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSarslRGGKMEDIIfagsdsRKRLNLAEV 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDS-EIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMI------KKGKNNLEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 81 TLTLDNDDHFLPIdfhEVSVTRRVYR-SGESEFLINNQPCR--LKDIIDLFMDSGLG--KEAF--SIIS-QGKVEEILSS 152
Cdd:PRK01156 70 ELEFRIGGHVYQI---RRSIERRGKGsRREAYIKKDGSIIAegFDDTTKYIEKNILGisKDVFlnSIFVgQGEMDSLISG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 153 KAEDRRSIFEEAAGVlkyktrkkkaeNKLFETQDNLNRVEDILhelegqveplkiQASIAK-DYLEKKKELEHVEIALTA 231
Cdd:PRK01156 147 DPAQRKKILDEILEI-----------NSLERNYDKLKDVIDML------------RAEISNiDYLEEKLKSSNLELENIK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 232 YDIEELHGKWS-TLKEKVQMAKEEELAESSAISAKEA--KIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLK 308
Cdd:PRK01156 204 KQIADDEKSHSiTLKEIERLSIEYNNAMDDYNNLKSAlnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHM 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 309 E-------RKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAVFETLqAEVKQLRAQVKEKQQALSLHNENVEEkIEQL 381
Cdd:PRK01156 284 KiindpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDLNNQILE-LEGY 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162902455 382 KSDYFELLNSQAS----IRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEIHS 450
Cdd:PRK01156 362 EMDYNSYLKSIESlkkkIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRA 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
663-1155 |
8.47e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 663 GAVKKKNNSLLGRSRELEDVTKRLAEMEEKTALLE---------QEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKG 733
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 734 QLYELQVAEKNINTHLELYDQEK-SALSESDEERKV---RKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSsTKESLS 809
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATeEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 810 NELTELKIAAA-------------------------------------KKEQACKGEEDNLARLKKELTETELALKEAKE 852
Cdd:COG4717 247 EARLLLLIAAAllallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 853 DLSFLTSEMSSSTSGEEKLEEAAK---HKLNDKTKTIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEV 929
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQellREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 930 KLGRMEVELDNLLQYLREeysLSFEGAKEKYQ--------LETDPEEARKRVKLIKLAIEELGTVnlgsiDEFERVNERY 1001
Cdd:COG4717 407 LEEQLEELLGELEELLEA---LDEEELEEELEeleeeleeLEEELEELREELAELEAELEQLEED-----GELAELLQEL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1002 KFLSEQKEDLTEAKNTLfQVIEEMDEEMTKRFNDTFV-QIRSHFDQVFRSLFGGGRAELRLTDpndllhsGVEIIAQPPG 1080
Cdd:COG4717 479 EELKAELRELAEEWAAL-KLALELLEEAREEYREERLpPVLERASEYFSRLTDGRYRLIRIDE-------DLSLKVDTED 550
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162902455 1081 KKLQNLNLLSGGERALTAIALLFSI---LKVRPVPFcVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTME 1155
Cdd:COG4717 551 GRTRPVEELSRGTREQLYLALRLALaelLAGEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVE 627
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-49 |
2.25e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.85 E-value: 2.25e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 1 MFLKRLDVIGFKSFaERISVDF--VKGVTAVVGPNGSGKSNITDAIRWVLG 49
Cdd:COG3950 1 MRIKSLTIENFRGF-EDLEIDFdnPPRLTVLVGENGSGKTTLLEAIALALS 50
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
665-1028 |
4.83e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 665 VKKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKN 744
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 745 INTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQ 824
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 825 ACKGEEDNLARLKKELTETELAL-------KEAKEDLSFLTSEMSSSTSGEEKLeEAAKHKLNDKTKTIElialrrDQRI 897
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELkklneekKELEEKVKDLTKKISSLKEKIEKL-ESEKKEKESKISDLE------DELN 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 898 KLQHGLDtyERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEyslsfegakekyqletdpeearkrVKLIK 977
Cdd:TIGR04523 549 KDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE------------------------KKDLI 602
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 978 LAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEE 1028
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
666-1076 |
6.23e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 666 KKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNI 745
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 746 NTHLELYDQEKSalSESDEERKVRKRKLEEELSAVSEKMKQLE----EDIDRLTKQKQTQSSTKESLSNELTELKIAAAK 821
Cdd:PTZ00121 1510 KKADEAKKAEEA--KKADEAKKAEEAKKADEAKKAEEKKKADElkkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 822 KEQACKGEEDNLARLKKELTETELALKEAKEDLSflTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQH 901
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 902 GLDTYERELKEMKRLYKQKTTLLKDEEvKLGRMEVE---LDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKL 978
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAE-ALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 979 AIEELgtvnlgSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKRFNDTFVQIRSHFDQVFRSLFGGGRAE 1058
Cdd:PTZ00121 1745 KAEEA------KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
410
....*....|....*...
gi 1162902455 1059 LRLTDPNDLLHSGVEIIA 1076
Cdd:PTZ00121 1819 LVINDSKEMEDSAIKEVA 1836
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-494 |
6.26e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 144 GKVEEILSSKAEDRRSIFEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQA----------SIAK 213
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaeavEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 214 DYLEKKKE-----LEHVEIALTAY--DIEELHGKWSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDEL 286
Cdd:PRK02224 317 EELEDRDEelrdrLEECRVAAQAHneEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 287 QQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLE-----------------------------------EAIVQFQQK 331
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEatlrtarerveeaealleagkcpecgqpvegsphvETIEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 332 ETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALSLHN--ENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQS 409
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 410 AVTLQRLADNNEKHLQERHDISARKAACETEFARIE--QEIHSQVGAYRD-MQTKYEQKKRQYEKNEsalyQAYQYVQQA 486
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDeIERLREKREALAELND----ERRERLAEK 632
|
....*...
gi 1162902455 487 RSKKDMLE 494
Cdd:PRK02224 633 RERKRELE 640
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
680-1177 |
6.79e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 680 EDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQqdvKGQLYELQVAEKNINTHLELYDQEKSAL 759
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQS---VCPVCGTTLGEEKSNHIINHYNEKKSRL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 760 SEsdeerkvRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTK----ESLSNELTELKIaaakKEQACKGEEDNLAR 835
Cdd:PRK01156 482 EE-------KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEynkiESARADLEDIKI----KINELKDKHDKYEE 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 836 LKKELTETELALKEAK-EDLSFLTSEMSS-STSGEEKLEEAAKHKLNDKTKTIELIALRRDQrikLQHGLDTYERELKEM 913
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKrTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPD---DKSYIDKSIREIENE 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 914 KRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAK---EKYQLETDPEEARKRVKLIKLAIEELGT---VN 987
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAKANRARLEStieIL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 988 LGSIDEFE-RVNERYKFLsEQKEDLTEAKNTLFQVIEEMDEemtkrfNDTFVQIRSHFDQVFRSLFGGGRAELRLtDPND 1066
Cdd:PRK01156 708 RTRINELSdRINDINETL-ESMKKIKKAIGDLKRLREAFDK------SGVPAMIRKSASQAMTSLTRKYLFEFNL-DFDD 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1067 LLHSGVEIIAQPPGKKLQNLNLLSGGERALTAIALLFSILKV--RPVPFCVLDEVEAALDE---ANVFRFAQYLKKYSSD 1141
Cdd:PRK01156 780 IDVDQDFNITVSRGGMVEGIDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPTAFLDEdrrTNLKDIIEYSLKDSSD 859
|
490 500 510
....*....|....*....|....*....|....*..
gi 1162902455 1142 T-QFIVITHRKGTMEEADVLYGVTmQESGVSKVISVK 1177
Cdd:PRK01156 860 IpQVIMISHHRELLSVADVAYEVK-KSSGSSKVIPLR 895
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1089-1157 |
1.03e-06 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 49.55 E-value: 1.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1089 LSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSD-TQFIVITHRKGTMEEA 1157
Cdd:cd00267 81 LSGGQRQRVALARAL----LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELA 146
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
231-448 |
1.31e-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: 52.07 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 231 AYDIEELHGKWSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKER 310
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 311 KKnavQNQEQLEEAIVQFQQKETVLKEEL---SKQEAVFETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSDYFE 387
Cdd:COG4942 99 LE---AQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 388 LLNSQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEI 448
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
679-1018 |
1.46e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 679 LEDVTKRLAEM----EEKTALLEQEVK---TLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLEl 751
Cdd:pfam15921 383 LADLHKREKELslekEQNKRLWDRDTGnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 752 ydqEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQA---CKG 828
Cdd:pfam15921 462 ---KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQElqhLKN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 829 EEDNLARLKKELTETELALKEAKEDLSFLTSEMssstsgEEKLEEAAKHKLNDKTKTIElialrrdqRIKLQHGLDTYER 908
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKVIEILRQQI------ENMTQLVGQHGRTAGAMQVE--------KAQLEKEINDRRL 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 909 ELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNL 988
Cdd:pfam15921 605 ELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684
|
330 340 350
....*....|....*....|....*....|.
gi 1162902455 989 GSIDEFERVNERYKF-LSEQKEDLTEAKNTL 1018
Cdd:pfam15921 685 NKSEEMETTTNKLKMqLKSAQSELEQTRNTL 715
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-241 |
1.58e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 51.24 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 26 VTAVVGPNGSGKSNITDAIRWVLGEQSA-------------------RSLRGGKMEDIIFAGSDSRKRLNLAEVTLTLDN 86
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALvigltdersrnggiggipsLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 87 DDHFLPIDFHEVSVTRRVYRSGESEFLINNQPCRLKDI-IDLFMDSGLGKEAFSIISQGKVEEILSSKAEDRRSIFEEAA 165
Cdd:pfam13304 81 EDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELrLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162902455 166 GVLKYKTRKKKAENKLFEtqdnlNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGKW 241
Cdd:pfam13304 161 LLLEDWAVLDLAADLALF-----PDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGE 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
147-404 |
1.94e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 147 EEILSSKAEDRRSIFEEAAGVLKYKTRKKKAENKLfetqdnlNRVEDiLHELEGQVEPLKIQASIAKDYLEKKKElehvE 226
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERL-------ERAED-LVEAEDRIERLEERREDLEELIAERRE----T 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 227 IALTAYDIEELHgkwstlKEKVQMAKEEELAESSAISAKEAkIEDTRDKIQALDESVDELQqvllvtsEELEKLEGRKEV 306
Cdd:PRK02224 532 IEEKRERAEELR------ERAAELEAEAEEKREAAAEAEEE-AEEAREEVAELNSKLAELK-------ERIESLERIRTL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 307 LKERKkNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLR-AQVKEKQQALSLHNENVEEKIEQLKSDY 385
Cdd:PRK02224 598 LAAIA-DAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREER 676
|
250
....*....|....*....
