|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
13-731 |
0e+00 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 1399.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 13 MTDKVRHSAAPVEGGDEIDIGRLVGTVVEARWWVLGITALFALGALIYVMFATPIYSADALVQIEQNQGNSLVQDISTAL 92
Cdd:PRK11519 1 MTEKVKQHAAPVTGSDEIDIGRLVGTVIEARWWVIGITAVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 93 QNKPPASDAEIQLIQSRLVLGKTVDDLDLDIAVQKKTFPLFGSGWERLMGRADETIKVTTFELPKGMAEDEFTVAVLGPK 172
Cdd:PRK11519 81 ANKPPASDAEIQLIRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTTFNRPKEMADQVFTLNVLDDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 173 QYQLTSSGGFSARGEVGKPLSKDGVKMMVDQIHAQEGSEFTVTKYSTLGMINQLQNNLTVTETGKDTGVLSLTYMGEDRD 252
Cdd:PRK11519 161 NYQLSSDGGFSARGQVGQMLKKDGVTLMVEAIHARPGTEFTVTKYSTLGMINNLQNNLTVTENGKDTGVLSLTYTGEDRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 253 QIRDILNSITRNYLEQNIERKSEEAAKSLAFLAKQLPEVRSNLDIAENKLNAYRQQQDSVDLPLEAKAVLDSMVNIDAQL 332
Cdd:PRK11519 241 QIRDILNSITRNYLEQNIERKSEEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 333 NELTFKEAEISKLYTKAHPAYRTLLEKRQALEDEKAKLNNRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITE 412
Cdd:PRK11519 321 NELTFKEAEISKLYTKEHPAYRTLLEKRKALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 413 ASTVGDVRIVDPAITQPGVVKPKKALIVLGSIILGLLLSIVIVLLRSLFNRGIESPLALEEAGINVYASIPLSEWQKSRD 492
Cdd:PRK11519 401 ASTVGDVRIVDPAITQPGVLKPKKALIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 493 SVKTVKGVKRFKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAPNNVLMLTGVSPSIGKTFVCANLAAVISQTHKRVLL 572
Cdd:PRK11519 481 SVKTIKGIKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 573 IDCDMRKGYTHELLGTTNVNGLSDVLAGQGDISRCAQKTSVPGFDLVPRGQVPPNPSELLMSERFAELVKWASANYDMVL 652
Cdd:PRK11519 561 IDCDMRKGYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVL 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260217726 653 IDTPPILAVTDAAVVGRHAGTTLMVARYAVNTLKEVQTSLSRFEQNGIEVRGVILNSIFRRASGYQDYGYYEYEYKSDH 731
Cdd:PRK11519 641 IDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASAYQDYGYYEYEYKSDA 719
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
13-732 |
0e+00 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 797.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 13 MTDKVRHSAAPVEGGDEIDIGRLVGTVVEARWWVLGITALFALGALIYVMFATPIYSADALVQIEQNQGNSLVQDISTAL 92
Cdd:PRK09841 1 MTTKNMNTPPGSTQENEIDLLRLVGELWDHRKFIISVTALFTLIAVAYSLLSTPIYQADTLVQVEQKQGNAILSGLSDMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 93 QNKPPASDAEIQLIQSRLVLGKTVDDLDLDIAVQKKTFPLFGSGWERLMGRADETIKVTTFELPKGMAEDE-FTVAVLGP 171
Cdd:PRK09841 81 PNSSPESAPEIQLLQSRMILGKTIAELNLRDIVEQKYFPIVGRGWARLTKEKPGELAISWMHIPQLNGQDQqLTLTVGEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 172 KQYQLTSSGgFSARGEVGKPLSKDGVKMMVDQIHAQEGSEFTVTKYSTLGMINQLQNNLTVTETGKDTGVLSLTYMGEDR 251
Cdd:PRK09841 161 GHYTLEGEE-FTVNGMVGQRLEKDGVALTIADIKAKPGTQFVLSQRTELEAINALQETFTVSERSKESGMLELTMTGDDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 252 DQIRDILNSITRNYLEQNIERKSEEAAKSLAFLAKQLPEVRSNLDIAENKLNAYRQQQDSVDLPLEAKAVLDSMVNIDAQ 331
Cdd:PRK09841 240 QLITRILNSIANNYLQQNIARQAAQDSQSLEFLQRQLPEVRSELDQAEEKLNVYRQQRDSVDLNLEAKAVLEQIVNVDNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 332 LNELTFKEAEISKLYTKAHPAYRTLLEKRQALEDEKAKLNNRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKIT 411
