|
Name |
Accession |
Description |
Interval |
E-value |
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1-716 |
1.49e-70 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 244.93 E-value: 1.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 1 MEKQDIDFRELLFRYVRHWKLFLLFVFAALFLAFLKLRYSVPKYQINAKIQIVEEGGAgelNVLKDLNVFGAEgNTEITD 80
Cdd:COG3206 10 EEEDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSD---VLLSGLSSLSAS-DSPLET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 81 EIELLKSRENFIEVVRKLKLnikysllgnvrdtelyDNYPFTINFITEDsllnkyshtffvkvlsktefryaleadeege 160
Cdd:COG3206 86 QIEILKSRPVLERVVDKLNL----------------DEDPLGEEASREA------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 161 kitfgsnistdnlgdiilipeeekrlkgfynklikvsinpvpfVAESYRNNVTVSAAGEySRILNISFKDAIPERGIAIL 240
Cdd:COG3206 119 -------------------------------------------AIERLRKNLTVEPVKG-SNVIEISYTSPDPELAAAVA 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 241 NSLIARNNLNEVEDKKAVADRTSEFINDRIAEIYSNLSSVDESAENYKESKGIADLGGQSSVNFQQSAASEQELQSANIQ 320
Cdd:COG3206 155 NALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 321 LSIASSMQNVISDQNGYEVIPTNVGLTDSNIDRAAAQYNELVSQRNRLLESSNEKNPVIVKLDQQLEGLKKSMQ------ 394
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqeaqri 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 395 -SSLNNVTNNLNLRVNSLSKSLSKINSRIYAAPSNERALRDISRKQQTTESLYLYLLQKREEAQIAFASAAPKSKVVDNA 473
Cdd:COG3206 315 lASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 474 hLANPIPVEPKRKIIYLAALMLGLFIPFSIIYVKDLMDNKVGNMVTLQKVIGEghSVLAEIPNVKNKEELIVKRRDRSIL 553
Cdd:COG3206 395 -VVPLKPVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLLLGL--PLLGPLPPLKSKRERRRARLALLLL 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 554 AESLRILRTNLDYVLRMRNkeqRGHRILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFGNEQKSRK 633
Cdd:COG3206 472 AAALAALLALLLALLLLLL---LLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLLLLLLLLL 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 634 DNVGFGLTefLSGEKLEPVDLINTLHIGESKIDVIYSGDIPPNPSELLLSERITELMDIVSSQYDYIIIDSAPLLAVTDT 713
Cdd:COG3206 549 LLLLLGGL--LLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLAALLAA 626
|
...
gi 1168746865 714 LLI 716
Cdd:COG3206 627 AVL 629
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
552-760 |
6.77e-51 |
|
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: 180.00 E-value: 6.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 552 ILAESLRILRTNLDYVLRMRNKEQRGHRILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFGNEQKS 631
Cdd:COG0489 67 LGLLLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 632 rkdnvgfGLTEFLSGEKlEPVDLIntLHIGESKIDVIYSGDIPPNPSELLLSERITELMDIVSSQYDYIIIDSAPLLAVT 711
Cdd:COG0489 147 -------GLSDVLAGEA-SLEDVI--QPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVA 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1168746865 712 DTLLIEKYADQVLYITKSGVTEKRILEYPLNLYKEGKLRSLSFIVNGVK 760
Cdd:COG0489 217 DATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNMVC 265
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
2-732 |
