|
Name |
Accession |
Description |
Interval |
E-value |
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-826 |
2.04e-74 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 257.25 E-value: 2.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 18 SSKNVPKREKTLIEIFQIIARNKKILIGTVSLFLIVALIYSFTATPLYEASATLKKEGNPNDRRLGSGTDIStllslQST 97
Cdd:COG3206 6 SAPPEEEDEIDLRDLLRILRRRKWLILLVFLLVLALALLYALLLPPVYEASATLLVEPQSSDVLLSGLSSLS-----ASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 98 DEIETELELIKTFKVASEVVKDLNLfvtikeiywansnekyeigkpfveinepfyieqistkfrlpDKFRLTSDNPEklp 177
Cdd:COG3206 81 SPLETQIEILKSRPVLERVVDKLNL-----------------------------------------DEDPLGEEASR--- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 178 kgdfsivktsedsyelydilsgaklaEGEIEKYQKpafspldtltgfsiqvdtisscklasenfvidinwsdapiksslt 257
Cdd:COG3206 117 --------------------------EAAIERLRK--------------------------------------------- 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 258 ftinnfnktsikiagDIKVSRVGKTNIFKLGFSSSSPFAAALITNKIVEKYREARMDQKKQTIRYSFNIVDKQLLEVQDK 337
Cdd:COG3206 126 ---------------NLTVEPVKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKE 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 338 LREAEEVLSNFKASGQIMTIDASSQNLIGYLSRLEAEKVNIDLQLSDYKNKVADLEKELSNKGYFDQSYLGpdgrgdgNT 417
Cdd:COG3206 191 LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-------SP 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 418 PFSQMMKQLADLELQKIELLQKRTENHPDVKAIDEQIKVLKEKLSGFNENTITAYKIMISTLEKKLLKINDLMSKYEAKL 497
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 498 QSLPSQENKLAQILRQKATYEKIFTILLDQREAMRVAELSSPQDISIVDDAKIPTGPSWPKKSFIVLISLVIGSFLGILL 577
Cdd:COG3206 344 AELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVVPLKPVSPKKLLILALGLLLGLLLGLGL 423
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 578 IFTIELKRTKFVNLDELEEEFKIPILSLVPKLSKeilkavenNPDHKVALLTVQDDGLKETYRVLKTKLYQNLNPDTKFL 657
Cdd:COG3206 424 ALLLELLDRTIEEELELLLLLGLPLLGPLPPLKS--------KRERRRARLALLLLAAALAALLALLLALLLLLLLLLLL 495
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 658 MITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKETRGLLDYLLNDSPPKIYTRVSKNIDIIPAG 737
Cdd:COG3206 496 LLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLLLLLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLL 575
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 738 GLNSDSGTLLDSTKMRMLLRSLDTSQYDLILLDTPPVTRVVDPLVLSHSIHNAIVVIRPEHSLLETVRWGISELLNSKIN 817
Cdd:COG3206 576 LLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLAALLAAAVLAVLVVVLLLVVALVALARLALLAAAL 655
|
....*....
gi 2556389616 818 IRGLVINAA 826
Cdd:COG3206 656 LLLLVLVVV 664
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
29-827 |
1.28e-49 |
|
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: 188.01 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 29 LIEIFQIIARNKKILIGTVSLFLIVALIYSFTATPLYEASATLKKEGNPNDrrlgSGTDISTLLSLQSTD-EIETELELI 107
Cdd:TIGR01005 6 LDRLLAALFANARLIAAFAAAFIALGAAYAFFARPVYEADIMILLDDNLNK----AAEEEGDPSNLFDLDtDAAAAIEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 108 KTFKVASEVVKDLNLFVTIKEIYWANSnekyeigkPFVEINEpfYIEQISTKFRLPDKFRLT-------------SDNPE 174
Cdd:TIGR01005 82 KSGELAGKAVDKLHLSENAKILNPPRF--------PVDLIGA--WIKSAAGLFSEPGGFDLGeeaagneridkaaADIPE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 175 KLPKGDFSIVKTSEDSYELYDILSGAKLAEGEIEKYQKpafsplDTLTGfSIQVDTISSCKLASENFVIDINwSDAPIKS 254
Cdd:TIGR01005 152 ALAGEPFKLISLGAGAFRLEDKLLAAPIAGGVAEALEA------DQLIA-NFEAQENALTAKAEALFDLEQD-SQAAALE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 255 SLTFTINNFNKTsiKIAGDIKVSRVGKTNifklgfsssspfaAALITnkivekyreARMDQKKQTIRYSfnivdkqllEV 334
Cdd:TIGR01005 224 MAHDKAEIAEKA--AQGEIIGEAQLADLN-------------PALIA---------AIADQAAAEARAD---------NI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 335 QDKLREAEEvlsnfkasgqimtidaSSQNLIGYLSRLEAEKVNIDLQLSDYKNKVADLEKELSNKGYFDQSYLgpdgrgd 414
Cdd:TIGR01005 271 KRIADEAEE----------------NAVFLAGILPKEGDELEIADLKTNELRNGKGEFDLSDEFGADHPEAVC------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 415 gNTPFSQMMKQladlelQKIELLQKRTENHPDVKAIDEQIKvlkEKLSGfnentitaykimistlekkllKINDLMSKye 494
Cdd:TIGR01005 328 -SAPSLQELKA------KIAEELQQFTASHKGEQAIAQQIE---ESLRG---------------------KINGIAGK-- 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 495 akLQSLPSQENKLAQILRQKATYEKIFTILLDQREAMRVAELSSPQDISIVDDAKIPTGPSWPKKSFIVLISLVIGSFLG 574
Cdd:TIGR01005 375 --LKDAPEIEQDLRELEQDAAADKELYESLLGDMEQAKLQKAFKIAKARLIDEAAVPEEPSKPKKLMTLALAAVLGMMLG 452
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 575 ILLIFTIELKRTKFVNLDELEEEFKIPILSLVP------KLSKEILKA------------VENNPDHKVALLTVQD--DG 634
Cdd:TIGR01005 453 GAAAAFLEALEGGFRDEGDIEEHLGHRSLATVPlldtqmDKKAQLTHAhfgsvkrhdeavDDTMPFQLLARIVPDAprST 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 635 LKETYRVLKTKLYQNL-NPDTKFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKETrGLLD 713
Cdd:TIGR01005 533 FAEAFRNAKLACDFALaDAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKP-GLLD 611
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 714 YLLNDS--PPKIYTRVSKNIDIIPAGGLN---SDSGTLLDSTKMRMLLRSLdTSQYDLILLDTPPVTRVVDPLVLSHSIH 788
Cdd:TIGR01005 612 LLAGEAsiEAGIHRDQRPGLAFIAAGGAShfpHNPNELLANPAMAELIDNA-RNAFDLVLVDLAALAAVADAAAFAALAD 690
|
810 820 830
....*....|....*....|....*....|....*....
