|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
1-719 |
0e+00 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 1453.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 1 MTEKVKQHAAPVTGSDEIDIGRLVGTVIEARWWVIGITTVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSAL 80
Cdd:PRK11519 1 MTEKVKQHAAPVTGSDEIDIGRLVGTVIEARWWVIGITAVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 81 ANKPPASDAEIQLIRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTTFNRPKEMADQVFTLNVLDNK 160
Cdd:PRK11519 81 ANKPPASDAEIQLIRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTTFNRPKEMADQVFTLNVLDDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 161 NYTLSSDGGFSARGQAGQMLKKEGVTLMVEAIHASPGSEFTVTKYSTLGMINQLQNSLTVTENGKDAGVLSLTYTGEDRE 240
Cdd:PRK11519 161 NYQLSSDGGFSARGQVGQMLKKDGVTLMVEAIHARPGTEFTVTKYSTLGMINNLQNNLTVTENGKDTGVLSLTYTGEDRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 241 QIRDILNSIARNYQEQNIERKSAEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQL 320
Cdd:PRK11519 241 QIRDILNSITRNYLEQNIERKSEEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 321 NELTFKEAEISKLYTKVHPAYRTLLEKRQALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKEQELKITE 400
Cdd:PRK11519 321 NELTFKEAEISKLYTKEHPAYRTLLEKRKALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 401 ASTVGDVRIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARD 480
Cdd:PRK11519 401 ASTVGDVRIVDPAITQPGVLKPKKALIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 481 SVKTIKGIKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLL 560
Cdd:PRK11519 481 SVKTIKGIKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 561 IDCDMRKGYTHELLGTNNVNGLSEILIGQGDITTAAKPTSIAKFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVL 640
Cdd:PRK11519 561 IDCDMRKGYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVL 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111377 641 IDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASAYQDYGYYEYEYKSDA 719
Cdd:PRK11519 641 IDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASAYQDYGYYEYEYKSDA 719
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
1-720 |
0e+00 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 815.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 1 MTEKVKQHAAPVTGSDEIDIGRLVGTVIEARWWVIGITTVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSAL 80
Cdd:PRK09841 1 MTTKNMNTPPGSTQENEIDLLRLVGELWDHRKFIISVTALFTLIAVAYSLLSTPIYQADTLVQVEQKQGNAILSGLSDMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 81 ANKPPASDAEIQLIRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTTFNRPK-EMADQVFTLNVLDN 159
Cdd:PRK09841 81 PNSSPESAPEIQLLQSRMILGKTIAELNLRDIVEQKYFPIVGRGWARLTKEKPGELAISWMHIPQlNGQDQQLTLTVGEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 160 KNYTLSSDGgFSARGQAGQMLKKEGVTLMVEAIHASPGSEFTVTKYSTLGMINQLQNSLTVTENGKDAGVLSLTYTGEDR 239
Cdd:PRK09841 161 GHYTLEGEE-FTVNGMVGQRLEKDGVALTIADIKAKPGTQFVLSQRTELEAINALQETFTVSERSKESGMLELTMTGDDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 240 EQIRDILNSIARNYQEQNIERKSAEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQ 319
Cdd:PRK09841 240 QLITRILNSIANNYLQQNIARQAAQDSQSLEFLQRQLPEVRSELDQAEEKLNVYRQQRDSVDLNLEAKAVLEQIVNVDNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 320 LNELTFKEAEISKLYTKVHPAYRTLLEKRQALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKEQELKIT 399
Cdd:PRK09841 320 LNELTFREAEISQLYKKDHPTYRALLEKRQTLEQERKRLNKRVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELSIS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 400 EASTVGDVRIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEW--QK 477
Cdd:PRK09841 400 KSSAIGNVRIIDPAVTQPQPVKPKKALNVVLGFILGLFISVGAVLARAMLRRGVEAPEQLEEHGISVYATIPMSEWldKR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 478 ARDSVKTIKGIK---RYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQT 554
Cdd:PRK09841 480 TRLRKKNLFSNQqrhRTKNIPFLAVDNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 555 NKRVLLIDCDMRKGYTHELLGTNNVNGLSEILIGQGDITTAAKPTSIAKFDLIPRGQVPPNPSELLMSERFAELVNWASK 634
Cdd:PRK09841 560 DQKVLFIDADLRRGYSHNLFTVSNEHGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWAND 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 635 NYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASAYQDYGYYEYE 714
Cdd:PRK09841 640 HYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNGVIKRASTAYSYGYNYYG 719
|
....*.
