|
Name |
Accession |
Description |
Interval |
E-value |
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
13-670 |
2.54e-73 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 250.70 E-value: 2.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 13 EGFIDFTPYFNKIKHKLIWCLAVVIVAAVASFILTRFMSSSYTATATVLFKAQSQDisPLPRLENYDSTRSDYYETKYAL 92
Cdd:COG3206 12 EDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSD--VLLSGLSSLSASDSPLETQIEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 93 MGSRVVLDAAVRKLKLYQDsefnggdYLDEATRIHNAIQALERGLTISGVRTTQLVSVSMEAKSPQKAADIANGVAQAFI 172
Cdd:COG3206 90 LKSRPVLERVVDKLNLDED-------PLGEEASREAAIERLRKNLTVEPVKGSNVIEISYTSPDPELAAAVANALAEAYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 173 DYSLQQKQNTLLQAQGWNEKMMDDLKRKMEQQKADIDHFLKENGLLTFRSMDGYETERLGIVINHLADATQRRLKAQTVW 252
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 253 DKVRRQQGKPVEQIislPEISGHPQIQDLRIALIQTRRNLSEAAKHYGPQHPKYLQAQAQLQAVNVQLGQVLGELFNGLR 332
Cdd:COG3206 243 AALRAQLGSGPDAL---PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 333 QQYQIALDDEQHYQKMLNDQKADFQALGAKRDQYNTMTTALNKTEELYKSLYQRANEQKLSESFSVPDEVIYDAAVPPDR 412
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVVPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 413 PSKPQRGLLIIMVTMLALALYIMYLIVSTALDKTVNSLSELKAKTALDGSGEFPQLTHLENVR------QIFHNVLYADM 486
Cdd:COG3206 400 PVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLLLGLPLLGPLPPLKSKRERRrarlalLLLAAALAALL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 487 IHSLRLALLNQRDKPATILVTSVQSRSGSSLIAELLAWSASKSRKTLLIDLDYLASQGLSAKFPQHKQGFNQLLNGSCTQ 566
Cdd:COG3206 480 ALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLLLLLLLLLLLLLLGGLLLL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 567 EQAIVKLDEKLDFMPRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLLAAQSDISLLVVKAGEQAA 646
Cdd:COG3206 560 LLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLAALLAAAVLAVLVVVLLLV 639
|
650 660
....*....|....*....|....
gi 1293418104 647 HIREAERRLQGAGKVQVANVLNLV 670
Cdd:COG3206 640 VALVALARLALLAAALLLLLVLVV 663
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
114-668 |
4.05e-29 |
|
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: 123.68 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 114 FNGGDYLDEATRIHNAIQALERGLTISGVRTTQLVSVSMEAKSPQKAADIANGVAQAFIDYSLQQKQNTLLQAQGWNEKM 193
Cdd:TIGR01005 130 FDLGEEAAGNERIDKAAADIPEALAGEPFKLISLGAGAFRLEDKLLAAPIAGGVAEALEADQLIANFEAQENALTAKAEA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 194 MDDLKRK-------MEQQKADIDHFLKENGLLTFRSMDGYETERLGIVINHLAdatqrrlkAQTVWDKVRRQQGKPVEQI 266
Cdd:TIGR01005 210 LFDLEQDsqaaaleMAHDKAEIAEKAAQGEIIGEAQLADLNPALIAAIADQAA--------AEARADNIKRIADEAEENA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 267 IS----LPEISGHPQIQDLRIALIQTRRNLSEAAKHYGPQHPKYLQAQAQLQAVNVQLGQVLGELFNGLRQQYQIALDDE 342
Cdd:TIGR01005 282 VFlagiLPKEGDELEIADLKTNELRNGKGEFDLSDEFGADHPEAVCSAPSLQELKAKIAEELQQFTASHKGEQAIAQQIE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 343 QHYQKMLNDQKADFQALGAKRDQYNTMTTALNKTEELYKSLYQRANEQKLSESFSVPDEVIYDAAVPPDRPSKPQRGLLI 422
