|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
1-722 |
0e+00 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 1047.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 1 MLSKNDYAQNDSTDPQQIDLFRMLLELFEYRMCILLVTVCFTIGGGMYAFLATPVYTADALVQIEDKQQNSLLKSLSQFT 80
Cdd:PRK09841 1 MTTKNMNTPPGSTQENEIDLLRLVGELWDHRKFIISVTALFTLIAVAYSLLSTPIYQADTLVQVEQKQGNAILSGLSDMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 81 PSFTPDSTAEIQLLKSRMILGKTVQDLNLQYEIVQSRLPVVGKIWARINNESPGVLKLAWLHFPSTYVGERSLTIITEDN 160
Cdd:PRK09841 81 PNSSPESAPEIQLLQSRMILGKTIAELNLRDIVEQKYFPIVGRGWARLTKEKPGELAISWMHIPQLNGQDQQLTLTVGEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 161 DRFRVEGKGISAKGVRGQLLTAAGVSLRVSELDAPPGTRFTVTLLSLPHAINALHARFSVKDMGKESGILSLSMTGFDPV 240
Cdd:PRK09841 161 GHYTLEGEEFTVNGMVGQRLEKDGVALTIADIKAKPGTQFVLSQRTELEAINALQETFTVSERSKESGMLELTMTGDDPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 241 LLTRILNSIAENYLQQNIARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSVDLTLEAKSVLEQIVNVDNQL 320
Cdd:PRK09841 241 LITRILNSIANNYLQQNIARQAAQDSQSLEFLQRQLPEVRSELDQAEEKLNVYRQQRDSVDLNLEAKAVLEQIVNVDNQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 321 NEITFREAEISQYYKKEHPTYRALREKRQTLEDERARLNKRVSGMPSVQQEILRLSRDVDSGRAIYQQLLTRQQELNISR 400
Cdd:PRK09841 321 NELTFREAEISQLYKKDHPTYRALLEKRQTLEQERKRLNKRVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELSISK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 401 SSTIGNVRIIDAALTQPDPVQPRKALIVLLSTLIGFILSATLVLLKVSLKRGIDSPDQLESQGLNVYATLPRSVWLNERT 480
Cdd:PRK09841 401 SSAIGNVRIIDPAVTQPQPVKPKKALNVVLGFILGLFISVGAVLARAMLRRGVEAPEQLEEHGISVYATIPMSEWLDKRT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 481 RLSRVNFFSSAEKHRTTNVPFLPVDRPLDNFVEAVRGLRTSLHFAMMDAENNILMFSGPTQNCGKTLVSTTLAALVAQVG 560
Cdd:PRK09841 481 RLRKKNLFSNQQRHRTKNIPFLAVDNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 561 ERVLLIDADMRKGYIHNIFSLSNDAGLSDVLSGKVAFSAAVQTYSEASFDVVTCGMAPPNPSELLMHDRFRQFMEWASER 640
Cdd:PRK09841 561 QKVLFIDADLRRGYSHNLFTVSNEHGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDH 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 641 YDMVIIDTPPILAVTDAAVIGHIAASTLLVARHNVTSVKEMLVSVRRLQKSKVEVKGVVVNDFVNSAIDYYSNGYKVYGY 720
Cdd:PRK09841 641 YDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNGVIKRASTAYSYGYNYYGY 720
|
..
gi 2265607537 721 GY 722
Cdd:PRK09841 721 SY 722
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
11-725 |
0e+00 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 825.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 11 DSTDPQQIDLFRMLLELFEYRMCILLVTVCFTIGGGMYAFLATPVYTADALVQIEDKQQNSLLKSLSQFTPSFTPDSTAE 90
Cdd:PRK11519 11 PVTGSDEIDIGRLVGTVIEARWWVIGITAVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSALANKPPASDAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 91 IQLLKSRMILGKTVQDLNLQYEIVQSRLPVVGKIWARINNESPGVLKLAWLHFPSTYvGERSLTIITEDNDRFRVE-GKG 169
Cdd:PRK11519 91 IQLIRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTTFNRPKEM-ADQVFTLNVLDDKNYQLSsDGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 170 ISAKGVRGQLLTAAGVSLRVSELDAPPGTRFTVTLLSLPHAINALHARFSVKDMGKESGILSLSMTGFDPVLLTRILNSI 249
Cdd:PRK11519 170 FSARGQVGQMLKKDGVTLMVEAIHARPGTEFTVTKYSTLGMINNLQNNLTVTENGKDTGVLSLTYTGEDREQIRDILNSI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 250 AENYLQQNIARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSVDLTLEAKSVLEQIVNVDNQLNEITFREAE 329
Cdd:PRK11519 250 TRNYLEQNIERKSEEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQLNELTFKEAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 330 ISQYYKKEHPTYRALREKRQTLEDERARLNKRVSGMPSVQQEILRLSRDVDSGRAIYQQLLTRQQELNISRSSTIGNVRI 409
Cdd:PRK11519 330 ISKLYTKEHPAYRTLLEKRKALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 410 IDAALTQPDPVQPRKALIVLLSTLIGFILSATLVLLKVSLKRGIDSPDQLESQGLNVYATLPRSVWLNERTRLsrvnfFS 489
Cdd:PRK11519 410 VDPAITQPGVLKPKKALIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARDSV-----KT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 490 SAEKHRTTNVPFLPVDRPLDNFVEAVRGLRTSLHFAMMDAENNILMFSGPTQNCGKTLVSTTLAALVAQVGERVLLIDAD 569
Cdd:PRK11519 485 IKGIKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCD 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 570 MRKGYIHNIFSLSNDAGLSDVLSGKVAFSAAVQTYSEASFDVVTCGMAPPNPSELLMHDRFRQFMEWASERYDMVIIDTP 649
Cdd:PRK11519 565 MRKGYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTP 644
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2265607537 650 PILAVTDAAVIGHIAASTLLVARHNVTSVKEMLVSVRRLQKSKVEVKGVVVNDFVNSAIDYYSNGYkvYGYGYEPD 725
Cdd:PRK11519 645 PILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASAYQDYGY--YEYEYKSD 718
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
17-732 |
3.59e-105 |
|
exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273391 [Multi-domain] Cd Length: 764 Bit Score: 338.62 E-value: 3.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 17 QIDLFRMLLELFEYRMCILLVTVCFTIGGGMYAFLATPVYTADALVQIEDkQQNSLLKSLSQFTPSFT--PDSTAEIQLL 94
Cdd:TIGR01005 3 EIDLDRLLAALFANARLIAAFAAAFIALGAAYAFFARPVYEADIMILLDD-NLNKAAEEEGDPSNLFDldTDAAAAIEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 95 KSRMILGKTVQDLNLqYEIVQSRLPV---VGKIWARINNES--------PGVLKLAW---------LHFPSTYVGERsLT 154
Cdd:TIGR01005 82 KSGELAGKAVDKLHL-SENAKILNPPrfpVDLIGAWIKSAAglfsepggFDLGEEAAgneridkaaADIPEALAGEP-FK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 155 IITEDNDRFRVEGKGISA--KGVRGQLLTA----AGVSLRVSELDAPPGTRFTVTLLSLPHAINALHARFSVKDMGKESG 228
Cdd:TIGR01005 160 LISLGAGAFRLEDKLLAApiAGGVAEALEAdqliANFEAQENALTAKAEALFDLEQDSQAAALEMAHDKAEIAEKAAQGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 229 ILSL-SMTGFDPVLLTRILNSIAENYLQQNIARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSVDLTLEAK 307
Cdd:TIGR01005 240 IIGEaQLADLNPALIAAIADQAAAEARADNIKRIADEAEENAVFLAGILPKEGDELEIADLKTNELRNGKGEFDLSDEFG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 308 SVLEQIVNVDNQLNEITFREAEISQYYKKEHPTYRALREKR-QTLEDERARLNKRVSGMPSVQQEILRLSRDVDSGRAIY 386
Cdd:TIGR01005 320 ADHPEAVCSAPSLQELKAKIAEELQQFTASHKGEQAIAQQIeESLRGKINGIAGKLKDAPEIEQDLRELEQDAAADKELY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 387 QQLLTRQQELNISRSSTIGNVRIIDAALTQPDPVQPRKALIVLLSTLIGFILSATLVLLKVSLKRGIDSPDQLESQ-GLN 465
Cdd:TIGR01005 400 ESLLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTLALAAVLGMMLGGAAAAFLEALEGGFRDEGDIEEHlGHR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 466 VYATLPRS-VWLNERTRLSRVNFfSSAEKHRTTNVPFLP--------VDRPLDNFVEAVRGLRTSLHFAMMDAENNILMF 536
Cdd:TIGR01005 480 SLATVPLLdTQMDKKAQLTHAHF-GSVKRHDEAVDDTMPfqllarivPDAPRSTFAEAFRNAKLACDFALADAENNLIAI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 537 SGPTQNCGKTLVSTTLAALVAQVGERVLLIDADMRKGYIHNIFSLSNDAGLSDVLSGKVAFSAAVQTYSEASFDVVTCGM 616
Cdd:TIGR01005 559 AGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLLAGEASIEAGIHRDQRPGLAFIAAGG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 617 A---PPNPSELLMHDRFRQFMEWASERYDMVIIDTPPILAVTDAAVIGHIAASTLLVARHNVTSVKEMLVSVRRLQKSKV 693
Cdd:TIGR01005 639 AshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVTEFERSPLGEIRDLIHQEPHANS 718
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2265607537 694 EVKGVVVNDFVNSAIDYYSNG-------YKVYGYGYEPDLPNAKKA 732
Cdd:TIGR01005 719 DVLGVIFNALDMNELGKYGDFdgaekyrHRQGGYTSENKIPEAEAA 764
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
5-718 |
1.74e-84 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 281.52 E-value: 1.74e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 5 NDYAQNDSTDPQQIDLFRMLLELFEYRMCILLVTVCFTIGGGMYAFLATPVYTADALVQIEDKQQNSLLKSLSQFTPSfT 84
Cdd:COG3206 2 NESSSAPPEEEDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSSLSAS-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 85 PDSTAEIQLLKSRMILGKTVQDLNLQYEIVQSRLpvvgkiwarinnespgvlklawlhfpstyvgersltiitedndrfr 164
Cdd:COG3206 81 SPLETQIEILKSRPVLERVVDKLNLDEDPLGEEA---------------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 165 vegkgisakgvrgqlltaagvslrvseldappgtrftvtllSLPHAINALHARFSVKDmGKESGILSLSMTGFDPVLLTR 244
Cdd:COG3206 115 -----------------------------------------SREAAIERLRKNLTVEP-VKGSNVIEISYTSPDPELAAA 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 245 ILNSIAENYLQQNIARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSVDLTLEAKSVLEQIVNVDNQLNEIT 324
Cdd:COG3206 153 VANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 325 --------------------------------------------FREAEISQYYKKEHPTYRALREKR------------ 348
Cdd:COG3206 233 aelaeaearlaalraqlgsgpdalpellqspviqqlraqlaeleAELAELSARYTPNHPDVIALRAQIaalraqlqqeaq 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 349 -----------------QTLEDERARLNKRVSGMPSVQQEILRLSRDVDSGRAIYQQLLTRQQELNISRSSTIGNVRIID 411
Cdd:COG3206 313 rilasleaelealqareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 412 AALTQPDPVQPRKALIVLLSTLIGFILSATLVLLKVSLKRGIDSPDQLESQGLNVYATLPRSVWLNERTRLSRVnffssa 491
Cdd:COG3206 393 PAVVPLKPVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLLLGLPLLGPLPPLKSKRERRRARL------ 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 492 ekhrttNVPFLPVDRPLDNFVEAVRGLRTSLHFAMMDAENNILMFSGPTQNCGKTLVSTTLAALVAQVGERVLLIDADMR 571
Cdd:COG3206 467 ------ALLLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLL 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 572 KGYIHNIFSLSNDAGLSDVLSGKVAFSAAVQTYSEASFDVVTCGMAPPNPSELLMHDRFRQFMEWASERYDMVIIDTPPI 651
Cdd:COG3206 541 LLLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLL 620
