|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
6-762 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 972.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 6 PGVSGYQGPAGGWGAVKAVTASVFSQKAVARDIIAMFKMNQVKGFDCPGCAWPDPGHRAPMELCENGVKAVSWETTSKKA 85
Cdd:PRK09939 3 KKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 86 SPEFFSRHPVSTLWHYSDYELENIGRLTHPMKYDAVSDTWQAVDWDIAFREIGERLRSYDSAQQVEFYTSGRTSNEAAFL 165
Cdd:PRK09939 83 NASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 166 YQLFAREYGSSNFPDCSNMCHGPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIIS 245
Cdd:PRK09939 163 YQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 246 INPLNERGLERFSFPQSAKEMFTGQATELSNDYYQVKMGGDASLLKGIMKALIEMDEARILLDQQPTLDHAFIDQHTAGY 325
Cdd:PRK09939 243 INPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 326 AALYDDLRQHNWAELEQDSGLTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPL 405
Cdd:PRK09939 323 DELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 406 RGHSNVQGDRSVGINEAASEDFLQRLEKHFSIRVPRKHGRSSVESIRAIERGDAKALICMGGNLAVAMPQPQRTFAAMKN 485
Cdd:PRK09939 403 RGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 486 LDLQVHVATKLNRSHLLLAKHNYLLPALGRTERDMQATGIQSVTVEDSMSMVHASCGALKPASRWLKSEPAIVAGMARAT 565
Cdd:PRK09939 483 LDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 566 LPHSPINWEAFTGDYTLIRDAIEAVIPAFHDYNARIAEPGGFRMDTPASRREWRTENGKANFIVSHQRAVEREHQPADAL 645
Cdd:PRK09939 563 LPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 646 VLATLRSHDQYNTTIYGMNDRYRGITGRRDVVFLSAEEATSRGLSQGDVVNVQALDDNGQPCADRiMYGLTVVIYNMAAG 725
Cdd:PRK09939 643 VMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRR-MDRLKVVIYPMADR 721
|
730 740 750
....*....|....*....|....*....|....*..
gi 1100260294 726 SIGAYLPEANVLLSLDAVDTQSLTPAYKSVPVTLTKA 762
Cdd:PRK09939 722 SLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPS 758
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
14-760 |
0e+00 |
|
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.
Pssm-ID: 273765 [Multi-domain] Cd Length: 743 Bit Score: 934.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 14 PAGGWGAVKAVTASVFSQKAVARDIIAMFKMNQVKGFDCPGCAWPD-PGHRAPMELCENGVKAVSWETTSKKASPEFFSR 92
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVsPQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 93 HPVSTLWHYSDYELENIGRLTHPMKYDAVSDTWQAVDWDIAFREIGERLRSYDSAQqVEFYTSGRTSNEAAFLYQLFARE 172
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLDPKQ-VAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 173 YGSSNFPDCSNMCHGPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPLNER 252
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 253 GLERFSFPQSAKEMFTGQATELSNDYYQVKMGGDASLLKGIMKALIEMDEARilldQQPTLDHAFIDQHTAGYAALYDDL 332
Cdd:TIGR01701 240 GLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQ----PGSLIDHEFIANHTNGFDELRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 333 RQHNWAELEQDSGLTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRGHSNVQ 412
Cdd:TIGR01701 316 LQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 413 GDRSVGINEAASEDFLQRLEKHFSIRVPRKHGRSSVESIRAIERGDAKALICMGGNLAVAMPQPQRTFAAMKNLDLQVHV 492
Cdd:TIGR01701 396 GDRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 493 ATKLNRSHLLLAKHNYLLPALGRTERDMQATGIQSVTVEDSMSMVHASCGALKPASRWLKSEPAIVAGMARATLPHSPIN 572
Cdd:TIGR01701 476 ATKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 573 WEAFTGDYTLIRDAIEAVIPAFHDYNARIAEPGGFRMDTPA-SRREWRTENGKANFIVSHQRAVEREHQPADALVLATLR 651
Cdd:TIGR01701 556 WEILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 652 SHDQYNTTIYGMNDRYRGITGRRDVVFLSAEEATSRGLSQGDVVNVQALDDNGQpcaDRIMYGLTVVIYNMAAGSIGAYL 731
Cdd:TIGR01701 636 SHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQ---KRKFDNLRIVFYDTPTGNAAAYY 712
|
730 740
....*....|....*....|....*....
gi 1100260294 732 PEANVLLSLDAVDTQSLTPAYKSVPVTLT 760
Cdd:TIGR01701 713 PEANPLLPLDHHDPQSKTPEYKTIPVRLE 741
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-627 |
0e+00 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 850.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 49 GFDCPGCAWPDPGHR-APMELCENGVKAVSWETTSKKASPEFFSRHPVSTLWHYSDYELENIGRLTHPMKYDAVSDTWQA 127
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 128 VDWDIAFREIGERLRSYDSaQQVEFYTSGRTSNEAAFLYQLFAREYGSSNFPDCSNMCHGPTSAGLTPAIGLGKGTVELD 207
Cdd:cd02767 81 ISWDEAFAEIAARLRALDP-DRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 208 DFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPLNERGLERFSFPQSAKEMFTGqATELSNDYYQVKMGGDA 287
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLTG-GTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 288 SLLKGIMKALIEMDEARILLdqqptLDHAFIDQHTAGYAALYDDLRQHNWAELEQDSGLTRSQMEDLAHSYSKSSATIVC 367
Cdd:cd02767 239 ALLNGMAKHLIERDDEPGNV-----LDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 368 YGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRGHSNVQGDRSVGINEAASEDFLQRLEKHFSIRVPRKHGRSS 447
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 448 VESIRAIERGDAKALICMGGNLAVAMPQPQRTFAAMKNLDLQVHVATKLNRSHLLLAKHNYLLPALGRTERDMQATGIQS 527
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 528 VTVEDSMSMVHASCGALKPASRWLKSEPAIVAGMARATLPHSPINWEAFTGDYTLIRDAIEAVIP-AFHDYNARIAEPGG 606
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGG 553
|
570 580
....*....|....*....|.