Cdd:PRK09841 320 LNELTFREAEISQLYKKDHPTYRALLEKRQTLEQERKRLNKRVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELSIS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 412 EASTVGDVRIVDPAITQPGVVKPKKALIVLGSIILGLLLSIVIVLLRSLFNRGIESPLALEEAGINVYASIPLSEW--QK 489
Cdd:PRK09841 400 KSSAIGNVRIIDPAVTQPQPVKPKKALNVVLGFILGLFISVGAVLARAMLRRGVEAPEQLEEHGISVYATIPMSEWldKR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 490 SRDSVKTVKGVK---RFKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAPNNVLMLTGVSPSIGKTFVCANLAAVISQT 566
Cdd:PRK09841 480 TRLRKKNLFSNQqrhRTKNIPFLAVDNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 567 HKRVLLIDCDMRKGYTHELLGTTNVNGLSDVLAGQGDISRCAQKTSVPGFDLVPRGQVPPNPSELLMSERFAELVKWASA 646
Cdd:PRK09841 560 DQKVLFIDADLRRGYSHNLFTVSNEHGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWAND 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 647 NYDMVLIDTPPILAVTDAAVVGRHAGTTLMVARYAVNTLKEVQTSLSRFEQNGIEVRGVILNSIFRRASGYQDYGYYEYE 726
Cdd:PRK09841 640 HYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNGVIKRASTAYSYGYNYYG 719
|
....*.
gi 260217726 727 YKSDHK 732
Cdd:PRK09841 720 YSYSEK 725
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
29-732 |
1.48e-109 |
|
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: 350.17 E-value: 1.48e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 29 EIDIGRLVGTVVEARWWVLGITALFALGALIYVMFATPIYSADALVQIEQN--QGNSLVQDISTaLQNKPPASDAEIQLI 106
Cdd:TIGR01005 3 EIDLDRLLAALFANARLIAAFAAAFIALGAAYAFFARPVYEADIMILLDDNlnKAAEEEGDPSN-LFDLDTDAAAAIEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 107 QSRLVLGKTVDDLDLDIAVQKKTFPLF-----------------GSGWERLMGRA--DETIKVTTFELPKGMAEDEFTVA 167
Cdd:TIGR01005 82 KSGELAGKAVDKLHLSENAKILNPPRFpvdligawiksaaglfsEPGGFDLGEEAagNERIDKAAADIPEALAGEPFKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 168 VLGPKQYQLTS-SGGFSARGEVGKPLSKD----GVKMMVDQIHAQEGSEFTVTKYSTLGMINQLQNNLTVTETGKDTGVL 242
Cdd:TIGR01005 162 SLGAGAFRLEDkLLAAPIAGGVAEALEADqliaNFEAQENALTAKAEALFDLEQDSQAAALEMAHDKAEIAEKAAQGEII 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 243 SLTYMGEDRDQ-IRDILNSITRNYLEQNIERKSEEAAKSLAFLAKQLPEVRSNLDIAENKLNAYRQQQDSVDLPLEAKAV 321
Cdd:TIGR01005 242 GEAQLADLNPAlIAAIADQAAAEARADNIKRIADEAEENAVFLAGILPKEGDELEIADLKTNELRNGKGEFDLSDEFGAD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 322 LDSMVNIDAQLNELTFKEAEISKLYTKAHPAYRTLLEKRQALEDEKAK-LNNRVTAMPKTQQEIVRLTRDVESGQQVYMQ 400
Cdd:TIGR01005 322 HPEAVCSAPSLQELKAKIAEELQQFTASHKGEQAIAQQIEESLRGKINgIAGKLKDAPEIEQDLRELEQDAAADKELYES 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 401 LLNKQQELKITEASTVGDVRIVDPAITQPGVVKPKKALIVLGSIILGLLLSIVIVLLRSLFNRGIESPLALEE-AGINVY 479
Cdd:TIGR01005 402 LLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTLALAAVLGMMLGGAAAAFLEALEGGFRDEGDIEEhLGHRSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 480 ASIPLSEWQ---------KSRDSVKTV-KGVKRFKQSQLLA---VGNPTDLAIEAIRSLRTSLHFAMMQAPNNVLMLTGV 546
Cdd:TIGR01005 482 ATVPLLDTQmdkkaqlthAHFGSVKRHdEAVDDTMPFQLLArivPDAPRSTFAEAFRNAKLACDFALADAENNLIAIAGA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 547 SPSIGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTNVNGLSDVLAGQGDISRCAQKTSVPGFDLVPRGQV-- 624
Cdd:TIGR01005 562 LPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLLAGEASIEAGIHRDQRPGLAFIAAGGAsh 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 625 -PPNPSELLMSERFAELVKWASANYDMVLIDTPPILAVTDAAVVGRHAGTTLMVARYAVNTLKEVQTSLSRFEQNGIEVR 703
