|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
1-759 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 1650.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 1 MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDK 80
Cdd:PRK09939 1 MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 81 QVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAA 160
Cdd:PRK09939 81 QVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 161 FLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKM 240
Cdd:PRK09939 161 FLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 241 IAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTV 320
Cdd:PRK09939 241 IAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 321 GFDELRRDVLNSEWKDIERISGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGIC 400
Cdd:PRK09939 321 GFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGIC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 401 PLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPYAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPL 480
Cdd:PRK09939 401 PLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 481 TQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQ 560
Cdd:PRK09939 481 TQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 561 ATLPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNS 640
Cdd:PRK09939 561 AALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 641 KLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMAD 720
Cdd:PRK09939 641 KLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMAD 720
|
730 740 750
....*....|....*....|....*....|....*....
gi 485875156 721 RSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN 759
Cdd:PRK09939 721 RSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN 759
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
11-758 |
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: 1276.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 11 AAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPD-PKHSASFDICENGAKAIAWEVTDKQVNASFFAE 89
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVsPQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 90 NTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYsDPNQVEFYTSGRTSNEAAFLYQLFARE 169
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSL-DPKQVAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 170 YGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQER 249
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 250 GLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASaagrPSLLDDEFIQTHTVGFDELRRDV 329
Cdd:TIGR01701 240 GLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQP----GSLIDHEFIANHTNGFDELRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 330 LNSEWKDIERISGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQ 409
Cdd:TIGR01701 316 LQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 410 GDRTVGITEKPSAEFLARLGERYGFTPPYAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHV 489
Cdd:TIGR01701 396 GDRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 490 ATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQATLPQSVVA 569
Cdd:TIGR01701 476 ATKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 570 WEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAA-ERRWMTPSGKANFITSKGLLEDPSSAFNSKLVMATVR 648
Cdd:TIGR01701 556 WEILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAALcERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 649 SHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGkrSSRRMDRLKVVIYPMADRSLVTYFP 728
Cdd:TIGR01701 636 SHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDG--QKRKFDNLRIVFYDTPTGNAAAYYP 713
|
730 740 750
....*....|....*....|....*....|
gi 485875156 729 ESNHMLTLDNHDPLSGIPGYKSIPVELEPS 758
Cdd:TIGR01701 714 EANPLLPLDHHDPQSKTPEYKTIPVRLEAS 743
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
46-624 |
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: 984.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 46 GFDCPGCAWPDPKHS-ASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKP 124
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 125 LSWQQAFDEIGARLQSYsDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLE 204
Cdd:cd02767 81 ISWDEAFAEIAARLRAL-DPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 205 DFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTnSETQLASAYYNVRIGGDM 284
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 285 ALLKGMMRLLIERDDAasaagRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYTAAERTIIC 364
Cdd:cd02767 239 ALLNGMAKHLIERDDE-----PGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 365 YGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPYAPGHAA 444
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 445 IASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQA 524
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 525 VTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQATLPQSVVAWEYLVEDYDRIRNDIEAVLPE-FADYNQRIRHPGG 603
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYEgFADFNQRGDQPGG 553
|
570 580
....*....|....*....|.