gi 1162902455 386 FELLNSQASIRNELQLLDD 404
Cdd:PRK02224 677 DDLQAEIGAVENELEELEE 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-475 |
2.09e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 251 AKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKER----KKNAVQNQEQLEEAIV 326
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 327 QFQQK-------ETVLKEE-----LSKQEAVfETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSDyfellnsQAS 394
Cdd:COG3883 94 ALYRSggsvsylDVLLGSEsfsdfLDRLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELEAL-------KAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 395 IRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNES 474
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
.
gi 1162902455 475 A 475
Cdd:COG3883 246 A 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
143-446 |
2.18e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 143 QGKVEEiLSSKAEDRRSIFEEAAG-VLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVeplkIQASIAKDYLEKKKE 221
Cdd:PRK04863 354 QADLEE-LEERLEEQNEVVEEADEqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRA----IQYQQAVQALERAKQ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 222 LEHVEiALTAYDIEELHgkwSTLKEKVQMAKEEELAE----SSAISAKEA---------KIEDTRDKIQALDESVDELQQ 288
Cdd:PRK04863 429 LCGLP-DLTADNAEDWL---EEFQAKEQEATEELLSLeqklSVAQAAHSQfeqayqlvrKIAGEVSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 289 V--LLVTSEELEKLEGRKEVLKERkknaVQNQEQLEEAIVQFQQK-------ETVLKEELSKQEAVFETLQAEVKQLRAQ 359
Cdd:PRK04863 505 LreQRHLAEQLQQLRMRLSELEQR----LRQQQRAERLLAEFCKRlgknlddEDELEQLQEELEARLESLSESVSEARER 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 360 VKEKQQALslhnENVEEKIEQLKSDYFELLNSQASI-RNELQLLDDQMSQSAVT--LQRLADNNEKHLQERHDISARKAA 436
Cdd:PRK04863 581 RMALRQQL----EQLQARIQRLAARAPAWLAAQDALaRLREQSGEEFEDSQDVTeyMQQLLERERELTVERDELAARKQA 656
|
330
....*....|
gi 1162902455 437 CETEFARIEQ 446
Cdd:PRK04863 657 LDEEIERLSQ 666
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
5-83 |
2.77e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 49.57 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 5 RLDVIGFKSFAERISVDFVK----GVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFAGSDSrkrlnlAEV 80
Cdd:cd03279 5 KLELKNFGPFREEQVIDFTGldnnGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDT------AEV 78
|
...
gi 1162902455 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. ... |
192-907 |
3.21e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 192 EDILHELEGQVEPLKIQASIAKDYLEKKK-ELEHVEIALTAYDiEELHGKWSTLKEkVQMAKEEELAESSAISAKEakie 270
Cdd:pfam15921 141 EDLRNQLQNTVHELEAAKCLKEDMLEDSNtQIEQLRKMMLSHE-GVLQEIRSILVD-FEEASGKKIYEHDSMSTMH---- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 271 dTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAV-----QNQEQLEEAIVQFQQKETVLKEELSKQEAV 345
Cdd:pfam15921 215 -FRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIelllqQHQDRIEQLISEHEVEITGLTEKASSARSQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 346 FETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSdyfELLNSQASIRNELQLLDDQ--MSQSAVTLQRladnnekh 423
Cdd:pfam15921 294 ANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRS---ELREAKRMYEDKIEELEKQlvLANSELTEAR-------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 424 lQERHDISARKAACETEFARIEQEIHSQvgaYRDMQTKYEQKKRQYEKN----------ESALYQAYQYVQQARSkkdML 493
Cdd:pfam15921 363 -TERDQFSQESGNLDDQLQKLLADLHKR---EKELSLEKEQNKRLWDRDtgnsitidhlRRELDDRNMEVQRLEA---LL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 494 ETMQGDFSGFYQGVKEVLKAK-ERLGGIRGAVLELISTEQKYE------TAIEIALGASAQHV--VTDDEQSARKAIQyl 564
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKnESLEKVSSLTAQLESTKEMLRkvveelTAKKMTLESSERTVsdLTASLQEKERAIE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 565 kqnsfgrATFLPLSVIRDR---QLQS-RDAETAARHSSFLGVASELVTFDPAYRSVIQNLLGTVLitedlkgaNELAKLL 640
Cdd:pfam15921 514 -------ATNAEITKLRSRvdlKLQElQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQI--------ENMTQLV 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 641 GHRYRivtlegdvvnpggsmTGGAVKKKNNSLlgrSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRET 720
Cdd:pfam15921 579 GQHGR---------------TAGAMQVEKAQL---EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNA 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 721 GEGLRLKQQDVKGQLYELQVAEKNINTHLelydqekSALSESDEERKVRKRKLEEELSAVSEKMK-QLEEDIDRLtkqKQ 799
Cdd:pfam15921 641 GSERLRAVKDIKQERDQLLNEVKTSRNEL-------NSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSEL---EQ 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 800 TQSSTKESLSNELTELKIAAAKKEQ--ACKGEEDNLAR----LKKELTETELALKEAKEDLSFLTSEMSS------STSG 867
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQitAKRGQIDALQSkiqfLEEAMTNANKEKHFLKEEKNKLSQELSTvateknKMAG 790
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 868 EEKLEEAAKHKLNDKTKTIEL--------------IALRRDQ---RIKLQHGLDTYE 907
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEValdkaslqfaecqdIIQRQEQesvRLKLQHTLDVKE 847
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
729-902 |
3.46e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 729 QDVKGQLYELQVAEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKE-- 806
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 807 SLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTI 886
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
170
....*....|....*.
gi 1162902455 887 ELIALRRDQRIKLQHG 902
Cdd:COG1579 173 PPELLALYERIRKRKN 188
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-130 |
3.47e-06 |
|
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: 49.89 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVigfKSFA--ERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQ-SARSLRGGKMEDII---FAGSdsrkrlN 76
Cdd:cd03241 1 LLELSI---KNFAliEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRaSADLIRSGAEKAVVegvFDIS------D 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 77 LAEVTLTLDNDDhflPIDFHEVSVTRRVYRSGESEFLINNQPC---RLKDIIDLFMD 130
Cdd:cd03241 72 EEEAKALLLELG---IEDDDDLIIRREISRKGRSRYFINGQSVtlkLLRELGSLLVD 125
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-87 |
5.05e-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: 49.60 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVIGFKSFAErISVDFVKGVTAVVGPNGSGKSNITDAIRWVLgeqSARSLRGGKMEDIIFAGSDSrkrlnlAEVTL 82
Cdd:cd03242 1 LKSLELRNFRNYAE-LELEFEPGVTVLVGENAQGKTNLLEAISLLA---TGKSHRTSRDKELIRWGAEE------AKISA 70
|
....*
gi 1162902455 83 TLDND 87
Cdd:cd03242 71 VLERQ 75
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
16-86 |
5.43e-06 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 48.36 E-value: 5.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 16 ERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMEDIIFAGSDSrkrlnlAEVTLTLDN 86
Cdd:cd03276 13 RHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESS------AKITVTLKN 77
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-495 |
7.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFAERiSVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEQSARSLrggkmeDIIFAGSDSRKRLNLAEv 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDR-TIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERLEKEA------DELFKPQGRKPELNLKE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 81 tltldnddhflpidFHEVSVTRRVYRSGESEFlinnqpcrlkdiidlfmdSGLGKEAFSIISQGKVEEILSSKAEDRRSI 160
Cdd:COG4717 73 --------------LKELEEELKEAEEKEEEY------------------AELQEELEELEEELEELEAELEELREELEK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 161 FEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGK 240
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 241 WSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALD--ESVDELQQVLLVTSE--ELEKLEGRKEVLKERKKNAVQ 316
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 317 NQEQLEEAIVQFQQKETVLKEELSKQEAVFETLQA-EVKQLRAQVKEKQQALSLHNENVEEKIEQLKsDYFELLNSQASI 395
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 396 RNELQLLDDQMSQSAVTLQRLADNNE------KHLQERHDISARKAACETEFARIEQEIHSQVGA--YRDMQTKYEQKKR 467
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGVEDEEelraalEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEE 439
|
490 500
....*....|....*....|....*...