Cdd:TIGR01005 642 fPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVTEFERSPLGEIRDLIHQEPHANSDVL 721
|
730 740 750
....*....|....*....|....*....|....*.
gi 260217726 704 GVILNSI-------FRRASGYQDYGYYEYEYKSDHK 732
Cdd:TIGR01005 722 GVIFNALdmnelgkYGDFDGAEKYRHRQGGYTSENK 757
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
20-725 |
8.66e-85 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 282.29 E-value: 8.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 20 SAAPVEGGDEIDIGRLVGTVVEARWWVLGITALFALGALIYVMFATPIYSADALVQIEQNQGNSLVQDISTALQNKPPAs 99
Cdd:COG3206 5 SSAPPEEEDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSSLSASDSPL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 100 DAEIQLIQSRLVLGKTVDDLDLDiavqkktfplfgsgwerlmgradetikvttfELPKGmaedeftvavlgpkqyqltss 179
Cdd:COG3206 84 ETQIEILKSRPVLERVVDKLNLD-------------------------------EDPLG--------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 180 ggfsargevgkplskdgvkmmvdqihaqegseftvTKYSTLGMINQLQNNLTVTETgKDTGVLSLTYMGEDRDQIRDILN 259
Cdd:COG3206 112 -----------------------------------EEASREAAIERLRKNLTVEPV-KGSNVIEISYTSPDPELAAAVAN 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 260 SITRNYLEQNIERKSEEAAKSLAFLAKQLPEVRSNLDIAENKLNAYRQQQDSVDLPLEAKAVLDSMVNIDAQLN------ 333
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAearael 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 334 --------------------------------------ELTFKEAEISKLYTKAHPAYRTLLEKR--------------- 360
Cdd:COG3206 236 aeaearlaalraqlgsgpdalpellqspviqqlraqlaELEAELAELSARYTPNHPDVIALRAQIaalraqlqqeaqril 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 361 --------------QALEDEKAKLNNRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRIVDPAI 426
Cdd:COG3206 316 asleaelealqareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPAV 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 427 TQPGVVKPKKALIVLGSIILGLLLSIVIVLLRSLFNRGIESPLALEEAGINVYASIPLSEWQKSRDSvktvkgvKRFKQS 506
Cdd:COG3206 396 VPLKPVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLLLGLPLLGPLPPLKSKRERR-------RARLAL 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 507 QLLAVGNPTDLAIEAIRSLRTSLHFAMMQAPNNVLMLTGVSPSIGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELL 586
Cdd:COG3206 469 LLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLLLLLLLLL 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 587 GTTNVNGLSDVLAGQGDISRCAQKTSVPGFDLVPRGQVPPNPSELLMSERFAELVKWASANYDMVLIDTPPILAVTDAAV 666
Cdd:COG3206 549 LLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLAALLAAAV 628
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 260217726 667 VGRHAGTTLMVARYAVNTLKEVQTSLSRFEQNGIEVRGVILNSIFRRASGYQDYGYYEY 725
Cdd:COG3206 629 LAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYYYYYYYYYYY 687
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
520-708 |
2.10e-75 |
|
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: 241.32 E-value: 2.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 520 EAIRSLRTSLHFAMMQAPNNVLMLTGVSPSIGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTNVNGLSDVLA 599
Cdd:cd05387 1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 600 GQGDISRCAQKTSVPGFDLVPRGQVPPNPSELLMSERFAELVKWASANYDMVLIDTPPILAVTDAAVVGRHAGTTLMVAR 679
Cdd:cd05387 81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160
|
170 180
....*....|....*....|....*....