gi 90111377 715 YKSDAK 720
Cdd:PRK09841 720 YSYSEK 725
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
17-720 |
2.55e-112 |
|
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: 357.11 E-value: 2.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 17 EIDIGRLVGTVIEARWWVIGITTVFALCAVVYTFFATPIYSADALVQIEQN--SGNSLVQDIGSALANKPPASdAEIQLI 94
Cdd:TIGR01005 3 EIDLDRLLAALFANARLIAAFAAAFIALGAAYAFFARPVYEADIMILLDDNlnKAAEEEGDPSNLFDLDTDAA-AAIEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 95 RSRLVLGKTVDDLDLDIAVSKNTFPIF-----GAGWDRLMGR--------------QNETVKVTTFNRPKEMADQVFTLN 155
Cdd:TIGR01005 82 KSGELAGKAVDKLHLSENAKILNPPRFpvdliGAWIKSAAGLfsepggfdlgeeaaGNERIDKAAADIPEALAGEPFKLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 156 VLDNKNYTLS--SDGGFSARGQAGQMLKKE---GVTLMVEAIHASPGSEFTVTKYSTLGMINQLQNSLTVTENGKDAGVL 230
Cdd:TIGR01005 162 SLGAGAFRLEdkLLAAPIAGGVAEALEADQliaNFEAQENALTAKAEALFDLEQDSQAAALEMAHDKAEIAEKAAQGEII 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 231 SL-TYTGEDREQIRDILNSIARNYQEQNIERKSAEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAV 309
Cdd:TIGR01005 242 GEaQLADLNPALIAAIADQAAAEARADNIKRIADEAEENAVFLAGILPKEGDELEIADLKTNELRNGKGEFDLSDEFGAD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 310 LDSMVNIDAQLNELTFKEAEISKLYTKVHPAYRTLLEKRQALEDEKAK-LNGRVTAMPKTQQEIVRLTRDVESGQQVYMQ 388
Cdd:TIGR01005 322 HPEAVCSAPSLQELKAKIAEELQQFTASHKGEQAIAQQIEESLRGKINgIAGKLKDAPEIEQDLRELEQDAAADKELYES 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 389 LLNKEQELKITEASTVGDVRIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEH-GISVY 467
Cdd:TIGR01005 402 LLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTLALAAVLGMMLGGAAAAFLEALEGGFRDEGDIEEHlGHRSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 468 ASIPLSEWQ---KARDSVKTIKGIKRYKQS-------QLLA---VGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGV 534
Cdd:TIGR01005 482 ATVPLLDTQmdkKAQLTHAHFGSVKRHDEAvddtmpfQLLArivPDAPRSTFAEAFRNAKLACDFALADAENNLIAIAGA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 535 SPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNGLSEILIGQGDITTAAKPTSIAKFDLIPRGQV-- 612
Cdd:TIGR01005 562 LPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLLAGEASIEAGIHRDQRPGLAFIAAGGAsh 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 613 -PPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVK 691
Cdd:TIGR01005 642 fPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVTEFERSPLGEIRDLIHQEPHANSDVL 721
|
730 740 750
....*....|....*....|....*....|....*.