Cdd:TIGR01005 362 ESLRGKINGIAGKLKDAPEIEQDLRELEQDAAADKELYESLLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 423 IMVTMLALALYIMYLIVSTALDKTVNSLSELKAKTALDGSGEFP----------QLTHLENVRQIFHN------------ 480
Cdd:TIGR01005 442 ALAAVLGMMLGGAAAAFLEALEGGFRDEGDIEEHLGHRSLATVPlldtqmdkkaQLTHAHFGSVKRHDeavddtmpfqll 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 481 ---------VLYADMIHSLRLAL--LNQRDKPATILVTSVQSRSGSSLI-AELLAWSASKSRKTLLIDLDyLASQGLSAK 548
Cdd:TIGR01005 522 arivpdaprSTFAEAFRNAKLACdfALADAENNLIAIAGALPDEGKSFIaANFAALIAAGGKRTLLIDAD-IRKGGLHQM 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 549 F-PQHKQGFNQLLNGSCTQEQAI-VKLDEKLDFMPRGKL----QDSSLLLLTAeRLPTLLADLHQTYDTLIIDTPALSQA 622
Cdd:TIGR01005 601 FgKAPKPGLLDLLAGEASIEAGIhRDQRPGLAFIAAGGAshfpHNPNELLANP-AMAELIDNARNAFDLVLVDLAALAAV 679
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1293418104 623 QDSLLLAAQSDISLLVVKAGEQAAH-IREAERRLQGAGKVQVANVLN 668
Cdd:TIGR01005 680 ADAAAFAALADGILFVTEFERSPLGeIRDLIHQEPHANSDVLGVIFN 726
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
472-667 |
2.90e-28 |
|
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: 111.89 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 472 ENVRQIFHNvlyadmihsLRLALLNQRDKpaTILVTSVQSRSGSSLIAELLAWSASKS-RKTLLIDLDyLASQGLSAKF- 549
Cdd:cd05387 1 EAFRTLRTN---------LLFAGSDAGPK--VIAVTSASPGEGKSTVAANLAVALAQSgKRVLLIDAD-LRRPSLHRLLg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 550 PQHKQGFNQLLNGSCTQEQAI-VKLDEKLDFMPRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLL 628
Cdd:cd05387 69 LPNEPGLSEVLSGQASLEDVIqSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALIL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1293418104 629 AAQSDISLLVVKAGE-QAAHIREAERRLQGAGkvqvANVL 667
Cdd:cd05387 149 APLVDGVLLVVRAGKtRRREVKEALERLEQAG----AKVL 184
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
357-640 |
3.50e-13 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 72.88 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 357 QALGAKRDQYNTMTTALNKTE--------------ELYKSLYQRANEQKLSESFSVPDEVIYDAAVPPDRPSKPQRGLLI 422
Cdd:PRK11519 349 KALEDEKAKLNGRVTAMPKTQqeivrltrdvesgqQVYMQLLNKQQELKITEASTVGDVRIVDPAITQPGVLKPKKALII 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 423 IMVTMLALALYIMYLIVSTALDKTVNS----------------LSELKAK--TALDGSG----EFPQLTHLENVRQifhn 480
Cdd:PRK11519 429 LGAIILGLMLSIVGVLLRSLFNRGIESpqvleehgisvyasipLSEWQKArdSVKTIKGikryKQSQLLAVGNPTD---- 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 481 vLYADMIHSLR----LALLNQRDKpaTILVTSVQSRSGSSLI-AELLAWSASKSRKTLLIDLDYLASQGLSAKFPQHKQG 555
Cdd:PRK11519 505 -LAIEAIRSLRtslhFAMMQAQNN--VLMMTGVSPSIGKTFVcANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNG 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 556 FNQLLNGSCTQEQAIVKLD-EKLDFMPRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLLAAQSDI 634
Cdd:PRK11519 582 LSDILIGQGDITTAAKPTSiANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGT 661
|
....*.
