|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
12-704 |
0e+00 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 943.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 12 DDDEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKQGNAILSNLSQMLPDSQPQSAPEISL 91
Cdd:PRK11519 14 GSDEIDIGRLVGTVIEARWWVIGITAVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSALANKPPASDAEIQL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 92 IQSRMILGKTVDDLNLQIMIKQNYFPIFGQGFARLLGEKPSNIEVTRLYVTNANDDVTqLELKIKDGEHYQIKYDGAV-F 170
Cdd:PRK11519 94 IRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTTFNRPKEMADQV-FTLNVLDDKNYQLSSDGGFsA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 171 NGRVGELLENKQLAIKVNDISAKPGDTFTIYYFNRLKAIADLLDNLNVSDQGKDTGILSISYTGENPQLIKNIVNSISEN 250
Cdd:PRK11519 173 RGQVGQMLKKDGVTLMVEAIHARPGTEFTVTKYSTLGMINNLQNNLTVTENGKDTGVLSLTYTGEDREQIRDILNSITRN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 251 YLAQNISRQAAQDAKSLDFLNIQLPKVRNDLDIAENKLNAYRRQSDSVDLSLEAKAVLDQIVNVDNQLNELTFRESEISQ 330
Cdd:PRK11519 253 YLEQNIERKSEEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQLNELTFKEAEISK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 331 LYTKEHPTYKALMEKRKTLQEEKLRLNKKVSSMPETQQEILRLSRDVESGRAVYMQLLNRQQELNIAKSSAIGNVRIIDD 410
Cdd:PRK11519 333 LYTKEHPAYRTLLEKRKALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRIVDP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 411 AVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRRGIETPEQLEEIGINVYASVPVAESLVSNDRsIKNIRKKITH 490
Cdd:PRK11519 413 AITQPGVLKPKKALIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARDS-VKTIKGIKRY 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 491 KEyTGLLATTNPADLAIEAIRGLRTSLHFAMIEARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYV 570
Cdd:PRK11519 492 KQ-SQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYT 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 571 HKVFDVENDNGLSNYLSGKLGLEATLKKIPEAGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVT 650
Cdd:PRK11519 571 HELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVT 650
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1031815719 651 DAAIIGHYAGTTLLVARFELNTVKEMDVAFKRFEQSGIVAKGCILNGIVKKASS 704
Cdd:PRK11519 651 DAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASA 704
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
13-696 |
2.12e-111 |
|
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: 354.80 E-value: 2.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 13 DDEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKqgnaiLSNLSQMLPDS------QPQSA 86
Cdd:TIGR01005 1 DGEIDLDRLLAALFANARLIAAFAAAFIALGAAYAFFARPVYEADIMILLDDN-----LNKAAEEEGDPsnlfdlDTDAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 87 PEISLIQSRMILGKTVDDLNLQIMIK---QNYFPIFGQG----FARLLGEKPSNIEVTRLYVTNANDDVTQLELKIK-DG 158
Cdd:TIGR01005 76 AAIEILKSGELAGKAVDKLHLSENAKilnPPRFPVDLIGawikSAAGLFSEPGGFDLGEEAAGNERIDKAAADIPEAlAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 159 EHYQIKYDGAV------------FNGRVGELLENKQL----AIKVNDISAKPGDTFTIYYFNRLKAIADLLDNLNVSDQG 222
Cdd:TIGR01005 156 EPFKLISLGAGafrledkllaapIAGGVAEALEADQLianfEAQENALTAKAEALFDLEQDSQAAALEMAHDKAEIAEKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 223 KDTGILSI-SYTGENPQLIKNIVNSISENYLAQNISRQAAQDAKSLDFLNIQLPKVRNDLDIAENKLNAYRRQSDSVDLS 301
Cdd:TIGR01005 236 AQGEIIGEaQLADLNPALIAAIADQAAAEARADNIKRIADEAEENAVFLAGILPKEGDELEIADLKTNELRNGKGEFDLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 302 LEAKAVLDQIVNVDNQLNELTFRESEISQLYTKEHPTYKALMEKRKTLQEEKLR-LNKKVSSMPETQQEILRLSRDVESG 380
Cdd:TIGR01005 316 DEFGADHPEAVCSAPSLQELKAKIAEELQQFTASHKGEQAIAQQIEESLRGKINgIAGKLKDAPEIEQDLRELEQDAAAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 381 RAVYMQLLNRQQELNIAKSSAIGNVRIIDDAVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRRGIETPEQLEEI 460
Cdd:TIGR01005 396 KELYESLLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTLALAAVLGMMLGGAAAAFLEALEGGFRDEGDIEEH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 461 -GINVYASVPVAES-------LVSNDR-SIKNIRKKITHKEYTGLLA---TTNPADLAIEAIRGLRTSLHFAMIEARNNI 528
Cdd:TIGR01005 476 lGHRSLATVPLLDTqmdkkaqLTHAHFgSVKRHDEAVDDTMPFQLLArivPDAPRSTFAEAFRNAKLACDFALADAENNL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 529 LMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFDVENDNGLSNYLSGKLGLEATLKKIPEAGFDFIS 608
Cdd:TIGR01005 556 IAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLLAGEASIEAGIHRDQRPGLAFIA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 609 RGVV---PPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVTDAAIIGHYAGTTLLVARFELNTVKEMDVAFKRFEQ 685
Cdd:TIGR01005 636 AGGAshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVTEFERSPLGEIRDLIHQEPH 715
|
730
....*....|.