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2265607537 652 LAVTDAAVIGHIAASTLLVARHNVTSVKEMLVSVRRLQKSKVEVKGVVVNDFVNSAIDYYSNGYKVY 718
Cdd:COG3206 621 AALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYYYYYYYYYYY 687
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
513-702 |
8.69e-64 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 210.50 E-value: 8.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 513 EAVRGLRTSLHFAMMDAENNILMFSGPTQNCGKTLVSTTLAALVAQVGERVLLIDADMRKGYIHNIFSLSNDAGLSDVLS 592
Cdd:cd05387 1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 593 GKVAFSAAVQTYSEASFDVVTCGMAPPNPSELLMHDRFRQFMEWASERYDMVIIDTPPILAVTDAAVIGHIAASTLLVAR 672
Cdd:cd05387 81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160
|
170 180 190
....*....|....*....|....*....|
gi 2265607537 673 HNVTSVKEMLVSVRRLQKSKVEVKGVVVND 702
Cdd:cd05387 161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
511-729 |
4.47e-60 |
|
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 204.27 E-value: 4.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 511 FVEAVRGLRTSLHFAMMDAENNILMFSGPTQNCGKTLVSTTLAALVAQVGERVLLIDADMRKGYIHNIFSLSNDAGLSDV 590
Cdd:COG0489 72 LLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 591 LSGKVAFSAAVQTYSEASFDVVTCGMAPPNPSELLMHDRFRQFMEWASERYDMVIIDTPPILAVTDAAVIGHIAASTLLV 670
Cdd:COG0489 152 LAGEASLEDVIQPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLV 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2265607537 671 ARHNVTSVKEMLVSVRRLQKSKVEVKGVVVNDFVNSAIDYYSnGYKVYGYGYEPDLPNA 729
Cdd:COG0489 232 VRPGKTALDDVRKALEMLEKAGVPVLGVVLNMVCPKGERYYG-GGEEYGYREYGDREIA 289
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
513-714 |
1.16e-40 |
|
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273392 [Multi-domain] Cd Length: 204 Bit Score: 147.97 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 513 EAVRGLRTSLHFAMmdAENNILMFSGPTQNCGKTLVSTTLAALVAQVGERVLLIDADMRKGYIHNIFSLSND-AGLSDVL 591
Cdd:TIGR01007 1 EYYNAIRTNIQFSG--AEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKiTGLTNFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 592 SGKVAFSAAVQTYSEASFDVVTCGMAPPNPSELLMHDRFRQFMEWASERYDMVIIDTPPILAVTDAAVIGHIAASTLLVA 671
Cdd:TIGR01007 79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2265607537 672 RHNVTSVKEMLVSVRRLQKSKVEVKGVVVNDF---VNSAIDYYSNG 714
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVdisVSKYGYYGYYG 204
|
|
| EpsG |
TIGR03029 |
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ... |
500-702 |
1.33e-34 |
|
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are homologs of the EpsG protein found in Methylobacillus strain 12S and are generally found in operons with other Eps homologs. The protein is believed to function as the protein tyrosine kinase component of the chain length regulator (along with the transmembrane component EpsF).
Pssm-ID: 132074 [Multi-domain] Cd Length: 274 Bit Score: 133.06 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 500 PFLPVdrpldnfVEAVRGLRTSLHFAMMDAENNILMFSGPTQNCGKTLVSTTLAALVAQVGERVLLIDADMRKGYIHNIF 579
Cdd:TIGR03029 79 PFSPQ-------VEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 580 SLSNDAGLSDVLSGKVAFSAAVQTYSEASFDVVTCGMAPPNPSELLMHDRFRQFMEWASERYDMVIIDTPPILAVTDAAV 659
Cdd:TIGR03029 152 KLSEQRGLSDILAGRSDLEVITHIPALENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQI 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2265607537 660 IGHIAASTLLVARHNVTSVKEMLVSVRRLQKSKVEVKGVVVND 702
Cdd:TIGR03029 232 VATRARGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLNQ 274
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
367-448 |
1.12e-31 |
|
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, pfam02706 and CbiA pfam01656. There is a highly conserved GNVR sequence motif which characterizes this domain. The function is not known.
Pssm-ID: 433492 [Multi-domain] Cd Length: 82 Bit Score: 118.08 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 367 SVQQEILRLSRDVDSGRAIYQQLLTRQQELNISRSSTIGNVRIIDAALTQPDPVQPRKALIVLLSTLIGFILSATLVLLK 446
Cdd:pfam13807 1 DTQQEILRLTRDVEVNTEIYTQLLNSNQELEVVKAGTVGNVRIVDTAVVPPKPVKPKKALIVVLALLLGLMLGVGLVLLR 80
|
..
gi 2265607537 447 VS 448
Cdd:pfam13807 81 RA 82
|
|
| Wzz |
pfam02706 |
Chain length determinant protein; This family includes proteins involved in lipopolysaccharide ... |
17-106 |
8.77e-21 |
|
Chain length determinant protein; This family includes proteins involved in lipopolysaccharide (lps) biosynthesis. This family comprises the whole length of chain length determinant protein (or wzz protein) that confers a modal distribution of chain length on the O-antigen component of lps. This region is also found as part of bacterial tyrosine kinases.