gi 2556389616 789 NAIVVIRPEHSLLETVRWGISELLNSKINIRGLVINAAD 827
Cdd:TIGR01005 691 GILFVTEFERSPLGEIRDLIHQEPHANSDVLGVIFNALD 729
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
39-825 |
1.80e-45 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 174.96 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 39 NKKILIGTVSLFLIVALIYSFTATPLYEASATLKKEGNPNDRRLgsgTDISTLLSlQSTDEIETELELIKTFKVASEVVK 118
Cdd:PRK11519 30 ARWWVIGITAVFALCAVVYTFFATPIYSADALVQIEQNSGNSLV---QDIGSALA-NKPPASDAEIQLIRSRLVLGKTVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 119 DLNLFVTIKEIYWansnekyeigkpfveinePFYIEQIStkfrlpdkfRLTSDNPEKLPKGDFSIVKTSEDSYELYDIL- 197
Cdd:PRK11519 106 DLDLDIAVSKNTF------------------PIFGAGWD---------RLMGRQNETVKVTTFNRPKEMADQVFTLNVLd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 198 --------SGAKLAEGEIEKyqkpafspLDTLTGFSIQVDTISScklasenfvidinwsdapiKSSLTFTINNFNK-TSI 268
Cdd:PRK11519 159 dknyqlssDGGFSARGQVGQ--------MLKKDGVTLMVEAIHA-------------------RPGTEFTVTKYSTlGMI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 269 -KIAGDIKVSRVGK-TNIFKLGFSSSSPFAAALITNKIVEKYREARMDQKKQTIRYSFNIVDKQLLEVQDKLREAEEVLS 346
Cdd:PRK11519 212 nNLQNNLTVTENGKdTGVLSLTYTGEDREQIRDILNSITRNYLEQNIERKSEEASKSLAFLAQQLPEVRSRLDVAENKLN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 347 NFKAsgQIMTIDASsqnligylsrLEAEKV-----NIDLQLSDYKNKVADLEKELsnkgyfdqsylgpdgrgdgntpfsq 421
Cdd:PRK11519 292 AFRQ--DKDSVDLP----------LEAKAVldsmvNIDAQLNELTFKEAEISKLY------------------------- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 422 mmkqladlelqkiellqkrTENHPDVKAIDEQIKvlkeklsgfnentitaykimisTLEKKLLKINDlmskyeaKLQSLP 501
Cdd:PRK11519 335 -------------------TKEHPAYRTLLEKRK----------------------ALEDEKAKLNG-------RVTAMP 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 502 SQENKLAQILRQKATYEKIFTILLDQREAMRVAELSSPQDISIVDDAKIPTGPSWPKKSFIVLISLVIGSFLGILLIfti 581
Cdd:PRK11519 367 KTQQEIVRLTRDVESGQQVYMQLLNKQQELKITEASTVGDVRIVDPAITQPGVLKPKKALIILGAIILGLMLSIVGV--- 443
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 582 eLKRTKF---VNLDELEEEFKIPILSLVP----KLSKEILKAVENNPDHKVA-LLTVQD--DGLKETYRVLKTKL-YQNL 650
Cdd:PRK11519 444 -LLRSLFnrgIESPQVLEEHGISVYASIPlsewQKARDSVKTIKGIKRYKQSqLLAVGNptDLAIEAIRSLRTSLhFAMM 522
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 651 NPDTKFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKeTRGLLDYLLN--DSPPKIYTRVS 728
Cdd:PRK11519 523 QAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNN-VNGLSDILIGqgDITTAAKPTSI 601
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 729 KNIDIIPAGGLNSDSGTLLDSTKMRMLLrSLDTSQYDLILLDTPPVTRVVDPLVLSHSIHNAIVVIRPEHSLLETVRWGI 808
Cdd:PRK11519 602 ANFDLIPRGQVPPNPSELLMSERFAELV-NWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSL 680
|
810
....*....|....*..
gi 2556389616 809 SELLNSKINIRGLVINA 825
Cdd:PRK11519 681 SRFEQNGIPVKGVILNS 697
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
637-824 |
3.78e-43 |
|
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: 155.04 E-value: 3.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 637 ETYRVLKTKL-YQNLNPDTKFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKEtRGLLDYL 715
Cdd:cd05387 1 EAFRTLRTNLlFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNE-PGLSEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 716 LNDSPPK--IYTRVSKNIDIIPAGGLNSDSGTLLDSTKMRMLLRSLDtSQYDLILLDTPPVTRVVDPLVLSHSIHNAIVV 793
Cdd:cd05387 80 SGQASLEdvIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELK-EQYDYVIIDTPPVLAVADALILAPLVDGVLLV 158
|
170 180 190
....*....|....*....|....*....|.