gi 1162902455 468 QYEKNESALYQAYQYVQQARSKKDMLET 495
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEE 467
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1089-1150 |
9.91e-06 |
|
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: 9.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162902455 1089 LSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHR 1150
Cdd:cd03245 141 LSGGQRQAVALARAL----LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHR 198
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
696-1031 |
1.81e-05 |
|
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: 48.74 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 696 LEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQvaekninthlelydQEKSALSESDEERKVRKRKLEE 775
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS--------------EEKDALLAQRAAHEARIRELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 776 ELSAVSEKMKQLEEDIDRLTK-------------------QKQTQSSTKE--SLSNELTELKIAAAKKEQACKGEEDNLA 834
Cdd:pfam07888 137 DIKTLTQRVLERETELERMKErakkagaqrkeeeaerkqlQAKLQQTEEElrSLSKEFQELRNSLAQRDTQVLQLQDTIT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 835 RLKKELTET---ELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELK 911
Cdd:pfam07888 217 TLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 912 EMK-RLYKQKTTLLKDEE---VKLGRMEVELDNLLQYLREEYSlsfegAKEKYQLETDPEEARKRVKLIKlaieelgtvn 987
Cdd:pfam07888 297 EGRaRWAQERETLQQSAEadkDRIEKLSAELQRLEERLQEERM-----EREKLEVELGREKDCNRVQLSE---------- 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1162902455 988 lgSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTK 1031
Cdd:pfam07888 362 --SRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET 403
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-926 |
2.09e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 675 RSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKgqlyELQVAEKNINTHLELYDQ 754
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 755 EKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEdIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLA 834
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 835 RL---KKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQHGLDTYERELK 911
Cdd:PRK03918 332 ELeekEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
250
....*....|....*
gi 1162902455 912 EMKRLYKQKTTLLKD 926
Cdd:PRK03918 412 ARIGELKKEIKELKK 426
|
|
| 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 1162902455 3 LKRLDVIGFKSF-AERISVDfVKGVTAVVGPNGSGKSNITDAIRWVL 48
Cdd:pfam13555 1 LTRLQLINWGTFdGHTIPID-PRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-309 |
3.11e-05 |
|
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: 47.59 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFAErISVDFVKGVTAVVGPNGSGKSNITDAIrwvlgeqsarslrggkmeDIIFAGSDSRKrlnlaEV 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKD-TEIDLDEDLTVLIGKNNSGKSSILEAL------------------DIFLNNKEKFF-----ED 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 81 TLTLDNDDHFLPIDFHEVSVTRRVYRSGesEFLINnqpcrLKDIIDLFMDSGLGKEAFSIISQGKVEEILSSKAEdrrSI 160
Cdd:pfam13175 57 DFLVLYLKDVIKIDKEDLNIFENISFSI--DIEID-----VEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHP---KG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 161 FEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEgqvepLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGK 240
Cdd:pfam13175 127 ANKADLLLELKISDLKKYLKQFKIYIYNNYYLDEKKNVF-----DKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINE 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 241 WSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQ-ALDESVDELQQVLLVTSEEL-EKLEGRKEVLKE 309
Cdd:pfam13175 202 LEKSINYHENVLENLQIKKLLISADRNASDEDSEKINsLLGALKQRIFEEALQEELELtEKLKETQNKLKE 272
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
140-476 |
3.67e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 140 IISQGKVEEI-LSSKAEDRRSIFEEAAGVLKYKTRKKKAENKLFETQdnLNRVEDILHELEGQVEPLKIQASIAKDYLEK 218
Cdd:pfam15921 272 LISEHEVEITgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ--LSDLESTVSQLRSELREAKRMYEDKIEELEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 219 KKELEHVEIALTAYDIEELHGKWSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELE 298
Cdd:pfam15921 350 QLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 299 KLEGRKEVLK-------ERKKNAVQNQ----EQLEEAIVQFQQKETVLK---EELSKQEAVFETLQAEVKQLRAQVKEKQ 364
Cdd:pfam15921 430 RLEALLKAMKsecqgqmERQMAAIQGKneslEKVSSLTAQLESTKEMLRkvvEELTAKKMTLESSERTVSDLTASLQEKE 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 365 QALSLHNENVE----------EKIEQLKSDYFELLNSQAsirnELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARK 434
Cdd:pfam15921 510 RAIEATNAEITklrsrvdlklQELQHLKNEGDHLRNVQT----ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTA 585
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1162902455 435 AACETEFARIEQEIHS---QVGAYRDMQTKYEQKKRQYEKNESAL 476
Cdd:pfam15921 586 GAMQVEKAQLEKEINDrrlELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1089-1158 |
6.59e-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: 6.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1089 LSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEAD 1158
Cdd:TIGR02857 459 LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
266-488 |
6.68e-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: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 266 EAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAV 345
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 346 FETLQAEVKQLRA--------QVKEKQQALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAVTLQRLA 417
Cdd:COG3883 95 LYRSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 418 DNNEKHLQERHDISARKAACETEFARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNESALYQAYQYVQQARS 488
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-384 |
7.73e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 234 IEELHGKWSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQqvllvtsEELEKLEGR-KEVLKERKK 312
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-------ARIKKYEEQlGNVRNNKEY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162902455 313 NAVQNQ-EQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSD 384
Cdd:COG1579 92 EALQKEiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1089-1161 |
8.78e-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: 8.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162902455 1089 LSGGERalTAIALLFSILKvRPvPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLY 1161
Cdd:COG2274 612 LSGGQR--QRLAIARALLR-NP-RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII 680
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
253-464 |
8.96e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 253 EEELAESSA-ISAKEAKIEDTR---------DKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLE 322
Cdd:COG3206 181 EEQLPELRKeLEEAEAALEEFRqknglvdlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 323 E--AIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALslhNENVEEKIEQLKSDYFELLNSQASIRNELQ 400
Cdd:COG3206 261 QspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLA 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162902455 401 LLDDQMSQSAVTlqrladnnekhlqerhdisarkaacETEFARIEQEIHSQVGAYRDMQTKYEQ 464
Cdd:COG3206 338 QLEARLAELPEL-------------------------EAELRRLEREVEVARELYESLLQRLEE 376
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
266-481 |
9.35e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 266 EAKIEDTRDKIQALDESVDELQQvllvtseELEKLEGRKEVLKERKK--NAVQNQEQLEEAIVQFQQKETVLKEELSKQE 343
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRK-------ELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 344 AVFETLQAEVKQLRAQVKEKQQALSLhnENVEEKIEQLKSDYFELLNSQ-------ASIRNELQLLDDQMSQSAVTLQRL 416
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162902455 417 ADNNEKHLQERhdisarkaacETEFARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNEsALYQAYQ 481
Cdd:COG3206 318 LEAELEALQAR----------EASLQAQLAQLEARLAELPELEAELRRLEREVEVAR-ELYESLL 371
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
171-368 |
1.04e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 171 KTRKKKAENKLFETQDNLNRVEDILHELEGQVEplKIQASIAKdyLEKKKELEHVEIALTAYDIEELHGKWSTLKEKV-- 248
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIA--ALARRIRA--LEQELAALEAELAELEKEIAELRAELEAQKEELae 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 249 ---------QMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQE 319
Cdd:COG4942 109 llralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1162902455 320 QLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALS 368
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
226-486 |
1.08e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 226 EIALTAYDIEELHGKWSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQqvllvtseelEKLEGRKE 305
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE----------AEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 306 VLKER------------KKNAVQNQEQLEEAIVQFQQKETVLK------EELSKQEAVFETLQAEVKQLRAQVKEKQQAL 367
Cdd:COG3883 87 ELGERaralyrsggsvsYLDVLLGSESFSDFLDRLSALSKIADadadllEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 368 SLHNENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQE 447
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 1162902455 448 IHSQVGAYRDMQTKYEQKKRQYEKNESALYQAYQYVQQA 486
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGG 285
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1084-1150 |
1.15e-04 |
|
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: 1.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162902455 1084 QNLNLLSGGERALTAIAllfSILKVRPvPFCVLDEVEAALDEANVFRFAQYLKKYSSD-TQFIVITHR 1150
Cdd:cd03225 130 RSPFTLSGGQKQRVAIA---GVLAMDP-DILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHD 193
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
677-912 |
1.46e-04 |
|
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: 45.83 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 677 RELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYelqvAEKNINTHLElydQEK 756
Cdd:pfam19220 69 RELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLA----AETEQNRALE---EEN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 757 SALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLArl 836
Cdd:pfam19220 142 KALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLA-- 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 837 kKELTETELALKEAKEDLSFLTSEMSSSTSgeeKLEEA-AKHKLNDKtktieLIALRRDQRIKLQHGLDTYERELKE 912
Cdd:pfam19220 220 -AEQAERERAEAQLEEAVEAHRAERASLRM---KLEALtARAAATEQ-----LLAEARNQLRDRDEAIRAAERRLKE 287
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-48 |
1.48e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 45.42 E-value: 1.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1162902455 2 FLKRLDVIGFKSFAERISVDFVKG------VTAVVGPNGSGKSNITDAIRWVL 48
Cdd:COG1106 1 MLISFSIENFRSFKDELTLSMVASglrllrVNLIYGANASGKSNLLEALYFLR 53
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1080-1148 |
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 1162902455 1080 GKKLQNLN--LLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEAN---VFRFAQYLKKYSSDTQFIVIT 1148
Cdd:cd03277 116 GEQLQELDphHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNerkVFDMLVETACKEGTSQYFLIT 189
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1080-1148 |
1.58e-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: 1.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162902455 1080 GKKLQNLNLLSGGERALTAIALLFSILKVRPVPFCVLDEVEAALDEANvFRFAQYL----KKYSSDTQFIVIT 1148
Cdd:cd03276 101 KAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN-RKISTDLlvkeAKKQPGRQFIFIT 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1089-1151 |
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 1162902455 1089 LSGGERALTAIALLFsILKVRpvpFCVLDEVEAALDEANVFRFAQYLKKYSsdTQFIVITHRK 1151
Cdd:cd03223 92 LSGGEQQRLAFARLL-LHKPK---FVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRP 148
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1087-1158 |
1.81e-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: 1.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162902455 1087 NLLSGGERALTAIALLFsilkVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEAD 1158
Cdd:cd03248 149 SQLSGGQKQRVAIARAL----IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERAD 216
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
283-497 |
1.93e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 283 VDELQQVLLVTSEELEKLEGRK--EVLKERKKNAVQNQEQLEEAIVQFQQKE--TVLKEELSKQEAVFETLQAEVKQLRA 358
Cdd:COG3206 154 ANALAEAYLEQNLELRREEARKalEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 359 QVKEKQQALslhnENVEEKIEQLKSDYFELLNSQAsIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACE 438
Cdd:COG3206 234 ELAEAEARL----AALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162902455 439 TEFARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNESAL----YQAYQYVQQARSKKDMLETMQ 497
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpeleAELRRLEREVEVARELYESLL 371
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
935-1149 |
1.99e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.69 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 935 EVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVN-ERYKFLSEQKEDLTE 1013
Cdd:pfam13304 92 TLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLlLDEGLLLEDWAVLDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1014 AKNTLFQvieemDEEMTKRFNDTfvqirSHFDQVFRSLFGGGRAELRLTDPNDLLHSGVEIIAQPPGKKLQNLNLLSGGE 1093
Cdd:pfam13304 172 AADLALF-----PDLKELLQRLV-----RGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGT 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1162902455 1094 -RALTAIALLFSILKVRPVpfCVLDEVEAALDEANVFRFAQYLKKYSS-DTQFIVITH 1149
Cdd:pfam13304 242 kRLLALLAALLSALPKGGL--LLIDEPESGLHPKLLRRLLELLKELSRnGAQLILTTH 297
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
673-915 |
2.29e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 673 LGRSRELEDVTK-RLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETgEGLRLKQQDVKGQL--------YELQVAEK 743
Cdd:pfam17380 312 VERRRKLEEAEKaRQAEMDRQAAIYAEQERMAMERERELERIRQEERKR-ELERIRQEEIAMEIsrmrelerLQMERQQK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 744 NINTHLELYDQEKSALSESDEERKVRKRKLE------EELSAVSEKMKQLEEDIDR---------LTKQKQTQSSTKESL 808
Cdd:pfam17380 391 NERVRQELEAARKVKILEEERQRKIQQQKVEmeqiraEQEEARQREVRRLEEERARemervrleeQERQQQVERLRQQEE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 809 SNELTELKIAAAKKEQAcKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGeeKLEEAAKHKLNDKTKTIEL 888
Cdd:pfam17380 471 ERKRKKLELEKEKRDRK-RAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA--IYEEERRREAEEERRKQQE 547
|
250 260
....*....|....*....|....*...
