|
Name |
Accession |
Description |
Interval |
E-value |
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
30-738 |
1.43e-59 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 213.73 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 30 VRVYLNLVLRKWFIIVAFAGAGLVVTSYLSTQDPSTYVGRFEILIEPVTSAEKLTDASVLTRSNDlpsqellnlDYPTQL 109
Cdd:COG3206 17 LRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSSLSASDS---------PLETQI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 110 KILKSTVLLSKIAAEVH----NILPQIPEAAMLQNLQKNLIVKRVQEgnsrfdyTKILEVIYEGNDAVLVETVLKVTAEQ 185
Cdd:COG3206 88 EILKSRPVLERVVDKLNldedPLGEEASREAAIERLRKNLTVEPVKG-------SNVIEISYTSPDPELAAAVANALAEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 186 YLQYSLQERENSLQAGVSFIDEQIPILETQIRALQGQQRTLQQRYNIISPNQQATNLNEAYQANQLDIQKIDEELEELRS 265
Cdd:COG3206 161 YLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 266 LKSNLESTLGLSPSEalvVLDLSQNPERQNLLQQLQEVETMIAAESSRFTNENPIMQDLFQKRNNLQTLLETRTKEILKS 345
Cdd:COG3206 241 RLAALRAQLGSGPDA---LPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 346 sslkgdnnpnifmfqntsritmldqlivTQNEIAKRLTRRQVLVANQERLRINLDQFPTIAAQYDEVARQLDLKKGLLDT 425
Cdd:COG3206 318 ----------------------------LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 426 LANQRETLRVEAAQQDVPWKIISAPAIPRGPDGlpisfpPDPKKKMIAGMGSGLVLGLLLAIAWERSRNIFYSNSDLKFG 505
Cdd:COG3206 370 LLQRLEEARLAEALTVGNVRVIDPAVVPLKPVS------PKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 506 LGYSVWGELPLLDSGIAHDKDALEDEVLPTEANEAIVAmgedRGQQIYTNFYFQYQEQGIRSMAMTAIDNESGQASVTMQ 585
Cdd:COG3206 444 LGLPLLGPLPPLKSKRERRRARLALLLLAAALAALLAL----LLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAA 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 586 FARAAVNAGQTVLVIDTNLQHPDIHHHGNNTDELEQGLVNVLNSDTDPQQLLNLVHYEDGLAIIPVGTMNAGHPIRLQRW 665
Cdd:COG3206 520 AAAAAALLLLLLLLLLLDLLLLLLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLL 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370134019 666 LSRLDPALQTlthkYDLVIYNAPLLTVPDTPFLLNRTDGVCLIVRLKYTSQSQTHQALTTVEKFQIPVLGVIA 738
Cdd:COG3206 600 LLLLLLLLLS----DDLILDLVPLLAALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVV 668
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
551-739 |
1.71e-22 |
|
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: 95.71 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 551 QIYTNFYFQYQEQGIRSMAMTAIDNESGQASVTMQFARAAVNAGQTVLVIDTNLQHPDIHHhgNNTDELEQGLVNVLNSD 630
Cdd:cd05387 5 TLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHR--LLGLPNEPGLSEVLSGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 631 TDPQQLLnLVHYEDGLAIIPVGTMNAGHPIRLQRwlSRLDPALQTLTHKYDLVIYNA-PLLTVPDTPFLLNRTDGVCLIV 709
Cdd:cd05387 83 ASLEDVI-QSTNIPNLDVLPAGTVPPNPSELLSS--PRFAELLEELKEQYDYVIIDTpPVLAVADALILAPLVDGVLLVV 159
|
170 180 190
....*....|....*....|....*....|
gi 1370134019 710 RLKYTSQSQTHQALTTVEKFQIPVLGVIAT 739
Cdd:cd05387 160 RAGKTRRREVKEALERLEQAGAKVLGVVLN 189
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
28-737 |
5.29e-15 |
|
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: 78.99 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 28 NLVRvYLNLVLRKWFIIVAFAGAGLVV-TSYLSTQDPsTYVGRFEILIE--PVTSAEKLTDASvltrsndlpSQELLNLD 104