gi 485875156 604 FHLINAAAERRWMTPSGKANF 624
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQF 574
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
99-757 |
9.58e-157 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 470.86 E-value: 9.58e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 99 GDHELEAAGRLTQPLKYDAV--SDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSG----RTSNEAAFLYQLFARE 169
Cdd:COG0243 69 LDERLYSPDRLTYPMKRVGPrgSGKFERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsagRLSNEAAYLAQRFARA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 170 YGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINPLQE 248
Cdd:COG0243 149 LGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLReAAKKRGAKIVVIDPRRT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 249 RGlerftapqnpfemltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRD 328
Cdd:COG0243 229 ET------------------AAIADEWLPIRPGTDAALLLALAHVLIEEG----------LYDRDFLARHTVGFDELAAY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 329 VLNSEWKDIERISGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHsnv 408
Cdd:COG0243 281 VAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE--- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 409 qgdrtvGITEkpsaeflarlGERYgftppyapghaaiasmqaictgQARALICMGGNFALAMPD----REAsavpLTQLD 484
Cdd:COG0243 358 ------AILD----------GKPY----------------------PIKALWVYGGNPAVSAPDtnrvREA----LRKLD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 485 LAVHVATKLNRSHLLTArhsYILPVLGRSEIDMqksgaQAVTVEDsmSMIHASRGVLKPAGvMLKSECAVVAGIAQATLP 564
Cdd:COG0243 396 FVVVIDTFLTETARYAD---IVLPATTWLERDD-----IVTNSED--RRVHLSRPAVEPPG-EARSDWEIFAELAKRLGF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 565 QSVVAWEYLVEDY--DRIRNDIEAVLPeFADYNQRirhpGGFHLINA-----AAERRWMTPSGKANFiTSKGLLEDPSSA 637
Cdd:COG0243 465 EEAFPWGRTEEDYlrELLEATRGRGIT-FEELREK----GPVQLPVPpepafRNDGPFPTPSGKAEF-YSETLALPPLPR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 638 FNSK------------LVMATVRSHDQYNTTIYGmDDRYRGVFGqRDVVFMSAKQAKICRVKNGERVNLialtpdgkrSS 705
Cdd:COG0243 539 YAPPyegaepldaeypLRLITGRSRDQWHSTTYN-NPRLREIGP-RPVVEINPEDAAALGIKDGDLVRV---------ES 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485875156 706 RR---------MDRLK--VVIYPMADRSLVTYFPESNH-MLTLDNHDPLSGIPGYKSIPVELEP 757
Cdd:COG0243 608 DRgevlarakvTEGIRpgVVFAPHGWWYEPADDKGGNVnVLTPDATDPLSGTPAFKSVPVRVEK 671
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
98-757 |
2.26e-110 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 350.72 E-value: 2.26e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 98 WGDHELEAAGRLTQPLKYDavSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREY-GSN 173
Cdd:COG3383 51 FGFEFVNSPDRLTTPLIRR--GGEFREVSWDEALDLVAERLREIQAehgPDAVAFYGSGQLTNEENYLLQKLARGVlGTN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 174 NFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleR 253
Cdd:COG3383 129 NIDNNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-------R 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 254 FTAPqnpfemltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSE 333
Cdd:COG3383 202 RTET-----------ARLADLHLQIKPGTDLALLNGLLHVIIEEG----------LVDEDFIAERTEGFEELKASVAKYT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 334 WKDIERISGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRT 413
Cdd:COG3383 261 PERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 414 VGI--TEKP------SAEFLARLGERYGFTP-PYAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
Cdd:COG3383 341 MGAlpNVLPgyrdvtDPEHRAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 485 LAVHVATKLNRshllTARHS-YILPVLGRSEidmqKSGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQATl 563
Cdd:COG3383 421 FLVVQDIFLTE----TAEYAdVVLPAASWAE----KDG----TFTNTERRVQRVRKAVEPPG-EARPDWEIIAELARRL- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 564 pqsVVAWEYlvEDYDRIRNDIEAVLPEFA--DYnQRIRHPGGFHLINAAAER---------RWMTPSGKANFI--TSKGL 630
Cdd:COG3383 487 ---GYGFDY--DSPEEVFDEIARLTPDYSgiSY-ERLEALGGVQWPCPSEDHpgtprlftgRFPTPDGKARFVpvEYRPP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 631 LEDPSSAFNskLVMATVRSHDQYNT-TIYGMDDRYRGVFGqRDVVFMSAKQAKICRVKNGERVNLialtpdgkrSSRRMD 709
Cdd:COG3383 561 AELPDEEYP--LVLTTGRLLDQWHTgTRTRRSPRLNKHAP-EPFVEIHPEDAARLGIKDGDLVRV---------SSRRGE 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 485875156 710 -RLKVVIYPMADRSLV--TY-FPESN-HMLTLDNHDPLSGIPGYKSIPVELEP 757
Cdd:COG3383 629 vVLRARVTDRVRPGTVfmPFhWGEGAaNALTNDALDPVSKQPEYKACAVRVEK 681
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
108-753 |
5.26e-84 |
|
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: 280.51 E-value: 5.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARL---QSYSDPNQVEFYTSGRTSNEAAFLYQLFARE-YGSNNFPDCSNMCH 183
Cdd:TIGR01591 53 RLTTPLI--REGDKFREVSWDEAISYIAEKLkeiKEKYGPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 184 EPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTapqnpfem 263
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-------RKT-------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 264 ltnsET-QLASAYYNVRIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISG 342
Cdd:TIGR01591 196 ----ETaKIADLHIPLKPGTDIALLNAMANVIIEE----------GLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 343 LSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI--TEKP 420
Cdd:TIGR01591 262 VPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGAlpDFLP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 421 ------SAEFLARLGERYGFTP-PYAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKL 493
Cdd:TIGR01591 342 gyqpvsDEEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 494 NRshllTARHS-YILPVLGRSEidmqKSGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQAT-LPqsvvaWE 571