gi 90111377 692 GVILNSI-------FRRASAYQDYGYYEYEYKSDAK 720
Cdd:TIGR01005 722 GVIFNALdmnelgkYGDFDGAEKYRHRQGGYTSENK 757
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1-713 |
6.47e-95 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 308.87 E-value: 6.47e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 1 MTEKVKQHAAPvtgSDEIDIGRLVGTVIEARWWVIGITTVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSAL 80
Cdd:COG3206 1 MNESSSAPPEE---EDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSSLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 81 ANKPPAsDAEIQLIRSRLVLGKTVDDLDLDiavskntfpifgagwdrlmgrqnetvkvttfnrpkemadqvftlnvldnk 160
Cdd:COG3206 78 ASDSPL-ETQIEILKSRPVLERVVDKLNLD-------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 161 nytlssdggfsargqagqmlkkegvtlmveaihaspgSEFTVTKYSTLGMINQLQNSLTVtENGKDAGVLSLTYTGEDRE 240
Cdd:COG3206 107 -------------------------------------EDPLGEEASREAAIERLRKNLTV-EPVKGSNVIEISYTSPDPE 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 241 QIRDILNSIARNYQEQNIERKSAEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQL 320
Cdd:COG3206 149 LAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQL 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 321 N--------------------------------------------ELTFKEAEISKLYTKVHPAYRTLLEKR-------- 348
Cdd:COG3206 229 AearaelaeaearlaalraqlgsgpdalpellqspviqqlraqlaELEAELAELSARYTPNHPDVIALRAQIaalraqlq 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 349 ---------------------QALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKEQELKITEASTVGDV 407
Cdd:COG3206 309 qeaqrilasleaelealqareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 408 RIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARDSVKTikg 487
Cdd:COG3206 389 RVIDPAVVPLKPVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLLLGLPLLGPLPPLKSKRERRRAR--- 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 488 ikryKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRK 567
Cdd:COG3206 466 ----LALLLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLL 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 568 GYTHELLGTNNVNGLSEILIGQGDITTAAKPTSIAKFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPIL 647
Cdd:COG3206 542 LLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLA 621
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111377 648 AVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASAYQDYGYYEY 713
Cdd:COG3206 622 ALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYYYYYYYYYYY 687
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
508-696 |
2.03e-76 |
|
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: 243.63 E-value: 2.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 508 EAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNGLSEILI 587
Cdd:cd05387 1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 588 GQGDITTAAKPTSIAKFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVAR 667
Cdd:cd05387 81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160
|
170 180
....*....|....*....|....*....
gi 90111377 668 YAVNTLKEVETSLSRFEQNGIPVKGVILN 696
Cdd:cd05387 161 AGKTRRREVKEALERLEQAGAKVLGVVLN 189
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
369-720 |
4.06e-61 |
|
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: 206.96 E-value: 4.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 369 QQEIVRLTRDVESGQQVYMQLLNKEQELKITEASTVGDVRIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLRSL 448
Cdd:COG0489 2 LLAALELLLLREEAQALLLLLLLLLLLLRLEEAAAAAALAAAAPAAAAPAPLPPAPALLLLLLLLLGLLLLLLLALALLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 449 FNRGIESPQVLEehgisvyasiplsewqkardsvktikgikrykqsqllavgnptdlaieairslrtslhfammqaqnnV 528
Cdd:COG0489 82 LLLLLLLRLLLE-------------------------------------------------------------------V 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 529 LMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNGLSEILIGQGDITTAAKPTSIAKFDLIP 608
Cdd:COG0489 95 IAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEVEGLDVLP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 609 RGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGI 688
Cdd:COG0489 175 AGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAGV 254
|
330 340 350
....*....|....*....|....*....|...
gi 90111377 689 PVKGVILNSI-FRRASAYQDYGYYEYEYKSDAK 720
Cdd:COG0489 255 PVLGVVLNMVcPKGERYYGGGEEYGYREYGDRE 287
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
508-711 |
5.17e-47 |
|
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: 165.30 E-value: 5.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 508 EAIRSLRTSLHFAMmqAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVN-GLSEIL 586
Cdd:TIGR01007 1 EYYNAIRTNIQFSG--AEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKItGLTNFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 587 IGQGDITTAAKPTSIAKFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVA 666
Cdd:TIGR01007 79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 90111377 667 RYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASAYQDYGYY 711
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYY 203
|
|
| EpsG |
TIGR03029 |
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ... |
495-697 |
9.19e-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: 133.45 E-value: 9.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 495 QLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELL 574
Cdd:TIGR03029 72 DLIAAYQPFSPQVEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 575 GTNNVNGLSEILIGQGDITTAAKPTSIAKFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAI 654
Cdd:TIGR03029 152 KLSEQRGLSDILAGRSDLEVITHIPALENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQI 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90111377 655 VGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNS 697
Cdd:TIGR03029 232 VATRARGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLNQ 274
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
367-448 |
1.31e-32 |
|
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: 120.78 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 367 KTQQEIVRLTRDVESGQQVYMQLLNKEQELKITEASTVGDVRIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLR 446
Cdd:pfam13807 1 DTQQEILRLTRDVEVNTEIYTQLLNSNQELEVVKAGTVGNVRIVDTAVVPPKPVKPKKALIVVLALLLGLMLGVGLVLLR 80
|
..