gi 1100260294 607 FRMDTPASRREWRTENGKANF 627
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQF 574
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
52-762 |
1.49e-143 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 436.97 E-value: 1.49e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 52 CPGCAwpdpghrapmELCENGVKAVSWETTSKKASPEffsrHPVSTLW-----HYSDYELENIGRLTHPMKYDAV--SDT 124
Cdd:COG0243 28 CPGCG----------VGCGLGVKVEDGRVVRVRGDPD----HPVNRGRlcakgAALDERLYSPDRLTYPMKRVGPrgSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 125 WQAVDWDIAFREIGERLR----SYDsAQQVEFYTSG----RTSNEAAFLYQLFAREYGSSNFPDCSNMCHGPTSAGLTPA 196
Cdd:COG0243 94 FERISWDEALDLIAEKLKaiidEYG-PEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 197 IGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAK-RGAKIISINPLNERGlerfsfpqsakemftgqaTELS 275
Cdd:COG0243 173 FGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKkRGAKIVVIDPRRTET------------------AAIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 276 NDYYQVKMGGDASLLKGIMKALIEMDEarilldqqptLDHAFIDQHTAGYAALYDDLRQHNWAELEQDSGLTRSQMEDLA 355
Cdd:COG0243 235 DEWLPIRPGTDAALLLALAHVLIEEGL----------YDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 356 HSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRGhsnvqgdrsvgineaasedflqrlekhf 435
Cdd:COG0243 305 REFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG---------------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 436 sirvprkhgrssvesiRAIERGD---AKALICMGGNLAVAMPQPQRTFAAMKNLDLQVHVATKLNRSHlLLAkhNYLLPA 512
Cdd:COG0243 357 ----------------EAILDGKpypIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETA-RYA--DIVLPA 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 513 LGRTERDMQATgiqsvTVEDsmSMVHASCGALKPASrWLKSEPAIVAGMARAtLPHSpinwEAFTGDYT---LIRDAIEA 589
Cdd:COG0243 418 TTWLERDDIVT-----NSED--RRVHLSRPAVEPPG-EARSDWEIFAELAKR-LGFE----EAFPWGRTeedYLRELLEA 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 590 VIPAFHDYnARIAEPGGFRMDTPASRR-----EWRTENGKANFIVS---------HQRAVEREHQPADA--LVLATLRSH 653
Cdd:COG0243 485 TRGRGITF-EELREKGPVQLPVPPEPAfrndgPFPTPSGKAEFYSEtlalpplprYAPPYEGAEPLDAEypLRLITGRSR 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 654 DQYNTTIYGmNDRYRGITGRRdVVFLSAEEATSRGLSQGDVVNVQAldDNGQpcadriMYGLTVVIYNMAAGSIGA---- 729
Cdd:COG0243 564 DQWHSTTYN-NPRLREIGPRP-VVEINPEDAAALGIKDGDLVRVES--DRGE------VLARAKVTEGIRPGVVFAphgw 633
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1100260294 730 -YLPE------ANVLLSlDAVDTQSLTPAYKSVPVTLTKA 762
Cdd:COG0243 634 wYEPAddkggnVNVLTP-DATDPLSGTPAFKSVPVRVEKA 672
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
92-762 |
3.24e-88 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 292.17 E-value: 3.24e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 92 RHPVS---------TLWHYSDYEleniGRLTHPMKYDavSDTWQAVDWDIAFREIGERLRSY------DSaqqVEFYTSG 156
Cdd:COG3383 37 DHPVNrgrlcvkgrFGFEFVNSP----DRLTTPLIRR--GGEFREVSWDEALDLVAERLREIqaehgpDA---VAFYGSG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 157 RTSNEAAFLYQLFAREY-GSSNFPDCSNMCHGPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRD 235
Cdd:COG3383 108 QLTNEENYLLQKLARGVlGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 236 VAKRGAKIISINPlnergleRfsfpqsaKEMFTGQATElsndYYQVKMGGDASLLKGIMKALIEMDEArilldqqptlDH 315
Cdd:COG3383 188 AKKNGAKLIVVDP-------R-------RTETARLADL----HLQIKPGTDLALLNGLLHVIIEEGLV----------DE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 316 AFIDQHTAGYAALYDDLRQHNWAELEQDSGLTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNM 395
Cdd:COG3383 240 DFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 396 GKPGAGICPLRGHSNVQGDRSVGIN--------EAASEDFLQRLEKHFSI-RVPRKHGRSSVESIRAIERGDAKALICMG 466
Cdd:COG3383 320 GRPGTGPFPLTGQNNVQGGRDMGALpnvlpgyrDVTDPEHRAKVADAWGVpPLPDKPGLTAVEMFDAIADGEIKALWIIG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 467 GNLAVAMPQPQRTFAAMKNLDLQVHVATKLNRShlllAKH-NYLLPALGRTERDmqatGiqsvTVEDSMSMVHASCGALK 545
Cdd:COG3383 400 ENPAVSDPDANHVREALEKLEFLVVQDIFLTET----AEYaDVVLPAASWAEKD----G----TFTNTERRVQRVRKAVE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 546 PASrWLKSEPAIVAGMARAtLPHsPINWEaftgDYTLIRDAIEAVIPAFH--DYnARIAEPGGFRM-----DTPASRR-- 616
Cdd:COG3383 468 PPG-EARPDWEIIAELARR-LGY-GFDYD----SPEEVFDEIARLTPDYSgiSY-ERLEALGGVQWpcpseDHPGTPRlf 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 617 --EWRTENGKANFIVSHQRAVEREHQPADALVLATLRSHDQYNTTIygMNDRYRGITGR--RDVVFLSAEEATSRGLSQG 692
Cdd:COG3383 540 tgRFPTPDGKARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGT--RTRRSPRLNKHapEPFVEIHPEDAARLGIKDG 617
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100260294 693 DVVNVQAldDNGQPCA-----DRIMYGLTVVIYNMAAGSigaylpeANVLLSlDAVDTQSLTPAYKSVPVTLTKA 762
Cdd:COG3383 618 DLVRVSS--RRGEVVLrarvtDRVRPGTVFMPFHWGEGA-------ANALTN-DALDPVSKQPEYKACAVRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