gi 1162902455 889 IALRRdqRIKLQHGLDTYER-ELKEMKR 915
Cdd:pfam17380 548 MEERR--RIQEQMRKATEERsRLEAMER 573
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
176-359 |
2.45e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 176 KAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAK---DYLEKKKELEHVEIALTAYD--IEELHGKWSTLKEKVQM 250
Cdd:COG3206 202 RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEarlAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 251 AKEEELAESSAISAKEAKIEDTRDKIQAldesvdELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQ 330
Cdd:COG3206 282 LSARYTPNHPDVIALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
170 180
....*....|....*....|....*....
gi 1162902455 331 ketvLKEELSKQEAVFETLQAEVKQLRAQ 359
Cdd:COG3206 356 ----LEREVEVARELYESLLQRLEEARLA 380
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
178-382 |
2.51e-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: 45.40 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 178 ENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLE-KKKELEHVEIALTAYDIE--ELHGKWSTLKEKVQMAKEE 254
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqKQKELKSKEKELKKLNEEkkELEEKVKDLTKKISSLKEK 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 255 ELAESSAISAKEAKIEDTRDKIQALDESV--DELQQVLLVTSEELEKLegrkevlKERKKNAVQNQEQLEEAIVQFQQKE 332
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEEL-------KQTQKSLKKKQEEKQELIDQKEKEK 598
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1162902455 333 TVLKEELSKQEAVFETLQAEVKqlraQVKEKQQALSLHNENVEEKIEQLK 382
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELE----KAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1089-1157 |
2.55e-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: 43.86 E-value: 2.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1089 LSGGERALTAIAllfSILKVRPvPFCVLDEVEAALDEANVFRFAQYLKKY-SSDTQFIVITHRkgtMEEA 1157
Cdd:COG1122 135 LSGGQKQRVAIA---GVLAMEP-EVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHD---LDLV 197
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-70 |
2.60e-04 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 44.65 E-value: 2.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1 MFLKRLDVIGFKSFaERISVDFVKGVTAVVGPNGSGKSNITDAIrWVLGeqSARSLRGGKMEDIIFAGSD 70
Cdd:TIGR00611 1 MYLSRLELTDFRNY-DAVDLELSPGVNVIVGPNGQGKTNLLEAI-YYLA--LGRSHRTSRDKPLIRFGAE 66
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
196-979 |
2.60e-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: 45.60 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 196 HELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGKWSTLKEKVQMakEEELAESSAISAKEaKIEDTRDK 275
Cdd:pfam12128 169 FALCDSESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRQQV--EHWIRDIQAIAGIM-KIRPEFTK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 276 IQALDESVDELQQVLLVTSEELEKLEGRKE-VLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVK 354
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIAsRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 355 QLRAQVKEKQQA----LSLHNEN---VEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAVTlqRLADNNEKHLQER 427
Cdd:pfam12128 326 ALEDQHGAFLDAdietAAADQEQlpsWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIR 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 428 HDISARKAACETEFARIEQEIHSQVGayrdmQTKYEQKKRQYEKnESALYQAYQYVQQARSKKDMLETMQgdfsgfyQGV 507
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELREQLE-----AGKLEFNEEEYRL-KSRLGELKLRLNQATATPELLLQLE-------NFD 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 508 KEVLKAKERLGGIRGAVLELISTEQKYETAieialgasaqhvvtDDEQSARkaiqylkqnsfgratfLPLSVIRDRQLQS 587
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKR--------------RDQASEA----------------LRQASRRLEERQS 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 588 RDAETaarHSSFLGVASELVTFDPAYRSVIQNLLGTVLITEDLkganelakllgHRYRIVTlEGDVVNPGGSMTGGAVKK 667
Cdd:pfam12128 521 ALDEL---ELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELL-----------HRTDLDP-EVWDGSVGGELNLYGVKL 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 668 KNNSLlgrsrELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLyelqvaEKNINT 747
Cdd:pfam12128 586 DLKRI-----DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAL------KNARLD 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 748 HLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSStkeslsneltELKIAAAKKEQACK 827
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR----------EARTEKQAYWQVVE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 828 GEEDN-LARLKKELTETELAlkeAKEDLSFLTSEMSSSTSG---EEKLEEAAKHKLNDKTKTIELIALRRDQ----RIKL 899
Cdd:pfam12128 725 GALDAqLALLKAAIAARRSG---AKAELKALETWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEvlryFDWY 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 900 QHGLDTYERELKEMKRLYKQKTTLLKDEevkLGRMEVELDNLLQYLREEyslsfEGAKEKYQLETDPEEARKRVKLIKLA 979
Cdd:pfam12128 802 QETWLQRRPRLATQLSNIERAISELQQQ---LARLIADTKLRRAKLEME-----RKASEKQQVRLSENLRGLRCEMSKLA 873
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1087-1150 |
2.78e-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: 2.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162902455 1087 NLLSGGERALTAIA-LLFSilkvRPvPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHR 1150
Cdd:COG4178 484 QVLSLGEQQRLAFArLLLH----KP-DWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
664-804 |
2.99e-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: 43.76 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 664 AVKKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEgLRLKQQDVKGQLYELQVAEK 743
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 744 NINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSST 804
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
679-913 |
3.15e-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: 44.81 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 679 LEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNI-----NTHLELYD 753
Cdd:pfam10174 361 LNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLqtdssNTDTALTT 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 754 QEKsALSESD-------EERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQAC 826
Cdd:pfam10174 441 LEE-ALSEKEriierlkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 827 KGEEDNLARLKKELTETELALKEAKEdlsfltSEMSSSTSGEekleeaakhkLNDKTKTIEL-IALRRDQRIKLQHGLDT 905
Cdd:pfam10174 520 KSLEIAVEQKKEECSKLENQLKKAHN------AEEAVRTNPE----------INDRIRLLEQeVARYKEESGKAQAEVER 583
|
....*...
gi 1162902455 906 YERELKEM 913
Cdd:pfam10174 584 LLGILREV 591
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
685-969 |
3.60e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 685 RLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLELYDQEKSALSESDE 764
Cdd:TIGR00618 294 PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 765 ERKVRK--RKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSStkESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTE 842
Cdd:TIGR00618 374 QHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDT--RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 843 TELALKEAkedlsfLTSEMSSSTSgEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQhgldtyERELKEMKRLYKQKTT 922
Cdd:TIGR00618 452 QCEKLEKI------HLQESAQSLK-EREQQLQTKEQIHLQETRKKAVVLARLLELQEE------PCPLCGSCIHPNPARQ 518
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1162902455 923 LLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEA 969
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
325-436 |
3.71e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 325 IVQFqqketVLKEELSKQEAVFETLQAEVKQLraqvkekQQALSL---HNENVEEKIEQLKSDyfelLNSQASIRNELQL 401
Cdd:PRK09039 39 VAQF-----FLSREISGKDSALDRLNSQIAEL-------ADLLSLerqGNQDLQDSVANLRAS----LSAAEAERSRLQA 102
|
90 100 110
....*....|....*....|....*....|....*
gi 1162902455 402 LDDQMSQSAVTLQRLADNNEKHLQERHDISARKAA 436
Cdd:PRK09039 103 LLAELAGAGAAAEGRAGELAQELDSEKQVSARALA 137
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
297-450 |
3.82e-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: 45.04 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 297 LEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAV-----FETLQAEVKQLRAQVKEKQQALSLHN 371
Cdd:TIGR01612 1485 INELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALaiknkFAKTKKDSEIIIKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162902455 372 ENVEEKIEQLKSDYFELLNSQASirnelqllDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEIHS 450
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAK--------NDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISS 1635
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
3-368 |
4.57e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 3 LKRLDVigfKSFA--ERISVDFVKGVTAVVGPNGSGKSNITDAIRWVLGEqsarslRGGKmeDIIFAGSDSrkrlnlAEV 80
Cdd:COG0497 2 LTELSI---RNFAliDELELEFGPGLTVLTGETGAGKSILLDALGLLLGG------RADA--SLVRHGADK------AEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 81 TLTLDND----------DHFLPIDFHEVSVTRRVYRSGESEFLINNQPC---RLKDIIDLFMD-------SGLGKEAFSI 140
Cdd:COG0497 65 EAVFDLSddpplaawleENGLDLDDGELILRREISADGRSRAFINGRPVtlsQLRELGELLVDihgqhehQSLLDPDAQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 141 isqgkveEILSS--KAEDRRSIFEEAAGVLKyktRKKKAENKLFETQDNLNRVEDIL-HELEgQVEPLKIQASIAKDYLE 217
Cdd:COG0497 145 -------ELLDAfaGLEELLEEYREAYRAWR---ALKKELEELRADEAERARELDLLrFQLE-ELEAAALQPGEEEELEE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 218 KKKELEHVE-IALTAYDI-EELHGKWSTLKEKVQMAKeeelAESSAISAKEAKIEDTRDKIQ----ALDESVDELQQVL- 290
Cdd:COG0497 214 ERRRLSNAEkLREALQEAlEALSGGEGGALDLLGQAL----RALERLAEYDPSLAELAERLEsaliELEEAASELRRYLd 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 291 -LVTS-EELEKLEGRKEVLKE-RKKNAVQNqeqleEAIVQFQQKetvLKEELSK---QEAVFETLQAEVKQLRAQVKEKQ 364
Cdd:COG0497 290 sLEFDpERLEEVEERLALLRRlARKYGVTV-----EELLAYAEE---LRAELAElenSDERLEELEAELAEAEAELLEAA 361
|
....