gi 1293418104 635 SLLVVK 640
Cdd:PRK11519 662 TLMVAR 667
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
521-617 |
2.81e-05 |
|
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: 45.27 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 521 LLAWSASKSRKTLLIDLDYL--ASQGLSAKFPQHKQGFNQLLNGSCTQEQAIVKLD-EKLDFMPRGK-LQDSSLLLLTAE 596
Cdd:pfam13614 22 LAAALAKKGKKVLLIDLDPQgnATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTViENLDLIPSNIdLAGAEIELIGIE 101
|
90 100
....*....|....*....|....*
gi 1293418104 597 ----RLPTLLADLHQTYDTLIIDTP 617
Cdd:pfam13614 102 nrenILKEALEPVKDNYDYIIIDCP 126
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
13-670 |
2.54e-73 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 250.70 E-value: 2.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 13 EGFIDFTPYFNKIKHKLIWCLAVVIVAAVASFILTRFMSSSYTATATVLFKAQSQDisPLPRLENYDSTRSDYYETKYAL 92
Cdd:COG3206 12 EDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSD--VLLSGLSSLSASDSPLETQIEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 93 MGSRVVLDAAVRKLKLYQDsefnggdYLDEATRIHNAIQALERGLTISGVRTTQLVSVSMEAKSPQKAADIANGVAQAFI 172
Cdd:COG3206 90 LKSRPVLERVVDKLNLDED-------PLGEEASREAAIERLRKNLTVEPVKGSNVIEISYTSPDPELAAAVANALAEAYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 173 DYSLQQKQNTLLQAQGWNEKMMDDLKRKMEQQKADIDHFLKENGLLTFRSMDGYETERLGIVINHLADATQRRLKAQTVW 252
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 253 DKVRRQQGKPVEQIislPEISGHPQIQDLRIALIQTRRNLSEAAKHYGPQHPKYLQAQAQLQAVNVQLGQVLGELFNGLR 332
Cdd:COG3206 243 AALRAQLGSGPDAL---PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 333 QQYQIALDDEQHYQKMLNDQKADFQALGAKRDQYNTMTTALNKTEELYKSLYQRANEQKLSESFSVPDEVIYDAAVPPDR 412
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVVPLK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 413 PSKPQRGLLIIMVTMLALALYIMYLIVSTALDKTVNSLSELKAKTALDGSGEFPQLTHLENVR------QIFHNVLYADM 486
Cdd:COG3206 400 PVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLLLGLPLLGPLPPLKSKRERRrarlalLLLAAALAALL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 487 IHSLRLALLNQRDKPATILVTSVQSRSGSSLIAELLAWSASKSRKTLLIDLDYLASQGLSAKFPQHKQGFNQLLNGSCTQ 566
Cdd:COG3206 480 ALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLLLLLLLLLLLLLLGGLLLL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 567 EQAIVKLDEKLDFMPRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLLAAQSDISLLVVKAGEQAA 646
Cdd:COG3206 560 LLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLAALLAAAVLAVLVVVLLLV 639
|
650 660
....*....|....*....|....
gi 1293418104 647 HIREAERRLQGAGKVQVANVLNLV 670
Cdd:COG3206 640 VALVALARLALLAAALLLLLVLVV 663
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
114-668 |
4.05e-29 |
|
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: 123.68 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 114 FNGGDYLDEATRIHNAIQALERGLTISGVRTTQLVSVSMEAKSPQKAADIANGVAQAFIDYSLQQKQNTLLQAQGWNEKM 193
Cdd:TIGR01005 130 FDLGEEAAGNERIDKAAADIPEALAGEPFKLISLGAGAFRLEDKLLAAPIAGGVAEALEADQLIANFEAQENALTAKAEA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 194 MDDLKRK-------MEQQKADIDHFLKENGLLTFRSMDGYETERLGIVINHLAdatqrrlkAQTVWDKVRRQQGKPVEQI 266
Cdd:TIGR01005 210 LFDLEQDsqaaaleMAHDKAEIAEKAAQGEIIGEAQLADLNPALIAAIADQAA--------AEARADNIKRIADEAEENA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 267 IS----LPEISGHPQIQDLRIALIQTRRNLSEAAKHYGPQHPKYLQAQAQLQAVNVQLGQVLGELFNGLRQQYQIALDDE 342