gi 90111377 447 SL 448
Cdd:pfam13807 81 RA 82
|
|
| Wzz |
pfam02706 |
Chain length determinant protein; This family includes proteins involved in lipopolysaccharide ... |
16-106 |
8.15e-23 |
|
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: 93.12 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 16 DEIDIGRLVGTVIEARWWVIGITTVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSALANKPPASDaEIQLIR 95
Cdd:pfam02706 1 DEIDLIELLGVLWKRKKLIILVTLLFTLLAAAYAFLATPKYTATAQILVPQKKGEAGSLLGSDLQAGLQLAST-EIEILK 79
|
90
....*....|.
gi 90111377 96 SRLVLGKTVDD 106
Cdd:pfam02706 80 SRDVLEKVIDE 90
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
209-500 |
2.09e-20 |
|
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: 95.12 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 209 GMINQLQNSLTVTENGKDaGVLSLTYTGEDREQIRDILNSIARNYQEQNIERKSAEASKSLAFLAQQLPEVRSRLDVAEN 288
Cdd:TIGR03007 104 ALITKLRKNISISLAGRD-NLFTISYEDKDPELAKDVVQTLLTIFVEETLGSKRQDSDSAQRFIDEQIKTYEKKLEAAEN 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 289 KLNAFRQdKDSVDLP------------------------LEAKAVLDSM-------------------VNIDAQLNELTF 325
Cdd:TIGR03007 183 RLKAFKQ-ENGGILPdqegdyyseiseaqeeleaarlelNEAIAQRDALkrqlggeepvllagssvanSELDGRIEALEK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 326 KEAEISKLYTKVHPAY----RTL--LEKR----------------------QALEDEKAKLNGRVTAM------------ 365
Cdd:TIGR03007 262 QLDALRLRYTDKHPDViatkREIaqLEEQkeeegsaknggpergeianpvyQQLQIELAEAEAEIASLearvaeltarie 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 366 ---------PKTQQEIVRLTRDVESGQQVYMQLLNKEQELKITEASTVGD----VRIVDPAITQPGVLKPKKGLIILGAI 432
Cdd:TIGR03007 342 rlesllrtiPEVEAELTQLNRDYEVNKSNYEQLLTRRESAEVSKQMEVQDkavsFRIIDPPIVPSKPSGPNRPLLMLAGL 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111377 433 ILGLMLSIVGVLLRSLFNRGIESPQVLEE-HGISVYASIPLSEWQKARDSVKtiKGIKRYKQSQLLAVG 500
Cdd:TIGR03007 422 LGGLGAGIGLAFLLSQLRPTVRSVRDLRElTGLPVLGVIPMIATPEERRRRR--RRLAAFLASAGLLIA 488
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
539-707 |
1.80e-14 |
|
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: 73.74 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 539 GKTFVCANLAAVISQTNKRVLLIDCD------MRKGYTHEllgtNNVNGLSEILIGQGDITTAAKPTSIAKFDLIP---- 608
Cdd:COG1192 14 GKTTTAVNLAAALARRGKRVLLIDLDpqgnltSGLGLDPD----DLDPTLYDLLLDDAPLEDAIVPTEIPGLDLIPanid 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 609 -----RGQVPPNPSELLMSERFAELvnwaSKNYDLVLIDTPPILAV-TDAAIVG-RHVGTTLMVARYAVNTLKEVETSLS 681
Cdd:COG1192 90 lagaeIELVSRPGRELRLKRALAPL----ADDYDYILIDCPPSLGLlTLNALAAaDSVLIPVQPEYLSLEGLAQLLETIE 165
|
170 180
....*....|....*....|....*....