gi 1162902455 365 QALS 368
Cdd:COG0497 362 EKLS 365
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
18-398 |
4.74e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 18 ISVDFVK-GVTAVVGPNGSGKSNITDAIRWVLGEQSARSLRGGKMediifAGSDSRKRLnLAEVTLTLDNDDHFlpidfh 96
Cdd:PHA02562 20 IEIQLDKvKKTLITGKNGAGKSTMLEALTFALFGKPFRDIKKGQL-----INSINKKDL-LVELWFEYGEKEYY------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 97 evsVTRrvyrsgeseflinnqpcrlkdiidlfmdsGLGKEAFSIISQGK-VEEILSSKaeDRRSIFEEAAGV-------- 167
Cdd:PHA02562 88 ---IKR-----------------------------GIKPNVFEIYCNGKlLDESASSK--DFQKYFEQMLGMnyksfkqi 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 168 -------------LKYKTRKKKAENKL----FETQDNLNRveDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALT 230
Cdd:PHA02562 134 vvlgtagyvpfmqLSAPARRKLVEDLLdisvLSEMDKLNK--DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 231 AYDIEELHGKWSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQAL-DESVDELQQVLLVTSEE------------- 296
Cdd:PHA02562 212 GENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLnTAAAKIKSKIEQFQKVIkmyekggvcptct 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 297 --LEKLEGRKEVLKERKKNAVQN-------QEQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQAL 367
Cdd:PHA02562 292 qqISEGPDRITKIKDKLKELQHSlekldtaIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQ 371
|
410 420 430
....*....|....*....|....*....|.
gi 1162902455 368 SLHNENVEEkIEQLKSDYFELLNSQASIRNE 398
Cdd:PHA02562 372 AEFVDNAEE-LAKLQDELDKIVKTKSELVKE 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
267-756 |
7.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 267 AKIEDTRDKIQALDESVDELQQVLlvtsEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQ--QKETVLKEELSKQEA 344
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 345 VFETLQAEVKQLRAQVKEKQQAlslhnenvEEKIEQLksdyfellnsQASIRNELQLLDDQMSQsavTLQRLADNNEKHL 424
Cdd:COG4717 147 RLEELEERLEELRELEEELEEL--------EAELAEL----------QEELEELLEQLSLATEE---ELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 425 QERHDISARKAACETEFARIEQEIhsqvgayrdmqTKYEQKKRQYEKNESalYQAYQYVQQARSKKDMLETMQGDFSGFY 504
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEEL-----------EQLENELEAAALEER--LKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 505 QGVKEVLKAkeRLGGIRGAVLELISTEQKYETAIEIALGASAQHVVTDDEQSARKAIQYLKQNSFGRATFLPLSVIRDRQ 584
Cdd:COG4717 273 LTIAGVLFL--VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 585 LQSRDAETAARHSSFLGVASElvtfdpayrsvIQNLLGTVLITED---LKGANELAKLLGHRYRIVTLEGDVVNPGGSMT 661
Cdd:COG4717 351 ELLREAEELEEELQLEELEQE-----------IAALLAEAGVEDEeelRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 662 GGAVKKKNNSLlgrSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEK--KLADLRETGEGLRLKQQDVKGQLYELQ 739
Cdd:COG4717 420 ELLEALDEEEL---EEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALK 496
|
490
....*....|....*..
gi 1162902455 740 VAEKNINTHLELYDQEK 756
Cdd:COG4717 497 LALELLEEAREEYREER 513
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1083-1172 |
7.77e-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: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1083 LQNLNLLSGGERALTAIALLFSILKVRPV--PFCVLDEVEAALDEANV-FRFAQYLKKYSSDT--QFIVITHRKGTMEEA 1157
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERKSQKnfQLIVITHDEELVDAA 189
|
90
....*....|....*
gi 1162902455 1158 DVLYGVTMQESGVSK 1172
Cdd:cd03240 190 DHIYRVEKDGRQKSR 204
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-515 |
9.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 145 KVEEILSSKAEDRRSIFEEA-----AGVLKYKTRKKKAE--NKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLE 217
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAeekaeAAEKKKEEAKKKADaaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 218 KKKELEHVEIALTAYDIEELHGKWSTLKEKVQMAKEEELAESSAISAKEA-----------KIEDTRDKIQALDESVDEL 286
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeakkkaeeakKADEAKKKAEEAKKKADEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 287 QQvllvTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEavfETLQAEVKQLRAQVK--EKQ 364
Cdd:PTZ00121 1503 KK----AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE---ELKKAEEKKKAEEAKkaEED 1575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 365 QALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARI 444
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 445 EQEIHSQVGAYRDMQTKYEQKKRQYEKNESALYQAYQYVQQARSKKDMLETMQGDFSGFYQGVKEVLKAKE 515
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
687-857 |
9.99e-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: 43.63 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 687 AEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLELYDQEKSALSESDEER 766
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 767 KVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELTETELA 846
Cdd:pfam01576 509 EEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVD 588
|
170
....*....|.
gi 1162902455 847 LKEAKEDLSFL 857
Cdd:pfam01576 589 LDHQRQLVSNL 599
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
142-366 |
1.02e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 142 SQGKVEEILSSKAEDRRSIFEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKE 221
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 222 lEHVEIALTAYdieeLHGKWSTLKEKVQMAKEEELAESSAI-----SAKEAKIEDTRDKIQALDESVDELQQvllvtseE 296
Cdd:COG4942 105 -ELAELLRALY----RLGRQPPLALLLSPEDFLDAVRRLQYlkylaPARREQAEELRADLAELAALRAELEA-------E 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 297 LEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQA 366
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-367 |
1.04e-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: 42.22 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 234 IEELHGKWSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDE------SVDELQQVllvtSEELEKLEGRKEVL 307
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrNNKEYEAL----QKEIESLKRRISDL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 308 KERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQAL 367
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
684-1025 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 684 KRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQL---YELQVAEKNINTHLE--LYDQEKSA 758
Cdd:pfam01576 264 KKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTaaqQELRSKREQEVTELKkaLEEETRSH 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 759 LSESDEERKVRKRKLEEelsaVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKK 838
Cdd:pfam01576 344 EAQLQEMRQKHTQALEE----LTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 839 ELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEaakhklndktktielialrrdQRIKLQHGLDTYERELKEMKRLYK 918
Cdd:pfam01576 420 RLSESERQRAELAEKLSKLQSELESVSSLLNEAEG---------------------KNIKLSKDVSSLESQLQDTQELLQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 919 QKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVN 998
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT 558
|
330 340
....*....|....*....|....*..
gi 1162902455 999 ERYKFLSEQKEDLTEAKNTLFQVIEEM 1025
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1084-1158 |
1.13e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 1084 QNLNLLSGGERALTAIA--LLfsilkvRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEAD 1158
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIAraLL------RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
677-834 |
1.15e-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: 41.83 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 677 RELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLELydqek 756
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY----- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162902455 757 SALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLA 834
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
720-923 |
1.18e-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: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 720 TGEGLRLKQQDvKGQLYELQVAEKNINTHLElydQEKSALSESDE-----ERKVRKRK-LEEELSAVSEKMKQLEEDIDR 793
Cdd:pfam17078 16 TKTNLQLTVQS-QNLLSKLEIAQQKESKFLE---NLASLKHENDNlssmlNRKERRLKdLEDQLSELKNSYEELTESNKQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 794 LTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDnlaRLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEE 873
Cdd:pfam17078 92 LKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKD---HYQQEINTLQESLEDLKLENEKQLENYQQRISSNDKDID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162902455 874 AAKHKLNDKTKTIELIALRRDQRI-----------KLQHGLDTYeRELKEMKRLYKQKTTL 923
Cdd:pfam17078 169 TKLDSYNNKFKNLDNIYVNKNNKLltkldslaqllDLPSWLNLY-PESRNKILEYAEKMEL 228
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
679-863 |
1.24e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 679 LEDVTKRLAEMEEKT-----ALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNIN---THLE 750
Cdd:PRK02224 189 LDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEdlrETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 751 LYDQEKSALSESDEERKVRKRKLEEELS--------------AVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELK 816
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDdllaeaglddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1162902455 817 IAAAKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSS 863
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
209-420 |
1.33e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 209 ASIAKDYLEKKKELEHVEIALTAYD---IEELHGKWSTLKEKvQMAKEEELAESSAISAKEAKIEDTRDKIQALDE---- 281
Cdd:PRK10929 19 AATAPDEKQITQELEQAKAAKTPAQaeiVEALQSALNWLEER-KGSLERAKQYQQVIDNFPKLSAELRQQLNNERDeprs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 282 -----SVDEL-QQVLLVTSEELEKleGRKevlkerkknAVQNQEQLEE---AIVQFQQKETVLKEELSKQE--------- 343
Cdd:PRK10929 98 vppnmSTDALeQEILQVSSQLLEK--SRQ---------AQQEQDRAREisdSLSQLPQQQTEARRQLNEIErrlqtlgtp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 344 ------AVFETLQAEVKQLRAQVKEKQQA-LSLHN--ENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAV-TL 413
Cdd:PRK10929 167 ntplaqAQLTALQAESAALKALVDELELAqLSANNrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALeST 246
|
....*..