Cdd:TIGR01005 282 VFlagiLPKEGDELEIADLKTNELRNGKGEFDLSDEFGADHPEAVCSAPSLQELKAKIAEELQQFTASHKGEQAIAQQIE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 343 QHYQKMLNDQKADFQALGAKRDQYNTMTTALNKTEELYKSLYQRANEQKLSESFSVPDEVIYDAAVPPDRPSKPQRGLLI 422
Cdd:TIGR01005 362 ESLRGKINGIAGKLKDAPEIEQDLRELEQDAAADKELYESLLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 423 IMVTMLALALYIMYLIVSTALDKTVNSLSELKAKTALDGSGEFP----------QLTHLENVRQIFHN------------ 480
Cdd:TIGR01005 442 ALAAVLGMMLGGAAAAFLEALEGGFRDEGDIEEHLGHRSLATVPlldtqmdkkaQLTHAHFGSVKRHDeavddtmpfqll 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 481 ---------VLYADMIHSLRLAL--LNQRDKPATILVTSVQSRSGSSLI-AELLAWSASKSRKTLLIDLDyLASQGLSAK 548
Cdd:TIGR01005 522 arivpdaprSTFAEAFRNAKLACdfALADAENNLIAIAGALPDEGKSFIaANFAALIAAGGKRTLLIDAD-IRKGGLHQM 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 549 F-PQHKQGFNQLLNGSCTQEQAI-VKLDEKLDFMPRGKL----QDSSLLLLTAeRLPTLLADLHQTYDTLIIDTPALSQA 622
Cdd:TIGR01005 601 FgKAPKPGLLDLLAGEASIEAGIhRDQRPGLAFIAAGGAshfpHNPNELLANP-AMAELIDNARNAFDLVLVDLAALAAV 679
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1293418104 623 QDSLLLAAQSDISLLVVKAGEQAAH-IREAERRLQGAGKVQVANVLN 668
Cdd:TIGR01005 680 ADAAAFAALADGILFVTEFERSPLGeIRDLIHQEPHANSDVLGVIFN 726
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
472-667 |
2.90e-28 |
|
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: 111.89 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 472 ENVRQIFHNvlyadmihsLRLALLNQRDKpaTILVTSVQSRSGSSLIAELLAWSASKS-RKTLLIDLDyLASQGLSAKF- 549
Cdd:cd05387 1 EAFRTLRTN---------LLFAGSDAGPK--VIAVTSASPGEGKSTVAANLAVALAQSgKRVLLIDAD-LRRPSLHRLLg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 550 PQHKQGFNQLLNGSCTQEQAI-VKLDEKLDFMPRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLL 628
Cdd:cd05387 69 LPNEPGLSEVLSGQASLEDVIqSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALIL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1293418104 629 AAQSDISLLVVKAGE-QAAHIREAERRLQGAGkvqvANVL 667
Cdd:cd05387 149 APLVDGVLLVVRAGKtRRREVKEALERLEQAG----AKVL 184
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
490-670 |
7.39e-25 |
|
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: 105.27 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 490 LRLALLNQRDKPATILVTSVQSRSGSSLIAELLAWSASKS-RKTLLIDLDyLASQGLSAKF-PQHKQGFNQLLNGSCTQE 567
Cdd:COG0489 81 LLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSgKRVLLIDAD-LRGPSLHRMLgLENRPGLSDVLAGEASLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 568 QAIVKLD-EKLDFMPRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLLAAQSDISLLVVKAGEQA- 645
Cdd:COG0489 160 DVIQPTEvEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTAl 239
|
170 180
....*....|....*....|....*
gi 1293418104 646 AHIREAERRLQGAGkvqvANVLNLV 670
Cdd:COG0489 240 DDVRKALEMLEKAG----VPVLGVV 260
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
504-672 |
2.79e-17 |
|
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: 80.94 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 504 ILVTSVQSRSGSSLIAELLAWS-ASKSRKTLLIDLDYLAS-QGLSAKFPQHKQGFNQLLNGSCTQEQAIVKLD-EKLDFM 580
Cdd:TIGR01007 20 LLITSVKPGEGKSTTSANIAIAfAQAGYKTLLIDGDMRNSvMSGTFKSQNKITGLTNFLSGTTDLSDAICDTNiENLDVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 581 PRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLLAAQSDISLLVVKAGE-QAAHIREAERRLQGAG 659
Cdd:TIGR01007 100 TAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVTDAGKiKKREVKKAKEQLEQAG 179
|
170
....*....|...
