|
Name |
Accession |
Description |
Interval |
E-value |
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
25-724 |
1.26e-105 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 338.14 E-value: 1.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 25 MTSSPQVEREDTDYIDLEQYWLILKRRWVPASVVAGSVVGLAALVTFMQKPIYEAKAELLFNKQSNVSSLTGLSGavgel 104
Cdd:COG3206 1 MNESSSAPPEEEDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSS----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 105 sgITNLSNPLETEAKVIRSNPIIQKTIDKFNLRDDDNEPIS-----IEDFLKQLKVKSAKGTDVLEISYKGTDPQQAAAI 179
Cdd:COG3206 76 --LSASDSPLETQIEILKSRPVLERVVDKLNLDEDPLGEEAsreaaIERLRKNLTVEPVKGSNVIEISYTSPDPELAAAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 180 VNSLMQDYIDNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENKVVALKEEAQFGVEGLKDSLQELNQAEA 259
Cdd:COG3206 154 ANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 260 KLAAANERSQALQRELDIEKQkavELSELSQSPAVQQALQEYQKVQDRLAVARTRLTNQHPTVIDLSNKERALRNQLEKR 339
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPD---ALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 340 VGQVvnnnsndssitednlqvgeikqtltseLLKSEVERLAVAKQVGVLRKAFALQQARLTVLPKLEQQQRQVERKLQIA 419
Cdd:COG3206 311 AQRI---------------------------LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 420 QLTYQNLLKKLQEVQVIENQNIGNARIISEALVPDKKISPRIALNLLLGGFLGILLGAGTALILETMDKSLKTVDQAKRL 499
Cdd:COG3206 364 RELYESLLQRLEEARLAEALTVGNVRVIDPAVVPLKPVSPKKLLILALGLLLGLLLGLGLALLLELLDRTIEEELELLLL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 500 LNYPVLGTIPQFEGKGFDGNPELPTLNNPYSVESSAFEMLQ-----TNLSFTSSDKTLKVLMVTSSVPGEGKSLVSANLA 574
Cdd:COG3206 444 LGLPLLGPLPPLKSKRERRRARLALLLLAAALAALLALLLAlllllLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAA 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 575 VTISQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLSNLLVGKAELQNSIQKPLATLDLLPAGKIPPNPGALVDSQSMVSLL 654
Cdd:COG3206 524 AALLLLLLLLLLLDLLLLLLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLL 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 655 EEAKKEYDFIIIDTPPLTAAADSLIFSKLVDGTLLVVRPGIATSDAVSAAKNQLEQSGQRVLGMALNGIN 724
Cdd:COG3206 604 LLLLLSDDLILDLVPLLAALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVV 673
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
534-722 |
1.68e-69 |
|
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: 225.91 E-value: 1.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 534 SAFEMLQTNLSFTSSDKTLKVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLSNLLV 613
Cdd:cd05387 1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 614 GKAELQNSIQK-PLATLDLLPAGKIPPNPGALVDSQSMVSLLEEAKKEYDFIIIDTPPLTAAADSLIFSKLVDGTLLVVR 692
Cdd:cd05387 81 GQASLEDVIQStNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160
|
170 180 190
....*....|....*....|....*....|
gi 2182208308 693 PGIATSDAVSAAKNQLEQSGQRVLGMALNG 722
Cdd:cd05387 161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
549-726 |
7.37e-64 |
|
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: 214.67 E-value: 7.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 549 DKTLKVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLSNLLVGKAELQNSIQKPLAT 628
Cdd:COG0489 89 RLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEVE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 629 -LDLLPAGKIPPNPGALVDSQSMVSLLEEAKKEYDFIIIDTPPLTAAADSLIFSKLVDGTLLVVRPGIATSDAVSAAKNQ 707
Cdd:COG0489 169 gLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEM 248
|
170
....*....|....*....
gi 2182208308 708 LEQSGQRVLGMALNGINRD 726
Cdd:COG0489 249 LEKAGVPVLGVVLNMVCPK 267
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
82-725 |
7.70e-60 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 215.02 E-value: 7.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 82 ELLFNKQSNVSSLTGLS--GAVGEL---SGITNLSNPLETEakvirsnPIIQKTIDKFNLRDddnepiSIEDFLKQLKV- 155
Cdd:PRK11519 155 NVLDDKNYQLSSDGGFSarGQVGQMlkkDGVTLMVEAIHAR-------PGTEFTVTKYSTLG------MINNLQNNLTVt 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 156 KSAKGTDVLEISYKGTDPQQAAAIVNSLMQDYIDNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENKVVA 235
Cdd:PRK11519 222 ENGKDTGVLSLTYTGEDREQIRDILNSITRNYLEQNIERKSEEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVD 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 236 LKEEAQFGVEGLKDSLQELNQAEAKLAaanersqalqreldiekqkavELSELsqspavqqalqeyqkvqdrlavartrL 315
Cdd:PRK11519 302 LPLEAKAVLDSMVNIDAQLNELTFKEA---------------------EISKL--------------------------Y 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 316 TNQHPtvidlsnkerALRNQLEKRvgqvvnnnsndssitednlqvgeikQTLTSEllKSEVERlavakqvgvlrkafalq 395
Cdd:PRK11519 335 TKEHP----------AYRTLLEKR-------------------------KALEDE--KAKLNG----------------- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 396 qaRLTVLPKLEQQQRQVERKLQIAQLTYQNLLKKLQEVQVIENQNIGNARIISEALVPDKKISPRIALNLLLGGFLGILL 475
Cdd:PRK11519 361 --RVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRIVDPAITQPGVLKPKKALIILGAIILGLML 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 476 GAGTALILETMDKSLKTVDQAKRLlNYPVLGTIPQFE------------GKGFDGNPELPTLNNPYSVESSAFEMLQTNL 543
Cdd:PRK11519 439 SIVGVLLRSLFNRGIESPQVLEEH-GISVYASIPLSEwqkardsvktikGIKRYKQSQLLAVGNPTDLAIEAIRSLRTSL 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 544 SFTSSDKTLKVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLSNLLVGKAELQNSIQ 623
Cdd:PRK11519 518 HFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNGLSDILIGQGDITTAAK 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 624 KP-LATLDLLPAGKIPPNPGALVDSQSMVSLLEEAKKEYDFIIIDTPPLTAAADSLIFSKLVDGTLLVVRPGIATSDAVS 702
Cdd:PRK11519 598 PTsIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVE 677
|
650 660
....*....|....*....|...