Cdd:TIGR01005 5 DLDR-LLAALFANARLIAAFAAAFIALgAAYAFFARP-VYEADIMILLDdnLNKAAEEEGDPS---------NLFDLDTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 105 YPTQLKILKSTVLLSKIAAEVH---NILPQIP-----------------------------EAAMLQNLQKN-LIVKRVQ 151
Cdd:TIGR01005 74 AAAAIEILKSGELAGKAVDKLHlseNAKILNPprfpvdligawiksaaglfsepggfdlgeEAAGNERIDKAaADIPEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 152 EGNsRFDYTKILEVIYEGNDAVLVETVLKVTAEQYL------QYSLQERENSLQAGVSFIDEQipilETQIRALQGQQRT 225
Cdd:TIGR01005 154 AGE-PFKLISLGAGAFRLEDKLLAAPIAGGVAEALEadqliaNFEAQENALTAKAEALFDLEQ----DSQAAALEMAHDK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 226 LQ-----QRYNIISpNQQATNLNEAYQANQLDIQKIDEELEELRSLKSNLESTL----GLSPSEA--LVVLDLSQNPERq 294
Cdd:TIGR01005 229 AEiaekaAQGEIIG-EAQLADLNPALIAAIADQAAAEARADNIKRIADEAEENAvflaGILPKEGdeLEIADLKTNELR- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 295 nLLQQLQEVETMIAAESSRFTNENPIMQDLFQKRNNLQTLLetrtkeilkSSSLKGdnnpnifmfqntsritmldqlivt 374
Cdd:TIGR01005 307 -NGKGEFDLSDEFGADHPEAVCSAPSLQELKAKIAEELQQF---------TASHKG------------------------ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 375 QNEIAKrlTRRQVLVANQERLRINLDQFPTIAAQYDEVARQLDLKKGLLDTLANQRETLRVEAAQQDVPWKIISAPAIPR 454
Cdd:TIGR01005 353 EQAIAQ--QIEESLRGKINGIAGKLKDAPEIEQDLRELEQDAAADKELYESLLGDMEQAKLQKAFKIAKARLIDEAAVPE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 455 GPDglpisfppDPKKKMIAGMGSGLVLGLLLAIAWERS--RNIFYSNSDLKFGLGYSVWGELPLLDS------------- 519
Cdd:TIGR01005 431 EPS--------KPKKLMTLALAAVLGMMLGGAAAAFLEalEGGFRDEGDIEEHLGHRSLATVPLLDTqmdkkaqlthahf 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 520 GIAHDKDALEDEVLPTEANEAIV-----AMGEDRGQQIYTNFYFQYQEQGIRSMAMTAIDNESGQASVTMQFARAAVNAG 594
Cdd:TIGR01005 503 GSVKRHDEAVDDTMPFQLLARIVpdaprSTFAEAFRNAKLACDFALADAENNLIAIAGALPDEGKSFIAANFAALIAAGG 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 595 QTVLVIDTNLQHPDIHHHgnNTDELEQGLVNVLNSDTDPQQLLNlVHYEDGLAIIPVGTMNaghpirLQRWLSR---LDP 671
Cdd:TIGR01005 583 KRTLLIDADIRKGGLHQM--FGKAPKPGLLDLLAGEASIEAGIH-RDQRPGLAFIAAGGAS------HFPHNPNellANP 653
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370134019 672 AL----QTLTHKYDLVIYN-APLLTVPDTPFLLNRTDGVCLIVRLKYTSQSQTHQALTTVEKFQIPVLGVI 737
Cdd:TIGR01005 654 AMaeliDNARNAFDLVLVDlAALAAVADAAAFAALADGILFVTEFERSPLGEIRDLIHQEPHANSDVLGVI 724
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
115-398 |
8.56e-04 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 42.83 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 115 TVLLSKIAAEVHNI--LPQIPEAAMLQNLQKNLIVkrVQEGNSrfdyTKILEVIYEGNDAVLVETVLKVTAEQYLQYSLQ 192
Cdd:PRK11519 186 TLMVEAIHARPGTEftVTKYSTLGMINNLQNNLTV--TENGKD----TGVLSLTYTGEDREQIRDILNSITRNYLEQNIE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 193 ERENSLQAGVSFIDEQIPiletQIRAlqgqqrtlqqryniispnqqatNLNEAyqANQLDIQKIDEELEELrslksnles 272
Cdd:PRK11519 260 RKSEEASKSLAFLAQQLP----EVRS----------------------RLDVA--ENKLNAFRQDKDSVDL--------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 273 tlglsPSEALVVLDLSQNPERQnlLQQLqeveTMIAAESSR-FTNENPIMQDLFQKRnnlQTLLETRTKeilksssLKGd 351