gi 260217726 680 YAVNTLKEVQTSLSRFEQNGIEVRGVILN 708
Cdd:cd05387 161 AGKTRRREVKEALERLEQAGAKVLGVVLN 189
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
540-732 |
1.06e-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: 205.81 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 540 VLMLTGVSPSIGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTNVNGLSDVLAGQGDISRCAQKTSVPGFDLV 619
Cdd:COG0489 94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEVEGLDVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 620 PRGQVPPNPSELLMSERFAELVKWASANYDMVLIDTPPILAVTDAAVVGRHAGTTLMVARYAVNTLKEVQTSLSRFEQNG 699
Cdd:COG0489 174 PAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAG 253
|
170 180 190
....*....|....*....|....*....|....
gi 260217726 700 IEVRGVILNSIFRRASG-YQDYGYYEYEYKSDHK 732
Cdd:COG0489 254 VPVLGVVLNMVCPKGERyYGGGEEYGYREYGDRE 287
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
520-723 |
5.34e-44 |
|
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: 157.21 E-value: 5.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 520 EAIRSLRTSLHFAMmqAPNNVLMLTGVSPSIGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTNVN-GLSDVL 598
Cdd:TIGR01007 1 EYYNAIRTNIQFSG--AEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKItGLTNFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 599 AGQGDISRCAQKTSVPGFDLVPRGQVPPNPSELLMSERFAELVKWASANYDMVLIDTPPILAVTDAAVVGRHAGTTLMVA 678
Cdd:TIGR01007 79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 260217726 679 RYAVNTLKEVQTSLSRFEQNGIEVRGVILNSIFRRASGYQDYGYY 723
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYY 203
|
|
| EpsG |
TIGR03029 |
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ... |
507-709 |
4.60e-35 |
|
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: 134.22 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 507 QLLAVGNPTDLAIEAIRSLRTSLHFAMMQAPNNVLMLTGVSPSIGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELL 586
Cdd:TIGR03029 72 DLIAAYQPFSPQVEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 587 GTTNVNGLSDVLAGQGDISRCAQKTSVPGFDLVPRGQVPPNPSELLMSERFAELVKWASANYDMVLIDTPPILAVTDAAV 666
Cdd:TIGR03029 152 KLSEQRGLSDILAGRSDLEVITHIPALENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQI 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 260217726 667 VGRHAGTTLMVARYAVNTLKEVQTSLSRFEQNGIEVRGVILNS 709
Cdd:TIGR03029 232 VATRARGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLNQ 274
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
379-440 |
2.62e-27 |
|
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: 105.37 E-value: 2.62e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260217726 379 KTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRIVDPAITQPGVVKPKKALIV 440
Cdd:pfam13807 1 DTQQEILRLTRDVEVNTEIYTQLLNSNQELEVVKAGTVGNVRIVDTAVVPPKPVKPKKALIV 62
|
|
| Wzz |
pfam02706 |
Chain length determinant protein; This family includes proteins involved in lipopolysaccharide ... |
28-118 |
1.51e-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: 89.27 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 28 DEIDIGRLVGTVVEARWWVLGITALFALGALIYVMFATPIYSADALVQIEQNQGNSLVQDISTALQNKPPASDaEIQLIQ 107
Cdd:pfam02706 1 DEIDLIELLGVLWKRKKLIILVTLLFTLLAAAYAFLATPKYTATAQILVPQKKGEAGSLLGSDLQAGLQLAST-EIEILK 79
|
90
....*....|.