9.30e-50 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 187.04 E-value: 9.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 2 EKQDIDFRELLFRYVRHWKLFL----LFVFAALFLAFLklrySVPKYQINAKIQIveEGGAGElNVLKDLNVFGAEGNTE 77
Cdd:PRK09841 14 QENEIDLLRLVGELWDHRKFIIsvtaLFTLIAVAYSLL----STPIYQADTLVQV--EQKQGN-AILSGLSDMIPNSSPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 78 ITDEIELLKSRENFIEVVRKLKLNIK-----YSLLGNVRdTELYDNYPFTINFI-TEDSLLNKYSHTFFVKVLSKTefRY 151
Cdd:PRK09841 87 SAPEIQLLQSRMILGKTIAELNLRDIveqkyFPIVGRGW-ARLTKEKPGELAISwMHIPQLNGQDQQLTLTVGENG--HY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 152 ALEADEEGEKITFGSNISTDNLGDII----------LIPEEEKRLKgfynklikvSINpvpfvaeSYRNNVTVSAAGEYS 221
Cdd:PRK09841 164 TLEGEEFTVNGMVGQRLEKDGVALTIadikakpgtqFVLSQRTELE---------AIN-------ALQETFTVSERSKES 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 222 RILNISFKDAIPERGIAILNSlIARNNLNEVEDKKAVAD-RTSEFINDRIAEIYSNLSSVDESAENYKESKGIADLggqs 300
Cdd:PRK09841 228 GMLELTMTGDDPQLITRILNS-IANNYLQQNIARQAAQDsQSLEFLQRQLPEVRSELDQAEEKLNVYRQQRDSVDL---- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 301 svNFQQSAASEQELqsaniqlsiassmqnvisdqngyeviptnvgltdsNIDRaaaQYNELVSQRNRLLESSNEKNP--- 377
Cdd:PRK09841 303 --NLEAKAVLEQIV-----------------------------------NVDN---QLNELTFREAEISQLYKKDHPtyr 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 378 VIVKLDQQLEGLKKsmqsslnnvtnnlnlrvnslskslsKINSRIYAAPSNERALRDISRKQQTTESLYLYLLQKREEAQ 457
Cdd:PRK09841 343 ALLEKRQTLEQERK-------------------------RLNKRVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELS 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 458 IAFASAAPKSKVVDNAhLANPIPVEPKRKIIYLAALMLGLFIPFSIIYVKDLMDNKVGnmvTLQKVIGEGHSVLAEIP-- 535
Cdd:PRK09841 398 ISKSSAIGNVRIIDPA-VTQPQPVKPKKALNVVLGFILGLFISVGAVLARAMLRRGVE---APEQLEEHGISVYATIPms 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 536 -------NVKNKEELIVKRRDRS-------------ILAESLRILRTNLDYVLrmrnKEQRGHRILVTSSVSGEGKTFVS 595
Cdd:PRK09841 474 ewldkrtRLRKKNLFSNQQRHRTknipflavdnpadSAVEAVRALRTSLHFAM----METENNILMITGATPDSGKTFVS 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 596 SNLALIFSSTDKKVLLIGADIRNPKIFSFFG--NEQksrkdnvgfGLTEFLSGeKLEPVDLINtlHIGESKIDVIYSGDI 673
Cdd:PRK09841 550 STLAAVIAQSDQKVLFIDADLRRGYSHNLFTvsNEH---------GLSEYLAG-KDELNKVIQ--HFGKGGFDVITRGQV 617
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168746865 674 PPNPSELLLSERITELMDIVSSQYDYIIIDSAPLLAVTDTLLIEKYADQVLYITKSGVT 732
Cdd:PRK09841 618 PPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLN 676
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
555-738 |
5.11e-49 |
|
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: 171.21 E-value: 5.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 555 ESLRILRTNLDYvlrmRNKEQRGHRILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFG--NEQksr 632
Cdd:cd05387 1 EAFRTLRTNLLF----AGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGlpNEP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 633 kdnvgfGLTEFLSGeKLEPVDLIntLHIGESKIDVIYSGDIPPNPSELLLSERITELMDIVSSQYDYIIIDSAPLLAVTD 712
Cdd:cd05387 74 ------GLSEVLSG-QASLEDVI--QSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVAD 144
|
170 180
....*....|....*....|....*.