gi 1293418104 660 KVQVANVLNLVQE 672
Cdd:TIGR01007 180 SNFLGVVLNKVDI 192
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
357-640 |
3.50e-13 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 72.88 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 357 QALGAKRDQYNTMTTALNKTE--------------ELYKSLYQRANEQKLSESFSVPDEVIYDAAVPPDRPSKPQRGLLI 422
Cdd:PRK11519 349 KALEDEKAKLNGRVTAMPKTQqeivrltrdvesgqQVYMQLLNKQQELKITEASTVGDVRIVDPAITQPGVLKPKKALII 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 423 IMVTMLALALYIMYLIVSTALDKTVNS----------------LSELKAK--TALDGSG----EFPQLTHLENVRQifhn 480
Cdd:PRK11519 429 LGAIILGLMLSIVGVLLRSLFNRGIESpqvleehgisvyasipLSEWQKArdSVKTIKGikryKQSQLLAVGNPTD---- 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 481 vLYADMIHSLR----LALLNQRDKpaTILVTSVQSRSGSSLI-AELLAWSASKSRKTLLIDLDYLASQGLSAKFPQHKQG 555
Cdd:PRK11519 505 -LAIEAIRSLRtslhFAMMQAQNN--VLMMTGVSPSIGKTFVcANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNG 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 556 FNQLLNGSCTQEQAIVKLD-EKLDFMPRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLLAAQSDI 634
Cdd:PRK11519 582 LSDILIGQGDITTAAKPTSiANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGT 661
|
....*.
gi 1293418104 635 SLLVVK 640
Cdd:PRK11519 662 TLMVAR 667
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
213-670 |
1.65e-11 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 67.63 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 213 KENGLLTFrSMDGYETERLGIVINHLADATQRRlkaqtvwdKVRRQQGKPVEQII----SLPEISGHPQIQDLRIALIQT 288
Cdd:PRK09841 225 KESGMLEL-TMTGDDPQLITRILNSIANNYLQQ--------NIARQAAQDSQSLEflqrQLPEVRSELDQAEEKLNVYRQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 289 RRNLSEAAkhygpqhpkyLQAQAQL-QAVNVQlgQVLGELFNGLRQQYQIALDDEQHYQKMLNDQkadfQALGAKRDQYN 367
Cdd:PRK09841 296 QRDSVDLN----------LEAKAVLeQIVNVD--NQLNELTFREAEISQLYKKDHPTYRALLEKR----QTLEQERKRLN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 368 TMTTALNKTEE--------------LYKSLYQRANEQKLSESFSVPDEVIYDAAVPPDRPSKPQRGLLIIMVTMLALALY 433
Cdd:PRK09841 360 KRVSAMPSTQQevlrlsrdveagraVYLQLLNRQQELSISKSSAIGNVRIIDPAVTQPQPVKPKKALNVVLGFILGLFIS 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 434 IMYLIVSTALDKTVNSLSELKA-----------------KTALDGSGEFPQLTHLENVRQIFHNV-----LYADMIHSLR 491
Cdd:PRK09841 440 VGAVLARAMLRRGVEAPEQLEEhgisvyatipmsewldkRTRLRKKNLFSNQQRHRTKNIPFLAVdnpadSAVEAVRALR 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 492 LAL--LNQRDKPATILVTSVQSRSGSSLIA-ELLAWSASKSRKTLLIDLDYLASQGLSAKFPQHKQGFNQLLNGSCTQEQ 568
Cdd:PRK09841 520 TSLhfAMMETENNILMITGATPDSGKTFVSsTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNEHGLSEYLAGKDELNK 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 569 AIVKLDE-KLDFMPRGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQDSLLLAAQSDISLLVVKAGEQAAH 647
Cdd:PRK09841 600 VIQHFGKgGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLNTAK 679
|
490 500
....*....|....*....|....
gi 1293418104 648 IREAE-RRLQGAGKVQVANVLNLV 670
Cdd:PRK09841 680 EVSLSmQRLEQAGVNIKGAILNGV 703
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
43-174 |
2.18e-10 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 62.39 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 43 SFILTRFMSSSYTATATVLFkAQSQDISPlpRLENYDSTRSDYYETKYA-LMGSRVVLDAAVRKLKLYQDSEfnggdyld 121
Cdd:COG3944 29 ALASSFLITPVYQASTTLLV-STSSGSDA--SDLYQGIQTAQQLVNTYAeLLKSPAVLEEVIDELGLDLSPE-------- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1293418104 122 eatrihnaiqALERGLTISGVRTTQLVSVSMEAKSPQKAADIANGVAQAFIDY 174
Cdd:COG3944 98 ----------ELAKKISVTSPPDTQVITITVTDTDPERAADIANAVAEVFAEE 140
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
526-686 |
4.28e-10 |
|
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: 60.29 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 526 ASKSRKTLLIDLD-YLASqgLSAKFP-QHKQGFNQLLNGSCTQEQAIVKLDEKLDFMPRGKLQDSSLLLLTAERLPTLLA 603
Cdd:COG0455 11 ARLGKRVLLVDADlGLAN--LDVLLGlEPKATLADVLAGEADLEDAIVQGPGGLDVLPGGSGPAELAELDPEERLIRVLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 604 DLHQTYDTLIIDTPA-LSqaQDSLLLAAQSDISLLVVKAGEQAAH-----IREAERRLqGAGKVQVanVLNLVQEEhlet 677
Cdd:COG0455 89 ELERFYDVVLVDTGAgIS--DSVLLFLAAADEVVVVTTPEPTSITdayalLKLLRRRL-GVRRAGV--VVNRVRSE---- 159
|
....*....