gi 90111377 682 RFEQN---GIPVKGVILNSIFRRASAYQD 707
Cdd:COG1192 166 EVREDlnpKLEILGILLTMVDPRTRLSRE 194
|
|
| WzzB |
COG3765 |
LPS O-antigen chain length determinant protein, WzzB/FepE family [Cell wall/membrane/envelope ... |
15-449 |
7.91e-14 |
|
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: 73.47 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 15 SDEIDIGRLVGTVIEARWWVIGITTVFALCAVVYTFFATPIYSADALVQieqnsgnslvqdigsalankpPASDAEIQLI 94
Cdd:COG3765 19 DDEIDLFELLRTLWQGKLWIIGITLLFALLALVYAFLLPQKWTSTAIVD---------------------PPTVNELGGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 95 RSRLVLGKTVDDLDLDIAVSKNTfpIFGagwdrlmgrqnetvkvtTFNRpkemadqvfTLNVLDNKNYTLSSDGGFSARg 174
Cdd:COG3765 78 YSQRQFLRNLDVKSVDPPVISSE--LFN-----------------EFIK---------QLSSYDLRREFLLQSDYYKQL- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 175 qaGQMLKKEGVTLmveaihaspgseftvtkystlgmINQLQNSLTVT-----ENGKDAGVLSLTYTGEDREQIRDIL--- 246
Cdd:COG3765 129 --QEGDEKEDAAL-----------------------LDELINNISITppddkKKSSPYTNYSVSFTAETPEDAQQLLrgy 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 247 ----NSIARNYQEQNIERKsaeaskslafLAQQLPEVRSRLDVAENKLNAFRQDK-DSVDLPLE-AKAV-LDSMVNIDAQ 319
Cdd:COG3765 184 idfaNQRVLKELNEELQGA----------IAARLQSLKAQIKRLEEVAKAQRQRRiERLKYALKiAQAAgIKKPVYSNGQ 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 320 LNeltFKEAEISKLYTKvhpAYRTLLEKRQALEDEK--AKLNGRVTAMPKTQQEIVRLTRDvESGQQVYMQLLNKEQELK 397
Cdd:COG3765 254 TP---AVKLDPSYLFLL---GTDALQAELEILKARGddYPLNADLYQLQAQLAQLNALPID-DVGFQPFRYLRTPEEPVK 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 90111377 398 iteastvgdvRIvdpaitqpgvlKPKKGLIILGAIILGLMLSIVGVLLRSLF 449
Cdd:COG3765 327 ----------KD-----------KPKRALILVLGALLGGMLGVGVVLIRHAL 357
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
539-696 |
1.23e-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: 67.76 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 539 GKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVN----GLSEILIGQGDITTA--AKPTSIAKFDLIPRGQV 612
Cdd:pfam01656 11 GKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIApalqALAEGLKGRVNLDPIllKEKSDEGGLDLIPGNID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 613 PPNPSELLMSERFAELVNWA----SKNYDLVLIDTPPILAVT--DAAIVGRHVGTTLMVARYAVNTLKEVETSLSR---- 682
Cdd:pfam01656 91 LEKFEKELLGPRKEERLREAlealKEDYDYVIIDGAPGLGELlrNALIAADYVIIPLEPEVILVEDAKRLGGVIAAlvgg 170
|
170
....*....|....
gi 90111377 683 FEQNGIPVKGVILN 696
Cdd:pfam01656 171 YALLGLKIIGVVLN 184
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
542-704 |
7.72e-12 |
|
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: 65.68 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 542 FVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNGLSEILIGQGDITTAAKPTSiAKFDLIPRGQVPPNPSELLM 621
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELAELDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 622 SERFAELVNWASKNYDLVLIDTPPilAVTDAAIVG-RHVGTTLMV-------ARYAVNTLKEVETslsrfeQNGIPVKGV 693
Cdd:COG0455 80 EERLIRVLEELERFYDVVLVDTGA--GISDSVLLFlAAADEVVVVttpeptsITDAYALLKLLRR------RLGVRRAGV 151
|
170
....*....|.