gi 2182208308 703 AAKNQLEQSGQRVLGMALNGINR 725
Cdd:PRK11519 678 TSLSRFEQNGIPVKGVILNSIFR 700
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
38-724 |
3.06e-57 |
|
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: 208.81 E-value: 3.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 38 YIDLEQYW-LILKRRWVPASVVAgSVVGLAALVTFMQKPIYEAKAELLFnkQSNVSSLTGLSGAVgelSGITNLSNPLET 116
Cdd:TIGR01005 3 EIDLDRLLaALFANARLIAAFAA-AFIALGAAYAFFARPVYEADIMILL--DDNLNKAAEEEGDP---SNLFDLDTDAAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 117 EAKVIRSNPIIQKTIDKFNLRDDD---NEPISIEDFLKQ-------------------------------------LKVK 156
Cdd:TIGR01005 77 AIEILKSGELAGKAVDKLHLSENAkilNPPRFPVDLIGAwiksaaglfsepggfdlgeeaagneridkaaadipeaLAGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 157 SAKGTDVLEISYKGTDPQQAAAIVNSLMQDYIDNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENKVVAL 236
Cdd:TIGR01005 157 PFKLISLGAGAFRLEDKLLAAPIAGGVAEALEADQLIANFEAQENALTAKAEALFDLEQDSQAAALEMAHDKAEIAEKAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 237 KEEAqFGVEGLKDSLQELNQAEAKLAAANERSQALQRELDIEKQKAVELSELSQspavqqalqeyqkvQDRLAVARTRLT 316
Cdd:TIGR01005 237 QGEI-IGEAQLADLNPALIAAIADQAAAEARADNIKRIADEAEENAVFLAGILP--------------KEGDELEIADLK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 317 NQHPTVIdlsNKERALRNQLEKRVGQVVnnnSNDSSITEDNLQVGEIKQTLTSellkSEVERLAVAKQV-GVLRKAFALQ 395
Cdd:TIGR01005 302 TNELRNG---KGEFDLSDEFGADHPEAV---CSAPSLQELKAKIAEELQQFTA----SHKGEQAIAQQIeESLRGKINGI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 396 QARLTVLPKLEQQQRQVERKLQIAQLTYQNLLKKLQEVQVIENQNIGNARIISEALVPDKKISPRIALNLLLGGFLGILL 475
Cdd:TIGR01005 372 AGKLKDAPEIEQDLRELEQDAAADKELYESLLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTLALAAVLGMML 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 476 GAGTALILETMDKSLKTVDQAKRLLNYPVLGTIPqFEGKGFDGNPELPT--------------------------LNNPY 529
Cdd:TIGR01005 452 GGAAAAFLEALEGGFRDEGDIEEHLGHRSLATVP-LLDTQMDKKAQLTHahfgsvkrhdeavddtmpfqllarivPDAPR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 530 SVESSAFEMLQTNLSFTSSDKTLKVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLS 609
Cdd:TIGR01005 531 STFAEAFRNAKLACDFALADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPGLL 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 610 NLLVGKAELQNSIQKPLAT-LDLLPAGKI---PPNPGALVDSQSMVSLLEEAKKEYDFIIIDTPPLTAAADSLIFSKLVD 685
Cdd:TIGR01005 611 DLLAGEASIEAGIHRDQRPgLAFIAAGGAshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALAD 690
|
730 740 750
....*....|....*....|....*....|....*....
gi 2182208308 686 GTLLVVRPGIATSDAVSAAKNQLEQSGQRVLGMALNGIN 724
Cdd:TIGR01005 691 GILFVTEFERSPLGEIRDLIHQEPHANSDVLGVIFNALD 729
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
155-723 |
5.51e-53 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 195.90 E-value: 5.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 155 VKSAKGTDVLEISYKGTDPQQAAAIVNSLMQDYIDNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENKVV 234
Cdd:PRK09841 221 SERSKESGMLELTMTGDDPQLITRILNSIANNYLQQNIARQAAQDSQSLEFLQRQLPEVRSELDQAEEKLNVYRQQRDSV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 235 ALKEEAQFGVEGLKDSLQELNQAEAKLAaanersqalqreldiekqkavELSELsqspavqqalqeYQKvqdrlavartr 314
Cdd:PRK09841 301 DLNLEAKAVLEQIVNVDNQLNELTFREA---------------------EISQL------------YKK----------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 315 ltnQHPTVidlsnkeRALRnqlEKRvgqvvnnnsndssitednlqvgeikQTLtsellksEVERLAVAKqvgvlrkafal 394
Cdd:PRK09841 337 ---DHPTY-------RALL---EKR-------------------------QTL-------EQERKRLNK----------- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 395 qqaRLTVLPKLEQQQRQVERKLQIAQLTYQNLLKKLQEVQVIENQNIGNARIISEALVPDKKISPRIALNLLLGGFLGIL 474
Cdd:PRK09841 361 ---RVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELSISKSSAIGNVRIIDPAVTQPQPVKPKKALNVVLGFILGLF 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 475 LGAGTALILETMDKSLKTVDQAKrLLNYPVLGTIPQFE---------GKGFDGN---------PELPtLNNPYSVESSAF 536
Cdd:PRK09841 438 ISVGAVLARAMLRRGVEAPEQLE-EHGISVYATIPMSEwldkrtrlrKKNLFSNqqrhrtkniPFLA-VDNPADSAVEAV 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 537 EMLQTNLSFTSSDKTLKVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLSNLLVGKA 616
Cdd:PRK09841 516 RALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNEHGLSEYLAGKD 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 617 ELQNSIQK-PLATLDLLPAGKIPPNPGALVDSQSMVSLLEEAKKEYDFIIIDTPPLTAAADSLIFSKLVDGTLLVVRPGI 695
Cdd:PRK09841 596 ELNKVIQHfGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGL 675
|
570 580
....*....|....*....|....*...
gi 2182208308 696 ATSDAVSAAKNQLEQSGQRVLGMALNGI 723
Cdd:PRK09841 676 NTAKEVSLSMQRLEQAGVNIKGAILNGV 703
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
536-726 |
1.81e-51 |
|
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: 178.01 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 536 FEMLQTNLSFtsSDKTLKVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKI-HSFSGLSNLLVG 614
Cdd:TIGR01007 3 YNAIRTNIQF--SGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSqNKITGLTNFLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 615 KAELQNSIQKP-LATLDLLPAGKIPPNPGALVDSQSMVSLLEEAKKEYDFIIIDTPPLTAAADSLIFSKLVDGTLLVVRP 693
Cdd:TIGR01007 81 TTDLSDAICDTnIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVTDA 160
|
170 180 190
....*....|....*....|....*....|...
gi 2182208308 694 GIATSDAVSAAKNQLEQSGQRVLGMALNGINRD 726
Cdd:TIGR01007 161 GKIKKREVKKAKEQLEQAGSNFLGVVLNKVDIS 193
|
|
| pepcterm_TyrKin |
TIGR03018 |
exopolysaccharide/PEP-CTERM locus tyrosine autokinase; Members of this protein family are ... |
524-721 |
3.80e-42 |
|
exopolysaccharide/PEP-CTERM locus tyrosine autokinase; Members of this protein family are related to a known protein-tyrosine autokinase and to numerous homologs from exopolysaccharide biosynthesis region proteins, many of which are designated as chain length determinants. Most members of this family contain a short region, immediately C-terminal to the region modeled here, with an abundance of Tyr residues. These C-terminal tyrosine residues are likely to be autophosphorylation sites. Some members of this family are fusion proteins.