gi 1168746865 713 TLLIEKYADQVLYITKSGVTEKRILE 738
Cdd:cd05387 145 ALILAPLVDGVLLVVRAGKTRRREVK 170
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
17-759 |
7.78e-45 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 172.26 E-value: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 17 RHWKLFLLFVFAALflAFLKLRYSVPKYQINAKIQIVEEGGAgelNVLKDLNVFGAEGNTEITDEIELLKSRENFIEVVR 96
Cdd:PRK11519 31 RWWVIGITAVFALC--AVVYTFFATPIYSADALVQIEQNSGN---SLVQDIGSALANKPPASDAEIQLIRSRLVLGKTVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 97 KLKLNIK-----YSLLGNVRDtELYDNYPFTINFITEDSLLNKYSHTFFVKVLSKTefRYALEADE----EGEkitFGSN 167
Cdd:PRK11519 106 DLDLDIAvskntFPIFGAGWD-RLMGRQNETVKVTTFNRPKEMADQVFTLNVLDDK--NYQLSSDGgfsaRGQ---VGQM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 168 ISTDNLG----DIILIPEEEKRLKGFyNKLikVSINPVpfvaesyRNNVTVSAAGEYSRILNISFKDAIPERGIAILNSl 243
Cdd:PRK11519 180 LKKDGVTlmveAIHARPGTEFTVTKY-STL--GMINNL-------QNNLTVTENGKDTGVLSLTYTGEDREQIRDILNS- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 244 IARNNLNE-VEDKKAVADRTSEFINDRIAEIYSNLSSVDESAENYKESKGIADLGGQSSvnfqqsaaseqelqsaniqlS 322
Cdd:PRK11519 249 ITRNYLEQnIERKSEEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAK--------------------A 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 323 IASSMQNVisdqngyeviptnvgltdsnidraAAQYNELVSQRNRLLESSNEKNPVIVKLdqqLEGLKksmqsslnnvtn 402
Cdd:PRK11519 309 VLDSMVNI------------------------DAQLNELTFKEAEISKLYTKEHPAYRTL---LEKRK------------ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 403 nlnlrvnSLSKSLSKINSRIYAAPSNERALRDISRKQQTTESLYLYLLQKREEAQIAFASAAPKSKVVDNAhLANPIPVE 482
Cdd:PRK11519 350 -------ALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRIVDPA-ITQPGVLK 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 483 PKRKIIYLAALMLGLFIPFSIIYVKDLMDNKVGNMVTLQKVigeGHSVLAEIP-----NVKNKEELI--VKR-RDRSILA 554
Cdd:PRK11519 422 PKKALIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEH---GISVYASIPlsewqKARDSVKTIkgIKRyKQSQLLA 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 555 ---------ESLRILRTNLDYVLrMRNKeqrgHRILVTSSVS-GEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSF 624
Cdd:PRK11519 499 vgnptdlaiEAIRSLRTSLHFAM-MQAQ----NNVLMMTGVSpSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHEL 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 625 FGNeqksrkDNVGfGLTEFLSGEKLEPVDLINTlhiGESKIDVIYSGDIPPNPSELLLSERITELMDIVSSQYDYIIIDS 704
Cdd:PRK11519 574 LGT------NNVN-GLSDILIGQGDITTAAKPT---SIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDT 643
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1168746865 705 APLLAVTDTLLIEKYADQVLYITKSGVTEKRILEYPLNLYKEGKLRSLSFIVNGV 759
Cdd:PRK11519 644 PPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSI 698
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
6-737 |
1.07e-42 |
|
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: 166.43 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 6 IDFRELLFRYVRHWKLFLLFVFAALFLAFLKLRYSVPKYQINAKIQiVEEGGAGELNVLKD-LNVFGAEgnTEITDEIEL 84
Cdd:TIGR01005 4 IDLDRLLAALFANARLIAAFAAAFIALGAAYAFFARPVYEADIMIL-LDDNLNKAAEEEGDpSNLFDLD--TDAAAAIEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 85 LKSRENFIEVVRKLKLnikysllgnvrdtelydnypftinFITEDSLLNKYSHTFFVKVLSKTefRYALEADEEGEKITf 164
Cdd:TIGR01005 81 LKSGELAGKAVDKLHL------------------------SENAKILNPPRFPVDLIGAWIKS--AAGLFSEPGGFDLG- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 165 gsnistdnlgdiilipEEEKRlkgfyNKLIKVSINPVPFVAESYRNNVTVSAAGEYsRILNISFkDAIPERGIA---ILN 241
Cdd:TIGR01005 134 ----------------EEAAG-----NERIDKAAADIPEALAGEPFKLISLGAGAF-RLEDKLL-AAPIAGGVAealEAD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 242 SLIARNNLnEVEDKKAVADRTSEFINDRIAEIYSNLSSVDESAENYKESKGIADlggqssvnfQQSAASEQELQSANI-Q 320