Cdd:PRK11519 303 -----PLEAKAVLDSMVNIDAQ--LNEL----TFKEAEISKlYTKEHPAYRTLLEKR---KALEDEKAK-------LNG- 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1370134019 352 nnpnifmfqntsRITMLDQlivTQNEIAkRLTR-----RQV---LVANQERLRIN 398
Cdd:PRK11519 361 ------------RVTAMPK---TQQEIV-RLTRdvesgQQVymqLLNKQQELKIT 399
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
586-739 |
1.65e-03 |
|
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: 40.79 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 586 FARAAVNAGQTVLVIDTNLQHPDIHHHG--NNTDELEQGLVNVLNSDTDPQQLLNLVHY-EDGLAIIP--VGTMNAGHPI 660
Cdd:pfam01656 19 LARALARRGLRVLLIDLDPQSNNSSVEGleGDIAPALQALAEGLKGRVNLDPILLKEKSdEGGLDLIPgnIDLEKFEKEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 661 RLQRWLSRLDPALQTLTHKYDLVIYNAP-----------------LLTVPDTPFLLNrtdGVCLIVRLkytsqsqTHQAL 723
Cdd:pfam01656 99 LGPRKEERLREALEALKEDYDYVIIDGApglgellrnaliaadyvIIPLEPEVILVE---DAKRLGGV-------IAALV 168
|
170
....*....|....*.
gi 1370134019 724 TTVEKFQIPVLGVIAT 739
Cdd:pfam01656 169 GGYALLGLKIIGVVLN 184
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
30-738 |
1.43e-59 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 213.73 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 30 VRVYLNLVLRKWFIIVAFAGAGLVVTSYLSTQDPSTYVGRFEILIEPVTSAEKLTDASVLTRSNDlpsqellnlDYPTQL 109
Cdd:COG3206 17 LRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSSLSASDS---------PLETQI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 110 KILKSTVLLSKIAAEVH----NILPQIPEAAMLQNLQKNLIVKRVQEgnsrfdyTKILEVIYEGNDAVLVETVLKVTAEQ 185
Cdd:COG3206 88 EILKSRPVLERVVDKLNldedPLGEEASREAAIERLRKNLTVEPVKG-------SNVIEISYTSPDPELAAAVANALAEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 186 YLQYSLQERENSLQAGVSFIDEQIPILETQIRALQGQQRTLQQRYNIISPNQQATNLNEAYQANQLDIQKIDEELEELRS 265
Cdd:COG3206 161 YLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 266 LKSNLESTLGLSPSEalvVLDLSQNPERQNLLQQLQEVETMIAAESSRFTNENPIMQDLFQKRNNLQTLLETRTKEILKS 345
Cdd:COG3206 241 RLAALRAQLGSGPDA---LPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 346 sslkgdnnpnifmfqntsritmldqlivTQNEIAKRLTRRQVLVANQERLRINLDQFPTIAAQYDEVARQLDLKKGLLDT 425
Cdd:COG3206 318 ----------------------------LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 426 LANQRETLRVEAAQQDVPWKIISAPAIPRGPDGlpisfpPDPKKKMIAGMGSGLVLGLLLAIAWERSRNIFYSNSDLKFG 505
Cdd:COG3206 370 LLQRLEEARLAEALTVGNVRVIDPAVVPLKPVS------PKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 506 LGYSVWGELPLLDSGIAHDKDALEDEVLPTEANEAIVAmgedRGQQIYTNFYFQYQEQGIRSMAMTAIDNESGQASVTMQ 585
Cdd:COG3206 444 LGLPLLGPLPPLKSKRERRRARLALLLLAAALAALLAL----LLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAA 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 586 FARAAVNAGQTVLVIDTNLQHPDIHHHGNNTDELEQGLVNVLNSDTDPQQLLNLVHYEDGLAIIPVGTMNAGHPIRLQRW 665
Cdd:COG3206 520 AAAAAALLLLLLLLLLLDLLLLLLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLL 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370134019 666 LSRLDPALQTlthkYDLVIYNAPLLTVPDTPFLLNRTDGVCLIVRLKYTSQSQTHQALTTVEKFQIPVLGVIA 738
Cdd:COG3206 600 LLLLLLLLLS----DDLILDLVPLLAALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVV 668
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