111-757 |
4.17e-66 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 231.97 E-value: 4.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKydAVSDTWQAVDWDIAFREIGERLRS----YDSaQQVEFYTSGRTSNEAAFLYQLFARE-YGSSNFPDCSNMC 185
Cdd:TIGR01591 53 RLTTPLI--REGDKFREVSWDEAISYIAEKLKEikekYGP-DSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 186 HGPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPlneRGLErfsfpqSAKE 265
Cdd:TIGR01591 130 HGPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP---RKTE------TAKI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 266 MftgqatelsnDYY-QVKMGGDASLLKGIMKALIEmdearilldqQPTLDHAFIDQHTAGYAALYDDLRQHNWAELEQDS 344
Cdd:TIGR01591 201 A----------DLHiPLKPGTDIALLNAMANVIIE----------EGLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDIT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 345 GLTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRGHSNVQG--------DRS 416
Cdd:TIGR01591 261 GVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGacdmgalpDFL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 417 VGINEAASEDFLQRLEKHFSI-RVPRKHGRSSVESIRAIERGDAKALICMGGNLAVAMPQPQRTFAAMKNLDLQVHVATK 495
Cdd:TIGR01591 341 PGYQPVSDEEVREKFAKAWGVvKLPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIF 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 496 LNRShlllAKH-NYLLPALGRTERDMQATgiqsvTVEDSMSMVHAscgALKPASRwLKSEPAIVAGMARAtlphspINWE 574
Cdd:TIGR01591 421 MTET----AKYaDVVLPAAAWLEKEGTFT-----NAERRIQRFFK---AVEPKGE-SKPDWEIIQELANA------LGLD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 575 AFTGDYTLIRDAIEAVIPAFHDYNARIAEPGGF-------RMDTPASR---REWRTENGKANFIVSHQRAVEREHQPADA 644
Cdd:TIGR01591 482 WNYNHPQEIMDEIRELTPLFAGLTYERLDELGSlqwpcndSDASPTSYlykDKFATPDGKAKFIPLEWVAPIEEPDDEYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 645 LVLATLRSHDQYNTTiyGMNDRYRGITGRRDVVFL--SAEEATSRGLSQGDVVNVQALDDNGQPCA---DRIMYGLTVVI 719
Cdd:TIGR01591 562 LILTTGRVLTHYNVG--EMTRRVAGLRRLSPEPYVeiNTEDAKKLGIKDGDLVKVKSRRGEITLRAkvsDRVNKGAIYIT 639
|
650 660 670
....*....|....*....|....*....|....*...
gi 1100260294 720 YNmaagsigAYLPEANVLLSLDAvDTQSLTPAYKSVPV 757
Cdd:TIGR01591 640 MH-------FWDGAVNNLTTDDL-DPISGTPEYKYTAV 669
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
111-490 |
4.32e-55 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 197.82 E-value: 4.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKydAVSDTWQAVDWDIAFREIGERLRSYDS---AQQVEFYTSGRTSNEAAFLYQLFAREYGSSNFPD-CSNMCH 186
Cdd:cd02753 54 RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDhCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 187 GPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPlNERGLERFSfpqsakem 266
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-RRTELARFA-------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 267 ftgqatelsnDYY-QVKMGGDASLLKGIMKALIEMDeariLLDQqptldhAFIDQHTAGYAALYDDLRQHNWAELEQDSG 345
Cdd:cd02753 203 ----------DLHlQLRPGTDVALLNAMAHVIIEEG----LYDE------EFIEERTEGFEELKEIVEKYTPEYAERITG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 346 LTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRGHSNVQGDRSVGineaASE 425
Cdd:cd02753 263 VPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG----ALP 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100260294 426 DFLqrlekhfsirvPrkhgrssvesiraierGDAKALICMGGNLAVAMPQPQRTFAAMKNLDLQV 490
Cdd:cd02753 339 NVL-----------P----------------GYVKALYIMGENPALSDPNTNHVRKALESLEFLV 376
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
110-519 |
1.54e-53 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 189.46 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 110 GRLTHPMKYDAVSDTWQAVDWDIAFREIGERLRSY---DSAQQVEFYTSGRTSNEAAFLYQLFAREYGSSNFPDCSNMCH 186
Cdd:cd00368 53 DRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIrekYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 187 GPTSAGLtPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPlnergleRFSfpqsakem 266
Cdd:cd00368 133 ASAVAAL-KAFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDP-------RRT-------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 267 ftgQATELSNDYYQVKMGGDASLLKGimkaliemdearilldqqptldhafidqhtagyaalyddlrqhnwAELEQDSGL 346
Cdd:cd00368 197 ---ETAAKADEWLPIRPGTDAALALA---------------------------------------------EWAAEITGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 347 TRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPlrghsnvqgdrsvgineaased 426
Cdd:cd00368 229 PAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP---------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 427 flqrlekhfsirvprkhgrssvesiraiergdakalicmGGNLAVAMPQPQRTFAAMKNLDLQVHVATKLNRSHlLLAkh 506
Cdd:cd00368 287 ---------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETA-AYA-- 324
|
410
....*....|...