gi 1162902455 414 QRLADNN 420
Cdd:PRK10929 247 ELLAEQS 253
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
677-850 |
1.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 677 RELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRET-GEGLRLKQQDVKGQLYELQVAE-KNINTHLE---- 750
Cdd:COG3883 44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARALYRSGGSVSYLDVLLGsESFSDFLDrlsa 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 751 ---LYDQEKSALSESDEERKV---RKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQ 824
Cdd:COG3883 124 lskIADADADLLEELKADKAEleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
170 180
....*....|....*....|....*.
gi 1162902455 825 ACKGEEDNLARLKKELTETELALKEA 850
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1022-1149 |
1.46e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.23 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 1022 IEEMDEEMTKRFNDTFVQIRSHFDQVFRSLFGGGRAELRLTDPNdllhsgveiiaqppGKKLQNLNLLSGGerALTAIAL 1101
Cdd:COG4637 206 LRETHPERFERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKG--------------LDRPFPARELSDG--TLRFLAL 269
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1162902455 1102 LFSILKVRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITH 1149
Cdd:COG4637 270 LAALLSPRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1089-1161 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162902455 1089 LSGGERALTAIA--LLfsilkvRPVPFCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEADVLY 1161
Cdd:COG4987 472 LSGGERRRLALAraLL------RDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
675-854 |
1.52e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 675 RSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLR-------LKQQDVKGQLYELQVAEKNINT 747
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaglddADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 748 HLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQACK 827
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
170 180 190
....*....|....*....|....*....|....
gi 1162902455 828 GEED-------NLARLKKELTETELALKEAKEDL 854
Cdd:PRK02224 409 NAEDfleelreERDELREREAELEATLRTARERV 442
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
169-405 |
1.59e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 169 KYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQasiaKDYLEKKKELEHVEIALTAYDIEELHGKWSTLKEKV 248
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE----KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 249 QMAKeeelaesSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQF 328
Cdd:TIGR04523 457 KNLD-------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162902455 329 QQKETVLKEELSKQEAVFETLQAEVK--QLRAQVKEKQQalslhnenveeKIEQLKSDYFELLNSQASIRNELQLLDDQ 405
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNK-----------EIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
281-407 |
1.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 281 ESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETV---LKEELSK-QEAVFETLQ--AEVK 354
Cdd:PRK04863 551 DDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARlREQSGEEFEdsQDVT 630
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1162902455 355 QLRAQVKEKQQALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMS 407
Cdd:PRK04863 631 EYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFG 683
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
678-876 |
1.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 678 ELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETgegLRLKQQDVKGQLYELQVAEKNINTHLELYDQEK- 756
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELGERARALYRSGGSVSYLDVLLGSESf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 757 ----------SALSESD----EERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKK 822
Cdd:COG3883 115 sdfldrlsalSKIADADadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1162902455 823 EQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAK 876
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
680-842 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 680 EDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRE----------------TGEGLRLKQQDVKGQLYELQVAEK 743
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknglvdlseeaklllqQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 744 NINTHLELYDQEKSALSESDEERKVRKR--KLEEELSAVSEK-------MKQLEEDIDRLTKQKQTQssTKESLSNELTE 814
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQE--AQRILASLEAE 321
|
170 180
....*....|....*....|....*...
gi 1162902455 815 LKIAAAKKEQAckgeEDNLARLKKELTE 842
Cdd:COG3206 322 LEALQAREASL----QAQLAQLEARLAE 345
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
786-1040 |
1.98e-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: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 786 QLEEDIDRLTKQKQTQSSTKESLSNELTELKIAaakkeqackgeednLARLKKELTETELALKEAKEDLSFLTSEMSSST 865
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGE--------------LEKASREETFARTALKNARLDLRRLFDEKQSEK 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 866 SGEEKLEEAAKHKLNDKTKTI--ELIALRRDQRIKLQHGLDTYeRELKEMKRLYKQktTLLKDEEVKLGRMEVELDNL-L 942
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLeaQLKQLDKKHQAWLEEQKEQK-REARTEKQAYWQ--VVEGALDAQLALLKAAIAARrS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 943 QYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELG--TVNLGSIDEFER-VNERYkflSEQKEDLTEAKNTLF 1019
Cdd:pfam12128 744 GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIEriAVRRQEVLRYFDwYQETW---LQRRPRLATQLSNIE 820
|
250 260
....*....|....*....|.
gi 1162902455 1020 QVIEEMDEEMTKRFNDTFVQI 1040
Cdd:pfam12128 821 RAISELQQQLARLIADTKLRR 841
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
180-527 |
2.17e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 180 KLFETQDNLNRVEDILHELEGQVEplkiqasiakDYLEKKKELEHVEiALTAYDIEELHGKWSTLKEKVqMAKEEELAES 259
Cdd:PRK04778 99 RFRKAKHEINEIESLLDLIEEDIE----------QILEELQELLESE-EKNREEVEQLKDLYRELRKSL-LANRFSFGPA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 260 -SAISAKEAKIEDTRDKIQALDESVDELQ--QVLLVTSEELEKLEGRKEVLKERKKNAVQN-QEQLEEaivqfqqketvL 335
Cdd:PRK04778 167 lDELEKQLENLEEEFSQFVELTESGDYVEarEILDQLEEELAALEQIMEEIPELLKELQTElPDQLQE-----------L 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 336 KE---ELSKQEAVFETLQ--AEVKQLRAQVKEKQQALS-LHNENVEEKIEQLKS---DYFELLNSQASIRNELQLLDDQM 406
Cdd:PRK04778 236 KAgyrELVEEGYHLDHLDieKEIQDLKEQIDENLALLEeLDLDEAEEKNEEIQEridQLYDILEREVKARKYVEKNSDTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 407 SQSavtLQRLADNNEK------HLQERHDISARkaacETEFAR-IEQEIHSQVGAYRDMQTKYEQKKRQYekneSALYQA 479
Cdd:PRK04778 316 PDF---LEHAKEQNKElkeeidRVKQSYTLNES----ELESVRqLEKQLESLEKQYDEITERIAEQEIAY----SELQEE 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1162902455 480 YQYVQQarsKKDMLETMQGDFSGFYQGV-KEVLKAKERLGGIRGAVLEL 527
Cdd:PRK04778 385 LEEILK---QLEEIEKEQEKLSEMLQGLrKDELEAREKLERYRNKLHEI 430
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
181-417 |
2.21e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 181 LFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKELEHVEIALTAYDIEELHGKWSTLKEKVQMAKEEELAESS 260
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 261 AISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEEL------------EKLEGRKEVLKERKkNAVQNQEQLEEAIVQF 328
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLaaredalnqslkELMHQARTVLKART-EAHFNNNEEVTAALQT 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 329 QQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEK----QQALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQLLDD 404
Cdd:TIGR00618 777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
250
....*....|...
gi 1162902455 405 QMSQSAVTLQRLA 417
Cdd:TIGR00618 857 CSKQLAQLTQEQA 869
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
725-941 |
2.23e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 725 RLKQQDVKGQLYELQVAEKNINTHLELYDQeksaLSESDEERKVRKRKLEEELSavsEKMKQLEEDIDRLTKQKQTQSST 804
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEE----QRKKNGENIARKQNKYDELV---EEAKTIKAEIEELTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 805 KESLSNELTELKIAAAKKeqacKGEEDNLARLKKELTETELAlKEAKEDLSfltsemssstSGEEKLEEAaKHKLNDKTK 884
Cdd:PHA02562 250 IEDPSAALNKLNTAAAKI----KSKIEQFQKVIKMYEKGGVC-PTCTQQIS----------EGPDRITKI-KDKLKELQH 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 885 TIELIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNL 941
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1087-1158 |
2.23e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 42.26 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162902455 1087 NLLSGGERALTAIALlfSILKVRPVpfCVLDEVEAALDEANVFRFAQYLKKYSSDTQFIVITHRKGTMEEAD 1158
Cdd:PRK13657 470 RQLSGGERQRLAIAR--ALLKDPPI--LILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNAD 537
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
672-1032 |
2.54e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 672 LLGRSRELEDVTK----RLAEMEEKTALLEQEVKTLKHSIQdMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINT 747
Cdd:pfam05483 386 LQKKSSELEEMTKfknnKEVELEELKKILAEDEKLLDEKKQ-FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 748 HLELYDQEKSALSESDEERKVRK--------------RKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELT 813
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNieltahcdklllenKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 814 ELK--IAAAKKEQACKGE---------EDNLARLKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEE---AAKHKL 879
Cdd:pfam05483 545 NLRdeLESVREEFIQKGDevkckldksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkALKKKG 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 880 NDKTKTIELIALRRDQ--------RIKLQHGLDTYERELkEMKRLYK-------QKTTLLKDEEVKLGRmevELDNLLQY 944
Cdd:pfam05483 625 SAENKQLNAYEIKVNKlelelasaKQKFEEIIDNYQKEI-EDKKISEeklleevEKAKAIADEAVKLQK---EIDKRCQH 700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 945 LREEYSLSFEgaKEKYQLETDPEEARKRVKLIKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEE 1024
Cdd:pfam05483 701 KIAEMVALME--KHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
....*...
gi 1162902455 1025 MDEEMTKR 1032
Cdd:pfam05483 779 NTAILKDK 786
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
666-838 |
2.90e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 666 KKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLY----ELQVA 741
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEeledELQAT 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 742 EkniNTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKiaaAK 821
Cdd:pfam01576 712 E---DAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELE---AQ 785
|
170
....*....|....*..