Cdd:TIGR01005 191 QLIANFEA-QENALTAKAEALFDLEQDSQAAALEMAHDKAEIAEKAAQGEIIGE---------AQLADLNPALIAAIAdQ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 321 LSIASSMQNV--ISDQnGYEVIPTNVGLTDS---NIDRAAAQYNELVSQRNRLLESSNEK---------NPVIVKLDQQL 386
Cdd:TIGR01005 261 AAAEARADNIkrIADE-AEENAVFLAGILPKegdELEIADLKTNELRNGKGEFDLSDEFGadhpeavcsAPSLQELKAKI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 387 EGLKKSMQSSLNNVTNNLNLRVNSLSKSLSKINSRIYAAPSNERALRDISRKQQTTESLYLYLLQKREEAQIAFASAAPK 466
Cdd:TIGR01005 340 AEELQQFTASHKGEQAIAQQIEESLRGKINGIAGKLKDAPEIEQDLRELEQDAAADKELYESLLGDMEQAKLQKAFKIAK 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 467 SKVVDNAhlANPI-PVEPKRKIIYLAALMLGLFIPFSIIYVKDLMDNKVgnmvTLQKVIGE--GHSVLAEIP----NVKN 539
Cdd:TIGR01005 420 ARLIDEA--AVPEePSKPKKLMTLALAAVLGMMLGGAAAAFLEALEGGF----RDEGDIEEhlGHRSLATVPlldtQMDK 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 540 KEELI------VKRRD--------------------RSILAESLRILRTNLDYVlrMRNKEQRghRILVTSSVSGEGKTF 593
Cdd:TIGR01005 494 KAQLThahfgsVKRHDeavddtmpfqllarivpdapRSTFAEAFRNAKLACDFA--LADAENN--LIAIAGALPDEGKSF 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 594 VSSNLALIFSSTDKKVLLIGADIRNPKIFSFFGNEQKSrkdnvgfGLTEFLSGEKLEPvdliNTLHIGE-SKIDVIYSGD 672
Cdd:TIGR01005 570 IAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKP-------GLLDLLAGEASIE----AGIHRDQrPGLAFIAAGG 638
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168746865 673 I---PPNPSELLLSERITELMDIVSSQYDYIIIDSAPLLAVTDTLLIEKYADQVLYITKSGVTEKRIL 737
Cdd:TIGR01005 639 AshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVTEFERSPLGEI 706
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
555-762 |
4.42e-35 |
|
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: 132.18 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 555 ESLRILRTNLDYvlrmRNKEQRghRILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFgneqKSRKD 634
Cdd:TIGR01007 1 EYYNAIRTNIQF----SGAEIK--VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTF----KSQNK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 635 NVGfgLTEFLSGeKLEPVDLINTLHIgeSKIDVIYSGDIPPNPSELLLSERITELMDIVSSQYDYIIIDSAPLLAVTDTL 714
Cdd:TIGR01007 71 ITG--LTNFLSG-TTDLSDAICDTNI--ENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1168746865 715 LIEKYADQVLYITKSGVTEKRILEYPLNLYKEGKLRSLSFIVNGVKET 762
Cdd:TIGR01007 146 IIARACDASILVTDAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDIS 193
|
|
| pepcterm_TyrKin |
TIGR03018 |
exopolysaccharide/PEP-CTERM locus tyrosine autokinase; Members of this protein family are ... |
550-732 |
1.68e-26 |
|
exopolysaccharide/PEP-CTERM locus tyrosine autokinase; Members of this protein family are related to a known protein-tyrosine autokinase and to numerous homologs from exopolysaccharide biosynthesis region proteins, many of which are designated as chain length determinants. Most members of this family contain a short region, immediately C-terminal to the region modeled here, with an abundance of Tyr residues. These C-terminal tyrosine residues are likely to be autophosphorylation sites. Some members of this family are fusion proteins.
Pssm-ID: 274392 [Multi-domain] Cd Length: 207 Bit Score: 107.77 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 550 RSILAESLRILRTNLdyVLRMRNKEQRGHR--ILVTSSVSGEGKTFVSSNLALIFS-STDKKVLLIGADIRNPKIFSFFG 626
Cdd:TIGR03018 8 RSRIAEEFRKIKRPL--LANAFSAATKKNNnlIMVTSSLPGEGKSFTAINLAISLAqEYDKTVLLIDADLRRPSLHRTLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 627 NEQKSrkdnvgfGLTEFLSGEKLEPVDLINTLHIGesKIDVIYSGDIPPNPSELLLSERITELMDIVSSQYD--YIIIDS 704
Cdd:TIGR03018 86 LEAEP-------GLSDCLLDPVLDLADVLVPTNIG--RLSLLPAGRRHPNPTELLASQRMRSLLHELARRYPdrIIIIDT 156
|
170 180
....*....|....*....|....*...