gi 1100260294 507 NYLLPALGRTERD 519
Cdd:cd00368 325 DVVLPAATYLEKE 337
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
645-759 |
9.56e-46 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 158.98 E-value: 9.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 645 LVLATLRSHDQYNTTIYGMNDRYRGITGRRDVVFLSAEEATSRGLSQGDVVNVQALDDNGQPcadRIMYGLTVVIYNMAA 724
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQG---RIVRGFRVVEYDIPR 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1100260294 725 GSIGAYLPEANVLLSLDAVDTQSLTPAYKSVPVTL 759
Cdd:cd02787 78 GCLAAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
110-490 |
3.85e-44 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 167.79 E-value: 3.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 110 GRLTHPMkYDAVSDTWQAVDWDIAFREIGERLRSY------DSaqqVEFYTSGRTSNEAAFLYQLFAREY-GSSNFPDCS 182
Cdd:cd02754 53 ERLTRPL-LRRNGGELVPVSWDEALDLIAERFKAIqaeygpDS---VAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 183 NMCHGPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAK--RGAKIISINPlnerglerfsfp 260
Cdd:cd02754 129 RLCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKanPGAKIIVVDP------------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 261 qsakemFTGQATELSNDYYQVKMGGDASLLKGIMKALIEMDEArilldqqptlDHAFIDQHTAGYAALYDDLRQHNWAEL 340
Cdd:cd02754 197 ------RRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLI----------DRDFIDAHTEGFEELKAFVADYTPEKV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 341 EQDSGLTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRGHSNVQGDRSVG-- 418
Cdd:cd02754 261 AEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGgl 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 419 ---------INEAASEDFLQRLEKHFSIRVPRKHGRSSVESIRAIERGDAKALICMGGNLAVAMPQPQRTFAAMKNLDLQ 489
Cdd:cd02754 341 anllpghrsVNNPEHRAEVAKFWGVPEGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFV 420
|
.
gi 1100260294 490 V 490
Cdd:cd02754 421 V 421
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
111-420 |
4.40e-32 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 132.91 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKYDAVSDTWQAVDWDIAFREIGERLRSYDSAQQVE---------------FYTSGRTSNEAAFLYQLFAREYGS 175
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRDASFVEknaagvvvnrpdsiaFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 176 SNFPDCSNMCHGPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHP-RMLTTLRDVAKRGAKIISINPlnergl 254
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 255 eRFSfPQSAKemftgqatelSNDYYQVKMGGDASLLKGIMKALIEMdearilldqqpTLDhafidqhtagyaalyddlrq 334
Cdd:cd02752 208 -RFT-RTAAK----------ADLYVPIRSGTDIAFLGGMINYIIRY-----------TPE-------------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 335 hnwaELEQDSGLTRSQMEDLAHSYSKSSA-----TIVcYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRGHS 409
Cdd:cd02752 245 ----EVEDICGVPKEDFLKVAEMFAATGRpdkpgTIL-YAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHS 319
|
330
....*....|.
gi 1100260294 410 NVQGDRSVGIN 420
Cdd:cd02752 320 NVQGATDLGLL 330
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
111-564 |
5.29e-27 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 115.96 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKYDAvsDTWQAVDWDIAFREIGERLRSYDSA---QQVEFYTSGRTSNEAA-------FLYQLFAREYGSSNFPD 180
Cdd:cd02762 54 RLRTPMRRRG--GSFEEIDWDEAFDEIAERLRAIRARhggDAVGVYGGNPQAHTHAggayspaLLKALGTSNYFSAATAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 181 csNMCHGPTSAGLtpaIGLGkGTVELDDFDHCDLVICIGHNPGTNHPRMLT-----TLRDVAK-RGAKIISINPLNERgl 254
Cdd:cd02762 132 --QKPGHFWSGLM---FGHP-GLHPVPDIDRTDYLLILGANPLQSNGSLRTapdrvLRLKAAKdRGGSLVVIDPRRTE-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 255 erfsfpqSAKemftgqateLSNDYYQVKMGGDASLLKGImkaliemdeARILLDQQPTlDHAFIDQHTAGYAALYDDLRQ 334
Cdd:cd02762 204 -------TAK---------LADEHLFVRPGTDAWLLAAM---------LAVLLAEGLT-DRRFLAEHCDGLDEVRAALAE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 335 HNWAELEQDSGLTRSQMEDLAHSYSkSSATIVCYG-LGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRGHSNVQG 413
Cdd:cd02762 258 FTPEAYAPRCGVPAETIRRLAREFA-AAPSAAVYGrLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFTTPALDLVGQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 414 DRSVGINEAASEDflqRLEKHFSIR--VPrkhGRSSVESIRAIERGDAKALICMGGNLAVAMPQPQRTFAAMKNLDLQVH 491