Pssm-ID: 274392 [Multi-domain] Cd Length: 207 Bit Score: 152.07 E-value: 3.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 524 TLNNPYSVESSAFEMLQTNL-SFTSSDKTLK---VLMVTSSVPGEGKSLVSANLAVTISQ-FGQRVLLIDGDMRRPRQHK 598
Cdd:TIGR03018 3 TPNSPRSRIAEEFRKIKRPLlANAFSAATKKnnnLIMVTSSLPGEGKSFTAINLAISLAQeYDKTVLLIDADLRRPSLHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 599 LWKIHSFSGLSNLLVGKAELQNSIQKP--LATLDLLPAGKIPPNPGALVDSQSMVSLLEEAKKEYD--FIIIDTPPLTAA 674
Cdd:TIGR03018 83 TLGLEAEPGLSDCLLDPVLDLADVLVPtnIGRLSLLPAGRRHPNPTELLASQRMRSLLHELARRYPdrIIIIDTPPLLVF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2182208308 675 ADSLIFSKLVDGTLLVVRPGIATSDAVSAAKNQLEqsGQRVLGMALN 721
Cdd:TIGR03018 163 SEARALARLVGQIVLVVEEGRTTQEAVKEALSALE--SCKVLGVVLN 207
|
|
| EpsG |
TIGR03029 |
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ... |
498-721 |
4.41e-39 |
|
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: 145.78 E-value: 4.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 498 RLLNYPVLgtiPQFEGkGFDgnPELPTLNNPYSVESSAFEMLQTNLSFTSSDKTLKVLMVTSSVPGEGKSLVSANLAVTI 577
Cdd:TIGR03029 55 RQFEYPYL---PPNDG-SFS--PDLIAAYQPFSPQVEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 578 SQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLSNLLVGKAELQNSIQKP-LATLDLLPAGKIPPNPGALVDSQSMVSLLEE 656
Cdd:TIGR03029 129 SQLGEKTLLIDANLRDPVQHRNFKLSEQRGLSDILAGRSDLEVITHIPaLENLSVLPAGAIPPNPQELLARPAFTDLLNK 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182208308 657 AKKEYDFIIIDTPPLTAAADSLIFSKLVDGTLLVVRPGIATSDAVSAAKNQLEQSGQRVLGMALN 721
Cdd:TIGR03029 209 VMGDYDVVIVDTPSAEHSSDAQIVATRARGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLN 273
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
40-509 |
3.32e-37 |
|
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: 146.35 E-value: 3.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 40 DLEQYW-LILKRRWvpASVVAGSVVGLAALVTFMQKP-IYEAKAELLFNKQSNVSSLtglsgavgeLSGIT---NLSNPL 114
Cdd:TIGR03007 2 QLLSYLkGIWRRRW--LFVAVAWVVMIVGWGVVYFLPdRYEASARVYVDTQSVLRPL---------LKGIAvtpNVDQKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 115 ETEAKVIRSNPIIQKTIDKFNL----RDDDNEPISIEDFLKQLKVKSAKGTDVLEISYKGTDPQQAAAIVNSLMQDYIDN 190
Cdd:TIGR03007 71 RIMSRTLLSRPNLEKVIRMLDLdlgaKSPAQLEALITKLRKNISISLAGRDNLFTISYEDKDPELAKDVVQTLLTIFVEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 191 NIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENKVVALKEEAQFgVEGLKDSLQELNQAEAKLAAANERSQA 270
Cdd:TIGR03007 151 TLGSKRQDSDSAQRFIDEQIKTYEKKLEAAENRLKAFKQENGGILPDQEGDY-YSEISEAQEELEAARLELNEAIAQRDA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 271 LQRELDIEKQKAVELSELSQSPAvQQALQEYQKVQDRLavaRTRLTNQHPTVIDLsnkeRALRNQLEKRVGQVVNNNSND 350
Cdd:TIGR03007 230 LKRQLGGEEPVLLAGSSVANSEL-DGRIEALEKQLDAL---RLRYTDKHPDVIAT----KREIAQLEEQKEEEGSAKNGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 351 SSITEDnlqVGEIKQTLTSELLKSEVERLAVAKQVGVLRKAFALQQARLTVLPKLEQQQRQVERKLQIAQLTYQNLLKKL 430
Cdd:TIGR03007 302 PERGEI---ANPVYQQLQIELAEAEAEIASLEARVAELTARIERLESLLRTIPEVEAELTQLNRDYEVNKSNYEQLLTRR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 431 QEVQV---IENQNIGNA-RIISEALVPDKKISPRIALNLLLGGFLGILLGAGTALILETMDKSLKTVDQAKRLLNYPVLG 506
Cdd:TIGR03007 379 ESAEVskqMEVQDKAVSfRIIDPPIVPSKPSGPNRPLLMLAGLLGGLGAGIGLAFLLSQLRPTVRSVRDLRELTGLPVLG 458
|
...
gi 2182208308 507 TIP 509
Cdd:TIGR03007 459 VIP 461
|
|
| EpsF |
TIGR03017 |
chain length determinant protein EpsF; Sequences in this family of proteins are members of the ... |
41-508 |
9.25e-27 |
|
chain length determinant protein EpsF; Sequences in this family of proteins are members of the chain length determinant family (pfam02706) which includes the wzc protein from E.coli. This family of proteins are homologous to the EpsF protein of the methanolan biosynthesis operon of Methylobacillus species strain 12S. The distribution of this protein appears to be restricted to a subset of exopolysaccharide operons containing a syntenic grouping of genes including a variant of the EpsH exosortase protein. Exosortase has been proposed to be involved in the targetting and processing of proteins containing the PEP-CTERM domain to the exopolysaccharide layer.