551-739 |
1.71e-22 |
|
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: 95.71 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 551 QIYTNFYFQYQEQGIRSMAMTAIDNESGQASVTMQFARAAVNAGQTVLVIDTNLQHPDIHHhgNNTDELEQGLVNVLNSD 630
Cdd:cd05387 5 TLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHR--LLGLPNEPGLSEVLSGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 631 TDPQQLLnLVHYEDGLAIIPVGTMNAGHPIRLQRwlSRLDPALQTLTHKYDLVIYNA-PLLTVPDTPFLLNRTDGVCLIV 709
Cdd:cd05387 83 ASLEDVI-QSTNIPNLDVLPAGTVPPNPSELLSS--PRFAELLEELKEQYDYVIIDTpPVLAVADALILAPLVDGVLLVV 159
|
170 180 190
....*....|....*....|....*....|
gi 1370134019 710 RLKYTSQSQTHQALTTVEKFQIPVLGVIAT 739
Cdd:cd05387 160 RAGKTRRREVKEALERLEQAGAKVLGVVLN 189
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
578-737 |
1.08e-17 |
|
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: 84.08 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 578 GQASVTMQFARAAVNAGQTVLVIDTNLQHPDIHHHGNNTDEleQGLVNVLNSDTDPQQLLNLVHYEdGLAIIPVGTMNAG 657
Cdd:COG0489 105 GKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENR--PGLSDVLAGEASLEDVIQPTEVE-GLDVLPAGPLPPN 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 658 HPIRLQRwlSRLDPALQTLTHKYDLVIYNA-PLLTVPDTPFLLNRTDGVCLIVRLKYTSQSQTHQALTTVEKFQIPVLGV 736
Cdd:COG0489 182 PSELLAS--KRLKQLLEELRGRYDYVIIDTpPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGV 259
|
.
gi 1370134019 737 I 737
Cdd:COG0489 260 V 260
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
28-737 |
5.29e-15 |
|
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: 78.99 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 28 NLVRvYLNLVLRKWFIIVAFAGAGLVV-TSYLSTQDPsTYVGRFEILIE--PVTSAEKLTDASvltrsndlpSQELLNLD 104
Cdd:TIGR01005 5 DLDR-LLAALFANARLIAAFAAAFIALgAAYAFFARP-VYEADIMILLDdnLNKAAEEEGDPS---------NLFDLDTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 105 YPTQLKILKSTVLLSKIAAEVH---NILPQIP-----------------------------EAAMLQNLQKN-LIVKRVQ 151
Cdd:TIGR01005 74 AAAAIEILKSGELAGKAVDKLHlseNAKILNPprfpvdligawiksaaglfsepggfdlgeEAAGNERIDKAaADIPEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 152 EGNsRFDYTKILEVIYEGNDAVLVETVLKVTAEQYL------QYSLQERENSLQAGVSFIDEQipilETQIRALQGQQRT 225
Cdd:TIGR01005 154 AGE-PFKLISLGAGAFRLEDKLLAAPIAGGVAEALEadqliaNFEAQENALTAKAEALFDLEQ----DSQAAALEMAHDK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 226 LQ-----QRYNIISpNQQATNLNEAYQANQLDIQKIDEELEELRSLKSNLESTL----GLSPSEA--LVVLDLSQNPERq 294
Cdd:TIGR01005 229 AEiaekaAQGEIIG-EAQLADLNPALIAAIADQAAAEARADNIKRIADEAEENAvflaGILPKEGdeLEIADLKTNELR- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 295 nLLQQLQEVETMIAAESSRFTNENPIMQDLFQKRNNLQTLLetrtkeilkSSSLKGdnnpnifmfqntsritmldqlivt 374
Cdd:TIGR01005 307 -NGKGEFDLSDEFGADHPEAVCSAPSLQELKAKIAEELQQF---------TASHKG------------------------ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 375 QNEIAKrlTRRQVLVANQERLRINLDQFPTIAAQYDEVARQLDLKKGLLDTLANQRETLRVEAAQQDVPWKIISAPAIPR 454
Cdd:TIGR01005 353 EQAIAQ--QIEESLRGKINGIAGKLKDAPEIEQDLRELEQDAAADKELYESLLGDMEQAKLQKAFKIAKARLIDEAAVPE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 455 GPDglpisfppDPKKKMIAGMGSGLVLGLLLAIAWERS--RNIFYSNSDLKFGLGYSVWGELPLLDS------------- 519