gi 260217726 108 SRLVLGKTVDD 118
Cdd:pfam02706 80 SRDVLEKVIDE 90
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
221-512 |
3.06e-17 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 85.49 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 221 GMINQLQNNLTVTETGKDtGVLSLTYMGEDRDQIRDILNSITRNYLEQNIERKSEEAAKSLAFLAKQLPEVRSNLDIAEN 300
Cdd:TIGR03007 104 ALITKLRKNISISLAGRD-NLFTISYEDKDPELAKDVVQTLLTIFVEETLGSKRQDSDSAQRFIDEQIKTYEKKLEAAEN 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 301 KLNAYRQQ------QDSVDLP-----------------LEAKAVLDSM-------------------VNIDAQLNELTFK 338
Cdd:TIGR03007 183 RLKAFKQEnggilpDQEGDYYseiseaqeeleaarlelNEAIAQRDALkrqlggeepvllagssvanSELDGRIEALEKQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 339 EAEISKLYTKAHPAY----RTL--LEKR----------------------QALEDEKAKLNNRVTAM------------- 377
Cdd:TIGR03007 263 LDALRLRYTDKHPDViatkREIaqLEEQkeeegsaknggpergeianpvyQQLQIELAEAEAEIASLearvaeltarier 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 378 --------PKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGD----VRIVDPAITQPGVVKPKKALIVLGSII 445
Cdd:TIGR03007 343 lesllrtiPEVEAELTQLNRDYEVNKSNYEQLLTRRESAEVSKQMEVQDkavsFRIIDPPIVPSKPSGPNRPLLMLAGLL 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260217726 446 LGLLLSIVIVLLRSLFNRGIESPLALEEA-GINVYASIPLSEWQKSRDSVKtvKGVKRFKQSQLLAVG 512
Cdd:TIGR03007 423 GGLGAGIGLAFLLSQLRPTVRSVRDLRELtGLPVLGVIPMIATPEERRRRR--RRLAAFLASAGLLIA 488
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
545-708 |
3.07e-16 |
|
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: 79.13 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 545 GVspsiGKTFVCANLAAVISQTHKRVLLIDCD------MRKGYTHELLGTTnvngLSDVLAGQGDISRCAQKTSVPGFDL 618
Cdd:COG1192 12 GV----GKTTTAVNLAAALARRGKRVLLIDLDpqgnltSGLGLDPDDLDPT----LYDLLLDDAPLEDAIVPTEIPGLDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 619 VP---------RGQVPPNPSELLMSERFAELvkwaSANYDMVLIDTPPILAV-TDAAVVgrhAGTTLMV----ARYAVNT 684
Cdd:COG1192 84 IPanidlagaeIELVSRPGRELRLKRALAPL----ADDYDYILIDCPPSLGLlTLNALA---AADSVLIpvqpEYLSLEG 156
|
170 180
....*....|....*....|....*..
gi 260217726 685 LKEVQTSLSRFEQN---GIEVRGVILN 708
Cdd:COG1192 157 LAQLLETIEEVREDlnpKLEILGILLT 183
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
554-716 |
5.18e-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: 78.01 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 554 FVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTNVNGLSDVLAGQGDISRCAQKTSvPGFDLVPRGQVPPNPSELLM 633
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELAELDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 634 SERFAELVKWASANYDMVLIDTPPilAVTDAAVVG-RHAGTTLMV-------ARYAVNTLKEVQTslsrfeQNGIEVRGV 705
Cdd:COG0455 80 EERLIRVLEELERFYDVVLVDTGA--GISDSVLLFlAAADEVVVVttpeptsITDAYALLKLLRR------RLGVRRAGV 151
|
170
....*....|.