gi 1162902455 822 KEQACKGEEDNLARLKK 838
Cdd:pfam01576 786 IDAANKGREEAVKQLKK 802
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
155-452 |
2.95e-03 |
|
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: 41.73 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 155 EDRRsifEEAAGVLKYKTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIAKDYLEKKKElehveiALTAYDi 234
Cdd:pfam10174 268 EDRE---EEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKE------SLTAKE- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 235 eelhGKWSTLKEKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNA 314
Cdd:pfam10174 338 ----QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDK 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 315 VQNQEQLEEAIVQFQQKE-------TVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSDYFE 387
Cdd:pfam10174 414 DKQLAGLKERVKSLQTDSsntdtalTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 388 LLNSQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQE--RHDISARKAACETEFARIEQEIHSQV 452
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEEcsKLENQLKKAHNAEEAVRTNPEINDRI 560
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
183-446 |
3.15e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 183 ETQDNLNRVEDILHELEGQVEPLK-----------------IQASIAKDYLEKKKELEHVEiALTAYDIEELHgkwSTLK 245
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEEVDSLKsqladyqqaldvqqtraIQYQQAVQALEKARALCGLP-DLTPENAEDYL---AAFR 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 246 EKVQMAKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQ--------QVLLVTSEELEKLEGRKEVLKERKKNAVQN 317
Cdd:COG3096 448 AKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVErsqawqtaRELLRRYRSQQALAQRLQQLRAQLAELEQR 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 318 QEQLEEAIVQFQQ----------KETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALslhnENVEEKIEQLKSDYFE 387
Cdd:COG3096 528 LRQQQNAERLLEEfcqrigqqldAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL----EQLRARIKELAARAPA 603
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162902455 388 LLNSQASirneLQLLDDQMSQS-----AVT--LQRLADNNEKHLQERHDISARKAACETEFARIEQ 446
Cdd:COG3096 604 WLAAQDA----LERLREQSGEAladsqEVTaaMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-493 |
3.63e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 171 KTRKKKAENKLFETQDNLNRVEDILHELEGQVEPLKIQASIakdyLEKKKELEHveialtaydIEELHGKWSTLKEKVQM 250
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD----LNNQKEQDW---------NKELKSELKNQEKKLEE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 251 AKEEELAESSAISAKEAKIEDTRDKIQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQ 330
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 331 KETVLKEELSKQEAVFETLQAEVKQLRAQV----------KEKQQALSLHNENVEEKIEQLKSDYFELLNSQASIR---- 396
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIiknnseikdlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKqnle 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 397 ----------NELQLLDDQMSQSAVTLQRLADNNEKHLQERHDISARKAACETEFARIEQEIHSQvgAYRDMQTKYEQKK 466
Cdd:TIGR04523 486 qkqkelkskeKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD--DFELKKENLEKEI 563
|
330 340
....*....|....*....|....*..
gi 1162902455 467 RQYEKNESALYQAYQYVQQARSKKDML 493
Cdd:TIGR04523 564 DEKNKEIEELKQTQKSLKKKQEEKQEL 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1014 |
4.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 677 RELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLELYDQEK 756
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 757 SALSESDE-ERKVRKRKLEEELSAVSEKMKQLEEdidrlTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLAR 835
Cdd:PTZ00121 1402 EDKKKADElKKAAAAKKKADEAKKKAEEKKKADE-----AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 836 LKKELTETELALKEAKEDLSFLTSEMSSSTSGEEKLEEAAK----------HKLNDKTKTIEliaLRRDQRIKLQHGLDT 905
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeeakkadeaKKAEEAKKADE---AKKAEEKKKADELKK 1553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 906 YERELK-EMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLAIEELG 984
Cdd:PTZ00121 1554 AEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350
....*....|....*....|....*....|
gi 1162902455 985 TVNLGSIDEFERVNERYKFLSEQKEDLTEA 1014
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
742-1032 |
4.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 742 EKNINTHLELYDQEKSA--LSESDEERKVRKRKLEEELSAvsekmkqlEEDIDRLTKQKQTQsstKESLSNELTELKiaa 819
Cdd:PRK03918 148 EKVVRQILGLDDYENAYknLGEVIKEIKRRIERLEKFIKR--------TENIEELIKEKEKE---LEEVLREINEIS--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 820 aKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSSStsgEEKLEEAAKhKLNDKTKTIELIALRRDQRIKL 899
Cdd:PRK03918 214 -SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL---EEKIRELEE-RIEELKKEIEELEEKVKELKEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 900 QHGLDTYeRELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKLIKLA 979
Cdd:PRK03918 289 KEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 980 IEELGTVN----LGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDEEMTKR 1032
Cdd:PRK03918 368 KAKKEELErlkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
665-941 |
4.16e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 665 VKKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLadlretgeglrlkqQDVKGQLYELQVAEKN 744
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKL--------------KKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 745 INTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKESLSNELTELKIAAAKKEQ 824
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 825 ACKgeEDNLARLKKELTETELALKEAKEDLsfLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQRIKLQHGLD 904
Cdd:TIGR04523 188 NID--KIKNKLLKLELLLSNLKKKIQKNKS--LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270
....*....|....*....|....*....|....*..
gi 1162902455 905 TYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNL 941
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
678-866 |
4.91e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 678 ELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEkklADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLELYDQEKS 757
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 758 ALSEsdeerkvrkrKLEEELSAVSEKMKQLEEDIDRLTKQ---KQTQSSTKESLSNELTELKIAAAKKEQackgeedNLA 834
Cdd:pfam09787 125 YLEE----------ELRRSKATLQSRIKDREAEIEKLRNQltsKSQSSSSQSELENRLHQLTETLIQKQT-------MLE 187
|
170 180 190
....*....|....*....|....*....|..
gi 1162902455 835 RLKKELTETELALKEAKEDLSFLTSEMSSSTS 866
Cdd:pfam09787 188 ALSTEKNSLVLQLERMEQQIKELQGEGSNGTS 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
752-1027 |
4.92e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 752 YDQEKSAlsesDEERKVRKRKLEEELSAVSEKMKQLEE----DIDRLTKQKQTQSSTKESLSNELTELKIAAAKK--EQA 825
Cdd:PTZ00121 1220 AEDAKKA----EAVKKAEEAKKDAEEAKKAEEERNNEEirkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 826 CKGEE----DNLARLKKELTETELALKEAKE------DLSFLTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIALRRDQ 895
Cdd:PTZ00121 1296 KKAEEkkkaDEAKKKAEEAKKADEAKKKAEEakkkadAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 896 RIKLQHGLDTYERELKEMKRLYKqkttllKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPEEARKRVKL 975
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKK------KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1162902455 976 IKLAIEELGTVNLGSIDEFERVNERYKFLSEQKEDLTEAKNTLFQVIEEMDE 1027
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-983 |
5.26e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 677 RELEDVtkRLAEMEEKTalleQEVKTLKHSIQDMEK-KLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLELYDQE 755
Cdd:PTZ00121 1212 RKAEEA--RKAEDAKKA----EAVKKAEEAKKDAEEaKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 756 KSALSESDEERKVRKRKLEEELSAVSEKMKQLEEdidrLTKQKQTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLAR 835
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE----AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 836 LKKELTETELALKEAKEDlsflTSEMSSSTSGEEKLEEAAKHKLNDKTKTIELiaLRRDQRIKLQHGLDTYERELKEMKR 915
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKK----ADAAKKKAEEKKKADEAKKKAEEDKKKADEL--KKAAAAKKKADEAKKKAEEKKKADE 1435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162902455 916 LYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEgAKEKYQLETDPEEARKRVKLIKLAIEEL 983
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE-AKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
276-403 |
5.42e-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: 40.39 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 276 IQALDESVDELQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETvlkEELSKQEAVFETLQAEVKQ 355
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP---TELDRAKEKLKKLLQEIMI 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1162902455 356 LRAQVKEKQQALSLHNENVEEKIEQlKSDYFELLNSQASIRNELQLLD 403
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNK-KSELNTEIAEAEKKLEQCRGFT 269
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
281-367 |
5.49e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 281 ESVDELQQVLLVTSEELEKLEGRKEVLKERKKNA------VQNQEQLEEAIVQFQ------------QKETV--LKEELS 340
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnlVQTALRQQEKIERYQedleelterleeQEEVVeeAAEQLA 378
|
90 100
....*....|....*....|....*..
gi 1162902455 341 KQEAVFETLQAEVKQLRAQVKEKQQAL 367
Cdd:COG3096 379 EAEARLEAAEEEVDSLKSQLADYQQAL 405
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
683-1030 |
5.52e-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: 40.93 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 683 TKRLAEMEEKTALLEQEVKTLKHSIQDMEKK------------------LADLRETGEGLRLKQQDVKGQLYELQVAEKN 744
Cdd:pfam01576 323 SKREQEVTELKKALEEETRSHEAQLQEMRQKhtqaleelteqleqakrnKANLEKAKQALESENAELQAELRTLQQAKQD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 745 INT---HLELYDQEKSA-LSESD---EERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSST---KESLSNELTE 814
Cdd:pfam01576 403 SEHkrkKLEGQLQELQArLSESErqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQlqdTQELLQEETR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 815 LKIAAAKKEQACkgeEDNLARLKKELTETELALKEAKEDLSFLTSEMSSStsgeekleeaaKHKLNDKTKTIELIalrRD 894
Cdd:pfam01576 483 QKLNLSTRLRQL---EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM-----------KKKLEEDAGTLEAL---EE 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 895 QRIKLQHGLDTYERELKE----MKRLYKQKTTL---LKDEEVKLGRMEVELDNLL-------QYLREEYSLSFEGAKEKY 960
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEkaaaYDKLEKTKNRLqqeLDDLLVDLDHQRQLVSNLEkkqkkfdQMLAEEKAISARYAEERD 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 961 QLETDPEEARKRVKLIKLAIEELgtvnLGSIDEFERVNERYKFLSEQ----KED-------LTEAKNTLFQVIEEMDEEM 1029
Cdd:pfam01576 626 RAEAEAREKETRALSLARALEEA----LEAKEELERTNKQLRAEMEDlvssKDDvgknvheLERSKRALEQQVEEMKTQL 701
|
.