Cdd:TIGR01591 422 TE----TAKYAdVVLPAAAWLE----KEG----TFTNAERRIQRFFKAVEPKG-ESKPDWEIIQELANALgLD-----WN 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 572 YlvEDYDRIRNDIEAVLPEFADYN----------QRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSK 641
Cdd:TIGR01591 484 Y--NHPQEIMDEIRELTPLFAGLTyerldelgslQWPCNDSDASPTSYLYKDKFATPDGKAKFIPLEWVAPIEEPDDEYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 642 LVMATVRSHDQYNTTiyGMDDRYRGV--FGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKV-VIY-P 717
Cdd:TIGR01591 562 LILTTGRVLTHYNVG--EMTRRVAGLrrLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVNKgAIYiT 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 485875156 718 MADrslvtYFPESNhMLTLDNHDPLSGIPGYKSIPV 753
Cdd:TIGR01591 640 MHF-----WDGAVN-NLTTDDLDPISGTPEYKYTAV 669
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
108-628 |
5.31e-80 |
|
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: 265.23 E-value: 5.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFARE-YGSNNFPDCSNMCH 183
Cdd:cd02753 54 RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 184 EPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTapqnpfEM 263
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-------RRT------EL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 264 ltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGL 343
Cdd:cd02753 199 -----ARFADLHLQLRPGTDVALLNAMAHVIIEEG----------LYDEEFIEERTEGFEELKEIVEKYTPEYAERITGV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 344 SQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGdrtvgitekpSAE 423
Cdd:cd02753 264 PAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQG----------ACD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 424 FlarlgeryGFTPPYAPGHaaiasmqaictgqARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRshllTARH 503
Cdd:cd02753 334 M--------GALPNVLPGY-------------VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTE----TAEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 504 S-YILPVLGRSEidmqKSGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQAT-LPqsvvaWEYL-VEDydrI 580
Cdd:cd02753 389 AdVVLPAASFAE----KDG----TFTNTERRVQRVRKAVEPPG-EARPDWEIIQELANRLgYP-----GFYShPEE---I 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 485875156 581 RNDIEAVLPEFADYN-QRIRHPGGFHL-INAAA--------ERRWMTPSGKANFITSK 628
Cdd:cd02753 452 FDEIARLTPQYAGISyERLERPGGLQWpCPDEDhpgtpilhTERFATPDGKARFMPVE 509
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
103-561 |
1.18e-69 |
|
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: 233.37 E-value: 1.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 103 LEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCS 179
Cdd:cd00368 49 LYSPDRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIREkygPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 180 NMCHEPTSVGLAAsIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGlerftapqn 259
Cdd:cd00368 129 RLCHASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTET--------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 260 pfemltnseTQLASAYYNVRIGGDMALLKGmmrllierddaasaagrpsllddefiqthtvgfdelrrdvlnsEWkdIER 339
Cdd:cd00368 199 ---------AAKADEWLPIRPGTDAALALA-------------------------------------------EW--AAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 340 ISGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPlrghsnvqgdrtvgitek 419
Cdd:cd00368 225 ITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP------------------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 420 psaeflarlgerygftppyapghaaiasmqaictgqaralicmGGNFALAMPDREASAVPLTQLDLAVHVATKLNRshll 499
Cdd:cd00368 287 -------------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTE---- 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485875156 500 TARHS-YILPVLGRSEidmqKSGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQA 561
Cdd:cd00368 320 TAAYAdVVLPAATYLE----KEG----TYTNTEGRVQLFRQAVEPPG-EARSDWEILRELAKR 373
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
103-626 |
3.44e-55 |
|
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: 199.37 E-value: 3.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 103 LEAAGRLTQPLKYDAVSDcYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREY-GSNNFPDC 178
Cdd:cd02754 49 LNGPERLTRPLLRRNGGE-LVPVSWDEALDLIAERFKAIQAeygPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 179 SNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSL--RALVKRGAKMIAINPlqergleRFTA 256
Cdd:cd02754 128 SRLCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLldRKKANPGAKIIVVDP-------RRTR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 257 PqnpfemltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKD 336
Cdd:cd02754 201 T-----------ADIADLHLPIRPGTDLALLNGLLHVLIEEG----------LIDRDFIDAHTEGFEELKAFVADYTPEK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 337 IERISGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVG- 415
Cdd:cd02754 260 VAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGg 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 416 ----------ITEKPSAEFLARL-GERYGFTPPyAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
Cdd:cd02754 340 lanllpghrsVNNPEHRAEVAKFwGVPEGTIPP-KPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 485 LAVhVATKLNRSHllTARHS-YILPVLGRSEidmqKSGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQA-- 561
Cdd:cd02754 419 FVV-VQDAFADTE--TAEYAdLVLPAASWGE----KEG----TMTNSERRVSLLRAAVEPPG-EARPDWWILADVARRlg 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 562 -------TLPQSVvaWEYLVE------------DYDRIRNdiEAVLPEFADYNqrirHPGGFHLInaaAERRWMTPSGKA 622
Cdd:cd02754 487 fgelfpyTSPEEV--FEEYRRlsrgrgadlsglSYERLRD--GGVQWPCPDGP----PEGTRRLF---EDGRFPTPDGRA 555
|
....