gi 1293418104 678 QEGKRLLDR 686
Cdd:COG0455 160 AEARDVFER 168
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
144-444 |
2.71e-09 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 59.48 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 144 TTQLVSVSMEAKSPQKAADIAngvaQAFIDYSlqqkqntllqaqgwnEKMMDDLKRKMEQQKadidhflkenglltfrsM 223
Cdd:COG3524 136 TSGIITLEVRAFDPEDAQAIA----EALLAES---------------EELVNQLSERAREDA-----------------V 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 224 DGYETErlgivinhLADATQRRLKAQTVWDKVRRQQGkpveqIISlPEISGHPQIQ---DLRIALIQTRRNLSEAAKHYG 300
Cdd:COG3524 180 RFAEEE--------VERAEERLRDAREALLAFRNRNG-----ILD-PEATAEALLQliaTLEGQLAELEAELAALRSYLS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 301 PQHPKYLQAQAQLQAVNVQLGQvlgelfngLRQQYQIALDDEQhyqkmLNDQKADFQALGAKR----DQYNTMTTALNKT 376
Cdd:COG3524 246 PNSPQVRQLRRRIAALEKQIAA--------ERARLTGASGGDS-----LASLLAEYERLELERefaeKAYTSALAALEQA 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1293418104 377 eelykslyqRANEQKLSESFSVpdeviYDAAVPPDRPSKPQRGLLIIMVTMLALALY-IMYLIVSTALD 444
Cdd:COG3524 313 ---------RIEAARQQRYLAV-----IVQPTLPDEALYPRRLYNILLVFLILLLLYgIGSLLVASIRE 367
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
484-668 |
3.70e-07 |
|
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: 52.81 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 484 ADMIHSLRLALLNQRDKPA-TILVTSVQSRSGSSLIAELLAWSASKS--RKTLLIDLDYL---ASQGLSAKfpqHKQGFN 557
Cdd:COG4963 84 DELRAALARLLDPGAARRGrVIAVVGAKGGVGATTLAVNLAWALAREsgRRVLLVDLDLQfgdVALYLDLE---PRRGLA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 558 QLLNGSCTQ-----EQAIVKLDEKLDFMPrGKLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPALSQAQdSLLLAAQS 632
Cdd:COG4963 161 DALRNPDRLdetllDRALTRHSSGLSVLA-APADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPW-TLAALEAA 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1293418104 633 DISLLVVkagEQ-AAHIREAERRLQ-------GAGKVQVanVLN 668
Cdd:COG4963 239 DEVVLVT---EPdLPSLRNAKRLLDllrelglPDDKVRL--VLN 277
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
522-632 |
1.84e-06 |
|
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: 49.86 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 522 LAWS-ASKSRKTLLIDLDYL--ASQGLSAKFPQHKQGFNQLLNGSCTQEQAIVKLD-EKLDFMPrgklqdSSLLLLTAE- 596
Cdd:COG1192 22 LAAAlARRGKRVLLIDLDPQgnLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEiPGLDLIP------ANIDLAGAEi 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1293418104 597 ----------RLPTLLADLHQTYDTLIIDT-PALSQAQDSLLLAAQS 632
Cdd:COG1192 96 elvsrpgrelRLKRALAPLADDYDYILIDCpPSLGLLTLNALAAADS 142
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
521-617 |
2.81e-05 |
|
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: 45.27 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 521 LLAWSASKSRKTLLIDLDYL--ASQGLSAKFPQHKQGFNQLLNGSCTQEQAIVKLD-EKLDFMPRGK-LQDSSLLLLTAE 596
Cdd:pfam13614 22 LAAALAKKGKKVLLIDLDPQgnATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTViENLDLIPSNIdLAGAEIELIGIE 101
|
90 100
....*....|....*....|....*
gi 1293418104 597 ----RLPTLLADLHQTYDTLIIDTP 617
Cdd:pfam13614 102 nrenILKEALEPVKDNYDYIIIDCP 126