gi 1031815719 686 SGIVAKGCILN 696
Cdd:TIGR01005 716 ANSDVLGVIFN 726
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1-704 |
1.03e-91 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 300.40 E-value: 1.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 1 MSSATSkNILKDDDEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKQGNAILSNLSQMlPD 80
Cdd:COG3206 1 MNESSS-APPEEEDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSSL-SA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 81 SQPQSAPEISLIQSRMILGKTVDDLNLQimikqnyfpifgqgfarllgEKPSNIEVTRLyvtnanddvtqlelkikdgeh 160
Cdd:COG3206 79 SDSPLETQIEILKSRPVLERVVDKLNLD--------------------EDPLGEEASRE--------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 161 yqikydgavfngrvgellenkqlaikvndisakpgdtftiyyfnrlKAIADLLDNLNVSDQgKDTGILSISYTGENPQLI 240
Cdd:COG3206 118 ----------------------------------------------AAIERLRKNLTVEPV-KGSNVIEISYTSPDPELA 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 241 KNIVNSISENYLAQNISRQAAQDAKSLDFLNIQLPKVRNDLDIAENKLNAYRRQSDSVDLSLEAKAVLDQIVNVDNQLN- 319
Cdd:COG3206 151 AAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAe 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 320 -------------------------------------------ELTFRESEISQLYTKEHPTYKALMEKR---------- 346
Cdd:COG3206 231 araelaeaearlaalraqlgsgpdalpellqspviqqlraqlaELEAELAELSARYTPNHPDVIALRAQIaalraqlqqe 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 347 -------------------KTLQEEKLRLNKKVSSMPETQQEILRLSRDVESGRAVYMQLLNRQQELNIAKSSAIGNVRI 407
Cdd:COG3206 311 aqrilasleaelealqareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 408 IDDAVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRRGIETPEQLEEIGINVYASVPvaeslvsndRSIKNIRKK 487
Cdd:COG3206 391 IDPAVVPLKPVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLLLGLPLLGPL---------PPLKSKRER 461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 488 ITHKEYTGLLATTNPADLAIEAIRGLRTSLHFAMIEARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRK 567
Cdd:COG3206 462 RRARLALLLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLL 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 568 GYVHKVFDVENDNGLSNYLSGKLGLEATLKKIPEAGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPIL 647
Cdd:COG3206 542 LLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLA 621
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031815719 648 AVTDAAIIGHYAGTTLLVARFELNTVKEMDVAFKRFEQSGIVAKGCILNGIVKKASS 704
Cdd:COG3206 622 ALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYY 678
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
508-697 |
1.74e-67 |
|
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: 220.13 E-value: 1.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 508 EAIRGLRTSLHFAMIEARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFDVENDNGLSNYLS 587
Cdd:cd05387 1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 588 GKLGLEATLKKIPEAGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVTDAAIIGHYAGTTLLVAR 667
Cdd:cd05387 81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160
|
170 180 190
....*....|....*....|....*....|
gi 1031815719 668 FELNTVKEMDVAFKRFEQSGIVAKGCILNG 697
Cdd:cd05387 161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
365-446 |
2.51e-36 |
|
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: 131.18 E-value: 2.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 365 ETQQEILRLSRDVESGRAVYMQLLNRQQELNIAKSSAIGNVRIIDDAVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLR 444
Cdd:pfam13807 1 DTQQEILRLTRDVEVNTEIYTQLLNSNQELEVVKAGTVGNVRIVDTAVVPPKPVKPKKALIVVLALLLGLMLGVGLVLLR 80
|
..