Pssm-ID: 460658 [Multi-domain] Cd Length: 90 Bit Score: 87.34 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 17 QIDLFRMLLELFEYRMCILLVTVCFTIGGGMYAFLATPVYTADALVQIEDKQQNSLLKSLSQFTPSFTPDSTaEIQLLKS 96
Cdd:pfam02706 2 EIDLIELLGVLWKRKKLIILVTLLFTLLAAAYAFLATPKYTATAQILVPQKKGEAGSLLGSDLQAGLQLAST-EIEILKS 80
|
90
....*....|
gi 2265607537 97 RMILGKTVQD 106
Cdd:pfam02706 81 RDVLEKVIDE 90
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
548-701 |
5.54e-16 |
|
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440223 [Multi-domain] Cd Length: 230 Bit Score: 77.62 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 548 VSTTLAALVAQVGERVLLIDADMRKGYIHNIFSLSNDAGLSDVLSGKVAFSAAVQTySEASFDVVTCGMAPPNPSELLMH 627
Cdd:COG0455 2 VAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQ-GPGGLDVLPGGSGPAELAELDPE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2265607537 628 DRFRQFMEWASERYDMVIIDTPPILavtDAAVIGHIAAS--TLLVARHNVTSVKEMLVSVRRL-QKSKVEVKGVVVN 701
Cdd:COG0455 81 ERLIRVLEELERFYDVVLVDTGAGI---SDSVLLFLAAAdeVVVVTTPEPTSITDAYALLKLLrRRLGVRRAGVVVN 154
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
533-701 |
1.41e-13 |
|
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443989 [Multi-domain] Cd Length: 358 Bit Score: 72.84 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 533 ILMFSGPTQNCGKTLVSTTLAALVAQ-VGERVLLIDADMRKGYIHNIFSLSNDAGLSDVLSG-----KVAFSAAVQTYSE 606
Cdd:COG4963 104 VIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNpdrldETLLDRALTRHSS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 607 aSFDVVtCGMAPPNPSELLMHDRFRQFMEWASERYDMVIIDTPPILAVTDAAVIGHiAASTLLVARHNVTSV---KEMLV 683
Cdd:COG4963 184 -GLSVL-AAPADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEA-ADEVVLVTEPDLPSLrnaKRLLD 260
|
170
....*....|....*...
gi 2265607537 684 SVRRLQKSKVEVKgVVVN 701
Cdd:COG4963 261 LLRELGLPDDKVR-LVLN 277
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
543-703 |
1.20e-12 |
|
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 68.35 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 543 CGKTLVSTTLAALVAQVGERVLLIDAD----MRKGYihNIFSLSNDAGLSDVLSGKVAFSAAVQTYSEASFDVVtcgmaP 618
Cdd:COG1192 13 VGKTTTAVNLAAALARRGKRVLLIDLDpqgnLTSGL--GLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGLDLI-----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 619 PNPS------ELL----MHDRFRQFMEWASERYDMVIIDTPPILAV-TDAAVighIAASTLLV-------ARHNVTSVKE 680
Cdd:COG1192 86 ANIDlagaeiELVsrpgRELRLKRALAPLADDYDYILIDCPPSLGLlTLNAL---AAADSVLIpvqpeylSLEGLAQLLE 162
|
170 180
....*....|....*....|...
gi 2265607537 681 MLVSVRRLQKSKVEVKGVVVNDF 703
Cdd:COG1192 163 TIEEVREDLNPKLEILGILLTMV 185
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
534-719 |
2.27e-12 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 66.99 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 534 LMFSGPTQNCGKTLVSTTLAALVAQVGERVLLIDAD---------MRKGYIHNIFSLsndagLSDVLSGKVAFSAAVQT- 603
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpqsnnssveGLEGDIAPALQA-----LAEGLKGRVNLDPILLKe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 604 -YSEASFDVVTCGMAPPNPSELLMHDRFRQFMEWA----SERYDMVIIDTPP---------ILAVTDAAVIGHiaASTLL 669
Cdd:pfam01656 76 kSDEGGLDLIPGNIDLEKFEKELLGPRKEERLREAlealKEDYDYVIIDGAPglgellrnaLIAADYVIIPLE--PEVIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2265607537 670 VArhnvtSVKEMLVSVRRLQKS----KVEVKGVVVNDFVN--------SAIDYYSNGYKVYG 719
Cdd:pfam01656 154 VE-----DAKRLGGVIAALVGGyallGLKIIGVVLNKVDGdnhgkllkEALEELLRGLPVLG 210
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
544-711 |
1.20e-11 |
|
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.