Pssm-ID: 132062 [Multi-domain] Cd Length: 444 Bit Score: 114.14 E-value: 9.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 41 LEQYWLILK-RRWVPASVVAGSVVGlAALVTFMQKPIYEAKAELLFNKQSNvsslTGLSGAVgeLSGITNLSNpLETEAK 119
Cdd:TIGR03017 3 LIQFLLILKaRYWIVLFTLLITVTT-TAVVSLLLPKEYTATTSVVLDYKGP----DPVTGMV--LPGQMSPGY-MATQVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 120 VIRSNPIIQKTIDKfnLRDDDNEPISiEDF------------------LKQLKVKSAKGTDVLEISYKGTDPQQAAAIVN 181
Cdd:TIGR03017 75 IINSDRVAKKVVDK--LKLDENPAVK-EKFeeatggqgslkewladllLKKLEVKPSRESSVISIEFSGVDPRFAATVAN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 182 SLMQDYIDNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENKVVALKEEAQFGVEGLKDSLQELNQAEAKL 261
Cdd:TIGR03017 152 AFAQAYIDTNIELKVEPAQKAALWFVQQIAALREDLARAQSKLSAYQQEKGIVSSDERLDVERARLNELSAQLVAAQAQV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 262 AAANERSQAlqreldieKQKAVELSELSQSPAVQQALQEYQKVQDRLAVARTRLTNQHPTVIDLSNKERALRNQLEKRVG 341
Cdd:TIGR03017 232 MDASSKEGG--------SSGKDALPEVIANPIIQNLKTDIARAESKLAELSQRLGPNHPQYKRAQAEINSLKSQLNAEIK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 342 QVVNNNSNDSSITEdnlqvgeikqtltsellkseverlavaKQVGVLRKAFALQQARLTVLPKLEQQQRQVERKLQIAQL 421
Cdd:TIGR03017 304 KVTSSVGTNSRILK---------------------------QREAELREALENQKAKVLELNRQRDEMSVLQRDVENAQR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 422 TYQNLLKKLQEVQVIENQNIGNARIISEALVPDKKISPRIALNLLLGGFLGILLGAGTALILETMDKSLKTVDQAKRLLN 501
Cdd:TIGR03017 357 AYDAAMQRYTQTRIEAQSNQTDISILNPAVPPLEPSSPRLLLNLVLSIFLGMLLGIGFAFLAELMDRRVRSADDIIEALD 436
|
....*..
gi 2182208308 502 YPVLGTI 508
Cdd:TIGR03017 437 VPVLATI 443
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
39-183 |
1.86e-20 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 92.82 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 39 IDLEQYWLILKRRWVPASVVAGSVVGLAALVTFMQKPIYEAKAELLFNKQSNvssltglSGAVGELSGITNLSNPLETEA 118
Cdd:COG3944 2 MDLREYLRILRRRWWLILLLTLLGALAALASSFLITPVYQASTTLLVSTSSG-------SDASDLYQGIQTAQQLVNTYA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182208308 119 KVIRSNPIIQKTIDKFNLrdddnePISIEDFLKQLKVKSAKGTDVLEISYKGTDPQQAAAIVNSL 183
Cdd:COG3944 75 ELLKSPAVLEEVIDELGL------DLSPEELAKKISVTSPPDTQVITITVTDTDPERAADIANAV 133
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
569-721 |
5.96e-19 |
|
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: 86.48 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 569 VSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLSNLLVGKAELQNSIQKPLATLDLLPAGKIPPNPGALVDSQ 648
Cdd:COG0455 2 VAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGPGGLDVLPGGSGPAELAELDPEE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182208308 649 SMVSLLEEAKKEYDFIIIDTPPlTAAADSLIFSKLVDGTLLVVRPGIAT-SDAVSAAKNQLEQSGQRVLGMALN 721
Cdd:COG0455 82 RLIRVLEELERFYDVVLVDTGA-GISDSVLLFLAAADEVVVVTTPEPTSiTDAYALLKLLRRRLGVRRAGVVVN 154
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
49-316 |
5.12e-14 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 74.50 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 49 KRRWVPASVVAgsVVGLAALVT-----FMQKPIYEAKAELLFNKQSNVSSLTGLSGAVGELSGITNLSNPLeTEAKVIRS 123
Cdd:COG3524 8 RRKLLLLLFLL--FVLLPTLLAalyygLIASDQYVSEARFVVRSAEGQSGSDGLGGLLGGTGFSSSSQDSY-IVQDYLRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 124 NPIIQKTIDKFNLR----DDDNEPI-------SIEDFL----KQLKVKSAKGTDVLEISYKGTDPQQAAAIVNSLMQdyi 188
Cdd:COG3524 85 RDAVERLDAELDLRahysRPGIDPLsrldpdaSIEDLYkyyrRRVKVEYDSTSGIITLEVRAFDPEDAQAIAEALLA--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 189 DNNIRVNTAEARAARE---FLNNQLPEVESRVVKAEAELRKFKEENKVVALKEEAQfGVEGLKDSLQ-ELNQAEAKLAA- 263
Cdd:COG3524 162 ESEELVNQLSERAREDavrFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAE-ALLQLIATLEgQLAELEAELAAl 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182208308 264 -------------ANERSQALQRELDIEKQKaveLSELSQSPAVQQALQEYQKVQDRLAVARTRLT 316
Cdd:COG3524 241 rsylspnspqvrqLRRRIAALEKQIAAERAR---LTGASGGDSLASLLAEYERLELEREFAEKAYT 303
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
553-693 |
2.51e-13 |
|
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: 69.91 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHSFSGLSNLLVGKAELQNSIQKPLATLDLL 632
Cdd:cd02038 1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGPEGLDII 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2182208308 633 PAGKippnpgalvDSQSMVSL-----------LEEAKKEYDFIIIDTPPLTaAADSLIFSKLVDGTLLVVRP 693
Cdd:cd02038 81 PGGS---------GMEELANLdpeqkaklieeLSSLESNYDYLLIDTGAGI-SRNVLDFLLAADEVIVVTTP 142
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
553-726 |
1.70e-12 |
|
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.