gi 1031815719 445 IM 446
Cdd:pfam13807 81 RA 82
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
538-655 |
2.05e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 42.92 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 538 AGKTFISSNLAAVVAQTGKKVLFIDTD----------MRKGyvhkvfdvendnglsnylsgklgleatlkkipEAGFDFI 607
Cdd:NF041546 11 VGKTTLATHLAAALARRGYRVLLVDADpqgsaldwaaARED--------------------------------ERPFPVV 58
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1031815719 608 SrgvvPPNPTellMHRRMEEMlkwaSQNYDLVILDTPPilAVTDAAII 655
Cdd:NF041546 59 G----LARPT---LHRELPSL----ARDYDFVVIDGPP--RAEDLARS 93
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
12-704 |
0e+00 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 943.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 12 DDDEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKQGNAILSNLSQMLPDSQPQSAPEISL 91
Cdd:PRK11519 14 GSDEIDIGRLVGTVIEARWWVIGITAVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSALANKPPASDAEIQL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 92 IQSRMILGKTVDDLNLQIMIKQNYFPIFGQGFARLLGEKPSNIEVTRLYVTNANDDVTqLELKIKDGEHYQIKYDGAV-F 170
Cdd:PRK11519 94 IRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTTFNRPKEMADQV-FTLNVLDDKNYQLSSDGGFsA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 171 NGRVGELLENKQLAIKVNDISAKPGDTFTIYYFNRLKAIADLLDNLNVSDQGKDTGILSISYTGENPQLIKNIVNSISEN 250
Cdd:PRK11519 173 RGQVGQMLKKDGVTLMVEAIHARPGTEFTVTKYSTLGMINNLQNNLTVTENGKDTGVLSLTYTGEDREQIRDILNSITRN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 251 YLAQNISRQAAQDAKSLDFLNIQLPKVRNDLDIAENKLNAYRRQSDSVDLSLEAKAVLDQIVNVDNQLNELTFRESEISQ 330
Cdd:PRK11519 253 YLEQNIERKSEEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQLNELTFKEAEISK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 331 LYTKEHPTYKALMEKRKTLQEEKLRLNKKVSSMPETQQEILRLSRDVESGRAVYMQLLNRQQELNIAKSSAIGNVRIIDD 410
Cdd:PRK11519 333 LYTKEHPAYRTLLEKRKALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRIVDP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 411 AVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRRGIETPEQLEEIGINVYASVPVAESLVSNDRsIKNIRKKITH 490
Cdd:PRK11519 413 AITQPGVLKPKKALIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARDS-VKTIKGIKRY 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 491 KEyTGLLATTNPADLAIEAIRGLRTSLHFAMIEARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYV 570
Cdd:PRK11519 492 KQ-SQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYT 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 571 HKVFDVENDNGLSNYLSGKLGLEATLKKIPEAGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVT 650
Cdd:PRK11519 571 HELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVT 650
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1031815719 651 DAAIIGHYAGTTLLVARFELNTVKEMDVAFKRFEQSGIVAKGCILNGIVKKASS 704
Cdd:PRK11519 651 DAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASA 704
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
13-703 |
0e+00 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 914.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 13 DDEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKQGNAILSNLSQMLPDSQPQSAPEISLI 92
Cdd:PRK09841 15 ENEIDLLRLVGELWDHRKFIISVTALFTLIAVAYSLLSTPIYQADTLVQVEQKQGNAILSGLSDMIPNSSPESAPEIQLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 93 QSRMILGKTVDDLNLQIMIKQNYFPIFGQGFARLLGEKPSNIEVTRLYVTNANDDVTQLELKIKDGEHYQIKYDGAVFNG 172
Cdd:PRK09841 95 QSRMILGKTIAELNLRDIVEQKYFPIVGRGWARLTKEKPGELAISWMHIPQLNGQDQQLTLTVGENGHYTLEGEEFTVNG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 173 RVGELLENKQLAIKVNDISAKPGDTFTIYYFNRLKAIADLLDNLNVSDQGKDTGILSISYTGENPQLIKNIVNSISENYL 252
Cdd:PRK09841 175 MVGQRLEKDGVALTIADIKAKPGTQFVLSQRTELEAINALQETFTVSERSKESGMLELTMTGDDPQLITRILNSIANNYL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 253 AQNISRQAAQDAKSLDFLNIQLPKVRNDLDIAENKLNAYRRQSDSVDLSLEAKAVLDQIVNVDNQLNELTFRESEISQLY 332