gi 90111377 694 ILNSIFRRASA 704
Cdd:COG0455 152 VVNRVRSEAEA 162
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
528-696 |
1.51e-11 |
|
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: 66.68 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 528 VLMMTGVSPSIGKTFVCANLAAVISQ-TNKRVLLIDCDMRKGYTHELLGTNNVNGLSEILIGQGDI------TTAAKPTS 600
Cdd:COG4963 104 VIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLdetlldRALTRHSS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 601 iaKFDLIPrGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVgRHVGTTLMVARYAVNTLKEVETSL 680
Cdd:COG4963 184 --GLSVLA-APADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAAL-EAADEVVLVTEPDLPSLRNAKRLL 259
|
170
....*....|....*...
gi 90111377 681 SRFEQNGIPVK--GVILN 696
Cdd:COG4963 260 DLLRELGLPDDkvRLVLN 277
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
538-647 |
5.39e-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: 61.83 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 538 IGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHEL-LGTNNV-NGLSEILIGQGDITTAAKPTSIAKFDLIPRG----Q 611
Cdd:pfam13614 13 VGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLgIDKNNVeKTIYELLIGECNIEEAIIKTVIENLDLIPSNidlaG 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 90111377 612 VPPNPSELLMSE-RFAELVNWASKNYDLVLIDTPPIL 647
Cdd:pfam13614 93 AEIELIGIENREnILKEALEPVKDNYDYIIIDCPPSL 129
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
17-114 |
2.22e-09 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 59.31 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 17 EIDIGRLVGTVIEaRWWVIGITT-VFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSALANKPPASDAeIQLIR 95
Cdd:COG3944 1 EMDLREYLRILRR-RWWLILLLTlLGALAALASSFLITPVYQASTTLLVSTSSGSDASDLYQGIQTAQQLVNTY-AELLK 78
|
90
....*....|....*....
gi 90111377 96 SRLVLGKTVDDLDLDIAVS 114
Cdd:COG3944 79 SPAVLEEVIDELGLDLSPE 97
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
397-562 |
1.49e-08 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 57.00 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 397 KITEASTVGDVRIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGisvyasiplsewq 476
Cdd:COG3944 140 EVKELMKVDNVTVLDPATVPASPVSPNPKLNLAIGLVLGLLLGVGLAFLRELLDTTIRSEEDIERLL------------- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 477 karDSVKTIKGIKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNK 556
Cdd:COG3944 207 ---GLLLGGAVPAARSARPLLLLLADASPRAAAARRRRRNLLFALAAVDARTVVVVSSSLSEGKSTTTAALALALAAAAA 283
|
....*.
gi 90111377 557 RVLLID 562
Cdd:COG3944 284 GVVLVL 289
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
538-645 |
1.05e-07 |
|
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: 53.34 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 538 IGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNGLSEILIGQGDITTAAKPTSiAKFDLIPRGQVPPNPS 617
Cdd:cd02038 12 VGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGP-EGLDIIPGGSGMEELA 90
|
90 100 110
....*....|....*....|....*....|
gi 90111377 618 EL--LMSERFAELVNWASKNYDLVLIDTPP 645
Cdd:cd02038 91 NLdpEQKAKLIEELSSLESNYDYLLIDTGA 120
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
259-447 |
1.25e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 51.39 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 259 ERKSAEAsksLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQLNELTFKEAEISKLYTKVH 338
Cdd:COG3524 172 ERAREDA---VRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQLIATLEGQLAELEAELAALRSYLSPNS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 339 PAYRTLLEKRQALEDEKAKLNGRVT------AMPKTQQEIVRLTRDVESGQQVYMQLLNKEQELKItEAS--TVGDVRIV 410
Cdd:COG3524 249 PQVRQLRRRIAALEKQIAAERARLTgasggdSLASLLAEYERLELEREFAEKAYTSALAALEQARI-EAArqQRYLAVIV 327
|
170 180 190
....*....|....*....|....*....|....*..