Cdd:TIGR01005 431 EPS--------KPKKLMTLALAAVLGMMLGGAAAAFLEalEGGFRDEGDIEEHLGHRSLATVPLLDTqmdkkaqlthahf 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 520 GIAHDKDALEDEVLPTEANEAIV-----AMGEDRGQQIYTNFYFQYQEQGIRSMAMTAIDNESGQASVTMQFARAAVNAG 594
Cdd:TIGR01005 503 GSVKRHDEAVDDTMPFQLLARIVpdaprSTFAEAFRNAKLACDFALADAENNLIAIAGALPDEGKSFIAANFAALIAAGG 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 595 QTVLVIDTNLQHPDIHHHgnNTDELEQGLVNVLNSDTDPQQLLNlVHYEDGLAIIPVGTMNaghpirLQRWLSR---LDP 671
Cdd:TIGR01005 583 KRTLLIDADIRKGGLHQM--FGKAPKPGLLDLLAGEASIEAGIH-RDQRPGLAFIAAGGAS------HFPHNPNellANP 653
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370134019 672 AL----QTLTHKYDLVIYN-APLLTVPDTPFLLNRTDGVCLIVRLKYTSQSQTHQALTTVEKFQIPVLGVI 737
Cdd:TIGR01005 654 AMaeliDNARNAFDLVLVDlAALAAVADAAAFAALADGILFVTEFERSPLGEIRDLIHQEPHANSDVLGVI 724
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
30-545 |
3.48e-13 |
|
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: 72.39 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 30 VRVYLN-LVLRKWFIIVAFAGAGLVvTSYLSTQDPSTYVGRFEILIEPVTSAEKLTDASVLTRSNDlpsqellnldypTQ 108
Cdd:TIGR03007 3 LLSYLKgIWRRRWLFVAVAWVVMIV-GWGVVYFLPDRYEASARVYVDTQSVLRPLLKGIAVTPNVD------------QK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 109 LKILKSTVL----LSKIAAEVhNILPQI--PEA--AMLQNLQKNLIVKRVQEGNsrfdytkILEVIYEGNDAVL----VE 176
Cdd:TIGR03007 70 IRIMSRTLLsrpnLEKVIRML-DLDLGAksPAQleALITKLRKNISISLAGRDN-------LFTISYEDKDPELakdvVQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 177 TVLKVTAEQYLQYSLQERENSLQagvsFIDEQIPILETQIRALQGQQRTLQQRYNIISPNQQAtNLNEAYQANQLDIQKI 256
Cdd:TIGR03007 142 TLLTIFVEETLGSKRQDSDSAQR----FIDEQIKTYEKKLEAAENRLKAFKQENGGILPDQEG-DYYSEISEAQEELEAA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 257 DEELEELRSLKSNLESTLGlSPSEALVVLDLSQNPERQNLLQQLqevETMIAAESSRFTNENPimqDLFQKRNNLQTLLE 336
Cdd:TIGR03007 217 RLELNEAIAQRDALKRQLG-GEEPVLLAGSSVANSELDGRIEAL---EKQLDALRLRYTDKHP---DVIATKREIAQLEE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 337 TRTKEI-LKSSSLKGDNNPNIFMFQNTSRITMLDQLIVTQNEIAKRLTRRqvlvanQERLRINLDQFPTIAAQYDEVARQ 415
Cdd:TIGR03007 290 QKEEEGsAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTAR------IERLESLLRTIPEVEAELTQLNRD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 416 LDLKKGLLDTLANQRETLRV--EAAQQD--VPWKIISAPAIPRGPDGlpisfpPDPKKKMIAGMGSGLVLGLLLAIAWER 491
Cdd:TIGR03007 364 YEVNKSNYEQLLTRRESAEVskQMEVQDkaVSFRIIDPPIVPSKPSG------PNRPLLMLAGLLGGLGAGIGLAFLLSQ 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1370134019 492 SRNIFYSNSDLKFGLGYSVWGELPLLDSGIAHDKDALEDEVLPTEANEAIVAMG 545
Cdd:TIGR03007 438 LRPTVRSVRDLRELTGLPVLGVIPMIATPEERRRRRRRLAAFLASAGLLIAVYG 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-441 |
1.16e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 183 AEQYLQYSLQERENSLQagvsfideqipILETQIRALQGQQRTLQQryniispnqQATNLNEAYQANQLDIQKIDEELEE 262
Cdd:TIGR02168 212 AERYKELKAELRELELA-----------LLVLRLEELREELEELQE---------ELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 263 LRSLKSNLESTLG-----------------------------LSPSEALVVLDLSQNPERQNLLQ--------QLQEVET 305