Pssm-ID: 131024 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHSFS-GLSNLLVGKAELQNSIQKPLATLDL 631
Cdd:TIGR01969 1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPvTLHDVLAGEADIKDAIYEGPFGVKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 632 LPAG----KI-PPNPGALVDsqsmvsLLEEAKKEYDFIIIDTPPlTAAADSLIFSKLVDGTLLVVRPGIAT-SDAVSaAK 705
Cdd:TIGR01969 81 IPAGvsleGLrKADPDKLED------VLKEIIDDTDFLLIDAPA-GLERDAVTALAAADELLLVVNPEISSiTDALK-TK 152
|
170 180
....*....|....*....|.
gi 2182208308 706 NQLEQSGQRVLGMALNGINRD 726
Cdd:TIGR01969 153 IVAEKLGTAILGVVLNRVTRD 173
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
553-726 |
5.39e-12 |
|
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: 66.07 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMrrprqhklwkihsfsGLSNL-----------------LVGK 615
Cdd:cd02036 1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADI---------------GLRNLdlilglenrivytlvdvLEGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 616 AELQNSI--QKPLATLDLLPAGKIPPNPGalVDSQSMVSLLEEAKKEYDFIIIDTPP-LTAAADSLIFSklVDGTLLVVR 692
Cdd:cd02036 66 CRLEQALikDKRWENLYLLPASQTRDKDA--LTPEKLEELVKELKDSFDFILIDSPAgIESGFINAIAP--ADEAIIVTN 141
|
170 180 190
....*....|....*....|....*....|....*
gi 2182208308 693 PGI-ATSDAVSaAKNQLEQSGQRVLGMALNGINRD 726
Cdd:cd02036 142 PEIsSVRDADR-VIGLLESKGIVNIGLIVNRYRPE 175
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
563-679 |
1.89e-11 |
|
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: 64.88 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 563 GEGKSLVSANLAVTISQFGQRVLLIDGDM---------RRPRQHKLwkihsfsGLSNLLVGKAELQNSIQK-PLATLDLL 632
Cdd:COG1192 12 GVGKTTTAVNLAAALARRGKRVLLIDLDPqgnltsglgLDPDDLDP-------TLYDLLLDDAPLEDAIVPtEIPGLDLI 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 633 PAG----KIPPNPGALVDSQSMVS-LLEEAKKEYDFIIIDTPP----LT----AAADSLI 679
Cdd:COG1192 85 PANidlaGAEIELVSRPGRELRLKrALAPLADDYDYILIDCPPslglLTlnalAAADSVL 144
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
553-710 |
2.98e-11 |
|
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443989 [Multi-domain] Cd Length: 358 Bit Score: 65.52 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQ-FGQRVLLIDGDMR----------RPRQhklwkihsfsGLSNLLVGKAE---- 617
Cdd:COG4963 103 RVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQfgdvalyldlEPRR----------GLADALRNPDRldet 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 618 -LQNSIQKPLATLDLLPAGKiPPNPGALVDSQSMVSLLEEAKKEYDFIIIDTPPLTAAADSLIFSkLVDGTLLVVRPGIA 696
Cdd:COG4963 173 lLDRALTRHSSGLSVLAAPA-DLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALE-AADEVVLVTEPDLP 250
|
170
....*....|....
gi 2182208308 697 tsdAVSAAKNQLEQ 710
Cdd:COG4963 251 ---SLRNAKRLLDL 261
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
555-721 |
7.20e-11 |
|
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: 62.75 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 555 LMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLWKIHS----FSGLSNLLVGKAELQNSIQKPLAT-- 628
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDiapaLQALAEGLKGRVNLDPILLKEKSDeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 629 -LDLLPAG----KIPPNPGALVDSQSMVSLLEEAKKEYDFIIIDTPP----LTAAADSlifskLVDGTLLVVRPG-IATS 698
Cdd:pfam01656 81 gLDLIPGNidleKFEKELLGPRKEERLREALEALKEDYDYVIIDGAPglgeLLRNALI-----AADYVIIPLEPEvILVE 155
|
170 180
....*....|....*....|....*....
gi 2182208308 699 DA------VSAAKNQLEQSGQRVLGMALN 721
Cdd:pfam01656 156 DAkrlggvIAALVGGYALLGLKIIGVVLN 184
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
563-679 |
2.17e-10 |
|
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: 60.29 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 563 GEGKSLVSANLAVTISQFGQRVLLIDGDMrrprQ------HKLWKIHSFSGLSNLLVGKAELQNSIQKPLA-TLDLLPAG 635
Cdd:pfam13614 12 GVGKTTTSVNLAAALAKKGKKVLLIDLDP----QgnatsgLGIDKNNVEKTIYELLIGECNIEEAIIKTVIeNLDLIPSN 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2182208308 636 K-----------IPPNPGALVDsqsmvsLLEEAKKEYDFIIIDTPP----LT----AAADSLI 679
Cdd:pfam13614 88 IdlagaeieligIENRENILKE------ALEPVKDNYDYIIIDCPPslglLTinalTASDSVL 144
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
343-595 |
3.21e-08 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 55.84 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 343 VVNNNSNDSSITEDNLQVGEiKQTLT-SELLKSEVERLAVAKQVGVLRKAFALQQaRLTVLPKLEQQQRQV-------ER 414
Cdd:COG3944 48 VSTSSGSDASDLYQGIQTAQ-QLVNTyAELLKSPAVLEEVIDELGLDLSPEELAK-KISVTSPPDTQVITItvtdtdpER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 415 KLQIAQLTYQNLLKKLQEVQvienqNIGNARIISEALVPDKKISPRIALNLLLGGFLGILLGAGTALILETMDKSLKTVD 494
Cdd:COG3944 126 AADIANAVAEVFAEEVKELM-----KVDNVTVLDPATVPASPVSPNPKLNLAIGLVLGLLLGVGLAFLRELLDTTIRSEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 495 QAKRLLNYPVLGTIPqfegkGFDGNPELPTLNNPYSVESSAFEMLQTNLSFTSSDKTLKVLMVTSSVPGEGKSLVSANLA 574
Cdd:COG3944 201 DIERLLGLLLGGAVP-----AARSARPLLLLLADASPRAAAARRRRRNLLFALAAVDARTVVVVSSSLSEGKSTTTAALA 275
|
250 260
....*....|....*....|.
gi 2182208308 575 VTISQFGQRVLLIDGDMRRPR 595
Cdd:COG3944 276 LALAAAAAGVVLVLADLDRRR 296
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
404-460 |
1.72e-07 |
|
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, pfam02706 and CbiA pfam01656. There is a highly conserved GNVR sequence motif which characterizes this domain. The function is not known.