gi 90111377 411 DPAITQpGVLKPKKGLIILGAIILGLMLSIVGVLLRS 447
Cdd:COG3524 328 QPTLPD-EALYPRRLYNILLVFLILLLLYGIGSLLVA 363
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
251-513 |
1.90e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 251 RNYQEQNIERKSAEAS-KSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQLNELtfkEAE 329
Cdd:COG4717 71 KELKELEEELKEAEEKeEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL---PER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 330 ISKLYTKVHPaYRTLLEKRQALEDEKAKLNGRVTAM-----PKTQQEIVRLTRDVESGQQVYMQLLNKEQELKITEASTV 404
Cdd:COG4717 148 LEELEERLEE-LRELEEELEELEAELAELQEELEELleqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 405 GDVRIVDPAITQPGVLKPKKGLIILgAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLS----EWQKARD 480
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLArekaSLGKEAE 305
|
250 260 270
....*....|....*....|....*....|....*..
gi 90111377 481 SVKTIKGIKRYKQ----SQLLAVGNPTDLAIEAIRSL 513
Cdd:COG4717 306 ELQALPALEELEEeeleELLAALGLPPDLSPEELLEL 342
|
|
| PRK11638 |
PRK11638 |
ECA polysaccharide chain length modulation protein; |
11-62 |
2.65e-05 |
|
ECA polysaccharide chain length modulation protein;
Pssm-ID: 236943 [Multi-domain] Cd Length: 342 Bit Score: 46.96 E-value: 2.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 90111377 11 PVTGSDEIDIGRLVGTVIEARWWVIGITTVFALCAVVYTFFATPIYSADALV 62
Cdd:PRK11638 3 AVSAENELDIRGLCRTLWAGKLWIIGMALLFALIALGYSFLARQEWSATAIT 54
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
538-655 |
3.27e-05 |
|
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: 44.07 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 538 IGKTFVCANLAAVISQTNKRVLLIDCDMrkgythellgtnnvnglseiligQGDITTAAkptsiakfdliprgqvppnps 617
Cdd:cd02042 12 VGKTTLAVNLAAALALRGKRVLLIDLDP-----------------------QGSLTSWL--------------------- 47
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 90111377 618 ellmserfaelvnwasknYDLVLIDTPP--------ILAVTDAAIV 655
Cdd:cd02042 48 ------------------YDYILIDTPPslglltrnALAAADLVLI 75
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
539-705 |
9.00e-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: 44.72 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 539 GKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVN-GLSEILIGQGDITtaakptsiakfDLIPRGQ-----V 612
Cdd:TIGR01969 13 GKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPvTLHDVLAGEADIK-----------DAIYEGPfgvkvI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 613 PPNPS-ELLMS---ERFAELVNWASKNYDLVLID-----------------------TPPILAVTDA---AIVGRHVGTT 662
Cdd:TIGR01969 82 PAGVSlEGLRKadpDKLEDVLKEIIDDTDFLLIDapaglerdavtalaaadelllvvNPEISSITDAlktKIVAEKLGTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90111377 663 LMVAryAVNTLKEVETSLSRFEQNGI---PVKGVIL-NSIFRRASAY 705
Cdd:TIGR01969 162 ILGV--VLNRVTRDKTELGREEIETIlevPVLGVVPeDPEVRRAAAF 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-372 |
2.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 237 EDREQIRDILNSIARNYQEQNIERksaeasksLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDL--PLEAKAVLDSMV 314
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDR--------LEQLEREIERLERELEERERRRARLEALLAALGLplPASAEEFAALRA 387
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 90111377 315 NIDAQLNELTFKEAEISKLYTKVHPAYRTLLEKRQALEDEKAKLNGRVTAMPKTQQEI 372
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
237-479 |
3.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 237 EDREQIRDILNSIARNYQEQNIERKSAEASKS-------LAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDlpleakav 309
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQllplyqeLEALEAELAELPERLEELEERLEELRELEEELE-------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 310 ldsmvNIDAQLNELTFKEAEISKLYT-KVHPAYRTLLEKRQALEDEKAKLNGRVTampKTQQEIVRLTRDVESGQQVyMQ 388
Cdd:COG4717 167 -----ELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQLENE-LE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 389 LLNKEQELKITEASTVGDVRIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYA 468
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250
....*....|.