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
503-639 |
1.16e-04 |
|
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: 44.10 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 503 TILVTSVQSRSGSSLIAELLAWS-ASKSRKTLLIDLDY-LASQ----GLSAKFPQHkqgfnQLLNGSCTQEQAIVKLDEK 576
Cdd:cd02038 2 IIAVTSGKGGVGKTNVSANLALAlSKLGKRVLLLDADLgLANLdillGLAPKKTLG-----DVLKGRVSLEDIIVEGPEG 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1293418104 577 LDFMPRGKLqDSSLLLLTAERLPTL---LADLHQTYDTLIIDTPA-LSQAQDSLLLAAQsdiSLLVV 639
Cdd:cd02038 77 LDIIPGGSG-MEELANLDPEQKAKLieeLSSLESNYDYLLIDTGAgISRNVLDFLLAAD---EVIVV 139
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
378-442 |
1.90e-04 |
|
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: 40.66 E-value: 1.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1293418104 378 ELYKSLYQRANEQKLSESFSVPDEVIYDAAVPPDRPSKPQRGLLIIMVTMLALALYIMYLIVSTA 442
Cdd:pfam13807 18 EIYTQLLNSNQELEVVKAGTVGNVRIVDTAVVPPKPVKPKKALIVVLALLLGLMLGVGLVLLRRA 82
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
560-668 |
2.40e-04 |
|
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: 43.34 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 560 LNGSCTQEQAIV--KLDEKLDFMPRGklQDSSLLLLTAERLPTLLADLHQTYDTLIIDTPA-LSQAQDSLLLAAQsdiSL 636
Cdd:cd02036 62 LEGECRLEQALIkdKRWENLYLLPAS--QTRDKDALTPEKLEELVKELKDSFDFILIDSPAgIESGFINAIAPAD---EA 136
|
90 100 110
....*....|....*....|....*....|....*
gi 1293418104 637 LVVKAGEQAAhIREAER---RLQGAGKVQVANVLN 668
Cdd:cd02036 137 IIVTNPEISS-VRDADRvigLLESKGIVNIGLIVN 170
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
504-638 |
1.84e-03 |
|
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.
Pssm-ID: 349765 [Multi-domain] Cd Length: 235 Bit Score: 40.34 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 504 ILVTSVQSRSGSSLIAELLAWSASK--SRKTLLIDLD-YLASQGLsakfpqhkqgfnqLLNGSCTQE-----QAIVKLDE 575
Cdd:cd03111 3 VAVVGAKGGVGASTLAVNLAQELAQraKDKVLLIDLDlPFGDLGL-------------YLNLRPDYDladviQNLDRLDR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 576 klDFMPRGKLQ-DSSLLLLT------------AERLPTLLADLHQTYDTLIIDTP---------ALSQAqDSLLLAAQSD 633
Cdd:cd03111 70 --TLLDSAVTRhSSGLSLLPapqeledlealgAEQVDKLLQVLRAFYDHIIVDLGhfldevtlaVLEAA-DEILLVTQQD 146
|
....*
gi 1293418104 634 ISLLV 638
Cdd:cd03111 147 LPSLR 151
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
504-694 |
7.65e-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: 38.48 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 504 ILVTSVQSRSGSSLIAELLAWSASKS-RKTLLIDLD----YLASQGLSAKFPQHKQGFNQLLNGSCTQEQAIVKLDEK-- 576
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRgLRVLLIDLDpqsnNSSVEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1293418104 577 -LDFMPRG----KLQDSSLLLLTAERLPTLLADLHQTYDTLIIDTP---------ALSQAqDSLLLAAQSDISLLV--VK 640
Cdd:pfam01656 81 gLDLIPGNidleKFEKELLGPRKEERLREALEALKEDYDYVIIDGApglgellrnALIAA-DYVIIPLEPEVILVEdaKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1293418104 641 AGEQAAHIREaERRLQGAGKVQVanVLNLVQEEHLEtqegkRLLDRQMRELIAP 694
Cdd:pfam01656 160 LGGVIAALVG-GYALLGLKIIGV--VLNKVDGDNHG-----KLLKEALEELLRG 205
|
|
| |