Pssm-ID: 349758 [Multi-domain] Cd Length: 230 Bit Score: 64.90 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 544 GKTLVSTTLAALVAQVGERVLLIDADMRKGYIHNIFSLSNDAGLSDVLSGKVAFSAAVQTYSEaSFDVV-----TCGMAP 618
Cdd:cd02038 13 GKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGPE-GLDIIpggsgMEELAN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 619 PNPSellMHDRFRQFMEWASERYDMVIIDTPP----------------IL-------AVTDA-AVIGHIAAS----TLLV 670
Cdd:cd02038 92 LDPE---QKAKLIEELSSLESNYDYLLIDTGAgisrnvldfllaadevIVvttpeptSITDAyALIKVLSRRggkkNFRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2265607537 671 ARHNVTSVKEMLVSVRRLQKskvevkgvVVNDFVNSAIDYY 711
Cdd:cd02038 169 IVNMARSPKEGRATFERLKK--------VAKRFLDINLDFV 201
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
227-450 |
2.94e-11 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 65.64 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 227 SGILSLSMTGFDP---VLLTRILNSIAENYLQQnIARQAAQDsqsldflqrQLPKVRSELDNAEQRLND-------YRRQ 296
Cdd:COG3524 137 SGIITLEVRAFDPedaQAIAEALLAESEELVNQ-LSERARED---------AVRFAEEEVERAEERLRDareallaFRNR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 297 RDSVDLTLEAKSVLEQIVNVDNQLNEITFREAEISQYYKKEHPTYRALREKRQTLEDERARLNKRVSG------MPSVQQ 370
Cdd:COG3524 207 NGILDPEATAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGasggdsLASLLA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 371 EILRLSRDVDSGRAIYQQLLTRQQElniSRSSTIGNVRIIdAALTQP----DPVQPRKALIVLLSTLIGFILSATLVLLK 446
Cdd:COG3524 287 EYERLELEREFAEKAYTSALAALEQ---ARIEAARQQRYL-AVIVQPtlpdEALYPRRLYNILLVFLILLLLYGIGSLLV 362
|
....
gi 2265607537 447 VSLK 450
Cdd:COG3524 363 ASIR 366
|
|
| WzzB |
COG3765 |
LPS O-antigen chain length determinant protein, WzzB/FepE family [Cell wall/membrane/envelope ... |
1-451 |
1.31e-10 |
|
LPS O-antigen chain length determinant protein, WzzB/FepE family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442979 [Multi-domain] Cd Length: 364 Bit Score: 63.84 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 1 MLSKNDYAQNDSTDPQQ----IDLFRMLLELFEYRMCILLVTVCFTIGGGMYAFLATPVYTADALVQIEDKQQNSLLKSL 76
Cdd:COG3765 1 MSSEESKQLYPNQYPPSqddeIDLFELLRTLWQGKLWIIGITLLFALLALVYAFLLPQKWTSTAIVDPPTVNELGGYYSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 77 SQF-----TPSFTPDSTAE------IQLLKSrmilgktvQDLNLQYeIVQSRLPvvgKIWARINNESPGVLkLAWLhfps 145
Cdd:COG3765 81 RQFlrnldVKSVDPPVISSelfnefIKQLSS--------YDLRREF-LLQSDYY---KQLQEGDEKEDAAL-LDEL---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 146 tyvgERSLTIITEDNdrfrvegkgisakgvrgqlltaagvslrvseldappgtrftvtllslphainalharfsvKDMGK 225
Cdd:COG3765 144 ----INNISITPPDD------------------------------------------------------------KKKSS 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 226 ESGILSLSMTGFDPVLLTRIL-------NSIAENYLQQNIARQAAQDSQSLDF-LQRQLPKVRSELDNAEQRLNdyrrqr 297
Cdd:COG3765 160 PYTNYSVSFTAETPEDAQQLLrgyidfaNQRVLKELNEELQGAIAARLQSLKAqIKRLEEVAKAQRQRRIERLK------ 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 298 dsvdltlEAKSVLEQivnvdnqlneitfreAEISQyykkehPTYRALREKRQTLEDE----------RARLnkrvsgmps 367
Cdd:COG3765 234 -------YALKIAQA---------------AGIKK------PVYSNGQTPAVKLDPSylfllgtdalQAEL--------- 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 368 vqqEILRLSRDVDSGRAIYQQLLTRQQELNISRSSTIG--NVRIIDAALTQPDPVQPRKALIVLLSTLIGFILSATLVLL 445
Cdd:COG3765 277 ---EILKARGDDYPLNADLYQLQAQLAQLNALPIDDVGfqPFRYLRTPEEPVKKDKPKRALILVLGALLGGMLGVGVVLI 353
|
....*.
gi 2265607537 446 KVSLKR 451
Cdd:COG3765 354 RHALRS 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
250-375 |
8.78e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 250 AENYLQQNIARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSVDLTL--EAKSVLEQIVNVDNQLNEITFRE 327
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpaSAEEFAALRAEAAALLEALEEEL 400
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2265607537 328 AEISQYYKKEHPTYRALREKRQTLEDERARLNKRVSGMPSVQQEILRL 375
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
403-569 |
3.99e-08 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 55.46 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 403 TIGNVRIIDAALTQPDPVQPRKALIVLLSTLIGFILSATLVLLKVSLKRGIDSPDQLEsqglnvyatlprsvwlnERTRL 482
Cdd:COG3944 146 KVDNVTVLDPATVPASPVSPNPKLNLAIGLVLGLLLGVGLAFLRELLDTTIRSEEDIE-----------------RLLGL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 483 SRVNFFSSAEKHRTTNVPFLPVDRPLDNFVEAVRGLRTSLHFAMMDAennILMFSGPTQNCGKTLVSTTLAALVAQVGER 562
Cdd:COG3944 209 LLGGAVPAARSARPLLLLLADASPRAAAARRRRRNLLFALAAVDART---VVVVSSSLSEGKSTTTAALALALAAAAAGV 285
|
....*..
gi 2265607537 563 VLLIDAD 569
Cdd:COG3944 286 VLVLADL 292
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
544-701 |
6.87e-08 |
|
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.