Cdd:PRK09841 255 QQNIARQAAQDSQSLEFLQRQLPEVRSELDQAEEKLNVYRQQRDSVDLNLEAKAVLEQIVNVDNQLNELTFREAEISQLY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 333 TKEHPTYKALMEKRKTLQEEKLRLNKKVSSMPETQQEILRLSRDVESGRAVYMQLLNRQQELNIAKSSAIGNVRIIDDAV 412
Cdd:PRK09841 335 KKDHPTYRALLEKRQTLEQERKRLNKRVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELSISKSSAIGNVRIIDPAV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 413 TQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRRGIETPEQLEEIGINVYASVPVAESL--VSNDRSIKNIRKKITH 490
Cdd:PRK09841 415 TQPQPVKPKKALNVVLGFILGLFISVGAVLARAMLRRGVEAPEQLEEHGISVYATIPMSEWLdkRTRLRKKNLFSNQQRH 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 491 K-EYTGLLATTNPADLAIEAIRGLRTSLHFAMIEARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGY 569
Cdd:PRK09841 495 RtKNIPFLAVDNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGY 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 570 VHKVFDVENDNGLSNYLSGKLGLEATLKKIPEAGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAV 649
Cdd:PRK09841 575 SHNLFTVSNEHGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAV 654
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1031815719 650 TDAAIIGHYAGTTLLVARFELNTVKEMDVAFKRFEQSGIVAKGCILNGIVKKAS 703
Cdd:PRK09841 655 SDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNGVIKRAS 708
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
13-696 |
2.12e-111 |
|
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: 354.80 E-value: 2.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 13 DDEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKqgnaiLSNLSQMLPDS------QPQSA 86
Cdd:TIGR01005 1 DGEIDLDRLLAALFANARLIAAFAAAFIALGAAYAFFARPVYEADIMILLDDN-----LNKAAEEEGDPsnlfdlDTDAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 87 PEISLIQSRMILGKTVDDLNLQIMIK---QNYFPIFGQG----FARLLGEKPSNIEVTRLYVTNANDDVTQLELKIK-DG 158
Cdd:TIGR01005 76 AAIEILKSGELAGKAVDKLHLSENAKilnPPRFPVDLIGawikSAAGLFSEPGGFDLGEEAAGNERIDKAAADIPEAlAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 159 EHYQIKYDGAV------------FNGRVGELLENKQL----AIKVNDISAKPGDTFTIYYFNRLKAIADLLDNLNVSDQG 222
Cdd:TIGR01005 156 EPFKLISLGAGafrledkllaapIAGGVAEALEADQLianfEAQENALTAKAEALFDLEQDSQAAALEMAHDKAEIAEKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 223 KDTGILSI-SYTGENPQLIKNIVNSISENYLAQNISRQAAQDAKSLDFLNIQLPKVRNDLDIAENKLNAYRRQSDSVDLS 301
Cdd:TIGR01005 236 AQGEIIGEaQLADLNPALIAAIADQAAAEARADNIKRIADEAEENAVFLAGILPKEGDELEIADLKTNELRNGKGEFDLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 302 LEAKAVLDQIVNVDNQLNELTFRESEISQLYTKEHPTYKALMEKRKTLQEEKLR-LNKKVSSMPETQQEILRLSRDVESG 380
Cdd:TIGR01005 316 DEFGADHPEAVCSAPSLQELKAKIAEELQQFTASHKGEQAIAQQIEESLRGKINgIAGKLKDAPEIEQDLRELEQDAAAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 381 RAVYMQLLNRQQELNIAKSSAIGNVRIIDDAVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRRGIETPEQLEEI 460
Cdd:TIGR01005 396 KELYESLLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTLALAAVLGMMLGGAAAAFLEALEGGFRDEGDIEEH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 461 -GINVYASVPVAES-------LVSNDR-SIKNIRKKITHKEYTGLLA---TTNPADLAIEAIRGLRTSLHFAMIEARNNI 528
Cdd:TIGR01005 476 lGHRSLATVPLLDTqmdkkaqLTHAHFgSVKRHDEAVDDTMPFQLLArivPDAPRSTFAEAFRNAKLACDFALADAENNL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 529 LMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFDVENDNGLSNYLSGKLGLEATLKKIPEAGFDFIS 608
Cdd:TIGR01005 556 IAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLLAGEASIEAGIHRDQRPGLAFIA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 609 RGVV---PPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVTDAAIIGHYAGTTLLVARFELNTVKEMDVAFKRFEQ 685
Cdd:TIGR01005 636 AGGAshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVTEFERSPLGEIRDLIHQEPH 715
|
730
....*....|.