Pssm-ID: 433492 [Multi-domain] Cd Length: 82 Bit Score: 49.13 E-value: 1.72e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2182208308 404 KLEQQQRQVERKLQIAQLTYQNLLKKLQEVQVIENQNIGNARIISEALVPDKKISPR 460
Cdd:pfam13807 1 DTQQEILRLTRDVEVNTEIYTQLLNSNQELEVVKAGTVGNVRIVDTAVVPPKPVKPK 57
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
553-715 |
2.32e-06 |
|
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: 49.58 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQ-FGQRVLLIDGDMR----------RPRQHKLWKIHSFSGLsnllvGKAELQNS 621
Cdd:cd03111 1 RVVAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDLPfgdlglylnlRPDYDLADVIQNLDRL-----DRTLLDSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 622 IQKPLATLDLLPAgkiPPNPGALVDSQ--SMVSLLEEAKKEYDFIIIDTPPL--TAAADSLIFSklvDGTLLVVRPGIAt 697
Cdd:cd03111 76 VTRHSSGLSLLPA---PQELEDLEALGaeQVDKLLQVLRAFYDHIIVDLGHFldEVTLAVLEAA---DEILLVTQQDLP- 148
|
170 180
....*....|....*....|....
gi 2182208308 698 sdAVSAAKN------QLEQSGQRV 715
Cdd:cd03111 149 --SLRNARRlldslrELEGSSDRL 170
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-443 |
3.76e-06 |
|
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: 50.44 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 197 AEARAAREFLNNQLPEVESRVVKAEAEL----RKFKEENKVVA-LKEEAQFGVEGLKDSLQELNQAEAKLAAANERSQAL 271
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELeelsRQISALRKDLArLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 272 QRELDIEKQKAVEL--------SELSQSPAVQQALQ-EYQKVQDRLAVARTRLTNQHPTVIDLSNKERALRNQLEKRVGQ 342
Cdd:TIGR02168 774 EEELAEAEAEIEELeaqieqlkEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 343 VVNNNS--NDSSITEDNLQ-----VGEIKQTLTSELLKSEVERLAVAKQVGVLRKAF-ALQQARLtvlpKLEQQQRQVER 414
Cdd:TIGR02168 854 IESLAAeiEELEELIEELEseleaLLNERASLEEALALLRSELEELSEELRELESKRsELRRELE----ELREKLAQLEL 929
|
250 260
....*....|....*....|....*....
gi 2182208308 415 KLQIAQLTYQNLLKKLQEVQVIENQNIGN 443
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
553-590 |
4.83e-06 |
|
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: 45.88 E-value: 4.83e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGD 590
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-502 |
6.21e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 197 AEARAAREFLNNQLPEVESRVVKAEAELRKfkEENKVVALKEEAQFGVEGLKDSLQELNQAEAKLAAANERSQALQRELD 276
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYE--LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 277 IEKQKAVELSElsqspAVQQALQEYQKVQDRLAVARTRLTNQHPTVIDLSNKERALRNQLEKRVGQVVNNNSNDSSITED 356
Cdd:COG1196 341 ELEEELEEAEE-----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 357 NLQVGEIKQTLTSELLKSEVERLAVAKQVGVLRKAFALQQARLT----VLPKLEQQQRQVERKLQIAQLTYQNLLKKLQE 432
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEalleLLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 433 VQVIENQNIGNARIISEALVPDKKISPRIALNLLLGGFLGILLGAGTALILETMDKSLKTVDQAKRLLNY 502
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
553-718 |
2.96e-05 |
|
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.
Pssm-ID: 431392 [Multi-domain] Cd Length: 246 Bit Score: 46.29 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDmrrprqhklwkIHSFS-----GLSNllvgkaelqnsiQKPLA 627
Cdd:pfam10609 4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD-----------IYGPSiprmlGLEG------------ERPEQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 628 TldllPAGKIPPNP--------GALVDSQS--------MVS-----LLEEAK-KEYDFIIIDTPP------LTaaadslI 679
Cdd:pfam10609 61 S----DGGIIPVEAhgikvmsiGFLLPDEDdaviwrgpMKSgaikqFLTDVDwGELDYLIIDLPPgtgdeqLT------L 130
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2182208308 680 FSKL-VDGTLLVVRP-GIATSDAVSAAkNQLEQSGQRVLGM 718
Cdd:pfam10609 131 AQLLpLTGAVIVTTPqDVALLDVRKAI-DMFKKVNVPVLGV 170
|
|
| MipZ |
pfam09140 |
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
563-679 |
5.32e-05 |
|
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.
Pssm-ID: 401181 [Multi-domain] Cd Length: 262 Bit Score: 45.52 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 563 GEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKLwkihsfsgLSNllvgKAELQNSIQKPLATLDLLpagKIPPNPG 642
Cdd:pfam09140 11 GSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRY--------FEN----RSATADRTGLSLPTPEHL---NLPDNDV 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2182208308 643 ALV------DSQSMVSLLEEAKKEYDFIIIDTP----PLT----AAADSLI 679
Cdd:pfam09140 76 AEVpdgeniDDARLEEAFADLEARCDFIVIDTPgsdsPLSrlahSRADTLV 126
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-445 |
8.49e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 189 DNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEE------------NKVVALKEEAQfGVEGLKDSLQEL-N 255
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleeleleleeaqAEEYELLAELA-RLEQDIARLEERrR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 256 QAEAKLAAANERSQALQRELDIEKQKAVELSElsqspAVQQALQEYQKVQDRLAVARTRLTNQHPTVIDLSNKERALRNQ 335
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEE-----ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 336 LEKRVGQVVNNNSNDSSITEDNLQVGEIKQTLTSELLKSEVERLAVAKQVGVLRKAFALQQARLtvlpkLEQQQRQVERK 415
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-----AELEEEEEALL 462
|
250 260 270
....*....|....*....|....*....|
gi 2182208308 416 LQIAQLTYQNLLKKLQEVQVIENQNIGNAR 445
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-451 |
1.18e-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: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 198 EARAAREFLNNQLPEVESRVVKAEAELRKFKEEnkvvalkeeaqfgVEGLKDSLQELNQAEAKLAAANERSQALQRELDI 277