gi 2556389616 794 IRPEHSLLETVRWGISELLNSKINIRGLVIN 824
Cdd:cd05387 159 VRAGKTRRREVKEALERLEQAGAKVLGVVLN 189
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
580-831 |
6.22e-43 |
|
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: 158.04 E-value: 6.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 580 TIELKRTKFVNLDELEEEFKIPILSLVPKLSKEILKAVENNPDHKVALLTVQDDGLKETYRVLKTKLYQNLNPDTKFLMI 659
Cdd:COG0489 18 LLLLLLLLLLLLRLEEAAAAAALAAAAPAAAAPAPLPPAPALLLLLLLLLGLLLLLLLALALLLLLLLLLLRLLLEVIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 660 TSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKEtRGLLDYLLNDSPPK--IYTRVSKNIDIIPAG 737
Cdd:COG0489 98 TSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENR-PGLSDVLAGEASLEdvIQPTEVEGLDVLPAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 738 GLNSDSGTLLDSTKMRMLLRSLDtSQYDLILLDTPPVTRVVDPLVLSHSIHNAIVVIRPEHSLLETVRWGISELLNSKIN 817
Cdd:COG0489 177 PLPPNPSELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVP 255
|
250
....*....|....
gi 2556389616 818 IRGLVINAADIEKS 831
Cdd:COG0489 256 VLGVVLNMVCPKGE 269
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
23-831 |
8.74e-40 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 157.76 E-value: 8.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 23 PKREKTLIEIFQIIARNKKILIGTVSLFLIVALIYSFTATPLYEASATLKKEGNPNDRRLGSGTDISTllslQSTDEIET 102
Cdd:PRK09841 14 QENEIDLLRLVGELWDHRKFIISVTALFTLIAVAYSLLSTPIYQADTLVQVEQKQGNAILSGLSDMIP----NSSPESAP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 103 ELELIKTFKVASEVVKDLNLFVTIKEIYWAnsnekyEIGKPFVeinepfyieqistkfrlpdkfRLTSDNPEKLPKGDFS 182
Cdd:PRK09841 90 EIQLLQSRMILGKTIAELNLRDIVEQKYFP------IVGRGWA---------------------RLTKEKPGELAISWMH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 183 IVKTSEDSYELYdilsgakLAEGEIEKYqkpafspldTLTGFSIQVDTISSCKLASENFVIDINWSDAPikSSLTFTINN 262
Cdd:PRK09841 143 IPQLNGQDQQLT-------LTVGENGHY---------TLEGEEFTVNGMVGQRLEKDGVALTIADIKAK--PGTQFVLSQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 263 fnKTSIKIAGDIK-----VSRVGKTNIFKLGFSSSSPFAAALITNKIVEKYREARMDQKKQTIRYSFNIVDKQLLEVQDK 337
Cdd:PRK09841 205 --RTELEAINALQetftvSERSKESGMLELTMTGDDPQLITRILNSIANNYLQQNIARQAAQDSQSLEFLQRQLPEVRSE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 338 LREAEEVLSNFKAsgQIMTIDASsqnligylsrLEAEKV-----NIDLQLSDYKNKVADLekelsnkgyfdqsylgpdgr 412
Cdd:PRK09841 283 LDQAEEKLNVYRQ--QRDSVDLN----------LEAKAVleqivNVDNQLNELTFREAEI-------------------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 413 gdgntpfSQMMKQladlelqkiellqkrteNHPDVKAIDEQIKvlkeklsgfnentitaykimisTLEKKLLKINDlmsk 492
Cdd:PRK09841 331 -------SQLYKK-----------------DHPTYRALLEKRQ----------------------TLEQERKRLNK---- 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 493 yeaKLQSLPSQENKLAQILRQKATYEKIFTILLDQREAMRVAELSSPQDISIVDDAKIPTGPSWPKKSFIVLISLVIGSF 572
Cdd:PRK09841 361 ---RVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELSISKSSAIGNVRIIDPAVTQPQPVKPKKALNVVLGFILGLF 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 573 LGILLIFT-IELKRTkfVNLDELEEEFKIPILSLVPK----------LSKEILKAVENNPDHKVALLTVQD--DGLKETY 639
Cdd:PRK09841 438 ISVGAVLArAMLRRG--VEAPEQLEEHGISVYATIPMsewldkrtrlRKKNLFSNQQRHRTKNIPFLAVDNpaDSAVEAV 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 640 RVLKTKLYQNL-NPDTKFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKEtRGLLDYLL-N 717
Cdd:PRK09841 516 RALRTSLHFAMmETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNE-HGLSEYLAgK 594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 718 DSPPKIYTRVSK-NIDIIPAGGLNSDSGTLLDSTKMRMLLRSLDtSQYDLILLDTPPVTRVVDPLVLSHSIHNAIVVIRP 796
Cdd:PRK09841 595 DELNKVIQHFGKgGFDVITRGQVPPNPSELLMRDRMRQLLEWAN-DHYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARF 673
|
810 820 830
....*....|....*....|....*....|....*
gi 2556389616 797 EHSLLETVRWGISELLNSKINIRGLVINaaDIEKS 831
Cdd:PRK09841 674 GLNTAKEVSLSMQRLEQAGVNIKGAILN--GVIKR 706
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
269-616 |
2.43e-30 |
|
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: 125.93 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 269 KIAGDIKVSRVGKTNIFKLGFSSSSPFAAALITNKIVEKYREARMDQKKQTIRYSFNIVDKQLLEVQDKLREAEEVLSNF 348
Cdd:TIGR03007 108 KLRKNISISLAGRDNLFTISYEDKDPELAKDVVQTLLTIFVEETLGSKRQDSDSAQRFIDEQIKTYEKKLEAAENRLKAF 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 349 KAS-GQIMTIDasSQNLIGYLSRLEAEKVNIDLQLSDYKNKVADLEKELSnkgyfDQSYLGPDGRGDGNTPFSQmmkQLA 427