gi 1031815719 686 SGIVAKGCILN 696
Cdd:TIGR01005 716 ANSDVLGVIFN 726
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1-704 |
1.03e-91 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 300.40 E-value: 1.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 1 MSSATSkNILKDDDEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKQGNAILSNLSQMlPD 80
Cdd:COG3206 1 MNESSS-APPEEEDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSSL-SA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 81 SQPQSAPEISLIQSRMILGKTVDDLNLQimikqnyfpifgqgfarllgEKPSNIEVTRLyvtnanddvtqlelkikdgeh 160
Cdd:COG3206 79 SDSPLETQIEILKSRPVLERVVDKLNLD--------------------EDPLGEEASRE--------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 161 yqikydgavfngrvgellenkqlaikvndisakpgdtftiyyfnrlKAIADLLDNLNVSDQgKDTGILSISYTGENPQLI 240
Cdd:COG3206 118 ----------------------------------------------AAIERLRKNLTVEPV-KGSNVIEISYTSPDPELA 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 241 KNIVNSISENYLAQNISRQAAQDAKSLDFLNIQLPKVRNDLDIAENKLNAYRRQSDSVDLSLEAKAVLDQIVNVDNQLN- 319
Cdd:COG3206 151 AAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAe 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 320 -------------------------------------------ELTFRESEISQLYTKEHPTYKALMEKR---------- 346
Cdd:COG3206 231 araelaeaearlaalraqlgsgpdalpellqspviqqlraqlaELEAELAELSARYTPNHPDVIALRAQIaalraqlqqe 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 347 -------------------KTLQEEKLRLNKKVSSMPETQQEILRLSRDVESGRAVYMQLLNRQQELNIAKSSAIGNVRI 407
Cdd:COG3206 311 aqrilasleaelealqareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 408 IDDAVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRRGIETPEQLEEIGINVYASVPvaeslvsndRSIKNIRKK 487
Cdd:COG3206 391 IDPAVVPLKPVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLLLGLPLLGPL---------PPLKSKRER 461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 488 ITHKEYTGLLATTNPADLAIEAIRGLRTSLHFAMIEARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRK 567
Cdd:COG3206 462 RRARLALLLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLL 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 568 GYVHKVFDVENDNGLSNYLSGKLGLEATLKKIPEAGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPIL 647
Cdd:COG3206 542 LLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLA 621
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031815719 648 AVTDAAIIGHYAGTTLLVARFELNTVKEMDVAFKRFEQSGIVAKGCILNGIVKKASS 704
Cdd:COG3206 622 ALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYY 678
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
508-697 |
1.74e-67 |
|
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: 220.13 E-value: 1.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 508 EAIRGLRTSLHFAMIEARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFDVENDNGLSNYLS 587
Cdd:cd05387 1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 588 GKLGLEATLKKIPEAGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVTDAAIIGHYAGTTLLVAR 667
Cdd:cd05387 81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160
|
170 180 190
....*....|....*....|....*....|
gi 1031815719 668 FELNTVKEMDVAFKRFEQSGIVAKGCILNG 697
Cdd:cd05387 161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
443-703 |
2.09e-56 |
|
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: 194.25 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 443 LRIMLRRGIETPEQLEEIGINVYASVPVAESLVSNDRSIKNIRKKITHKEYTGLLATTNPADLAIEAIRGLRTSLHFAMI 522
Cdd:COG0489 9 LLLREEAQALLLLLLLLLLLLRLEEAAAAAALAAAAPAAAAPAPLPPAPALLLLLLLLLGLLLLLLLALALLLLLLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 523 EARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFDVENDNGLSNYLSGKLGLEATLKKIPEA 602
Cdd:COG0489 89 RLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 603 GFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVTDAAIIGHYAGTTLLVARFELNTVKEMDVAFKR 682
Cdd:COG0489 169 GLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEM 248
|
250 260
....*....|....*....|.
gi 1031815719 683 FEQSGIVAKGCILNGIVKKAS 703
Cdd:COG0489 249 LEKAGVPVLGVVLNMVCPKGE 269
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
508-698 |
1.44e-41 |
|
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: 150.28 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 508 EAIRGLRTSLHFAMieARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFDVENDN-GLSNYL 586
Cdd:TIGR01007 1 EYYNAIRTNIQFSG--AEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKItGLTNFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 587 SGKLGLEATLKKIPEAGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVTDAAIIGHYAGTTLLVA 666
Cdd:TIGR01007 79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158
|
170 180 190
....*....|....*....|....*....|..
gi 1031815719 667 RFELNTVKEMDVAFKRFEQSGIVAKGCILNGI 698
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKV 190
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
365-446 |
2.51e-36 |
|
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: 131.18 E-value: 2.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 365 ETQQEILRLSRDVESGRAVYMQLLNRQQELNIAKSSAIGNVRIIDDAVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLR 444
Cdd:pfam13807 1 DTQQEILRLTRDVEVNTEIYTQLLNSNQELEVVKAGTVGNVRIVDTAVVPPKPVKPKKALIVVLALLLGLMLGVGLVLLR 80
|
..
gi 1031815719 445 IM 446
Cdd:pfam13807 81 RA 82
|
|
| EpsG |
TIGR03029 |
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ... |
496-696 |
1.52e-32 |
|
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are homologs of the EpsG protein found in Methylobacillus strain 12S and are generally found in operons with other Eps homologs. The protein is believed to function as the protein tyrosine kinase component of the chain length regulator (along with the transmembrane component EpsF).