gi 90111377 469 SIPLSEWQKAR 479
Cdd:COG4717 318 EEELEELLAAL 328
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
538-590 |
5.07e-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: 42.35 E-value: 5.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 90111377 538 IGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNGLSEILIGQG 590
Cdd:cd02117 11 IGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDEMLTEDG 63
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
529-696 |
5.74e-04 |
|
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.
Pssm-ID: 433259 [Multi-domain] Cd Length: 198 Bit Score: 41.86 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 529 LMMTGVSPSIGKTFVCANLAAvisqtnkrvLLIDCDMRKGYtHELLGTNNVNGlseiliGQGDITTAAKPTSIAKFDLIP 608
Cdd:pfam13500 3 LFVTGTDTGVGKTVVSLGLAR---------ALKRRGVKVGY-WKPVQTGLVED------GDSELVKRLLGLDQSYEDPEP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 609 RGQVPPNPSELLM-----SERFAELVNWASKNYDLVLI------DTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVE 677
Cdd:pfam13500 67 FRLSAPLSPHLAArqegvTIDLEKIIYELPADADPVVVegagglLVPINEDLLNADIAANLGLPVILVARGGLGTINHTL 146
|
170
....*....|....*....
gi 90111377 678 TSLSRFEQNGIPVKGVILN 696
Cdd:pfam13500 147 LTLEALRQRGIPVLGVILN 165
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
538-644 |
2.52e-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: 40.26 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 538 IGKTFVCANLAAVISQTNKRVLLIDCD--MRKgyTHELLGTNN--VNGLSEILIGQGDITTA-AKPTSIAKFDLIPRGQv 612
Cdd:cd02036 12 VGKTTTTANLGVALAKLGKKVLLIDADigLRN--LDLILGLENriVYTLVDVLEGECRLEQAlIKDKRWENLYLLPASQ- 88
|
90 100 110
....*....|....*....|....*....|..
gi 90111377 613 pPNPSELLMSERFAELVNWASKNYDLVLIDTP 644
Cdd:cd02036 89 -TRDKDALTPEKLEELVKELKDSFDFILIDSP 119
|
|
| BchX |
cd02033 |
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ... |
538-575 |
3.22e-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: 40.20 E-value: 3.22e-03
10 20 30
....*....|....*....|....*....|....*...
gi 90111377 538 IGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLG 575
Cdd:cd02033 42 IGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFG 79
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
527-643 |
3.24e-03 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 39.45 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 527 NVLMMTGVSPSiGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTnNVNGLSEILIGQGditTAAKPTSIAKFDL 606
Cdd:pfam00448 1 NVILLVGLQGS-GKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQ-LAEKLGVPVFGSK---TGADPAAVAFDAV 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 90111377 607 iprgqvppnpsellmsERFAElvnwasKNYDLVLIDT 643
Cdd:pfam00448 76 ----------------EKAKA------ENYDVVLVDT 90
|
|
| PRK10381 |
PRK10381 |
LPS O-antigen length regulator; Provisional |
389-460 |
7.59e-03 |
|
LPS O-antigen length regulator; Provisional
Pssm-ID: 182422 [Multi-domain] Cd Length: 377 Bit Score: 39.28 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111377 389 LLNKEQELKITEASTVGDVRIVdP-----AITQPgVLK--PKKGLIILGAIILGLMLSIVGVLLRSLF---NRGIESPQV 458
Cdd:PRK10381 298 LRNRQYYVEQLKKLNINDVNFT-PfkyqlSPSLP-VKKdgPGKALIVILAALIGGMLACGFVLLRHAMrsrKQDLMLADH 375
|
..
gi 90111377 459 LE 460
Cdd:PRK10381 376 LV 377
|
|
| |