Cdd:TIGR03007 188 KQEnGGILPDQ--EGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLG-----GEEPVLLAGSSVANSELDG---RIE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 428 DLELQKIELLQKRTENHPDVKAIDEQIKVLKEKLSGFNENTITA----------YKIM----------ISTLEKKLLKIN 487
Cdd:TIGR03007 258 ALEKQLDALRLRYTDKHPDVIATKREIAQLEEQKEEEGSAKNGGpergeianpvYQQLqielaeaeaeIASLEARVAELT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 488 DLMSKYEAKLQSLPSQENKLAQILRQKATYEKIFTILLDQREAMRVAELSSPQD----ISIVDDAKIPTGPSWPKKSFIV 563
Cdd:TIGR03007 338 ARIERLESLLRTIPEVEAELTQLNRDYEVNKSNYEQLLTRRESAEVSKQMEVQDkavsFRIIDPPIVPSKPSGPNRPLLM 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2556389616 564 LISLVIGSFLGILLIFTIELKRTKFVNLDELEEEFKIPILSLVPKLSKEILKA 616
Cdd:TIGR03007 418 LAGLLGGLGAGIGLAFLLSQLRPTVRSVRDLRELTGLPVLGVIPMIATPEERR 470
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
637-831 |
7.32e-26 |
|
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: 105.98 E-value: 7.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 637 ETYRVLKTKLyQNLNPDTKFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKETRGLLDYLL 716
Cdd:TIGR01007 1 EYYNAIRTNI-QFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 717 ND---SPPKIYTRVSkNIDIIPAGGLNSDSGTLLDSTKMRMLLRSLdTSQYDLILLDTPPVTRVVDPLVLSHSIHNAIVV 793
Cdd:TIGR01007 80 GTtdlSDAICDTNIE-NLDVITAGPVPPNPTELLQSSNFKTLIETL-RKRFDYIIIDTPPIGTVTDAAIIARACDASILV 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2556389616 794 IRPEHSLLETVRWGISELLNSKINIRGLVINAADIEKS 831
Cdd:TIGR01007 158 TDAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVS 195
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
666-827 |
1.78e-23 |
|
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: 100.70 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 666 SGKTTVVANLAASLSIEGKRVLLIDCDLRkADLSTLFGLSKET--RGLLDYLLNDSPPK--IYTRVSKNIDIIPAG---- 737
Cdd:COG1192 13 VGKTTTAVNLAAALARRGKRVLLIDLDPQ-GNLTSGLGLDPDDldPTLYDLLLDDAPLEdaIVPTEIPGLDLIPANidla 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 738 GLNSDSGTLLDS-TKMRMLLRSLDtSQYDLILLDTPP----VTRVVdpLVLSHSIhnaIVVIRPEH-------SLLETVR 805
Cdd:COG1192 92 GAEIELVSRPGReLRLKRALAPLA-DDYDYILIDCPPslglLTLNA--LAAADSV---LIPVQPEYlsleglaQLLETIE 165
|
170 180
....*....|....*....|..
gi 2556389616 806 wGISELLNSKINIRGLVINAAD 827
Cdd:COG1192 166 -EVREDLNPKLEILGILLTMVD 186
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
670-827 |
6.76e-20 |
|
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: 89.56 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 670 TVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSkETRGLLDYLLNDSPPK--IYtRVSKNIDIIPAGglnSDSGTLL 747
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLE-PKATLADVLAGEADLEdaIV-QGPGGLDVLPGG---SGPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 748 DSTKMRMLLRSLDT--SQYDLILLDTPP-VTR-VVDPLVLSHSIhnaIVVIRPEHSLLETVRWGIsELLNSKINIR--GL 821
Cdd:COG0455 76 ELDPEERLIRVLEEleRFYDVVLVDTGAgISDsVLLFLAAADEV---VVVTTPEPTSITDAYALL-KLLRRRLGVRraGV 151
|
....*.
gi 2556389616 822 VINAAD 827
Cdd:COG0455 152 VVNRVR 157
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
667-797 |
2.16e-17 |
|
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: 82.23 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 667 GKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKEtRGLLDYLLNDSPPK-IYTRVSKNIDIIPAGglnSDSGT 745
Cdd:cd02038 13 GKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPK-KTLGDVLKGRVSLEdIIVEGPEGLDIIPGG---SGMEE 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2556389616 746 L--LDSTKMRMLLRSLDT--SQYDLILLDTPP-VTRVVDPLVLshSIHNAIVVIRPE 797
Cdd:cd02038 89 LanLDPEQKAKLIEELSSleSNYDYLLIDTGAgISRNVLDFLL--AADEVIVVTTPE 143
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
532-705 |
4.34e-14 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 73.95 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 532 RVAELSSPQDISIVDDAKIPTGPSWPKKSFIVLISLVIGSFLGILLIFTIELKRTKFVNLDELEEEFKIPILSLVPKLSK 611
Cdd:COG3944 140 EVKELMKVDNVTVLDPATVPASPVSPNPKLNLAIGLVLGLLLGVGLAFLRELLDTTIRSEEDIERLLGLLLGGAVPAARS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 612 EILKAVENNPDHKVAlltvqddglKETYRVLKTKLYQNLNPDTKFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDC 691
Cdd:COG3944 220 ARPLLLLLADASPRA---------AAARRRRRNLLFALAAVDARTVVVVSSSLSEGKSTTTAALALALAAAAAGVVLVLA 290
|
170
....*....|....