gi 260217726 706 ILNSIFRRASG 716
Cdd:COG0455 152 VVNRVRSEAEA 162
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
540-708 |
2.47e-14 |
|
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: 75.15 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 540 VLMLTGVSPSIGKTFVCANLAAVISQTH-KRVLLIDCDMRKGYTHELLGTTNVNGLSDVLAGQGD-----ISRCAQKTSv 613
Cdd:COG4963 104 VIAVVGAKGGVGATTLAVNLAWALARESgRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRldetlLDRALTRHS- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 614 PGFDLVPrGQVPPNPSELLMSERFAELVKWASANYDMVLIDTPPILAVTDAAVVgRHAGTTLMVARYAVNTLKEVQTSLS 693
Cdd:COG4963 183 SGLSVLA-APADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAAL-EAADEVVLVTEPDLPSLRNAKRLLD 260
|
170
....*....|....*..
gi 260217726 694 RFEQNGI--EVRGVILN 708
Cdd:COG4963 261 LLRELGLpdDKVRLVLN 277
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
551-708 |
2.49e-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: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 551 GKTFVCANLAAVISQTHKRVLLIDCD--MRKGYTHELLGTTN--VNGLSDVLAGQGDI--SRCAQKTSVPGFDLVPRGQV 624
Cdd:pfam01656 11 GKTTLAANLARALARRGLRVLLIDLDpqSNNSSVEGLEGDIApaLQALAEGLKGRVNLdpILLKEKSDEGGLDLIPGNID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 625 PPNPSELLMSERFAELVKWA----SANYDMVLIDTPP------ILAVTDAAVVGRHAGTTlmvaRYAVNTLKEVQTSLSR 694
Cdd:pfam01656 91 LEKFEKELLGPRKEERLREAlealKEDYDYVIIDGAPglgellRNALIAADYVIIPLEPE----VILVEDAKRLGGVIAA 166
|
170
....*....|....*...
gi 260217726 695 ----FEQNGIEVRGVILN 708
Cdd:pfam01656 167 lvggYALLGLKIIGVVLN 184
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
550-659 |
4.33e-11 |
|
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: 62.22 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 550 IGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHEL-----LGTTNVNglsDVLAGQGDISRCAQKTSVPGFDLVPRG-- 622
Cdd:pfam13614 13 VGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLgidknNVEKTIY---ELLIGECNIEEAIIKTVIENLDLIPSNid 89
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 260217726 623 --QVPPNPSELLMSE-RFAELVKWASANYDMVLIDTPPIL 659
Cdd:pfam13614 90 laGAEIELIGIENREnILKEALEPVKDNYDYIIIDCPPSL 129
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
550-657 |
5.10e-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: 63.36 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 550 IGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTNVNGLSDVLAGQGDISRCAQKTSvPGFDLVPRGQVPPNPS 629
Cdd:cd02038 12 VGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGP-EGLDIIPGGSGMEELA 90
|
90 100 110
....*....|....*....|....*....|
gi 260217726 630 EL--LMSERFAELVKWASANYDMVLIDTPP 657
Cdd:cd02038 91 NLdpEQKAKLIEELSSLESNYDYLLIDTGA 120
|
|
| WzzB |
COG3765 |
LPS O-antigen chain length determinant protein, WzzB/FepE family [Cell wall/membrane/envelope ... |
28-74 |
1.10e-09 |
|
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: 60.76 E-value: 1.10e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 260217726 28 DEIDIGRLVGTVVEARWWVLGITALFALGALIYVMFATPIYSADALV 74
Cdd:COG3765 20 DEIDLFELLRTLWQGKLWIIGITLLFALLALVYAFLLPQKWTSTAIV 66
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
29-123 |
6.64e-09 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 58.16 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 29 EIDIGRLVGTVVEARWWVLGITALFALGALIYVMFATPIYSADALVQIEQNQGNS---LVQDISTALQNkppaSDAEIQL 105
Cdd:COG3944 1 EMDLREYLRILRRRWWLILLLTLLGALAALASSFLITPVYQASTTLLVSTSSGSDasdLYQGIQTAQQL----VNTYAEL 76
|
90
....*....|....*...