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEK-------------LEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 278 EKQKAVE-LSELSQSPA--------VQQALQEYQK----VQDRLAVART-------RLTNQHPTVIDLSNKERALRNQLE 337
Cdd:TIGR02168 303 QKQILRErLANLERQLEeleaqleeLESKLDELAEelaeLEEKLEELKEelesleaELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 338 KRVGQV--------VNNN---SNDSSITEDNLQVGEIKQTLTSELLK-SEVERLAVAKQVGVLRKAFALQQARL----TV 401
Cdd:TIGR02168 383 TLRSKVaqlelqiaSLNNeieRLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELerleEA 462
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2182208308 402 LPKLEQQQRQVERKLQIAQLTYQNLLKKLQEVQVIENQNIGNARIISEAL 451
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
553-669 |
1.37e-04 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 44.38 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMrrprqhKLWKIHSFSGLSN--------LLVGKAELQNSI-- 622
Cdd:CHL00175 16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADI------GLRNLDLLLGLENrvlytamdVLEGECRLDQALir 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2182208308 623 QKPLATLDLLPAGKippNPGAL-VDSQSMVSLLEEAKKE-YDFIIIDTP 669
Cdd:CHL00175 90 DKRWKNLSLLAISK---NRQRYnVTRKNMNMLVDSLKNRgYDYILIDCP 135
|
|
| CBP_BcsQ |
pfam06564 |
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ... |
552-693 |
1.44e-04 |
|
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: 43.91 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 552 LKVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLID---GDMRrpRQHKLWKIHSFSGLSNLLVGKAELQNSIQKPLAT 628
Cdd:pfam06564 1 MKILALQGVRGGVGTTSILAALAWALQRLGERVLLIDlspDNLL--RLHFNVPFEHRQGWARAELDGADWRDAALEYTPG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182208308 629 LDLLPAGKIP----PNPGALV-DSQSMVSLLEEAKKEYDFIIIDTP----PLTAAADSlifskLVDGTLLVVRP 693
Cdd:pfam06564 79 LDLLPFGRLSveeqENLQQLQpDPGAWCRRLQQLKGRYDWVLFDLPagpsPLTRQLLS-----LADLSLLVVNP 147
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
192-431 |
1.45e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.06 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 192 IRVNTAEARAAREFLNNQLpevesrvvKAEAE-LRKFKEENKvvALKEEAQFGVEGLKDSLQELNQAEAKLAAANERSQA 270
Cdd:pfam19220 109 LRIELRDKTAQAEALERQL--------AAETEqNRALEEENK--ALREEAQAAEKALQRAEGELATARERLALLEQENRR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 271 LQRELDiekQKAVELSELSQ-----SPAVQQALQEYQKVQDRLA---VARTRLTNQHPTVIDLSNKERA----------- 331
Cdd:pfam19220 179 LQALSE---EQAAELAELTRrlaelETQLDATRARLRALEGQLAaeqAERERAEAQLEEAVEAHRAERAslrmklealta 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 332 -----------LRNQLEKR--VGQVVNNNSNDSSITEDNLQ--VGEIKQTL---TSELLKSEVERLAVAKQVGVLRKAF- 392
Cdd:pfam19220 256 raaateqllaeARNQLRDRdeAIRAAERRLKEASIERDTLErrLAGLEADLerrTQQFQEMQRARAELEERAEMLTKALa 335
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2182208308 393 ----ALQQA--RLTVLP-KLEQQQRQVERKLQIAQLTYQNLLKKLQ 431
Cdd:pfam19220 336 akdaALERAeeRIASLSdRIAELTKRFEVERAALEQANRRLKEELQ 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
199-450 |
2.14e-04 |
|
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: 44.37 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 199 ARAAREFLNNQLPEVESRVVKAEAELRKFKEEnkvvalkeeaqfgvegLKDSLQELNQAEAKLAAANERSQALQRELDIE 278
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE----------------EKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 279 KQKAVELSELSQspAVQQALQEYQKVQDRLAVARTRLTNQHPTVIDLSNKERALRNQLEKRVGQVVNnnsndssitEDNL 358
Cdd:COG4942 82 EAELAELEKEIA--ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP---------ARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 359 QVGEIKQTLtsELLKSEVERLAVAKQVgvLRKAFALQQARLTVLPKLEQQQRQVERKLQIAQLTYQNLLKKLQEVQVIEN 438
Cdd:COG4942 151 QAEELRADL--AELAALRAELEAERAE--LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|..
gi 2182208308 439 QNIgnARIISEA 450
Cdd:COG4942 227 ALI--ARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
252-432 |
2.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 252 QELNQAEAKLAAANERSQALQRELDIEKQKAVELSELSQSPAVQQALQEYQKVQDRLAVARTRLTNQHPTVidlsnkeRA 331
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL-------AA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 332 LRNQLEKRVGQVvnnNSNDSSITEDNLQVGEIKQTLTS--ELLKSEVERLAVAKQVGVLRKAFALQQARLTVLpkLEQQQ 409
Cdd:COG4913 690 LEEQLEELEAEL---EELEEELDELKGEIGRLEKELEQaeEELDELQDRLEAAEDLARLELRALLEERFAAAL--GDAVE 764
|
170 180
....*....|....*....|...
gi 2182208308 410 RQVERKLQIAQLTYQNLLKKLQE 432
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEE 787
|
|
| Wzz |
pfam02706 |
Chain length determinant protein; This family includes proteins involved in lipopolysaccharide ... |
39-133 |
2.64e-04 |
|
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: 40.35 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 39 IDLEQYWLILKRRWVPASVVAGSVVGLAALVTFMQKPIYEAKAELLFNKQSNVSSLtglsgavGELSGITNLSNPLETEA 118
Cdd:pfam02706 3 IDLIELLGVLWKRKKLIILVTLLFTLLAAAYAFLATPKYTATAQILVPQKKGEAGS-------LLGSDLQAGLQLASTEI 75
|
90
....*....|....*
gi 2182208308 119 KVIRSNPIIQKTIDK 133
Cdd:pfam02706 76 EILKSRDVLEKVIDE 90
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
553-717 |
3.77e-04 |
|
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.
Pssm-ID: 349757 [Multi-domain] Cd Length: 213 Bit Score: 42.49 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 553 KVLMVTSSVPGEGKSLVSANLAVTISQFGQRVLLIDGDMRRPRQHKL-----WKIH-SFSGLSNLLVGKAELQnSIQkpl 626
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLlgvegKPLHqSEEGIVPVEVGGIKVM-SIG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 627 atldLLpagkIPPNPGALVDSQSMVSLLEEAKK-----EYDFIIIDTPPLTAAADSLIFSKL-VDGTLLVVRP-GIATSD 699
Cdd:cd02037 77 ----FL----LPEDDAVIWRGPMKSGAIKQFLKdvdwgELDYLIIDLPPGTGDEHLSLVQLIpIDGAVVVTTPqEVSLID 148
|
170
....*....|....*...