Pssm-ID: 131024 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 544 GKTLVSTTLAALVAQVGERVLLIDADMRKGYIHNIFSLSN-DAGLSDVLSGKVAFSAAVqtYsEASFDVVtcgMAPPNPS 622
Cdd:TIGR01969 13 GKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDkPVTLHDVLAGEADIKDAI--Y-EGPFGVK---VIPAGVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 623 -ELLMH---DRFRQFMEWASERYDMVIIDTPPILAVTDAAVIGhIAASTLLVARHNVTSVKEMLVSVRRLQKSKVEVKGV 698
Cdd:TIGR01969 87 lEGLRKadpDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALA-AADELLLVVNPEISSITDALKTKIVAEKLGTAILGV 165
|
...
gi 2265607537 699 VVN 701
Cdd:TIGR01969 166 VLN 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
243-445 |
7.33e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 243 TRILNSIAENYLQQNIaRQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSVDLTLEAKSVLEQIVNVDNQLNE 322
Cdd:COG4717 65 KPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 323 ITFR----EAEISQYYKKEHpTYRALREKRQTLEDERARLNKRVSgmPSVQQEILRLSRDVDSGRAIYQQLLTRQQELNI 398
Cdd:COG4717 144 LPERleelEERLEELRELEE-ELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2265607537 399 SRSSTIGNVRIIDAALTQPDPVQPRKALIVLLstligFILSATLVLL 445
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLL-----LIAAALLALL 262
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
544-670 |
1.70e-06 |
|
AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.
Pssm-ID: 433350 [Multi-domain] Cd Length: 177 Bit Score: 48.73 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 544 GKTLVSTTLAALVAQVGERVLLIDADM------RKGYIHNifslSNDAGLSDVLSGKVAFSAAVQTYSEASFDVVtcgma 617
Cdd:pfam13614 14 GKTTTSVNLAAALAKKGKKVLLIDLDPqgnatsGLGIDKN----NVEKTIYELLIGECNIEEAIIKTVIENLDLI----- 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2265607537 618 ppnPS---------ELLM----HDRFRQFMEWASERYDMVIIDTPPILAVTdaAVIGHIAASTLLV 670
Cdd:pfam13614 85 ---PSnidlagaeiELIGienrENILKEALEPVKDNYDYIIIDCPPSLGLL--TINALTASDSVLI 145
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
543-670 |
3.08e-06 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 48.70 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 543 CGKTLVSTTLAALVAQVGERVLLIDADMRKgyihnifSLSndaglsdvlsgkvAFSAAVQTysEASFDVVtcGMAPPNps 622
Cdd:NF041546 11 VGKTTLATHLAAALARRGYRVLLVDADPQG-------SAL-------------DWAAARED--ERPFPVV--GLARPT-- 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2265607537 623 ellmhdrFRQFMEWASERYDMVIIDTPPilAVTDAAVIGHIAASTLLV 670
Cdd:NF041546 65 -------LHRELPSLARDYDFVVIDGPP--RAEDLARSAIKAADLVLI 103
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
544-701 |
1.76e-05 |
|
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.
Pssm-ID: 349755 [Multi-domain] Cd Length: 250 Bit Score: 46.73 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 544 GKTLVSTTLAALVAQVGERVLLI------------DADMRKGYIHNIFS-LS------------NDAGLSDVLSGKVAFS 598
Cdd:cd02035 12 GKTTIAAATAVRLAEQGKRVLLVstdpahslsdafGQKLGGETPVKGAPnLWameidpeealeeYWEEVKELLAQYLRLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 599 AAVQTYSEASfdvvtcgMAPPNPSELLMHDRFRQFMEwaSERYDMVIIDTPPilavTdaaviGHiaasTL---------- 668
Cdd:cd02035 92 GLDEVYAEEL-------LSLPGMDEAAAFDELREYVE--SGEYDVIVFDTAP----T-----GH----TLrllslpleqv 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2265607537 669 -------------LVARHNVTSVKEMLVSVRRLQKSKVEVKGVVVN 701
Cdd:cd02035 150 rellrdperttfvLVTIPEKLSIYETERLWGELQQYGIPVDGVVVN 195
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
549-708 |
2.47e-05 |
|
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.
Pssm-ID: 349765 [Multi-domain] Cd Length: 235 Bit Score: 46.12 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 549 STTLAALVAQV-----GERVLLIDADMRKGYIHNIFSLSNDAGLSDVLS-----GKVAFSAAVQTYSeASFDVVTCgmap 618
Cdd:cd03111 14 ASTLAVNLAQElaqraKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQnldrlDRTLLDSAVTRHS-SGLSLLPA---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 619 PNPSELLMH---DRFRQFMEWASERYDMVIIDTPPILAVTDAAVIGHiAASTLLVARHNVTSV---KEMLVSVRRLQKSK 692
Cdd:cd03111 89 PQELEDLEAlgaEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEA-ADEILLVTQQDLPSLrnaRRLLDSLRELEGSS 167
|
170
....*....|....*..
gi 2265607537 693 VEVKgVVVNDF-VNSAI 708
Cdd:cd03111 168 DRLR-LVLNRYdKKSEI 183
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
18-111 |
3.08e-05 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 46.60 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 18 IDLFRMLLELFEYRMCILLVTVCFTIGGGMYAFLATPVYTADA--LVQIEDKQQNSLLKSLSQFTPSFTPDSTaeiQLLK 95
Cdd:COG3944 2 MDLREYLRILRRRWWLILLLTLLGALAALASSFLITPVYQASTtlLVSTSSGSDASDLYQGIQTAQQLVNTYA---ELLK 78
|
90
....*....|....*.