gi 2556389616 692 DLRKADLSTLFGLS 705
Cdd:COG3944 291 DLDRRRRVALLGLL 304
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
657-824 |
9.04e-14 |
|
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: 71.61 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 657 LMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLrKADLSTLFGLSKETRGLL---------DYLLNDSPPKIYTRV 727
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDP-QSNNSSVEGLEGDIAPALqalaeglkgRVNLDPILLKEKSDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 728 SkNIDIIPAG-GLNSDSGTLLDSTKMRMLLRSLDT--SQYDLILLDTPP--VTRVVDPLVLSHSIhnaIVVIRPEHSLLE 802
Cdd:pfam01656 80 G-GLDLIPGNiDLEKFEKELLGPRKEERLREALEAlkEDYDYVIIDGAPglGELLRNALIAADYV---IIPLEPEVILVE 155
|
170 180 190
....*....|....*....|....*....|
gi 2556389616 803 TVRwGISELLNS--------KINIRGLVIN 824
Cdd:pfam01656 156 DAK-RLGGVIAAlvggyallGLKIIGVVLN 184
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
666-831 |
2.37e-13 |
|
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: 72.45 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 666 SGKTTVVANLAASLSIE-GKRVLLIDCDLRKADLSTLFGLsKETRGL---------LDYLLNDSppkIYTRVSKNIDIIP 735
Cdd:COG4963 114 VGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDL-EPRRGLadalrnpdrLDETLLDR---ALTRHSSGLSVLA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 736 AGGlNSDSGTLLDSTKMRMLLRSLdTSQYDLILLDTPPVTRVVDPLVLSHSiHNAIVVIRPE-HSLLETVRW--GISELL 812
Cdd:COG4963 190 APA-DLERAEEVSPEAVERLLDLL-RRHFDYVVVDLPRGLNPWTLAALEAA-DEVVLVTEPDlPSLRNAKRLldLLRELG 266
|
170 180
....*....|....*....|....*...
gi 2556389616 813 NSKINIRgLVIN---------AADIEKS 831
Cdd:COG4963 267 LPDDKVR-LVLNrvpkrgeisAKDIEEA 293
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
666-813 |
2.63e-13 |
|
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: 68.76 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 666 SGKTTVVANLAASLSIEGKRVLLIDCDlRKADLSTLFGLSK--ETRGLLDYLLNDSPPK--IYTRVSKNIDIIPAGGLNS 741
Cdd:pfam13614 13 VGKTTTSVNLAAALAKKGKKVLLIDLD-PQGNATSGLGIDKnnVEKTIYELLIGECNIEeaIIKTVIENLDLIPSNIDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 742 DSGTLLDSTKMR--MLLRSLDT--SQYDLILLDTPP----VTRVVdpLVLSHSIhnaIVVIRPEHSLLEtvrwGISELLN 813
Cdd:pfam13614 92 GAEIELIGIENRenILKEALEPvkDNYDYIIIDCPPslglLTINA--LTASDSV---LIPVQCEYYALE----GLSQLLN 162
|
|
| Wzz |
pfam02706 |
Chain length determinant protein; This family includes proteins involved in lipopolysaccharide ... |
29-119 |
4.93e-11 |
|
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: 59.61 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 29 LIEIFQIIARNKKILIGTVSLFLIVALIYSFTATPLYEASATLKKEGNPNDRRLGSGTDISTLLSLQStdeieTELELIK 108
Cdd:pfam02706 5 LIELLGVLWKRKKLIILVTLLFTLLAAAYAFLATPKYTATAQILVPQKKGEAGSLLGSDLQAGLQLAS-----TEIEILK 79
|
90
....*....|.
gi 2556389616 109 TFKVASEVVKD 119
Cdd:pfam02706 80 SRDVLEKVIDE 90
|
|
| YveK |
COG3944 |
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis]; |
26-129 |
1.15e-10 |
|
Capsular polysaccharide biosynthesis protein YveK [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443144 [Multi-domain] Cd Length: 309 Bit Score: 63.55 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 26 EKTLIEIFQIIARNKKILIGTVSLFLIVALIYSFTATPLYEASATL----KKEGNPNDrrlgSGTDISTLLSLqstdeIE 101
Cdd:COG3944 1 EMDLREYLRILRRRWWLILLLTLLGALAALASSFLITPVYQASTTLlvstSSGSDASD----LYQGIQTAQQL-----VN 71
|
90 100
....*....|....*....|....*...