gi 485875156 623 NFIT 626
Cdd:cd02754 556 RFVA 559
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
642-755 |
1.64e-52 |
|
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: 177.47 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 642 LVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRssRRMDRLKVVIYPMADR 721
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQG--RIVRGFRVVEYDIPRG 78
|
90 100 110
....*....|....*....|....*....|....
gi 485875156 722 SLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVEL 755
Cdd:cd02787 79 CLAAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
108-410 |
4.02e-43 |
|
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: 166.04 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVE---------------FYTSGRTSNEAAFLYQLFAREYGS 172
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRDASFVEknaagvvvnrpdsiaFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 173 NNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHP-RMLTSLRALVKRGAKMIAINPlqergl 251
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 252 eRFTApqnpfemlTNSEtqlASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrPsllddefiqthtvgfdelrrdvln 331
Cdd:cd02752 208 -RFTR--------TAAK---ADLYVPIRSGTDIAFLGGMINYIIRYT--------P------------------------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 332 sewKDIERISGLSQTQIAELADAYTAAER-----TIIcYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHS 406
Cdd:cd02752 244 ---EEVEDICGVPKEDFLKVAEMFAATGRpdkpgTIL-YAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHS 319
|
....
gi 485875156 407 NVQG 410
Cdd:cd02752 320 NVQG 323
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
108-514 |
1.87e-34 |
|
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: 138.68 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKYDAvsDCYKPLSWQQAFDEIGARL---QSYSDPNQVEFYTSGRTSNEAA-------FLYQLFAREYGSNNFPD 177
Cdd:cd02762 54 RLRTPMRRRG--GSFEEIDWDEAFDEIAERLraiRARHGGDAVGVYGGNPQAHTHAggayspaLLKALGTSNYFSAATAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 178 csNMCHEPTSVGLAASigvgKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTS------LRALVKRGAKMIAINPlqergl 251
Cdd:cd02762 132 --QKPGHFWSGLMFGH----PGLHPVPDIDRTDYLLILGANPLQSNGSLRTApdrvlrLKAAKDRGGSLVVIDP------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 252 erftapqnpfemlTNSET-QLASAYYNVRIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVL 330
Cdd:cd02762 200 -------------RRTETaKLADEHLFVRPGTDAWLLAAMLAVLLAE----------GLTDRRFLAEHCDGLDEVRAALA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 331 NSEWKDIERISGLSQTQIAELADAYTAAeRTIICYG-MGITQHEHGTQNvQQLVNLL-LMKGNIGKPGAGIC-----PLR 403
Cdd:cd02762 257 EFTPEAYAPRCGVPAETIRRLAREFAAA-PSAAVYGrLGVQTQLFGTLC-SWLVKLLnLLTGNLDRPGGAMFttpalDLV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 404 GHSnvqGDRTVGITEKPSAefLARLGERYGFTPPyapghAAIAsmQAICT---GQARALICMGGNFALAMPDREASAVPL 480
Cdd:cd02762 335 GQT---SGRTIGRGEWRSR--VSGLPEIAGELPV-----NVLA--EEILTdgpGRIRAMIVVAGNPVLSAPDGARLEAAL 402
|
410 420 430
....*....|....*....|....*....|....*
gi 485875156 481 TQLDLAVHVATKLNRshllTARHS-YILPVLGRSE 514
Cdd:cd02762 403 GGLEFMVSVDVYMTE----TTRHAdYILPPASQLE 433
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
108-638 |
1.84e-29 |
|
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: 122.80 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKY--DAVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFY-TSGRTSNEAAFLYQL-FAREYGSNNFPDCSN 180
Cdd:cd02759 54 RLLYPLKRvgERGENKWERISWDEALDEIAEKLAEIKAeygPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 181 MCHEPTSVGLAASIGVGkGTVLLEDFEKCDLVICIGHNPG-TNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApqn 259