gi 2265607537 96 SRMILGKTVQDLNLQY 111
Cdd:COG3944 79 SPAVLEEVIDELGLDL 94
|
|
| PRK15471 |
PRK15471 |
chain length determinant protein WzzB; Provisional |
1-69 |
3.60e-05 |
|
chain length determinant protein WzzB; Provisional
Pssm-ID: 185368 [Multi-domain] Cd Length: 325 Bit Score: 46.67 E-value: 3.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2265607537 1 MLSKNDYAQNDSTDPQQIDLFRMLLELFEYRMCILLVTVCFTIGGGMYAFLATPVYTADALVQIEDKQQ 69
Cdd:PRK15471 1 MRVENNNVSGQNHDPEQIDLIDLLVQLWRGKMTIIISVIVAIALAVGYLAVAKEKWTSTAIITQPDVGQ 69
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
254-473 |
1.22e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.52 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 254 LQQNIARQAAQDSQSLdflQRQLPKVRSELDNAEQRLN---DYRRQRDSVDLTLEAKSVLEQIVNV-DNQLNEITFREAE 329
Cdd:pfam09731 299 LSKKLAELKKREEKHI---ERALEKQKEELDKLAEELSarlEEVRAADEAQLRLEFEREREEIRESyEEKLRTELERQAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 330 ISQYYKKEhptyrALREKRQTLEDERAR-LNKRVSgmpsvQQEILRLSrDVDSG----RAIYQQLLTRQQELNISRSST- 403
Cdd:pfam09731 376 AHEEHLKD-----VLVEQEIELQREFLQdIKEKVE-----EERAGRLL-KLNELlanlKGLEKATSSHSEVEDENRKAQq 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2265607537 404 -IGNVRIIDAALTQPDPVQPRKALIVLLSTLIG------FILSATLVLLKVSLKRGIDSPDQLESQGLNVYATLPRS 473
Cdd:pfam09731 445 lWLAVEALRSTLEDGSADSRPRPLVRELKALKElasddeVVKAALASLPEEAYQRGVYTEAALRERFRRVAKEVRKV 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
282-378 |
2.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 282 ELDNAEQRLNDYRRQRDSVDLTLEAKSvlEQIVNVDNQLNEITFREAEISQYYKKEhpTYRALREKRQTLEDERARLNKR 361
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAF--EELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAE 681
|
90
....*....|....*..
gi 2265607537 362 VSGMPSVQQEILRLSRD 378
Cdd:PRK03918 682 LEELEKRREEIKKTLEK 698
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-395 |
4.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 258 IARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSVDLTLEAKSVLEQIVNVDNQLNEITFREAEISQYYKKe 337
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQ- 693
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2265607537 338 hptYRALREKRQTLEDERARLNKRVSGmpsVQQEILRLSRDVDSGRAIYQQLLTRQQE 395
Cdd:COG4913 694 ---LEELEAELEELEEELDELKGEIGR---LEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
247-399 |
4.95e-04 |
|
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: 43.51 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 247 NSIAEnyLQQNIARQAAQdsqsLDFLQRQLPKVRSELDNAEQRLNDYRRQ-----RDSVDLTLEAKSVLEQIVNVDNQLN 321
Cdd:TIGR02168 677 REIEE--LEEKIEELEEK----IAELEKALAELRKELEELEEELEQLRKEleelsRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2265607537 322 EITFREAEISQYYKKEHPTYRALREKRQTLEDERARLnkrvsgmpsvQQEILRLSRDVDSGRAIYQQLLTRQQELNIS 399
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL----------EAQIEQLKEELKALREALDELRAELTLLNEE 818
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
254-431 |
9.21e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 254 LQQNIARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSVDLTLEAKSvlEQIVNVDNQLNEItfrEAEISQY 333
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR--SELEQLEEELEEL---NEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 334 YKKEHPTYRALREKRQTLEDERARLNKRVSGMPSVQQEILRLSRDVDSGRAIYQQLLTRQQELNISRSSTIGNVRIIDAA 413
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170
....*....|....*...
gi 2265607537 414 LTQPDPVQPRKALIVLLS 431
Cdd:COG4372 173 LQALSEAEAEQALDELLK 190
|
|
| PRK10381 |
PRK10381 |
LPS O-antigen length regulator; Provisional |
422-460 |
1.44e-03 |
|
LPS O-antigen length regulator; Provisional
Pssm-ID: 182422 [Multi-domain] Cd Length: 377 Bit Score: 41.59 E-value: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2265607537 422 PRKALIVLLSTLIGFILSATLVLLK---VSLKRGIDSPDQLE 460
Cdd:PRK10381 336 PGKALIVILAALIGGMLACGFVLLRhamRSRKQDLMLADHLV 377
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-395 |
1.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 259 ARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDsvDLTLEAKSVLEQIVNVD-NQLNEItfrEAEIsqyykke 337
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD--ALREELDELEAQIRGNGgDRLEQL---EREI------- 347
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2265607537 338 hptyRALREKRQTLEDERARLNKRVSGM----PSVQQEILRLSRDVDSGRAIYQQLLTRQQE 395
Cdd:COG4913 348 ----ERLERELEERERRRARLEALLAALglplPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| BexC_CtrB_KpsE |
TIGR01010 |
polysaccharide export inner-membrane protein, BexC/CtrB/KpsE family; This family contains ... |
227-450 |
3.39e-03 |
|
polysaccharide export inner-membrane protein, BexC/CtrB/KpsE family; This family contains gamma proteobacterial proteins involved in capsule polysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130083 [Multi-domain] Cd Length: 362 Bit Score: 40.47 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 227 SGILSLSMTGFDPVLLTRilnsIAENYLQQN------IARQAAQDsqSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSV 300
Cdd:TIGR01010 130 SGILTLNVTAFDAEEAQK----INQRLLKEGerlinrLNERARKD--TIAFAENEVKEAEQRLNATKAELLKYQIKNKVF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 301 DLTLEAKSVLEQIVNVDNQLNEITFREAEISQYYKKEHPTYRALREKRQTLE----DERARL-NKRVSGMPSVQQEILRL 375
Cdd:TIGR01010 204 DPKAQSSAQLSLISTLEGELIRVQAQLAQLRSITPEQNPQVPSLQARIKSLRkqidEQRNQLsGGLGDSLNEQTADYQRL 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2265607537 376 SRDVDSGRAIYQQLLTRQQELNISRSSTIGNVRIIDAALTQPDPVQPRKALIVLLSTLIGFILSATLVLLKVSLK 450
Cdd:TIGR01010 284 VLQNELAQQQLKAALTSLQQTRVEADRQQLYLEVISQPSLPDDALEPYRLYNILATFVILLILYGVLSLLLASIR 358
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
274-363 |
3.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 274 RQLPKVRSELDNAEQRLNDYRRQRDSVDLTLEA-------KSVLEQIVNVDNQLNEITFREAEisqyykKEHPTYRALRE 346
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliklKELAEQLKELEEKLKKYNLEELE------KKAEEYEKLKE 532
|
90
....*....|....*..