gi 2556389616 102 TELELIKTFKVASEVVKDLNLFVTIKEI 129
Cdd:COG3944 72 TYAELLKSPAVLEEVIDELGLDLSPEEL 99
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
667-824 |
2.92e-10 |
|
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: 60.98 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 667 GKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSketrgllDYLLNDSPPKIYTRVSKNIDIIPAGGL-NSDSGT 745
Cdd:cd02037 13 GKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVE-------GKPLHQSEEGIVPVEVGGIKVMSIGFLlPEDDAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 746 LLDSTK----MRMLLRSLDTSQYDLILLDTPPVTRVVdPLVLSHSIHN--AIVVIRPEHSLLETVRWGISELLNSKINIR 819
Cdd:cd02037 86 IWRGPMksgaIKQFLKDVDWGELDYLIIDLPPGTGDE-HLSLVQLIPIdgAVVVTTPQEVSLIDVRKAIDMCKKLNIPVL 164
|
....*
gi 2556389616 820 GLVIN 824
Cdd:cd02037 165 GIVEN 169
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
659-772 |
3.06e-10 |
|
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: 61.45 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 659 ITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLskETRG---LLDYLLNDSPPK---IYTRVSKNID 732
Cdd:cd02036 5 ITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGL--ENRIvytLVDVLEGECRLEqalIKDKRWENLY 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2556389616 733 IIPAGglNSDSGTLLDSTKMRMLLRSLDTSqYDLILLDTP 772
Cdd:cd02036 83 LLPAS--QTRDKDALTPEKLEELVKELKDS-FDFILIDSP 119
|
|
| GNVR |
pfam13807 |
G-rich domain on putative tyrosine kinase; This domain is found between two families, Wzz, ... |
509-579 |
1.17e-09 |
|
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: 55.68 E-value: 1.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2556389616 509 QILRQKATYE---KIFTILLDQREAMRVAELSSPQDISIVDDAKIPTGPSWPKKSFIVLISLVIGSFLGILLIF 579
Cdd:pfam13807 5 EILRLTRDVEvntEIYTQLLNSNQELEVVKAGTVGNVRIVDTAVVPPKPVKPKKALIVVLALLLGLMLGVGLVL 78
|
|
| cellulose_yhjQ |
TIGR03371 |
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ... |
655-773 |
1.17e-08 |
|
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274549 [Multi-domain] Cd Length: 246 Bit Score: 56.59 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 655 KFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKAdLSTLFGLS-KETRGLLDYLLNDSPPKIYT-RVSKNID 732
Cdd:TIGR03371 2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNL-LRLHFGMDwSVRDGWARALLNGADWAAAAyRSPDGVL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2556389616 733 IIPAGGLNSDS---GTLLDSTKMRMLLRSLDTSQYDLILLDTPP 773
Cdd:TIGR03371 81 FLPYGDLSADEreaYQAHDAGWLARLLQQLDLAARDWVLIDLPR 124
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
666-721 |
1.41e-07 |
|
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: 51.00 E-value: 1.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2556389616 666 SGKTTVVANLAASLSIEGKRVLLIDCDlRKADLstlfglskeTRGLLDYLLNDSPP 721
Cdd:cd02042 12 VGKTTLAVNLAAALALRGKRVLLIDLD-PQGSL---------TSWLYDYILIDTPP 57
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
649-797 |
2.17e-07 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 53.24 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 649 NLNPDTKFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLskETRGL------------LDYLL 716
Cdd:CHL00175 10 KSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGL--ENRVLytamdvlegecrLDQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 717 ndsppkIYTRVSKNIDIIPAgglnSDSGTLLDSTK--MRMLLRSLDTSQYDLILLDTPPVTRvVDPLVLSHSIHNAIVVI 794
Cdd:CHL00175 88 ------IRDKRWKNLSLLAI----SKNRQRYNVTRknMNMLVDSLKNRGYDYILIDCPAGID-VGFINAIAPAQEAIVVT 156
|
...
gi 2556389616 795 RPE 797
Cdd:CHL00175 157 TPE 159
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
657-824 |
2.72e-07 |
|
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: 49.74 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 657 LMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDlrkadlstlfglsketrgllDYLLNDSPPKIytrvsknidiipa 736
Cdd:cd01983 3 IAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD--------------------DYVLIDGGGGL------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 737 gglnsDSGTLLDSTKMRMLLRSLDtsqydlilldtppvtrvvdplvlshsihNAIVVIRPEH-SLLETVRWGISELLNSK 815
Cdd:cd01983 50 -----ETGLLLGTIVALLALKKAD----------------------------EVIVVVDPELgSLLEAVKLLLALLLLGI 96
|
170
....*....|
gi 2556389616 816 INIR-GLVIN 824
Cdd:cd01983 97 GIRPdGIVLN 106
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
659-824 |
2.79e-07 |
|
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: 52.81 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 659 ITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKETRGLLDYLLNDSPPK--IYtRVSKNIDIIPA 736
Cdd:TIGR01969 5 IASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAGEADIKdaIY-EGPFGVKVIPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 737 gGLNSDSGTLLDSTKMRMLLRSLdTSQYDLILLDTPPVTRvVDPLVLSHSIHNAIVVIRPE-HSLLETVRWGIS-ELLNs 814
Cdd:TIGR01969 84 -GVSLEGLRKADPDKLEDVLKEI-IDDTDFLLIDAPAGLE-RDAVTALAAADELLLVVNPEiSSITDALKTKIVaEKLG- 159