gi 260217726 106 IQSRLVLGKTVDDLDLDI 123
Cdd:COG3944 77 LKSPAVLEEVIDELGLDL 94
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
550-656 |
3.44e-06 |
|
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: 48.74 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 550 IGKTFVCANLAAVISQTHKRVLLIDCD--MRKgyTHELLGTTN--VNGLSDVLAGQGDISRCAQKTS-VPGFDLVPRGQv 624
Cdd:cd02036 12 VGKTTTTANLGVALAKLGKKVLLIDADigLRN--LDLILGLENriVYTLVDVLEGECRLEQALIKDKrWENLYLLPASQ- 88
|
90 100 110
....*....|....*....|....*....|..
gi 260217726 625 pPNPSELLMSERFAELVKWASANYDMVLIDTP 656
Cdd:cd02036 89 -TRDKDALTPEKLEELVKELKDSFDFILIDSP 119
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-384 |
9.76e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 249 EDRDQIRDILNSITRNYLEQNIERKSEeaakslafLAKQLPEVRSNLDIAENKLNAYRQQQDSVDL--PLEAKAVLDSMV 326
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLEQ--------LEREIERLERELEERERRRARLEALLAALGLplPASAEEFAALRA 387
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 260217726 327 NIDAQLNELTFKEAEISKLYTKAHPAYRTLLEKRQALEDEKAKLNNRVTAMPKTQQEI 384
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
239-398 |
1.32e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.92 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 239 TGVLSLTYMGEDRDQIRDILNSITRnYLEQNIERKSEEAAKS-LAFLAKQLPEVRSNLDIAENKLNAYRQQQDSVDLPLE 317
Cdd:COG3524 137 SGIITLEVRAFDPEDAQAIAEALLA-ESEELVNQLSERAREDaVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEAT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 318 AKAVLDSMVNIDAQLNELTFKEAEISKLYTKAHPAYRTLLEKRQALEDEKAKLNNRVT------AMPKTQQEIVRLTRDV 391
Cdd:COG3524 216 AEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTgasggdSLASLLAEYERLELER 295
|
....*..
gi 260217726 392 ESGQQVY 398
Cdd:COG3524 296 EFAEKAY 302
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
551-712 |
7.32e-05 |
|
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: 45.11 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 551 GKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTNVN-GLSDVLAGQGDISRCAQKTSVpGFDLVPRGQvppnPS 629
Cdd:TIGR01969 13 GKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPvTLHDVLAGEADIKDAIYEGPF-GVKVIPAGV----SL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 630 ELLMS---ERFAELVKWASANYDMVLIDTPPILAVtDAAVVGRHAGTTLMVARYAVNTLKEVQTSLSRFEQNGIEVRGVI 706
Cdd:TIGR01969 88 EGLRKadpDKLEDVLKEIIDDTDFLLIDAPAGLER-DAVTALAAADELLLVVNPEISSITDALKTKIVAEKLGTAILGVV 166
|
....*.
gi 260217726 707 LNSIFR 712
Cdd:TIGR01969 167 LNRVTR 172
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
551-708 |
8.47e-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: 44.58 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 551 GKTFVCANLAAVISQTHK-RVLLIDCDMRKGYTHELLGTTNVNGLSDVLAGQGDISRCAQKTSV----PGFDLVPRgqvp 625
Cdd:cd03111 13 GASTLAVNLAQELAQRAKdKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDRLDRTLLDSAVtrhsSGLSLLPA---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 626 PNPSELLMS---ERFAELVKWASANYDMVLIDTPPILAVTDAAVVgRHAGTTLMVARYAVNTLKEVQ---TSLSRFEQNG 699
Cdd:cd03111 89 PQELEDLEAlgaEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVL-EAADEILLVTQQDLPSLRNARrllDSLRELEGSS 167
|
....*....