gi 1168746865 705 APLLAVTDTLLIEKYADQVLYITKSGVT 732
Cdd:TIGR03018 157 PPLLVFSEARALARLVGQIVLVVEEGRT 184
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
206-554 |
1.19e-19 |
|
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: 93.19 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 206 ESYRNNVTVSAAGEySRILNISFKDAIPERGIAILNSLIARNNLNEVEDKKAVADRTSEFINDRIAEIYSNLSSVDESAE 285
Cdd:TIGR03007 107 TKLRKNISISLAGR-DNLFTISYEDKDPELAKDVVQTLLTIFVEETLGSKRQDSDSAQRFIDEQIKTYEKKLEAAENRLK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 286 NYKESKGiADLGGQSSVNFQQSAASEQELQSANIQLSIASSMQNVISDQNGYEvipTNVGLTDSNIDRAAAQ--YNELVS 363
Cdd:TIGR03007 186 AFKQENG-GILPDQEGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLGGE---EPVLLAGSSVANSELDgrIEALEK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 364 QRNRLLESSNEKNPVIVKLDQQLEGLKKSMQSSLNNVTNNLN---------------------------LRVNSLSKSLS 416
Cdd:TIGR03007 262 QLDALRLRYTDKHPDVIATKREIAQLEEQKEEEGSAKNGGPErgeianpvyqqlqielaeaeaeiasleARVAELTARIE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 417 KINSRIYAAPSNERALRDISRKQQTTESLYLYLLQKREEAQIA----FASAAPKSKVVDNAHLANpIPVEPKRKIIYLAA 492
Cdd:TIGR03007 342 RLESLLRTIPEVEAELTQLNRDYEVNKSNYEQLLTRRESAEVSkqmeVQDKAVSFRIIDPPIVPS-KPSGPNRPLLMLAG 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168746865 493 LMLGLFIPFSIIYVKDLMDNKVGNMVTLQKVIgeGHSVLAEIPNVKN-KEELIVKRRDRSILA 554
Cdd:TIGR03007 421 LLGGLGAGIGLAFLLSQLRPTVRSVRDLRELT--GLPVLGVIPMIATpEERRRRRRRLAAFLA 481
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
576-727 |
2.65e-12 |
|
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: 68.99 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 576 RGHRILVTSSVSGEGKTFVSSNLALIFS-STDKKVLLIGADIRNPKIFSFFGNEQKsrkdnvgFGLTEFL-SGEKLEPVD 653
Cdd:COG4963 101 RGRVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFGDVALYLDLEPR-------RGLADALrNPDRLDETL 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168746865 654 LINTLHIGESKIDVIySGDIPPNPSELLLSERITELMDIVSSQYDYIIIDSAPLL-AVTDTLLIEkyADQVLYIT 727
Cdd:COG4963 174 LDRALTRHSSGLSVL-AAPADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLnPWTLAALEA--ADEVVLVT 245
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
593-761 |
2.69e-11 |
|
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: 64.14 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 593 FVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFGNEQKsrkdnvgFGLTEFLSGEKlepvDLINTLHIGESKIDVIYSGD 672
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPK-------ATLADVLAGEA----DLEDAIVQGPGGLDVLPGGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 673 IPPNPSELLLSERITELMDIVSSQYDYIIIDSAPLL--AVTDTLLIekyADQVLYIT---KSGVTE-KRILEYplnLYKE 746
Cdd:COG0455 70 GPAELAELDPEERLIRVLEELERFYDVVLVDTGAGIsdSVLLFLAA---ADEVVVVTtpePTSITDaYALLKL---LRRR 143
|
170
....*....|....*
gi 1168746865 747 GKLRSLSFIVNGVKE 761
Cdd:COG0455 144 LGVRRAGVVVNRVRS 158
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
468-621 |
3.23e-08 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 55.84 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 468 KVVDNAhLANPIPVEPKRKIIYLAALMLGLFIPFSIIYVKDLMDNKVGNMVTLQKVIgeGHSVLAEIPNVKNKEELIVKR 547
Cdd:COG3944 151 TVLDPA-TVPASPVSPNPKLNLAIGLVLGLLLGVGLAFLRELLDTTIRSEEDIERLL--GLLLGGAVPAARSARPLLLLL 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168746865 548 RDRSILAESLRILRTNLdyvLRMRNKEQRGHRILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKI 621
Cdd:COG3944 228 ADASPRAAAARRRRRNL---LFALAAVDARTVVVVSSSLSEGKSTTTAALALALAAAAAGVVLVLADLDRRRRV 298
|
|
| Wzz |
pfam02706 |
Chain length determinant protein; This family includes proteins involved in lipopolysaccharide ... |
5-97 |
8.16e-08 |
|
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: 50.36 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 5 DIDFRELLFRYVRHWKLFLLFVFAALFLAFLKLRYSVPKYQINAKIQIVEEGGAGELNVLKDLNvfgaEGNTEITDEIEL 84
Cdd:pfam02706 2 EIDLIELLGVLWKRKKLIILVTLLFTLLAAAYAFLATPKYTATAQILVPQKKGEAGSLLGSDLQ----AGLQLASTEIEI 77
|
90
....*....|...