|
170
....*....|
gi 2556389616 815 kINIRGLVIN 824
Cdd:TIGR01969 160 -TAILGVVLN 168
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
666-738 |
7.08e-07 |
|
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction
Pssm-ID: 349761 Cd Length: 266 Bit Score: 51.60 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 666 SGKTTVVANLAASLSIEGKRVLLIDCDlRKADLS-TLFGlSKETRGLLDYLLNDSPPK------IYTRVSKNIDIIPAGG 738
Cdd:cd02117 11 IGKSTTASNLSAALAEGGKKVLHVGCD-PKHDSTlLLTG-GKVPPTIDEMLTEDGTAEelrredLLFSGFNGVDCVEAGG 88
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
297-581 |
2.18e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 51.00 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 297 AALITNKIVeKYREARMDQ-----KKQTIRYSfnivDKQLLEVQDKLREAEEVLSNFKASGQIMTIDASSQNLIGYLSRL 371
Cdd:COG3524 152 AQAIAEALL-AESEELVNQlseraREDAVRFA----EEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQLIATL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 372 EAEKvnidlqlsdyknkvADLEKELSNKgyfdQSYLGPdgrgdgNTPfsqmmkqladlelqKIELLQKRtenhpdVKAID 451
Cdd:COG3524 227 EGQL--------------AELEAELAAL----RSYLSP------NSP--------------QVRQLRRR------IAALE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 452 EQIKVLKEKLSGFNENTitaykimistlekkllKINDLMSKYEAkLQSlpsqENKLAQILRQKA--TYEKIftilldQRE 529
Cdd:COG3524 263 KQIAAERARLTGASGGD----------------SLASLLAEYER-LEL----EREFAEKAYTSAlaALEQA------RIE 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2556389616 530 AMR----VAELSSPQdisivddakIPTGPSWPKKSFIVLISLVIgsFLGILLIFTI 581
Cdd:COG3524 316 AARqqryLAVIVQPT---------LPDEALYPRRLYNILLVFLI--LLLLYGIGSL 360
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
667-824 |
4.68e-06 |
|
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: 49.04 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 667 GKTTVVANLAASLSIEGKRVLLIdcdlrkadlST--------LFGLSketrglldyLLNDSPPKIYTRVS-KNIDIIPA- 736
Cdd:cd02035 12 GKTTIAAATAVRLAEQGKRVLLV---------STdpahslsdAFGQK---------LGGETPVKGAPNLWaMEIDPEEAl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 737 -------GGLNSDSGTLLDSTKMRM-----------------LLRSLDTSQYDLILLDTP-----------PVTRVV--- 778
Cdd:cd02035 74 eeyweevKELLAQYLRLPGLDEVYAeellslpgmdeaaafdeLREYVESGEYDVIVFDTAptghtlrllslPLEQVRell 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2556389616 779 -DPLVLShsihnAIVVIRPEH-SLLETVRWgISELLNSKINIRGLVIN 824
Cdd:cd02035 154 rDPERTT-----FVLVTIPEKlSIYETERL-WGELQQYGIPVDGVVVN 195
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
667-824 |
9.82e-06 |
|
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: 47.83 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 667 GKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFGLSKETRGLLDYLLndSPPKIYtrvskNIDIIPAGGL--NSDS- 743
Cdd:pfam10609 16 GKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGI--IPVEAH-----GIKVMSIGFLlpDEDDa 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 744 ----GTLLDSTkMRMLLRSLDTSQYDLILLDTPPVTRVVdPLVLSHSI--HNAIVVIRPEHSLLETVRWGISELLNSKIN 817
Cdd:pfam10609 89 viwrGPMKSGA-IKQFLTDVDWGELDYLIIDLPPGTGDE-QLTLAQLLplTGAVIVTTPQDVALLDVRKAIDMFKKVNVP 166
|
....*..
gi 2556389616 818 IRGLVIN 824
Cdd:pfam10609 167 VLGVVEN 173
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
666-797 |
1.26e-04 |
|
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: 44.58 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 666 SGKTTVVANLAASLSIEGK-RVLLIDCDLRKADLSTLFGLsKETRGLLDYLLN------DSPPKIYTRVSKNIDIIPA-- 736
Cdd:cd03111 12 VGASTLAVNLAQELAQRAKdKVLLIDLDLPFGDLGLYLNL-RPDYDLADVIQNldrldrTLLDSAVTRHSSGLSLLPApq 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2556389616 737 --GGLNSDSGtlLDSTKMRMLLRsldtSQYDLILLDTPPVTRVVDPLVLSHSiHNAIVVIRPE 797
Cdd:cd03111 91 elEDLEALGA--EQVDKLLQVLR----AFYDHIIVDLGHFLDEVTLAVLEAA-DEILLVTQQD 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
326-637 |
1.44e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 326 IVDKQLLEVQDKLREAEEVLSNFKAsgqimtidassqnLIGYLSRLEAEKVNIDLQLSDYKNKVADLEKELSNKGYF--- 402
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAE-------------LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqel 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 403 ---DQSYLGPDGRGDGntpFSQMMKQLADLELQKIELLQKRTENHpdvkaidEQIKVLKEKLSGFNENTITAYKIMISTL 479
Cdd:COG4717 135 ealEAELAELPERLEE---LEERLEELRELEEELEELEAELAELQ-------EELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 480 EKKLLKINDLMSKYEAKLQSLPSQENKLAQILRQKATYEKIFTILLDQREAMRVAELSspqdisivddakiptGPSWPKK 559
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALL---------------GLGGSLL 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2556389616 560 SFIVLISLVIGSFLGILLIFTIELKRTKFVNLDELEEEFKIPILS-LVPKLSKEILKAVENNPDHKVALLTVQDDGLKE 637
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEeLEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
|
| NifH |
cd02040 |
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
667-715 |
1.91e-04 |
|
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.