gi 260217726 700 IEVRgVILN 708
Cdd:cd03111 168 DRLR-LVLN 175
|
|
| cellulose_yhjQ |
TIGR03371 |
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ... |
539-657 |
9.53e-05 |
|
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274549 [Multi-domain] Cd Length: 246 Bit Score: 44.64 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 539 NVLMLTGVSPSIGKTFVCANLAAVISQTHKRVLLIDCDmrkgyTHELLG------TTNVNGLSDVLAGQGDISRCAQKtS 612
Cdd:TIGR03371 2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLD-----PQNLLRlhfgmdWSVRDGWARALLNGADWAAAAYR-S 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 260217726 613 VPGFDLVPRGQVPPNPSELLMSER----FAELVKWASANYDMVLIDTPP 657
Cdd:TIGR03371 76 PDGVLFLPYGDLSADEREAYQAHDagwlARLLQQLDLAARDWVLIDLPR 124
|
|
| PRK11638 |
PRK11638 |
ECA polysaccharide chain length modulation protein; |
23-74 |
2.29e-04 |
|
ECA polysaccharide chain length modulation protein;
Pssm-ID: 236943 [Multi-domain] Cd Length: 342 Bit Score: 43.88 E-value: 2.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 260217726 23 PVEGGDEIDIGRLVGTVVEARWWVLGITALFALGALIYVMFATPIYSADALV 74
Cdd:PRK11638 3 AVSAENELDIRGLCRTLWAGKLWIIGMALLFALIALGYSFLARQEWSATAIT 54
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
550-708 |
2.66e-04 |
|
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: 41.37 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 550 IGKTFVCANLAAVISQTHKRVLLIDCDMrkgythellgttnvnglsdvlagQGDISrcaqktsvpgfdlvprgqvppnps 629
Cdd:cd02042 12 VGKTTLAVNLAAALALRGKRVLLIDLDP-----------------------QGSLT------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 630 ellmserfaelvKWAsanYDMVLIDTPP--------ILAVTDAAVVgrhagtTLMVARYAVNTLKEVQTSLSRFEQ---N 698
Cdd:cd02042 45 ------------SWL---YDYILIDTPPslglltrnALAAADLVLI------PVQPSPFDLDGLAKLLDTLEELKKqlnP 103
|
170
....*....|
gi 260217726 699 GIEVRGVILN 708
Cdd:cd02042 104 PLLILGILLT 113
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
550-602 |
8.77e-04 |
|
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction
Pssm-ID: 349761 Cd Length: 266 Bit Score: 41.97 E-value: 8.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 260217726 550 IGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTNVNGLSDVLAGQG 602
Cdd:cd02117 11 IGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDG 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
249-408 |
1.94e-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: 41.58 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 249 EDRDQIRDILNSITRNYleQNIERKSEeAAKSLAFLAKQLPEVRsnLDIAENKLNAYRQQQDSVDLplEAKAVLDSMVNI 328
Cdd:TIGR02168 186 ENLDRLEDILNELERQL--KSLERQAE-KAERYKELKAELRELE--LALLVLRLEELREELEELQE--ELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 329 DAQLNELtfkEAEISKLYTKahpayrtLLEKRQALEDEKAKLNNrvtampkTQQEIVRLTRDVESGQQVYMQLLNKQQEL 408
Cdd:TIGR02168 259 TAELQEL---EEKLEELRLE-------VSELEEEIEELQKELYA-------LANEISRLEQQKQILRERLANLERQLEEL 321
|
|
| BchX |
cd02033 |
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ... |
550-587 |
6.18e-03 |
|
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.
Pssm-ID: 349753 Cd Length: 329 Bit Score: 39.43 E-value: 6.18e-03
10 20 30
....*....|....*....|....*....|....*...
gi 260217726 550 IGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLG 587
Cdd:cd02033 42 IGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFG 79
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
539-576 |
7.15e-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: 7.15e-03
10 20 30
....*....|....*....|....*....|....*...
gi 260217726 539 NVLMLTGVSPSIGKTFVCANLAAVISQTHKRVLLIDCD 576
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
539-655 |
7.34e-03 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 38.51 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260217726 539 NVLMLTGVSPSiGKTFVCANLAAVISQTHKRVLLIDCDMRKGYTHELLGTTnvnglsdvlagqgdisrcAQKTSVPGFDl 618
Cdd:cd03115 1 NVILLVGLQGS-GKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTL------------------AEKLGVPVFE- 60
|
90 100 110
....*....|....*....|....*....|....*..
gi 260217726 619 VPRGQVPpnpsellMSERFAELVKWASANYDMVLIDT 655
Cdd:cd03115 61 SYTGTDP-------ASIAQEAVEKAKLEGYDVLLVDT 90
|
|
| |