Cdd:cd02762 337 TSGRTIGRGEWRS---RVSGLPEIAgeLP---VNVLAEEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVS 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1100260294 492 VATKLNRShlllAKH-NYLLPALGRTERDmQATGIQSVTVEDSMSMVHascgALKPASRWLKSEPAIVAGMARA 564
Cdd:cd02762 411 VDVYMTET----TRHaDYILPPASQLEKP-HATFFNLEFPRNAFRYRR----PLFPPPPGTLPEWEILARLVEA 475
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
111-519 |
2.98e-23 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 103.92 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKY--DAVSDTWQAVDWDIAFREIGERLRSY---DSAQQVEFY-TSGRTSNEAAFLYQL-FAREYGSSNFPDCSN 183
Cdd:cd02759 54 RLLYPLKRvgERGENKWERISWDEALDEIAEKLAEIkaeYGPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 184 MCHGPTSAGLTPAIGLGKGTVELDdFDHCDLVICIGHNPG-TNHPRMLTTLRDVAKRGAKIISINPlneRGlerfsfpqs 262
Cdd:cd02759 134 SCYWPRDMAHALTTGFGLGYDEPD-WENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDP---RL--------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 263 akemfTGQATElSNDYYQVKMGGDASLLKGIMKALIEMDEArilldqqptlDHAFIDQHTAGYAALYDDLRQHNWAELEQ 342
Cdd:cd02759 201 -----TWLAAR-ADLWLPIRPGTDAALALGMLNVIINEGLY----------DKDFVENWCYGFEELAERVQEYTPEKVAE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 343 DSGLTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAgicplrghsnvqgdrsvginea 422
Cdd:cd02759 265 ITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGG---------------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 423 asedflqrlekhfSIRVPRKhgrssvesiraiergdAKALICMGGNLAVAMPQPQRTFAAMKNLDLQVHVatklNRSHLL 502
Cdd:cd02759 323 -------------NLLIPYP----------------VKMLIVFGTNPLASYADTAPVLEALKALDFIVVV----DLFMTP 369
|
410
....*....|....*...
gi 1100260294 503 LAKH-NYLLPALGRTERD 519
Cdd:cd02759 370 TAMLaDIVLPVAMSLERP 387
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
111-402 |
3.37e-21 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 97.70 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKYD-AVSDTWQAVDWDIAFREIGERLR---SYDSAQQV--EFYTSGRTSNEAAFLYQLFAReYGSSNF--PDCS 182
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKeikAEYGPESIlpYSYAGTMGLLQRAARGRFFHA-LGASELrgTICS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 183 nmchgptSAGLTpAIGLGKGT---VELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPlnerglerfsf 259
Cdd:cd02766 134 -------GAGIE-AQKYDFGAslgNDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDP----------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 260 pqsakeMFTGQAtELSNDYYQVKMGGDASLLKGIMKALIEMDearilldqqpTLDHAFIDQHTAGYAALYDDLRQHNWAE 339
Cdd:cd02766 195 ------YRTATA-ARADLHIQIRPGTDGALALGVAKVLFREG----------LYDRDFLARHTEGFEELKAHLETYTPEW 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100260294 340 LEQDSGLTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGI 402
Cdd:cd02766 258 AAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
108-529 |
1.49e-20 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 95.44 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 108 NIGRLTHPMKYDAVSDT--WQAVDWDIAFREIGERLRSYDSAQQVEFYTSGRTSNEAAFLYQLFAREYGSSNFPDCSNMC 185
Cdd:cd02755 52 DPDRLKKPLIRVGERGEgkFREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHESTC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 186 HGPTSAGLTPAIGLGkGTVELDDFDHCDLVICIGHN--PGTNHP---RMLTTLrdvaKRGAKIISINPlnergleRFSfp 260
Cdd:cd02755 132 LASKNLAWKLVIDSF-GGEVNPDFENARYIILFGRNlaEAIIVVdarRLMKAL----ENGAKVVVVDP-------RFS-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 261 qsakemftgQATELSNDYYQVKMGGDASLLKGIMKALIEMDeariLLDQqptldhAFIDQHTAGYAALYDDLRQHN--WA 338
Cdd:cd02755 198 ---------ELASKADEWIPIKPGTDLAFVLALIHVLISEN----LYDA------AFVEKYTNGFELLKAHVKPYTpeWA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 339 ELEqdSGLTRSQMEDLAHSYSKS-SATIVCYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGaGICPLRGHSnvqgdrsv 417
Cdd:cd02755 259 AQI--TDIPADTIRRIAREFAAAaPHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRG-GLYYAGSAK-------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 418 gineaasedflqrlekhfsirvPRKhgrssvesiraiergdAKALICMGGNLAVAMPQPQRTFAAMKNLDLQVHVATKLN 497
Cdd:cd02755 328 ----------------------PYP----------------IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPS 369
|
410 420 430
....*....|....*....|....*....|..