Pssm-ID: 349759 Cd Length: 265 Bit Score: 44.04 E-value: 1.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2556389616 667 GKTTVVANLAASLSIEGKRVLLIDCDlRKADlST---LFGLSKETrgLLDYL 715
Cdd:cd02040 12 GKSTTASNLSAALAEMGKKVLHVGCD-PKAD-STrllLGGKAIPT--VLDTL 59
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
666-771 |
1.96e-04 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 44.00 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 666 SGKTTVVANLAASLSIEGKRVLLIDCDlrkAD--LSTLFGLsKETRGLLDYL------------------------LNDS 719
Cdd:COG3640 11 VGKTTLSALLARYLAEKGKPVLAVDAD---PNanLAEALGL-EVEADLIKPLgemrelikertgapgggmfklnpkVDDI 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2556389616 720 PPKiYTRVSKNIDIIPAGGL-NSDSG------TLLdstkmRMLLRSLDTSQYDLILLDT 771
Cdd:COG3640 87 PEE-YLVEGDGVDLLVMGTIeEGGSGcycpenALL-----RALLNHLVLGNYEYVVVDM 139
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-515 |
2.11e-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: 45.05 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 303 KIVEKYREARMDQKKQTIRYS---FNIVDKQLLEVQDKLREAEEVLsnFKASGQIMTIDASSQNLIGYLSRLEAEKVNID 379
Cdd:TIGR02168 210 EKAERYKELKAELRELELALLvlrLEELREELEELQEELKEAEEEL--EELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 380 LQLSDYKNKVADLEKElsnKGYFDQSylgpdgrgdgntpFSQMMKQLADLELQKIELLQKRTENHPDVKAIDEQIKVLKE 459
Cdd:TIGR02168 288 KELYALANEISRLEQQ---KQILRER-------------LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2556389616 460 KLSGFNENtitaykimistLEKKLLKINDLMSKYEAKLQSLPSQENKLAQILRQKA 515
Cdd:TIGR02168 352 ELESLEAE-----------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
655-708 |
6.52e-04 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 43.13 E-value: 6.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2556389616 655 KFLMITSCEEDSGKTTVVANLAASLSIEGKRVLLIDCDlRKADLSTLFGLSKET 708
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLD-PQASLSALLGVLPET 174
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
666-830 |
1.05e-03 |
|
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.
Pssm-ID: 349754 [Multi-domain] Cd Length: 249 Bit Score: 41.91 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 666 SGKTTVVANLAASLSIEGKRVLLIDCDlRKADLSTLFGLSKE------TRGLLDYLLNDSPPKIYTRVSKN--IDIIPAG 737
Cdd:cd02034 11 VGKTTIAALLIRYLAKKGGKVLAVDAD-PNSNLAETLGVEVEklplikTIGDIRERTGAKKGEPPEGMSLNpyVDDIIKE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 738 GLNSDSG-TLL---------------DSTKMRMLLRSLDTSQYDLILLDTPP--------VTRVVDPLvlshsihnaIVV 793
Cdd:cd02034 90 IIVEPDGiDLLvmgrpegggsgcycpVNALLRELLRHLALKNYEYVVIDMEAgiehlsrgTIRAVDLL---------IIV 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2556389616 794 IRPEHSLLETVRwGISELLNS-KINIRGLVINAADIEK 830
Cdd:cd02034 161 IEPSKRSIQTAK-RIKELAEElGIKKIYLIVNKVRNEE 197
|
|
| PRK13230 |
PRK13230 |
nitrogenase reductase-like protein; Reviewed |
667-703 |
1.25e-03 |
|
nitrogenase reductase-like protein; Reviewed
Pssm-ID: 183903 Cd Length: 279 Bit Score: 41.68 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2556389616 667 GKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFG 703
Cdd:PRK13230 13 GKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVG 49
|
|
| Bchl-like |
cd02032 |
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ... |
667-770 |
1.62e-03 |
|
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.
Pssm-ID: 349752 Cd Length: 267 Bit Score: 41.13 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 667 GKTTVVANLAASLSIEGKRVLLIDCDlRKADlSTlFGLSK-------ETRGLLDYLLNDSPPK--IYTRVSkNIDIIPAG 737
Cdd:cd02032 12 GKSTTSSNLSAAFAKRGKKVLQIGCD-PKHD-ST-FTLTGfliptviDVLQSVDFHYEEVWPEdvIFTGYG-GVDCVEAG 87
|
90 100 110
....*....|....*....|....*....|....*...
gi 2556389616 738 GLNSDSG----TLLDSTKmrmLLRSLDT-SQYDLILLD 770
Cdd:cd02032 88 GPPAGTGcggyVVGETVK---LLKELNAfDEYDVILFD 122
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
657-703 |
5.37e-03 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 39.68 E-value: 5.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2556389616 657 LMITSCEEDSGKTTVVANLAASLsiegKRVLLIDCDLRKADLSTLFG 703
Cdd:cd03110 2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLG 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
329-563 |
6.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 329 KQLLEVQDKLREAEEVLSNFKAS-----GQIMTIDASSQNLIGYLSRLEAEKVNIDLQLSDYKNKVADLEKEL-SNKGYF 402
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEekallKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELeAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 403 -----------DQSY----LGPDGRGDGNTpFSQMMKQLADLELQKIELLQKRTEnhpDVKAIDEQIKVLKEKLsgfnen 467
Cdd:COG4942 107 aellralyrlgRQPPlallLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAEL------ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556389616 468 titayKIMISTLEKKLLKINDLMSKYEAKLQSLPSQENKLAQILRQKATYEKIFTILLD--QREAMRVAELSSPQDISiV 545
Cdd:COG4942 177 -----EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIArlEAEAAAAAERTPAAGFA-A 250
|
250
....*....|....*...
gi 2556389616 546 DDAKIPtgpsWPKKSFIV 563
Cdd:COG4942 251 LKGKLP----WPVSGRVV 264
|
|
| Fer4_NifH |
pfam00142 |
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family; |
666-703 |
8.50e-03 |
|
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
Pssm-ID: 395090 Cd Length: 271 Bit Score: 38.96 E-value: 8.50e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2556389616 666 SGKTTVVANLAASLSIEGKRVLLIDCDLRKADLSTLFG 703
Cdd:pfam00142 11 IGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLG 48
|
|
| |