Pssm-ID: 132074 [Multi-domain] Cd Length: 274 Bit Score: 127.29 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 496 LLATTNPADLAIEAIRGLRTSLHFAMIEARNNILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFD 575
Cdd:TIGR03029 73 LIAAYQPFSPQVEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNFK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 576 VENDNGLSNYLSGKLGLEAtLKKIPE-AGFDFISRGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVTDAAI 654
Cdd:TIGR03029 153 LSEQRGLSDILAGRSDLEV-ITHIPAlENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQI 231
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1031815719 655 IGHYAGTTLLVARFELNTVKEMDVAFKRFEQSGIVAKGCILN 696
Cdd:TIGR03029 232 VATRARGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLN 273
|
|
| Wzz |
pfam02706 |
Chain length determinant protein; This family includes proteins involved in lipopolysaccharide ... |
14-104 |
4.01e-24 |
|
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: 96.59 E-value: 4.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 14 DEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKQGNAILSNLSQMLPDSQPQSApEISLIQ 93
Cdd:pfam02706 1 DEIDLIELLGVLWKRKKLIILVTLLFTLLAAAYAFLATPKYTATAQILVPQKKGEAGSLLGSDLQAGLQLAST-EIEILK 79
|
90
....*....|.
gi 1031815719 94 SRMILGKTVDD 104
Cdd:pfam02706 80 SRDVLEKVIDE 90
|
|
| WzzB |
COG3765 |
LPS O-antigen chain length determinant protein, WzzB/FepE family [Cell wall/membrane/envelope ... |
1-449 |
4.59e-16 |
|
LPS O-antigen chain length determinant protein, WzzB/FepE family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442979 [Multi-domain] Cd Length: 364 Bit Score: 80.40 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 1 MSSATSKNILK------DDDEMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANsliqveqkqgnAILSnl 74
Cdd:COG3765 1 MSSEESKQLYPnqyppsQDDEIDLFELLRTLWQGKLWIIGITLLFALLALVYAFLLPQKWTST-----------AIVD-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 75 sqmlpdsqpqsAPEISLIQSrmilgktvddLNLQimikqnyfpifgQGFARLLGEKPSNIEVTR-----LYVTNANDDVT 149
Cdd:COG3765 68 -----------PPTVNELGG----------YYSQ------------RQFLRNLDVKSVDPPVISselfnEFIKQLSSYDL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 150 QLElkikdgehYQIKYDgaVFNGRVGELLENKQLAIK--VNDISAKPGDtftiyyfnrlkaiadlldnlnVSDQGKDTGI 227
Cdd:COG3765 115 RRE--------FLLQSD--YYKQLQEGDEKEDAALLDelINNISITPPD---------------------DKKKSSPYTN 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 228 LSISYTGENPQLIKNIVNsiseNYLaQNISRQAAQDaksldflniqlpkVRNDLDIA-ENKLNAYRRQSDSVDLSLEAK- 305
Cdd:COG3765 164 YSVSFTAETPEDAQQLLR----GYI-DFANQRVLKE-------------LNEELQGAiAARLQSLKAQIKRLEEVAKAQr 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 306 ----AVLDQIVNVDNQLNELTFRESEISQLYTKEHPTYKALMeKRKTLQEEKlrlnkkvssmpetqqEILRLSRDVESGR 381
Cdd:COG3765 226 qrriERLKYALKIAQAAGIKKPVYSNGQTPAVKLDPSYLFLL-GTDALQAEL---------------EILKARGDDYPLN 289
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031815719 382 AVYMQLLNRQQELN---IAKSSAIGnVRIIDDAVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRR 449
Cdd:COG3765 290 ADLYQLQAQLAQLNalpIDDVGFQP-FRYLRTPEEPVKKDKPKRALILVLGALLGGMLGVGVVLIRHALRS 359
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
338-566 |
5.81e-13 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 70.48 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 338 TYKALMEKRKTLQE--EKLRLNK---------KVSSMPETQqeILRLSrdVESGRAvymqllnrQQELNIAKSSA----- 401
Cdd:COG3944 72 TYAELLKSPAVLEEviDELGLDLspeelakkiSVTSPPDTQ--VITIT--VTDTDP--------ERAADIANAVAevfae 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 402 -------IGNVRIIDDAVTQLKPVKPKKILVVIIGFILGLSIAIGVVFLRIMLRRGIETPEQLEEI-GInvyasvpvaes 473
Cdd:COG3944 140 evkelmkVDNVTVLDPATVPASPVSPNPKLNLAIGLVLGLLLGVGLAFLRELLDTTIRSEEDIERLlGL----------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 474 lvsndrsIKNIRKKITHKEYTGLLATTNPADLAIEAIRGLRTSLHFAMIEARNNILMISgASPNAGKTFISSNLAAVVAQ 553
Cdd:COG3944 209 -------LLGGAVPAARSARPLLLLLADASPRAAAARRRRRNLLFALAAVDARTVVVVS-SSLSEGKSTTTAALALALAA 280
|
250
....*....|...