Cdd:TIGR02168 272 LRLEVSELEEEIEelqkelyalaneisrleqqkqilrerlanLERQLEELEAQLEELESKLDELAeelaeleeKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 306 MIAAESSRFTNENPIMQDLFQKRNNLQTLLET-RTKEILKSSSLKgdnnpnifmfQNTSRITMLDQLIvtqNEIAKRLTR 384
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETlRSKVAQLELQIA----------SLNNEIERLEARL---ERLEDRRER 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370134019 385 RQvlvANQERLRINLDqfptiAAQYDEVARQLDLKKGLLDTLANQRETLRVEAAQQD 441
Cdd:TIGR02168 419 LQ---QEIEELLKKLE-----EAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-440 |
1.46e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 182 TAEQYLQYSLQERE----------NSLQAGVSFIDEQIPILETQIRALQGQQRTLQQRYNIIspNQQATNLNEAYQANQL 251
Cdd:COG1196 211 KAERYRELKEELKEleaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEEL--RLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 252 DIQKIDEELEELRSLKSNLESTLglspsEALVVLDLSQNPERQNLLQQLQEVETMIAAESSRFTNENPIMQDLFQKRNNL 331
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERR-----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 332 QTLLETRTKEILKSSSLKGDnnpnifmfQNTSRITMLDQLIVTQNEIAKRLTRRQVLVANQERLRINLDQfptIAAQYDE 411
Cdd:COG1196 364 EEALLEAEAELAEAEEELEE--------LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---LEEALAE 432
|
250 260
....*....|....*....|....*....
gi 1370134019 412 VARQLDLKKGLLDTLANQRETLRVEAAQQ 440
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
202-316 |
3.85e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 202 VSFIDEQIPILETQIRALQGQQRTLQQRYNIISPNQQATNLNEayQANQLDIQKIDEELeELRSLKSNlestlgLSPSea 281
Cdd:COG3524 179 VRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ--LIATLEGQLAELEA-ELAALRSY------LSPN-- 247
|
90 100 110
....*....|....*....|....*....|....*
gi 1370134019 282 lvvldlsqNPERQNLLQQLQEVETMIAAESSRFTN 316
Cdd:COG3524 248 --------SPQVRQLRRRIAALEKQIAAERARLTG 274
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
581-715 |
5.63e-04 |
|
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: 42.18 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 581 SVTMQFARAAVNAGQTVLVIDTNLQHPDIHHHGNNTDelEQGLVNVLNSDTDPQQLlnLVHYEDGLAIIPVGTmnaghpi 660
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEP--KATLADVLAGEADLEDA--IVQGPGGLDVLPGGS------- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370134019 661 RLQRWlSRLDP------ALQTLTHKYDLVIYNAPLLTVPDTPFLLNRTDGVCLIVRLKYTS 715
Cdd:COG0455 70 GPAEL-AELDPeerlirVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTS 129
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
115-398 |
8.56e-04 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 42.83 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 115 TVLLSKIAAEVHNI--LPQIPEAAMLQNLQKNLIVkrVQEGNSrfdyTKILEVIYEGNDAVLVETVLKVTAEQYLQYSLQ 192
Cdd:PRK11519 186 TLMVEAIHARPGTEftVTKYSTLGMINNLQNNLTV--TENGKD----TGVLSLTYTGEDREQIRDILNSITRNYLEQNIE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 193 ERENSLQAGVSFIDEQIPiletQIRAlqgqqrtlqqryniispnqqatNLNEAyqANQLDIQKIDEELEELrslksnles 272
Cdd:PRK11519 260 RKSEEASKSLAFLAQQLP----EVRS----------------------RLDVA--ENKLNAFRQDKDSVDL--------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 273 tlglsPSEALVVLDLSQNPERQnlLQQLqeveTMIAAESSR-FTNENPIMQDLFQKRnnlQTLLETRTKeilksssLKGd 351