gi 2265607537 347 KRQTLEDERARLNKRVS 363
Cdd:PRK03918 533 KLIKLKGEIKSLKKELE 549
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-397 |
4.15e-03 |
|
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: 40.81 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 261 QAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRDSV-----DLTLEAKSVLEQIVNVDNQLNEITFR----EAEIS 331
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskvaQLELQIASLNNEIERLEARLERLEDRrerlQQEIE 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265607537 332 QYYKKEHP-----TYRALREKRQTLEDERARLNKRVSGMPSVQQEILRLSRDVDSGRAIYQQLLTRQQELN 397
Cdd:TIGR02168 425 ELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
543-701 |
4.43e-03 |
|
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.
Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 37.90 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 543 CGKTLVSTTLAALVAQVGERVLLIDADMRKgyihnifSLSndaglsdvlsgkvafsaavqtyseasfdvvtcgmappnps 622
Cdd:cd02042 12 VGKTTLAVNLAAALALRGKRVLLIDLDPQG-------SLT---------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 623 ellmhdrfrqfmEWAserYDMVIIDTPPIL-AVTDAAvighIAASTLLV--------ARHNVTSVKEMLVSVRRLQKSKV 693
Cdd:cd02042 45 ------------SWL---YDYILIDTPPSLgLLTRNA----LAAADLVLipvqpspfDLDGLAKLLDTLEELKKQLNPPL 105
|
....*...
gi 2265607537 694 EVKGVVVN 701
Cdd:cd02042 106 LILGILLT 113
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
544-701 |
5.45e-03 |
|
septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.
Pssm-ID: 349756 [Multi-domain] Cd Length: 236 Bit Score: 39.11 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 544 GKTLVSTTLAALVAQVGERVLLIDAD--MRkgyihN---IFSLSNDA--GLSDVLSGKVAFSAAVqtYSEASFDVVtCGM 616
Cdd:cd02036 13 GKTTTTANLGVALAKLGKKVLLIDADigLR-----NldlILGLENRIvyTLVDVLEGECRLEQAL--IKDKRWENL-YLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 617 APPNPSELLMHDR--FRQFMEWASERYDMVIIDTPpilavtdaAVIG---HIAAS----TLLVARHNVTSVKEMLVSVRR 687
Cdd:cd02036 85 PASQTRDKDALTPekLEELVKELKDSFDFILIDSP--------AGIEsgfINAIApadeAIIVTNPEISSVRDADRVIGL 156
|
170
....*....|....
gi 2265607537 688 LQKSKVEVKGVVVN 701
Cdd:cd02036 157 LESKGIVNIGLIVN 170
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
241-439 |
6.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 241 LLTRILNSIAENYLQQNiARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLndyRRQRDSVDLTLEAKSVLEQIVNVDNQL 320
Cdd:PRK04863 481 LVRKIAGEVSRSEAWDV-ARELLRRLREQRHLAEQLQQLRMRLSELEQRL---RQQQRAERLLAEFCKRLGKNLDDEDEL 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 321 NEITFR-EAEI---SQYYKKEHPTYRALREKRQTLEDERARLNKRVSGMPSVQQEILRL----------SRDVDSGRaiy 386
Cdd:PRK04863 557 EQLQEElEARLeslSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLreqsgeefedSQDVTEYM--- 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2265607537 387 QQLLTRQQELNISRSSTIGNVRIIDA---ALTQPD-PVQPRkaLIVLLSTLIGFILS 439
Cdd:PRK04863 634 QQLLERERELTVERDELAARKQALDEeieRLSQPGgSEDPR--LNALAERFGGVLLS 688
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
259-439 |
7.01e-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: 39.94 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 259 ARQAAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRR-QRDSVDLTLEAKSVLEQIVNVDNQLNEITFREAEISQYYKKE 337
Cdd:COG3096 497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNaERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 338 HPTYRALREKRQTLEDERARLNKRVSGMPSVQQEILRL----------SRDVDSGRaiyQQLLTRQQELNISRSSTIGNV 407
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLreqsgealadSQEVTAAM---QQLLEREREATVERDELAARK 653
|
170 180 190
....*....|....*....|....*....|....*.
gi 2265607537 408 RIIDAA---LTQPD-PVQPRkaLIVLLSTLIGFILS 439
Cdd:COG3096 654 QALESQierLSQPGgAEDPR--LLALAERLGGVLLS 687
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
262-397 |
7.31e-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: 39.36 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265607537 262 AAQDSQSLDFLQRQLPKVRSELDNAEQRLNDYRRQRdsvdltleaKSVLEQIVNVDNQLNeitfreaeisqyykkehpty 341
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE---------KALLKQLAALERRIA-------------------- 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2265607537 342 rALREKRQTLEDERARLNKRVSgmpSVQQEILRLSRDVDSGRAIYQQLLTRQQELN 397
Cdd:COG4942 66 -ALARRIRALEQELAALEAELA---ELEKEIAELRAELEAQKEELAELLRALYRLG 117
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
532-569 |
7.51e-03 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 36.64 E-value: 7.51e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2265607537 532 NILMFSGPTQNCGKTLVSTTLAALVAQVGERVLLIDAD 569
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| |