gi 1100260294 498 rSHLLLAkhNYLLPALGRTERDMQATGIQSVT 529
Cdd:cd02755 370 -DTALYA--DVILPEATYLERDEPFSDKGGPA 398
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
111-519 |
4.24e-20 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 92.85 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKYDAvSDTWQAVDWDIAFREIGERLRSY-----DSAQQVEFYTSGRTSNEAAFLYQLFAREYGSSNF---PDCS 182
Cdd:pfam00384 1 RLKYPMVRRG-DGKFVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 183 NMCHGPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRG-AKIISINPlnergleRFSFPQ 261
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGkAKVIVIGP-------RLDLTY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 262 SAkemftgqatelsnDYYQVKMGGDASLLKGIMKALIemdeaRILLDQQPTLDHAFIDqhtagyaalyddlrqhnwaele 341
Cdd:pfam00384 153 AD-------------EHLGIKPGTDLALALAGAHVFI-----KELKKDKDFAPKPIII---------------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 342 qdsgltrsqmedlahsyskssativcYGLGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRghsNVQGDRS-VGIN 420
Cdd:pfam00384 193 --------------------------VGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGAASpVGAL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 421 EaasedflqrlekhfsirVPRKHGRSSVESIRAIERGDAKALICMGGNLAVAMPQPQRTFAAMKNLDL----QVHVATKl 496
Cdd:pfam00384 244 D-----------------LGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLfvvyDGHHGDK- 305
|
410 420
....*....|....*....|....
gi 1100260294 497 nrshllLAKH-NYLLPALGRTERD 519
Cdd:pfam00384 306 ------TAKYaDVILPAAAYTEKN 323
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
111-260 |
5.29e-14 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 74.63 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKydAVSDTWQAVDWDIAFREIGERLRSYdSAQQVEFYTSGRTSNEAAFLYQLFAREYGSSNFpDCSNmchGPTS 190
Cdd:cd02768 54 RLTQPLI--KKGGKLVPVSWEEALKTVAEGLKAV-KGDKIGGIAGPRADLESLFLLKKLLNKLGSNNI-DHRL---RQSD 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100260294 191 AGLTP-AIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKR-GAKIISINPLNERGLERFSFP 260
Cdd:cd02768 127 LPADNrLRGNYLFNTSIAEIEEADAVLLIGSNLRKEAPLLNARLRKAVKKkGAKIAVIGPKDTDLIADLTYP 198
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
186-420 |
1.66e-11 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 67.64 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 186 HGPTSAGLTPAIG---------LGKGTVELDDFDHCDLVICIGHNPGTN--------HPRMLTTLRDVAKRGAKIISINP 248
Cdd:cd02751 135 YGTYSTGAAQVILphvvgsdevYEQGTSWDDIAEHSDLVVLFGANPLKTrqgggggpDHGSYYYLKQAKDAGVRFICIDP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 249 LNERGlerfsfpqsakemftgqATELSNDYYQVKMGGDASLLKGIMKALIEMDeariLLDQqptldhAFIDQHTAGYAAL 328
Cdd:cd02751 215 RYTDT-----------------AAVLAAEWIPIRPGTDVALMLAMAHTLITED----LHDQ------AFLARYTVGFDEF 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 329 YDDLRQHN--------WAEleQDSGLTRSQMEDLAHSYSKSSATIVCyGLGITQHKNGTENVQQLVNLLLLKGNMGKPGA 400
Cdd:cd02751 268 KDYLLGESdgvpktpeWAA--EITGVPAETIRALAREIASKRTMIAQ-GWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGG 344
|
250 260
....*....|....*....|
gi 1100260294 401 GICPLRGHSNVQGDRSVGIN 420
Cdd:cd02751 345 GFGFGYGYSNGGGPPRGGAG 364
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
111-265 |
7.54e-11 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 64.68 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKydAVSDTWQAVDWDIAFREIGERL---RSYDSAQQVEFYTSGRTSNEAAFLYQLFAREYGSSNFP------DC 181
Cdd:cd02772 54 RLTKPMI--KKDGQWQEVDWETALEYVAEGLsaiIKKHGADQIGALASPHSTLEELYLLQKLARGLGSDNIDhrlrqsDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 182 SnmchgpTSAGLTPAIGLGKGTVELDDFDhcdLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPLNerglERFSFPQ 261
Cdd:cd02772 132 R------DDAKASGAPWLGMPIAEISELD---RVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPAD----DDFLFPL 198
|
....
gi 1100260294 262 SAKE 265
Cdd:cd02772 199 SGKA 202
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
111-369 |
2.59e-09 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 60.84 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKY--DAVSDTWQAVDWDIAFREIGERL---RSYDSAQQVEFytSGRTSNEAAFLYQlFAREYGSSNFPDCSNMC 185
Cdd:PRK15488 98 RIVKPLKRvgERGEGKWQEISWDEAYQEIAAKLnaiKQQHGPESVAF--SSKSGSLSSHLFH-LATAFGSPNTFTHASTC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 186 hgPTSAGLTPAIGLGkGTVELdDFDHCDLVICIGHN--PGTNHPRMLTTLRDVAKRGAKIISINPlnergleRFSfpqsa 263
Cdd:PRK15488 175 --PAGYAIAAKVMFG-GKLKR-DLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------RFS----- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 264 keMFTGQATElsndYYQVKMGGDASLLKGIMKALIEMDearilldqqpTLDHAFIDQHTAGYAALYDDLRQHN--WAELE 341
Cdd:PRK15488 239 --VVASKADE----WHAIRPGTDLAVVLALCHVLIEEN----------LYDKAFVERYTSGFEELAASVKEYTpeWAEAI 302
|
250 260
....*....|....*....|....*....