gi 1031815719 554 TGKKVLFIDTDMR 566
Cdd:COG3944 281 AAAGVVLVLADLD 293
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
542-645 |
1.21e-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: 62.21 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 542 FISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFDVENDNGLSNYLSGKLGLEATLKKIPEaGFDFISRGVVPPNPTELLM 621
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGPG-GLDVLPGGSGPAELAELDP 79
|
90 100
....*....|....*....|....
gi 1031815719 622 HRRMEEMLKWASQNYDLVILDTPP 645
Cdd:COG0455 80 EERLIRVLEELERFYDVVLVDTGA 103
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
502-688 |
2.95e-10 |
|
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: 62.44 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 502 PADLAIEAIRGLRTSLHfamiEARNNILMISGASPNAGKTFISSNLAAVVAQ-TGKKVLFIDTDMRKGYVHKVFDVENDN 580
Cdd:COG4963 82 SPDELRAALARLLDPGA----ARRGRVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFGDVALYLDLEPRR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 581 GLSNYLSG-----KLGLEATLKKIPEaGFDFISrGVVPPNPTELLMHRRMEEMLKWASQNYDLVILDTPPILAVTDAAII 655
Cdd:COG4963 158 GLADALRNpdrldETLLDRALTRHSS-GLSVLA-APADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAAL 235
|
170 180 190
....*....|....*....|....*....|...
gi 1031815719 656 GHyAGTTLLVARFELNTVKEMDVAFKRFEQSGI 688
Cdd:COG4963 236 EA-ADEVVLVTEPDLPSLRNAKRLLDLLRELGL 267
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
539-655 |
1.11e-09 |
|
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: 59.49 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 539 GKTFISSNLAAVVAQTGKKVLFIDTD----MRKGYvhKVFDVENDNGLSNYLSGKLGLEATLKKIPEAGFDfisrgVVPP 614
Cdd:COG1192 14 GKTTTAVNLAAALARRGKRVLLIDLDpqgnLTSGL--GLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGLD-----LIPA 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1031815719 615 NP------TELLMHRRMEEMLKWA----SQNYDLVILDTPPILAV-TDAAII 655
Cdd:COG1192 87 NIdlagaeIELVSRPGRELRLKRAlaplADDYDYILIDCPPSLGLlTLNALA 138
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
539-645 |
2.74e-09 |
|
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: 57.96 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 539 GKTFISSNLAAVVAQTGKKVLFIDTDMRKGYVHKVFDVENDNGLSNYLSGKLGLEATLKKIPEaGFDFISRGVVPPNPTE 618
Cdd:cd02038 13 GKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGPE-GLDIIPGGSGMEELAN 91
|
90 100
....*....|....*....|....*....
gi 1031815719 619 L--LMHRRMEEMLKWASQNYDLVILDTPP 645
Cdd:cd02038 92 LdpEQKAKLIEELSSLESNYDYLLIDTGA 120
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
15-109 |
4.38e-08 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 55.46 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 15 EMDLGKLIGELIDHRKLIIAITSFCTLISLVYAIFATPIYQANSLIQVEQKQGNAILSNLSQMLPDSQP-QSAPEIslIQ 93
Cdd:COG3944 1 EMDLREYLRILRRRWWLILLLTLLGALAALASSFLITPVYQASTTLLVSTSSGSDASDLYQGIQTAQQLvNTYAEL--LK 78
|
90
....*....|....*.
gi 1031815719 94 SRMILGKTVDDLNLQI 109
Cdd:COG3944 79 SPAVLEEVIDELGLDL 94
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
529-650 |
2.40e-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: 52.35 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 529 LMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTD----MRKGYVHKVFDVENDNGLSNYLSGKLGLEATLKKIP--EA 602
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpqsnNSSVEGLEGDIAPALQALAEGLKGRVNLDPILLKEKsdEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1031815719 603 GFDFISRGVVPPNPTELLMHRRMEEMLKWA----SQNYDLVILDTPPILAVT 650
Cdd:pfam01656 81 GLDLIPGNIDLEKFEKELLGPRKEERLREAlealKEDYDYVIIDGAPGLGEL 132
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
539-647 |
8.53e-06 |
|
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: 46.81 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 539 GKTFISSNLAAVVAQTGKKVLFIDTDMR----KGYVHKVFDVENDngLSNYLSGKLGLEATLKKIPEAGFDFIsrgvvPP 614
Cdd:pfam13614 14 GKTTTSVNLAAALAKKGKKVLLIDLDPQgnatSGLGIDKNNVEKT--IYELLIGECNIEEAIIKTVIENLDLI-----PS 86
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1031815719 615 N------PTELLM----HRRMEEMLKWASQNYDLVILDTPPIL 647
Cdd:pfam13614 87 NidlagaEIELIGienrENILKEALEPVKDNYDYIIIDCPPSL 129
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
538-655 |
2.05e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 42.92 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 538 AGKTFISSNLAAVVAQTGKKVLFIDTD----------MRKGyvhkvfdvendnglsnylsgklgleatlkkipEAGFDFI 607
Cdd:NF041546 11 VGKTTLATHLAAALARRGYRVLLVDADpqgsaldwaaARED--------------------------------ERPFPVV 58
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1031815719 608 SrgvvPPNPTellMHRRMEEMlkwaSQNYDLVILDTPPilAVTDAAII 655
Cdd:NF041546 59 G----LARPT---LHRELPSL----ARDYDFVVIDGPP--RAEDLARS 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-373 |
5.46e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 258 RQAAQDAKSLDFLNIQLPKVRNDLDIAENKLNAYRRQSDSVDLSL--EAKAVLDQIVNVDNQLNELTFRESEISQLYTKE 335
Cdd:COG4913 331 QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpaSAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
90 100 110
....*....|....*....|....*....|....*...