Cdd:cd02759 134 SCYWPRDMAHALTTGFG-LGYDEPDWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDP-------RLTW--- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 260 pfemltnsETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDV--LNSEWkdI 337
Cdd:cd02759 203 --------LAARADLWLPIRPGTDAALALGMLNVIINEG----------LYDKDFVENWCYGFEELAERVqeYTPEK--V 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 338 ERISGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGicplrghsnvqgdrtvgit 417
Cdd:cd02759 263 AEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGN------------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 418 ekpsaeflaRLGerygftpPYAPghaaiasmqaictgqaRALICMGGNFALAMPDREASAVPLTQLDLAVHVatklNRSH 497
Cdd:cd02759 324 ---------LLI-------PYPV----------------KMLIVFGTNPLASYADTAPVLEALKALDFIVVV----DLFM 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 498 LLTARHS-YILPVLGRSEIDmqksgaqavtvedsmsmihasrgvlkpaGVMLKSECAVVAGIAQAtlpqsvvaweyLVED 576
Cdd:cd02759 368 TPTAMLAdIVLPVAMSLERP----------------------------GLRGGFEAENFVQLRQK-----------AVEP 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485875156 577 YDRIRNDIEAVLpEFAdynQRIrHPGGFHlinaaaERRWMT----PSGKANFITSKGLLEDPSSAF 638
Cdd:cd02759 409 YGEAKSDYEIVL-ELG---KRL-GPEEAE------YYKYEKgllrPDGQPGFNTPTGKVELYSTML 463
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
108-399 |
1.11e-27 |
|
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: 117.73 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKYD-AVSDCYKPLSWQQAFDEIGARLQSYSDPNQVE-----FYTSGRTSNEAAFLYQLFAREYGSNNF-PDCSN 180
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKEIKAEYGPEsilpySYAGTMGLLQRAARGRFFHALGASELRgTICSG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 181 MCHEPTSVGLAASIGVgkgtvLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERglerfTApqnp 260
Cdd:cd02766 135 AGIEAQKYDFGASLGN-----DPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTA-----TA---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 261 femltnsetQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERI 340
Cdd:cd02766 201 ---------ARADLHIQIRPGTDGALALGVAKVLFREG----------LYDRDFLARHTEGFEELKAHLETYTPEWAAEI 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 485875156 341 SGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGI 399
Cdd:cd02766 262 TGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
107-522 |
1.30e-26 |
|
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: 113.93 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 107 GRLTQPLKYDAV--SDCYKPLSWQQAFDEIGARLQSYSD--PNQVEFYTSGRTSNEAAFlyQLFAREYGSNNFPDCSNMC 182
Cdd:cd02755 54 DRLKKPLIRVGErgEGKFREASWDEALQYIASKLKEIKEqhGPESVLFGGHGGCYSPFF--KHFAAAFGSPNIFSHESTC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 183 HEPTSVGLAASIGVGkGTVLLEDFEKCDLVICIGHN--PGTNHPRMLTSLRALvKRGAKMIAINPlqergleRFtapqnp 260
Cdd:cd02755 132 LASKNLAWKLVIDSF-GGEVNPDFENARYIILFGRNlaEAIIVVDARRLMKAL-ENGAKVVVVDP-------RF------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 261 femltnSET-QLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLN--SEWkdI 337
Cdd:cd02755 197 ------SELaSKADEWIPIKPGTDLAFVLALIHVLISEN----------LYDAAFVEKYTNGFELLKAHVKPytPEW--A 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 338 ERISGLSQTQIAELADAY-TAAERTIICYG-MGI-TQHEHGTQNVQQLVNLLLmkGNIGKPGaGICPLRGHSnvqgdrtv 414
Cdd:cd02755 259 AQITDIPADTIRRIAREFaAAAPHAVVDPGwRGTfYSNSFQTRRAIAIINALL--GNIDKRG-GLYYAGSAK-------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 415 gitekpsaeflarlgerygftpPYapghaaiasmqaictgQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLN 494
Cdd:cd02755 328 ----------------------PY----------------PIKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPS 369
|
410 420 430
....*....|....*....|....*....|.