gi 1100260294 342 qdSGLTRSQMEDLAHSYSKSS-ATIVCYG 369
Cdd:PRK15488 303 --SDVPADDIRRIARELAAAApHAIVDFG 329
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
111-242 |
7.95e-09 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 58.55 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKydAVSDTWQAVDWDIAFREIGERLRsyDSAQQVEFYTSGRTSNEAAFLYQLFAREYGSSNFPDCSNMCHGPTS 190
Cdd:cd02771 54 RLTQPLI--RRGGTLVPVSWNEALDVAAARLK--EAKDKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRARRLIAEI 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1100260294 191 AGLTPAIglgkgTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAK 242
Cdd:cd02771 130 LRNGPIY-----IPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAV 176
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
111-413 |
1.27e-08 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 58.49 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKY--DAVSDTWQAVDWDIAFREIGERLRsydsaQQVEFYtsgrtSNEAAFL-YQ---LFAREYGSSNFPDCSNM 184
Cdd:cd02770 59 RLKYPMKRvgKRGEGKFVRISWDEALDTIASELK-----RIIEKY-----GNEAIYVnYGtgtYGGVPAGRGAIARLLNL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 185 C------HGPTSAG----LTPAIGLGKGT-VELDDFDHCDLVICIGHNPGTNhpRM---LTT--LRDVAKRGAKIISINP 248
Cdd:cd02770 129 TggylnyYGTYSWAqittATPYTYGAAASgSSLDDLKDSKLVVLFGHNPAET--RMgggGSTyyYLQAKKAGAKFIVIDP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 249 lnerglerfsfpqsakeMFTGQATELSNDYYQVKMGGDASLLKGIMKALIemdearilldQQPTLDHAFIDQHTAGY--- 325
Cdd:cd02770 207 -----------------RYTDTAVTLADEWIPIRPGTDAALVAAMAYVMI----------TENLHDQAFLDRYCVGFdae 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 326 -----AALYDDLRQH-------------NWAelEQDSGLTRSQMEDLAHSYSKSSATIVCYGLGITQHKNGTENVQQLVN 387
Cdd:cd02770 260 hlpegAPPNESYKDYvlgtgydgtpktpEWA--SEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMM 337
|
330 340
....*....|....*....|....*.
gi 1100260294 388 LLLLKGNMGKPGAGICPLRGHSNVQG 413
Cdd:cd02770 338 LAAMTGNVGIPGGNTGARPGGSAYNG 363
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
652-753 |
1.37e-08 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 53.09 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 652 SHDQYNTTIYGMNDRYRGITgRRDVVFLSAEEATSRGLSQGDVVNVQAldDNGQPCA-----DRIMYGlTVVIYnMAAGS 726
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELA-PEPVVEINPEDAAALGIKDGDLVRVES--RRGSVVLrakvtDGVPPG-VVFLP-HGWGH 75
|
90 100
....*....|....*....|....*..
gi 1100260294 727 IGAYLPEANVLLSlDAVDTQSLTPAYK 753
Cdd:cd02775 76 RGGRGGNANVLTP-DALDPPSGGPAYK 101
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
126-475 |
2.99e-07 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 53.49 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 126 QAVDWDIAFREIGERLRSydsAQQVEFYTSGRTSNEA-AFLYQLfaREYGSSNFPDCSNMCHGPTSAGLTPAiglGKGTV 204
Cdd:cd02761 52 KPVSLEEAIEKAAEILKE---AKRPLFYGLGTTVCEAqRAGIEL--AEKLGAIIDHAASVCHGPNLLALQDS---GWPTT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 205 ELDDF-DHCDLVICIGHNPGTNHPRML--------TTLRDVAKRGAKIISINPlnergleRFSfpqsakemftgQATELS 275
Cdd:cd02761 124 TLGEVkNRADVIVYWGTNPMHAHPRHMsrysvfprGFFREGGREDRTLIVVDP-------RKS-----------DTAKLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 276 NDYYQVKMGGDASLLkgimkaliemdearilldqqptldhafidqhtagyAALYDDLRQHNwAELEQDSGLTRSQMEDLA 355
Cdd:cd02761 186 DIHLQIDPGSDYELL-----------------------------------AALRALLRGAG-LVPDEVAGIPAETILELA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 356 HSYSKSSATIVCYGLGITQ----HKNGtENVQQLVNLLLLKGNmgkpgAGICPLRGHSNVQgdrsvGINEAASEDFLQRL 431
Cdd:cd02761 230 ERLKNAKFGVIFWGLGLLPsrgaHRNI-EAAIRLVKALNEYTK-----FALLPLRGHYNVR-----GFNQVLTWLTGYPF 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1100260294 432 EKHFSIRVPRKH-GRSSVesIRAIERGDAKALICMGGNLAVAMPQ 475
Cdd:cd02761 299 RVDFSRGYPRYNpGEFTA--VDLLAEGEADALLIIASDPPAHFPQ 341
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
645-756 |
3.48e-06 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 46.50 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 645 LVLATLRSHDQYNTTIYGMNDRYRGItGRRDVVFLSAEEATSRGLSQGDVVNVQAldDNGQPCA-----DRIMYGlTVVI 719
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAK-PEPEVVEIHPEDAAALGIKDGDLVEVTS--RRGSVVVrakvtDRVRPG-VVFM 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1100260294 720 YnMAAGSiGAYLPEANVLLSlDAVDTQSLTPAYKSVP 756
Cdd:pfam01568 77 P-FGWWY-EPRGGNANALTD-DATDPLSGGPEFKTCA 110
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
111-322 |
4.04e-06 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 50.22 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPM--KYDAVSDTWQAVDWDIAFREIGERL---RSYDSaQQVEFYTsGRTSNEAafLYQLFAREYGSSNFPDCSNMC 185