gi 1162902455 1030 T 1030
Cdd:pfam01576 702 E 702
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
675-863 |
5.57e-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: 40.56 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 675 RSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLK--------------------------- 727
Cdd:pfam15905 92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKfsedgtqkkmsslsmelmklrnkleak 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 728 -------QQDVKGQLyelQVAEKNINTHLELYDQEKSALSESDEERKVRKRKLE------EELSAVSEKMKQLEEDIDRL 794
Cdd:pfam15905 172 mkevmakQEGMEGKL---QVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEklleyiTELSCVSEQVEKYKLDIAQL 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162902455 795 TKQKQTQSSTKESLSNELTElkiaaaKKEQACKGEEDNLARLKKELTETELALKEAKEDLSFLTSEMSS 863
Cdd:pfam15905 249 EELLKEKNDEIESLKQSLEE------KEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEE 311
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
648-1032 |
6.40e-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: 40.71 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 648 TLEGDVVNPGGSMTGGAVKKKNNSLLGRSRELEDVTKRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLK 727
Cdd:COG5185 172 LNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 728 QQDVKgqlyelQVAEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELSAVSEKMKQLEEDIDRLTKQKQTQSSTKEs 807
Cdd:COG5185 252 SDKLE------KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAE- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 808 lsNELTELKIAAAKKEQACKGEednlarLKKELTETELALKEAKEDLSFLTSEMSSSTSgEEKLEEAakhKLNDKTKTIE 887
Cdd:COG5185 325 --QELEESKRETETGIQNLTAE------IEQGQESLTENLEAIKEEIENIVGEVELSKS-SEELDSF---KDTIESTKES 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 888 LIALRRDQRIKLQHGLDTYERELKEMKRLYKQKTTLLKDEEVKLGRMEVELDNLLQYLREEYSLSFEGAKEKYQLETDPE 967
Cdd:COG5185 393 LDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEI 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162902455 968 EARKRVKLIKLAIEELGTVNlgSIDEFERVNERYKFLSEQKedLTEAKNTLFQVIEEMDEEMTKR 1032
Cdd:COG5185 473 NRSVRSKKEDLNEELTQIES--RVSTLKATLEKLRAKLERQ--LEGVRSKLDQVAESLKDFMRAR 533
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
145-383 |
6.49e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 145 KVEEILSSKAEDRRSIFEEAAGVLKYKT-----RKKKAENKLFETQDNLNRVEDI----------LHELEGQVEPLKIQA 209
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKnelseLRRQIQRAELELQSTNSELEELqerldllkakASEAEQLRQNLEKQQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 210 SIAKDYLEKKKELEhVEIALTAYDIEELHGKWSTLKEKVQMAKEEElaessAISAKEAKIEDTRDKIQALDESVDELQQV 289
Cdd:pfam05557 163 SSLAEAEQRIKELE-FEIQSQEQDSEIVKNSKSELARIPELEKELE-----RLREHNKHLNENIENKLLLKEEVEDLKRK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 290 LLV---TSEELEKLEGRKEVLkERKKNAVQNQEQ-----------LEEAIVQFQQKETVLKEELSkqeavfeTLQAEVKQ 355
Cdd:pfam05557 237 LEReekYREEAATLELEKEKL-EQELQSWVKLAQdtglnlrspedLSRRIEQLQQREIVLKEENS-------SLTSSARQ 308
|
250 260
....*....|....*....|....*...
gi 1162902455 356 LRAQVKEKQQALSLHNENVEEKIEQLKS 383
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDLNKKLKR 336
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
212-922 |
7.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 212 AKDYLEKKKELEHVEIALTAYDIEELH----GKWSTLKEKVQMAKEEELAESS--AISAKEAKIEDTRDKIQALDESVDE 285
Cdd:PTZ00121 1120 AKKKAEDARKAEEARKAEDARKAEEARkaedAKRVEIARKAEDARKAEEARKAedAKKAEAARKAEEVRKAEELRKAEDA 1199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 286 LQQVLLVTSEELEKLEGRKEVLKERKKNAVQNQEQLEEAIVQFQQKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQ 365
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 366 ALSLHNENVEEKIEQLKSDYFELLNSQASIRNELQLLDDQMSQSAVTLQRLADNNEKHLQERHdiSARKAACETEFARIE 445
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK--KAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 446 QEIHSQVGAYRDMQTKYEQKKRQYEKNESAlyQAYQYVQQARSKKDMLETMQGDFSGFYQGVKEVLKAKERLGGIRGA-- 523
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKA--EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAde 1435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 524 VLELISTEQKYETAIEIALGASAQHVVTDDEQSARKAIQYLKQNSFGRatflplsviRDRQLQSRDAETAARHSSFLGVA 603
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK---------KADEAKKKAEEAKKKADEAKKAA 1506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 604 SELVTFDPAYRSVIQNLLGTVLITEDLKGANELAKLLGHRyrivtlEGDVVNPGGSMTGGAVKKKNNSllgRSRELEDVT 683
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK------KADELKKAEELKKAEEKKKAEE---AKKAEEDKN 1577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 684 KRLAEMEEKTALLEQEVKTLKHSIQDMEKKLADLRETGEGLRLKQQDVKGQLYELQVAEKNINTHLElYDQEKSALSESD 763
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-EKKKAEELKKAE 1656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 764 EERKVRKRKL---EEELSAVSEKMKQLEEDidrlTKQKQTQSSTKESLSNELTELKIAAAkkEQACKGEEdnlarLKKEL 840
Cdd:PTZ00121 1657 EENKIKAAEEakkAEEDKKKAEEAKKAEED----EKKAAEALKKEAEEAKKAEELKKKEA--EEKKKAEE-----LKKAE 1725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 841 TETELALKEAKEDlsfltSEMSSSTSGEEKLEEAAKHKLNDKTKTIELIA--LRRDQRIKLQHGLDtyerELKEMKRLYK 918
Cdd:PTZ00121 1726 EENKIKAEEAKKE-----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAeeIRKEKEAVIEEELD----EEDEKRRMEV 1796
|
....
gi 1162902455 919 QKTT 922
Cdd:PTZ00121 1797 DKKI 1800
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1089-1158 |
7.58e-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: 7.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 1089 LSGGERALTAIA--LLF--SILkvrpvpfcVLDEVEAALD---EANVFrfaQYLKKYSSDTQFIVITHRKGTMEEAD 1158
Cdd:COG1132 477 LSGGQRQRIAIAraLLKdpPIL--------ILDEATSALDtetEALIQ---EALERLMKGRTTIVIAHRLSTIRNAD 542
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
256-851 |
7.73e-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: 40.48 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 256 LAESSAISA-KEAKIEDTRDKIQALDESVDELQQVLLVTSEEL--EKLEGRKEV---LKERKKNAVQNQEQLEEAIVQFQ 329
Cdd:pfam05483 160 LKETCARSAeKTKKYEYEREETRQVYMDLNNNIEKMILAFEELrvQAENARLEMhfkLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 330 QKETVLKEELSKQEAVFETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLKSDYFELLNSQASIRNEL---QLLDDQM 406
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMstqKALEEDL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 407 SQSAVTLQRLADNNEKHLQERHDISARKAACETEF----ARIEQEIHSQVGAYRDMQTKYEQKKRQYEKNESALYQAYQY 482
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFeattCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 483 VQQARSKKDMLETMQGDFSGFYQGVKEVLKAKERLGGIRGAVLELISTEQKYETAIEIALGAsaqhvVTDDEQSARKAIQ 562
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA-----IKTSEEHYLKEVE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 563 YLKqnsfgraTFLPLSVIRDRQLQSRDAETAARHSSFLGVASELV-TFDPAYRSVIQNLLGTVLITEDLKGANELAKLLg 641
Cdd:pfam05483 475 DLK-------TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIENLEEKEMNL- 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 642 hRYRIVTLEGDVVNPGGSMTGGAVKKKNNSllgRSRELEDVTKrlaemEEKTALLEQEVKTLKHSIQDMEKKLADLRETG 721
Cdd:pfam05483 547 -RDELESVREEFIQKGDEVKCKLDKSEENA---RSIEYEVLKK-----EKQMKILENKCNNLKKQIENKNKNIEELHQEN 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 722 EGLRLKQQDVKGQL--YELQV--AEKNINTHLELYDQEKSALSESDEERKVRKRKLEEELS---AVSEKMKQLEEDIDRL 794
Cdd:pfam05483 618 KALKKKGSAENKQLnaYEIKVnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEkakAIADEAVKLQKEIDKR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 795 TKQK---------------------------------QTQSSTKESLSNELTELKIAAAKKEQACKGEEDNLARLKKELT 841
Cdd:pfam05483 698 CQHKiaemvalmekhkhqydkiieerdselglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
650
....*....|
gi 1162902455 842 ETELALKEAK 851
Cdd:pfam05483 778 ENTAILKDKK 787
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
266-468 |
8.96e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 266 EAKIEDTRDKIQALDESVDELQQvllvTSEELEKLEGRKEVLKERKknavQNQEQLEEAIVQFQQKETVLK--------- 336
Cdd:COG3096 892 ADRLEELREELDAAQEAQAFIQQ----HGKALAQLEPLVAVLQSDP----EQFEQLQADYLQAKEQQRRLKqqifalsev 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162902455 337 ----EELSKQEAV--FETLQAEVKQLRAQVKEKQQALSLHNENVEEKIEQLkSDYFELLNSQASIRN----ELQLLDDQM 406
Cdd:COG3096 964 vqrrPHFSYEDAVglLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQY-SQYNQVLASLKSSRDakqqTLQELEQEL 1042
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162902455 407 SQSAVTL-----QRLADNNEKHLQERHDISARKAACETEFARIEQEIHSQVGAYRDMQTKYEQKKRQ 468
Cdd:COG3096 1043 EELGVQAdaeaeERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| |