Cdd:PRK11519 303 -----PLEAKAVLDSMVNIDAQ--LNEL----TFKEAEISKlYTKEHPAYRTLLEKR---KALEDEKAK-------LNG- 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1370134019 352 nnpnifmfqntsRITMLDQlivTQNEIAkRLTR-----RQV---LVANQERLRIN 398
Cdd:PRK11519 361 ------------RVTAMPK---TQQEIV-RLTRdvesgQQVymqLLNKQQELKIT 399
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
191-411 |
1.20e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 191 LQERENSLQAGVSFIDEQIPILETQIRALQGQQRTLQQRYNIIspNQQATNLNEAYQANQLDIQKIDEELEE-LRSL-KS 268
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL--EAELAELEKEIAELRAELEAQKEELAElLRALyRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 269 NLESTLGL-----SPSEALVVLDLSQ--NPERQNLLQQLQEVETMIAAessrftnenpIMQDLFQKRNNLQTLLETRTKE 341
Cdd:COG4942 117 GRQPPLALllspeDFLDAVRRLQYLKylAPARREQAEELRADLAELAA----------LRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 342 ILKSSSLKgdnnpnifmfqnTSRITMLDQLivtQNEIAKRLTRRQVLVANQERLRINLDQFPTIAAQYDE 411
Cdd:COG4942 187 RAALEALK------------AERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
586-739 |
1.65e-03 |
|
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: 40.79 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 586 FARAAVNAGQTVLVIDTNLQHPDIHHHG--NNTDELEQGLVNVLNSDTDPQQLLNLVHY-EDGLAIIP--VGTMNAGHPI 660
Cdd:pfam01656 19 LARALARRGLRVLLIDLDPQSNNSSVEGleGDIAPALQALAEGLKGRVNLDPILLKEKSdEGGLDLIPgnIDLEKFEKEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 661 RLQRWLSRLDPALQTLTHKYDLVIYNAP-----------------LLTVPDTPFLLNrtdGVCLIVRLkytsqsqTHQAL 723
Cdd:pfam01656 99 LGPRKEERLREALEALKEDYDYVIIDGApglgellrnaliaadyvIIPLEPEVILVE---DAKRLGGV-------IAALV 168
|
170
....*....|....*.
gi 1370134019 724 TTVEKFQIPVLGVIAT 739
Cdd:pfam01656 169 GGYALLGLKIIGVVLN 184
|
|
| CBP_BcsQ |
pfam06564 |
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ... |
567-721 |
2.10e-03 |
|
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.
Pssm-ID: 429004 [Multi-domain] Cd Length: 234 Bit Score: 40.44 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 567 SMAMTAIDNESGQASVTMQFARAAVNAGQTVLVIDTNlqhPD--IHHHGNNTDELEQGLVNVLNSDTDPQQllNLVHYED 644
Cdd:pfam06564 3 ILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLS---PDnlLRLHFNVPFEHRQGWARAELDGADWRD--AALEYTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 645 GLAIIPVGTMNAGHPIRLQRWLSRLD---PALQTLTHKYDLVIYNAPLLTVPDTPFLLNRTDGVCLIVRLKYTSQSQTHQ 721
Cdd:pfam06564 78 GLDLLPFGRLSVEEQENLQQLQPDPGawcRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPDANCHVLLHQ 157
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
581-739 |
2.19e-03 |
|
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: 40.61 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 581 SVTMQFARAAVNAGQTVLVIDTNLQHPDIHHHGNNTDELEQGLVNVLNSDTDPQQLLNLVHYEdGLAIIPVGTMNAGHPI 660
Cdd:COG1192 17 TTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIP-GLDLIPANIDLAGAEI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 661 RL---QRWLSRLDPALQTLTHKYDLVIYnaplltvpDTP---FLLNR-----TDGVCLIVRLKYTSQSQTHQALTTVEKF 729
Cdd:COG1192 96 ELvsrPGRELRLKRALAPLADDYDYILI--------DCPpslGLLTLnalaaADSVLIPVQPEYLSLEGLAQLLETIEEV 167
|
170
....*....|....*.