gi 1031815719 336 HPTYKALMEKRKTLQEEKLRLNKKVSSMPETQQEILRL 373
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
538-564 |
1.20e-03 |
|
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.
Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 39.45 E-value: 1.20e-03
10 20
....*....|....*....|....*..
gi 1031815719 538 AGKTFISSNLAAVVAQTGKKVLFIDTD 564
Cdd:cd02042 12 VGKTTLAVNLAAALALRGKRVLLIDLD 38
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
533-688 |
1.24e-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: 41.11 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 533 GASPNAGKTFISSNLAAVVAQ-TGKKVLFIDTDMRKGYVHKVFDVENDNGLSNYLS-----GKLGLEATLKKIPeAGFDF 606
Cdd:cd03111 7 GAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQnldrlDRTLLDSAVTRHS-SGLSL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 607 ISRgvvppnPTELLMHRRMEE-----MLKWASQNYDLVILDTPPILAVTDAAIIGHyAGTTLLVARFELNTVKEMDVAFK 681
Cdd:cd03111 86 LPA------PQELEDLEALGAeqvdkLLQVLRAFYDHIIVDLGHFLDEVTLAVLEA-ADEILLVTQQDLPSLRNARRLLD 158
|
....*..
gi 1031815719 682 RFEQSGI 688
Cdd:cd03111 159 SLRELEG 165
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
524-643 |
1.77e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 41.04 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 524 ARNNILMISGAsPNAGKTFISSNLAAVVAqTGK----------KVLFIDTDMRKGYVHK-VFDVENDNGLSnylsgklgl 592
Cdd:COG3598 11 PEGGVTLLAGP-PGTGKSFLALQLAAAVA-AGGpwlgrrvppgKVLYLAAEDDRGELRRrLKALGADLGLP--------- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1031815719 593 eatlKKIPEAGFDFISrGVVPPNPTELLmhRRMEEMLKwaSQNYDLVILDT 643
Cdd:COG3598 80 ----FADLDGRLRLLS-LAGDLDDTDDL--EALERAIE--EEGPDLVVIDP 121
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
536-642 |
4.03e-03 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 39.46 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 536 PNAGKTFISSNLAAVVAQTGKKVLFIDTDmrkgyvhkvfdvendnGLSnylsgklgLEaTLKKIPEAGFDFISRGVVPPN 615
Cdd:PRK09361 32 PGSGKTNICLQLAVEAAKNGKKVIYIDTE----------------GLS--------PE-RFKQIAGEDFEELLSNIIIFE 86
|
90 100
....*....|....*....|....*...
gi 1031815719 616 PTELLMHRR-MEEMLKWASQNYDLVILD 642
Cdd:PRK09361 87 PSSFEEQSEaIRKAEKLAKENVGLIVLD 114
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
539-699 |
5.94e-03 |
|
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.
Pssm-ID: 349755 [Multi-domain] Cd Length: 250 Bit Score: 39.03 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 539 GKTFISSNLAAVVAQTGKKVLFIDTD----------MRKGYVHKVFDVEN--------DNGLSNYLSGKLGLEATLKKIP 600
Cdd:cd02035 12 GKTTIAAATAVRLAEQGKRVLLVSTDpahslsdafgQKLGGETPVKGAPNlwameidpEEALEEYWEEVKELLAQYLRLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031815719 601 EAGFDFISRGVVPPNPTELLMhrrMEEMLKW-ASQNYDLVILDTPP---------------ILAVTDAAIighyagTTL- 663
Cdd:cd02035 92 GLDEVYAEELLSLPGMDEAAA---FDELREYvESGEYDVIVFDTAPtghtlrllslpleqvRELLRDPER------TTFv 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1031815719 664 LVARFELNTVKEMDVAFKRFEQSGIVAKGCILNGIV 699
Cdd:cd02035 163 LVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVL 198
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
527-564 |
5.96e-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: 37.03 E-value: 5.96e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1031815719 527 NILMISGASPNAGKTFISSNLAAVVAQTGKKVLFIDTD 564
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
|