Cdd:cd02763 54 RLTKPLlrKGPRGSGQFEEIEWEEAFSIATKRLkaaRATDP-KKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 186 HGPTSAGLTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPLNerglerfsfpqsake 265
Cdd:cd02763 130 SVNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVR--------------- 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1100260294 266 mfTGQATeLSNDYYQVKMGGDASLLKGIMKALIEMDearilldqqpTLDHAFIDQHT 322
Cdd:cd02763 195 --TGYAA-IADEWVPIKPGTDGAFILALAHELLKAG----------LIDWEFLKRYT 238
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
111-432 |
1.36e-05 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 48.63 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKydAVSD----TWQAVDWDIAFREIGERLRSYDS---AQQVEFYTSgrtSNEAAFLYQLFAREYGSSNFPDCSN 183
Cdd:cd02765 55 RLKYPMK--RVGErgegKFERITWDEALDTIADKLTEAKReygGKSILWMSS---SGDGAILSYLRLALLGGGLQDALTY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 184 MCHGPTSAGLTPAIGLG--KGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKRGAKIISINPlnerglerfsfpq 261
Cdd:cd02765 130 GIDTGVGQGFNRVTGGGfmPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDP------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 262 sakeMFTGQATElSNDYYQVKMGGDASLLKGIMKALIE---MDEARI----------------LLDQQPTLDHAFIDQH- 321
Cdd:cd02765 197 ----VYSTTAAK-ADQWVPIRPGTDPALALGMINYILEhnwYDEAFLksntsapflvredngtLLRQADVTATPAEDGYv 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 322 --------------------------------TAGYAALYDDLRQHNWAELEQDSGLTRSQMEDLAHSYSKSSATIVCYG 369
Cdd:cd02765 272 vwdtnsdspepvaatninpalegeytingvkvHTVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGF 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100260294 370 LGITQHKNGTENVQQLVNLLLLKGNMGKPGAGICPLRG----HSNVQGDrsvGINEAASEDFLQRLE 432
Cdd:cd02765 352 GGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQIKFmyfmGSNFLGN---QPDRDRWLKVMKNLD 415
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
111-378 |
1.75e-05 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 48.11 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 111 RLTHPMKYDAV--SDTWQAVDWDIAFREI---------GER-----LRSYDS---AQQVEF--------YTSGRTSNEAA 163
Cdd:cd02758 83 RVLQPLKRVGPrgSGKWKPISWEQLIEEVveggdlfgeGHVeglkaIRDLDTpidPDHPDLgpkanqllYTFGRDEGRTP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 164 FLYQLFAREYGSSNFPDCSNMCHGPTSAG-LTPAIGLGKGTVELDDFDHCDLVICIGHNPGTNHPRMLTTLRDVAKR--- 239
Cdd:cd02758 163 FIKRFANQAFGTVNFGGHGSYCGLSYRAGnGALMNDLDGYPHVKPDFDNAEFALFIGTSPAQAGNPFKRQARRLAEArte 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 240 -GAKIISINPLnerglerfsFPQSAkemftgQATELSNDYYQVKMGGDASLLKGIMKALIEMD--EARILLdqQPTLDHA 316
Cdd:cd02758 243 gNFKYVVVDPV---------LPNTT------SAAGENIRWVPIKPGGDGALAMAMIRWIIENEryNAEYLS--IPSKEAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 317 fidqHTAGYAA-------------------LYDDLRQHNWAELEQDSGLTRSQMEDLAHSYSK--SSATIVCYglGITQH 375
Cdd:cd02758 306 ----KAAGEPSwtnathlvitvrvksalqlLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTShgRAAAVVHH--GGTMH 379
|
...
gi 1100260294 376 KNG 378
Cdd:cd02758 380 SNG 382
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
110-482 |
3.24e-03 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 40.60 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 110 GRLTHPMKYdavsdtWQAVDWDIAFREIGERLRSydsAQQVEFYTSGRTSNEAA-FLYQLfaREYGSSNFPDCSNMCHGP 188
Cdd:COG1029 50 HRITSPRIR------GKEVSLEEAIDKAAEILAN---AKRPLIYGLSSTDCEAMrAGLAL--AERVGAVVDNTASVCHGP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 189 TSAGLT----PAIGLG--KgtvelddfDHCDLVICIGHNPGTNHPRMLT----------TLRDVAKRgaKIISINPLner 252
Cdd:COG1029 119 SLLALQdvgwPTCTLGevK--------NRADVIIYWGCNPVHAHPRHMSrysvfprgffTPKGRKDR--TVIVVDPR--- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 253 glerfsfpqsakemFTGQAtELSNDYYQVKMGGDASLLkgimkaliemdearilldqqptldhafidqhtagyAALYDDL 332
Cdd:COG1029 186 --------------PTDTA-KVADLHLQVKPGRDYEVL-----------------------------------SALRALV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 333 RQHnwaELEQDS--GLTRSQMEDLAHSYSKSSATIVCYGLGITQ----HKNG-------------TEnvqqlvnllllkg 393
Cdd:COG1029 216 RGK---ELSPEEvaGIPVEDLEELAERLKNAKYGVIFWGMGLTQspgkHLNVdaaielvrdlnryTK------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260294 394 nmgkpgAGICPLRGHSNVqgdrsVGINEAASedflqrLEKHFSIRV------PRKH-GRSSveSIRAIERGDAKALICMG 466
Cdd:COG1029 280 ------FSILPLRGHYNV-----AGANQVAS------WQTGYPFRVdfsrgyPRYNpGETS--AVDLLARGEVDALLWVA 340
|
410
....*....|....*.
gi 1100260294 467 GNLAVAMPQPQRTFAA 482
Cdd:COG1029 341 SDPGAHFPPDAVEHLA 356
|
|
| |