gi 1168746865 85 LKSRENFIEVVRK 97
Cdd:pfam02706 78 LKSRDVLEKVIDE 90
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
578-706 |
8.82e-08 |
|
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.
Pssm-ID: 349757 [Multi-domain] Cd Length: 213 Bit Score: 53.27 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 578 HRILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFGNEQKSRKDnvgfglteflSGEKLEPV--DLI 655
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQ----------SEEGIVPVevGGI 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1168746865 656 NTLHIG---ESKIDVIYSGDIppnpsellLSERITE-LMDIVSSQYDYIIIDSAP 706
Cdd:cd02037 71 KVMSIGfllPEDDAVIWRGPM--------KSGAIKQfLKDVDWGELDYLIIDLPP 117
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
580-711 |
2.04e-07 |
|
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: 52.73 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 580 ILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSF-FGNEQKSRKDNVGFGLTeflSGEKLEPVdlINTL 658
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEgLEGDIAPALQALAEGLK---GRVNLDPI--LLKE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168746865 659 HIGESKIDVIYSG----DIPPNPSELLLSERITELMDIVSSQYDYIIIDSAPLLAVT 711
Cdd:pfam01656 76 KSDEGGLDLIPGNidleKFEKELLGPRKEERLREALEALKEDYDYVIIDGAPGLGEL 132
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
580-760 |
3.17e-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: 52.19 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 580 ILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFGNEQKsrkdnvgFGLTEFLSGEK-LEpvDLINTl 658
Cdd:cd02038 3 IAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPK-------KTLGDVLKGRVsLE--DIIVE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 659 hiGESKIDVIYSG-------DIPPNPSELLlserITELMDIVsSQYDYIIIDSAPLLA--VTDTLLIekyADQVLYITKS 729
Cdd:cd02038 73 --GPEGLDIIPGGsgmeelaNLDPEQKAKL----IEELSSLE-SNYDYLLIDTGAGISrnVLDFLLA---ADEVIVVTTP 142
|
170 180 190
....*....|....*....|....*....|....
gi 1168746865 730 GVTEkrILE-YPL--NLYKEGKLRSLSFIVNGVK 760
Cdd:cd02038 143 EPTS--ITDaYALikVLSRRGGKKNFRLIVNMAR 174
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
436-507 |
3.27e-07 |
|
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: 48.36 E-value: 3.27e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168746865 436 SRKQQTTESLYLYLLQKREEAQIAFASAAPKSKVVDNAhLANPIPVEPKRKIIYLAALMLGLFIPFSIIYVK 507
Cdd:pfam13807 10 TRDVEVNTEIYTQLLNSNQELEVVKAGTVGNVRIVDTA-VVPPKPVKPKKALIVVLALLLGLMLGVGLVLLR 80
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
588-716 |
1.89e-05 |
|
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: 46.78 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 588 GEGKTFVSSNLALIFSSTDKKVLLIGADirnP-----KIFSFfgneqksRKDNVGFGLTEFLSGEKlEPVDLINTLHIge 662
Cdd:COG1192 12 GVGKTTTAVNLAAALARRGKRVLLIDLD---PqgnltSGLGL-------DPDDLDPTLYDLLLDDA-PLEDAIVPTEI-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168746865 663 SKIDVIysgdippnPSELLLSERITELMDI-------------VSSQYDYIIIDSAPL--------LAVTDTLLI 716
Cdd:COG1192 79 PGLDLI--------PANIDLAGAEIELVSRpgrelrlkralapLADDYDYILIDCPPSlglltlnaLAAADSVLI 145
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
6-111 |
2.30e-04 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 43.90 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 6 IDFRELLFRYVRHWKLFLLFVFAALFLAFLKLRYSVPKYQINAKIQIVEEGGAGELNVLKDLNVfgaeGNTEITDEIELL 85
Cdd:COG3944 2 MDLREYLRILRRRWWLILLLTLLGALAALASSFLITPVYQASTTLLVSTSSGSDASDLYQGIQT----AQQLVNTYAELL 77
|
90 100
....*....|....*....|....*..