gi 1370134019 730 Q------IPVLGVIAT 739
Cdd:COG1192 168 RedlnpkLEILGILLT 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
188-441 |
3.02e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 188 QYSLQERENSLQAGVSFIDEQIPILETQIRALQGQQRTLQQRYniispNQQATNLNEAYQANQLDIQKIDEELEELRSLK 267
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL-----EELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 268 SNLESTLglspsEALVVLDLSQNPERQNLLQQLQEVETMIAAESSRFTNENPIMQDLFQKRNNLQTLLETRTKEILKSSS 347
Cdd:COG1196 351 EELEEAE-----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 348 LkgdnnpnifmfqNTSRITMLDQLIVTQNEIAKRLTRRQVLVANQERLRINLDQfptIAAQYDEVARQLDLKKGLLDTLA 427
Cdd:COG1196 426 L------------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE---LLEEAALLEAALAELLEELAEAA 490
|
250
....*....|....
gi 1370134019 428 NQRETLRVEAAQQD 441
Cdd:COG1196 491 ARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-434 |
5.46e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 138 LQNLQKNL--IVKRVQEGNSRfdYTKILEVIYEGNdavlvETVLKVTAEQYLQysLQERENSLQAGVSFIDEQIPILETQ 215
Cdd:TIGR02169 246 LASLEEELekLTEEISELEKR--LEEIEQLLEELN-----KKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 216 IRALQGQQRTLQQRYNiispnqqatnlneayqANQLDIQKIDEELEELRSLKSNLESTLGlspsealvvldlSQNPERQN 295
Cdd:TIGR02169 317 LEDAEERLAKLEAEID----------------KLLAEIEELEREIEEERKRRDKLTEEYA------------ELKEELED 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 296 LLQQLQEVETMIAAESSRFTNENPIMQDLFQKRNNLQTLLETRTKEILKSSSLKGDNNPNIFMFQntSRITMLD-QLIVT 374
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE--AKINELEeEKEDK 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 375 QNEIAKRLTRRQVLVANQERLRinlDQFPTIAAQYDEVARQLDLKKGLLDTLANQRETLR 434
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYE---QELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-337 |
6.10e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 118 LSKIAAEVHNILPQIPEAAMLQNLQKNLIVKRVQEGNSRFDYTKILEVIYEGNDAVLVETVLKVT-AEQYLQYSLQEREn 196
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEeAEEELAEAEAEIE- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 197 SLQAGVSFIDEQIPILETQIRALQGQQRTLQQRY------------NIISPNQQATNLNEAYQANQLDIQKIDEELEELR 264
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrerleslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370134019 265 SLKSNLESTLglspsEALVVLDLSQNPERQNLLQQLQEVETMIAAESSRftnenpiMQDLFQKRNNLQTLLET 337
Cdd:TIGR02168 866 ELIEELESEL-----EALLNERASLEEALALLRSELEELSEELRELESK-------RSELRRELEELREKLAQ 926
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
190-445 |
9.98e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 190 SLQERENSLQAGVSFIDEQIPILETQIRALQGQQRTLQQRY-----NIISPNQQATNLNEAYQANQLDIQKIDEELEELR 264
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLeeleeDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 265 SLKSNLESTLGLSPSEALVVLDLSQNPERQNLLQQLQEVETMIAAESSRFTNENPIMQDLFQKRNNLQTLLETRTKEILK 344
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370134019 345 SSSLKGDnnpnifmfqntsritMLDQLIVTQNEIAKRLTRRQVLVANQERLRINLDQfptIAAQYDEVARQLDLKKGLLD 424
Cdd:TIGR02169 859 LNGKKEE---------------LEEELEELEAALRDLESRLGDLKKERDELEAQLRE---LERKIEELEAQIEKKRKRLS 920
|
250 260
....*....|....*....|.
gi 1370134019 425 TLANQRETLRVEAAQQDVPWK 445
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKG 941
|
|
| |