gi 2182208308 700 AVSAAkNQLEQSGQRVLG 717
Cdd:cd02037 149 VRKAI-DMCKKLNIPVLG 165
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-420 |
1.07e-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: 42.75 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 181 NSLMQDYidNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENKvvALKEEAQFGVEGLKDSLQELNQAEAK 260
Cdd:TIGR02169 691 SSLQSEL--RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE--ELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 261 LAaanersqalQRELDIEKQKAvELSELSQSPA---VQQALQEYQKVQDRLAVARTRLTNQHPTVIDLSNKERALRNQLE 337
Cdd:TIGR02169 767 IE---------ELEEDLHKLEE-ALNDLEARLShsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 338 KRVGQVV----NNNSNDSSITEDNLQVGEIKQ----------TLTSELLKSEVERLAVAKQVGVLRKafALQQARLTVlP 403
Cdd:TIGR02169 837 ELQEQRIdlkeQIKSIEKEIENLNGKKEELEEeleeleaalrDLESRLGDLKKERDELEAQLRELER--KIEELEAQI-E 913
|
250
....*....|....*..
gi 2182208308 404 KLEQQQRQVERKLQIAQ 420
Cdd:TIGR02169 914 KKRKRLSELKAKLEALE 930
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
197-432 |
1.49e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 197 AEARAAREFLNNQLPEVESRVVKAEAELRKFKEE------------------NKVVALKEEAQ-------FGVEGLKDSL 251
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyqqaldvqqtraiqyQQAVQALERAKqlcglpdLTADNAEDWL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 252 -----------QELNQAEAKL----AAANERSQALQ--REL--DIE----KQKAVELseLSQSPAVQQALQEYQKVQDRL 308
Cdd:PRK04863 445 eefqakeqeatEELLSLEQKLsvaqAAHSQFEQAYQlvRKIagEVSrseaWDVAREL--LRRLREQRHLAEQLQQLRMRL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 309 AVARTRLTNQHptvidlsNKERALRnQLEKRVGQVVNNnsndssitEDNLQVGEIKQTLTSELLKSEVERLAvakqvgvl 388
Cdd:PRK04863 523 SELEQRLRQQQ-------RAERLLA-EFCKRLGKNLDD--------EDELEQLQEELEARLESLSESVSEAR-------- 578
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2182208308 389 rkafalqQARLTVLPKLEQQQRQVERKLQIAQ--LTYQNLLKKLQE 432
Cdd:PRK04863 579 -------ERRMALRQQLEQLQARIQRLAARAPawLAAQDALARLRE 617
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-338 |
1.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 185 QDYIDNNIRVNTAEARAARefLNNQLPEVESRVVKAEAELRKFKE-----ENKVVALKEE-AQFGVEGLKDSLQELNQAE 258
Cdd:COG4913 274 LEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEArldalREELDELEAQiRGNGGDRLEQLEREIERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 259 AKLAAANERSQALQRELdiekqKAVELSElsqsPAVQQALQEYQK-VQDRLAVARTRLTNQHPTVIDLSNKERALRNQLE 337
Cdd:COG4913 352 RELEERERRRARLEALL-----AALGLPL----PASAEEFAALRAeAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
.
gi 2182208308 338 K 338
Cdd:COG4913 423 E 423
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
181-424 |
1.80e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 181 NSLMQ--DYIDNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENkvvalkEEAQFGVEGLKDSLQELNQAE 258
Cdd:pfam07888 44 AELLQaqEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKH------EELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 259 AKLAAANERSQALQRELDIEKQ--------KAVELSELSQSpaVQQALQEYQKVQDRLAVARTRLTNQHPTVIDLSNKER 330
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKtltqrvleRETELERMKER--AKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 331 ALRNQLEKRVGQVVNNNSNDSSITE--DNLQVGEIKQTLTSELLKSEVERLAVAKqvgvlRKAFALQQARLTVLPKLEQQ 408
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTLTQklTTAHRKEAENEALLEELRSLQERLNASE-----RKVEGLGEELSSMAAQRDRT 270
|
250
....*....|....*..
gi 2182208308 409 QRQVER-KLQIAQLTYQ 424
Cdd:pfam07888 271 QAELHQaRLQAAQLTLQ 287
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-338 |
2.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 174 QQAAAIVNSLMQDYIDNNIRVNTAEARAAREFLNNQLPEVESRVVKAEAELRKFKEENKVV-ALKEEAQFGVEGLKDSLQ 252
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLaALEEQLEELEAELEELEE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 253 ELNQAEAKLAAANERSQALQRELDIEKQKAVELSELSQSPAVQQALQEYQKVQDRLAVARTR--LTNQhptVIDLSNKER 330
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRenLEER---IDALRARLN 783
|
....*...
gi 2182208308 331 ALRNQLEK 338
Cdd:COG4913 784 RAEEELER 791
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
563-679 |
2.29e-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: 38.68 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 563 GEGKSLVSANLAVTISQFGQRVLLIDGDmrrPRQHklwkihsfsgLSNLLvgkaelqnsiqkplatldllpagkippnpg 642
Cdd:cd02042 11 GVGKTTLAVNLAAALALRGKRVLLIDLD---PQGS----------LTSWL------------------------------ 47
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2182208308 643 alvdsqsmvslleeakkeYDFIIIDTPP----LT----AAADSLI 679
Cdd:cd02042 48 ------------------YDYILIDTPPslglLTrnalAAADLVL 74
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-417 |
3.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 232 KVVALKEEAQFGVEGLKDSLQELNQAEAKLAAANERSQALQR-------ELDIEK------QKAVELSELSQSPAVQQAL 298
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdEIDVASaereiaELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 299 QEyqkvqdRLAVARTRLTNQHPTVIDLSNKERALRNQLEKRVGQVVNNnsndssitEDNLQ-VGEIKQTLTSELLKSEVE 377
Cdd:COG4913 691 EE------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL--------QDRLEaAEDLARLELRALLEERFA 756
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2182208308 378 RLAVAKQVGVLRKAFALQQARLTvlPKLEQQQRQVERKLQ 417
Cdd:COG4913 757 AALGDAVERELRENLEERIDALR--ARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
247-434 |
3.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 247 LKDSLQELNQAEAKLAAANERSQALQ---------RELDIEKQKAVELSELSQSPAVQQALQEYQKVQDRLAVARTRLTN 317
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELLEpirelaeryAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182208308 318 QhptVIDLSNKERALRNQLEKRVGQVVNNNSNDssitEDNLQvGEIKQtLTSELLKSEVERLAVAKQVGVL-------RK 390
Cdd:COG4913 310 E---LERLEARLDALREELDELEAQIRGNGGDR----LEQLE-REIER-LERELEERERRRARLEALLAALglplpasAE 380
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2182208308 391 AFALQQARL-TVLPKLEQQQRQVERKLQIAQLTYQNLLKKLQEVQ 434
Cdd:COG4913 381 EFAALRAEAaALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| |