gi 1168746865 86 KSRENFIEVVRKLKLNIKYS-LLGNVR 111
Cdd:COG3944 78 KSPAVLEEVIDELGLDLSPEeLAKKIS 104
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
588-724 |
2.54e-04 |
|
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: 42.57 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 588 GEGKTFVSSNLALIFSSTDKKVLLIGADirnPKIFSFFGNeqKSRKDNVGFGLTEFLSGEKlEPVDLINtlHIGESKIDV 667
Cdd:pfam13614 12 GVGKTTTSVNLAAALAKKGKKVLLIDLD---PQGNATSGL--GIDKNNVEKTIYELLIGEC-NIEEAII--KTVIENLDL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168746865 668 IysgdippnPSELLLSERITELMDI-------------VSSQYDYIIIDSAPLLAV-TDTLLIEkyADQVL 724
Cdd:pfam13614 84 I--------PSNIDLAGAEIELIGIenrenilkealepVKDNYDYIIIDCPPSLGLlTINALTA--SDSVL 144
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
580-706 |
1.15e-03 |
|
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: 41.64 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 580 ILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFGNEQKsrkdnvgfglteflsgeklePVDLINTLh 659
Cdd:TIGR01969 3 ITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDK--------------------PVTLHDVL- 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168746865 660 IGESKI-DVIYSG--DIPPNPSELLLS-------ERITELMDIVSSQYDYIIIDsAP 706
Cdd:TIGR01969 62 AGEADIkDAIYEGpfGVKVIPAGVSLEglrkadpDKLEDVLKEIIDDTDFLLID-AP 117
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
579-615 |
1.31e-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: 38.95 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1168746865 579 RILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGAD 615
Cdd:cd01983 2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
588-654 |
3.25e-03 |
|
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: 40.04 E-value: 3.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168746865 588 GEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKIFSFFGneqKSRKDNVGFGLTEFLSGEKLEPVDL 654
Cdd:cd02117 10 GIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTG---GKVPPTIDEMLTEDGTAEELRREDL 73
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
580-738 |
3.38e-03 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 40.06 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 580 ILVTSSVSGEGKTFVSSNLALIFsstdKKVLLIGADIRNPKIFSFFGNEQKSRKDNVGFGLTE----------------- 642
Cdd:cd03110 2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFidqekcircgncervck 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 643 ---FLSGEKLEPVDL--------------INTLHIGESKIDVIY---SGDIPPNPSELLLSER-----ITELMDIVSSQ- 696
Cdd:cd03110 78 fgaILEFFQKLIVDEslcegcgacviicpRGAIYLKDRDTGKIFissSDGGPLVHGRLNIGEEnsgklVTELRKKALERs 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1168746865 697 --YDYIIIDSAPLLA--VTDTLlieKYADQVLYI---TKSGVTE-KRILE 738
Cdd:cd03110 158 keCDLAIIDGPPGTGcpVVASI---TGADAVLLVtepTPSGLHDlKRAIE 204
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
578-706 |
6.61e-03 |
|
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.
Pssm-ID: 396792 Cd Length: 302 Bit Score: 39.26 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 578 HRILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIG-------ADIRNPKifsfFGNEQKSRKDN---VGFGLTEFLSGE 647
Cdd:pfam02374 1 MRWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLIStdpahslSDSFNQK----FGHEPTKVKENlsaMEIDPNMELEEY 76
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168746865 648 KLEPVDLINTLHIGESKIDVIYSG-DIPPNPSELLLSERITELMDivSSQYDYIIIDSAP 706
Cdd:pfam02374 77 WQEVQKYMNALLGLRMLEGILAEElASLPGIDEAASFDEFKKYMD--EGEYDVVVFDTAP 134
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| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
578-621 |
8.62e-03 |
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NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.
Pssm-ID: 431392 [Multi-domain] Cd Length: 246 Bit Score: 38.59 E-value: 8.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1168746865 578 HRILVTSSVSGEGKTFVSSNLALIFSSTDKKVLLIGADIRNPKI 621
Cdd:pfam10609 4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSI 47
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