gi 485875156 495 rSHLLTArhSYILP---VLGRSEIDMQKSGA 522
Cdd:cd02755 370 -DTALYA--DVILPeatYLERDEPFSDKGGP 397
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
122-412 |
2.42e-25 |
|
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: 111.55 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 122 YKPLSWQQAFDEIGARLQSYSDpnqvefyTSGrtsNEAaflyqLFAREYG---SNNFPDCSNMCHE-------------P 185
Cdd:cd02751 73 FVRISWDEALDLVASELKRIRE-------KYG---NEA-----IFGGSYGwasAGRLHHAQSLLHRflnliggylgsygT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 186 TSVGLAA--------SIGVGKGTVLLED-FEKCDLVICIGHNPGTN--------HPRMLTSLRALVKRGAKMIAINPLQE 248
Cdd:cd02751 138 YSTGAAQvilphvvgSDEVYEQGTSWDDiAEHSDLVVLFGANPLKTrqgggggpDHGSYYYLKQAKDAGVRFICIDPRYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 249 RGLERFTAPQNPfemltnsetqlasayynVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRD 328
Cdd:cd02751 218 DTAAVLAAEWIP-----------------IRPGTDVALMLAMAHTLITED----------LHDQAFLARYTVGFDEFKDY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 329 VL--------NSEWKdiERISGLSQTQIAELADAYtAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGIC 400
Cdd:cd02751 271 LLgesdgvpkTPEWA--AEITGVPAETIRALAREI-ASKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFG 347
|
330
....*....|..
gi 485875156 401 PLRGHSNVQGDR 412
Cdd:cd02751 348 FGYGYSNGGGPP 359
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
108-508 |
1.76e-24 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 105.95 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKYDAVSDcYKPLSWQQAFDEIGARLQSY-----SDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNF---PDCS 179
Cdd:pfam00384 1 RLKYPMVRRGDGK-FVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 180 NMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINPlqergleRFTApq 258
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRkAALKGKAKVIVIGP-------RLDL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 259 npfemltnsetQLASAYYNVRIGGDMALLKGMMrllierddaasaagrpsllddefiqtHTVgfdelrrdvlnsewkdie 338
Cdd:pfam00384 151 -----------TYADEHLGIKPGTDLALALAGA--------------------------HVF------------------ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 339 risglsqtqIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVqgdrtvgite 418
Cdd:pfam00384 176 ---------IKELKKDKDFAPKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA---------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 419 kpsAEFLARLGEryGFTPPYapghAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAV----HVATKln 494
Cdd:pfam00384 237 ---ASPVGALDL--GLVPGI----KSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDK-- 305
|
410
....*....|....*
gi 485875156 495 rshllTARHS-YILP 508
Cdd:pfam00384 306 -----TAKYAdVILP 315
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
108-396 |
1.97e-21 |
|
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: 99.72 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKYDAV--SDCYKPLSWQQAFDEI--GARL---------------QSYSDPNQVEF--------YTSGRTSNEAA 160
Cdd:cd02758 83 RVLQPLKRVGPrgSGKWKPISWEQLIEEVveGGDLfgeghveglkairdlDTPIDPDHPDLgpkanqllYTFGRDEGRTP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 161 FLYQLFAREYGSNNFPDCSNMCHEPTSVG-LAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMltslralvKRGAK 239
Cdd:cd02758 163 FIKRFANQAFGTVNFGGHGSYCGLSYRAGnGALMNDLDGYPHVKPDFDNAEFALFIGTSPAQAGNPF--------KRQAR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 240 MIAiNPLQERGLERFTApqNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERD------------DAASAAGRP 307
Cdd:cd02758 235 RLA-EARTEGNFKYVVV--DPVLPNTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENErynaeylsipskEAAKAAGEP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 308 SLLDdefiQTHTV-------GFDELRRDVLNSEWKDIERISGLSQTQIAELADAYTAAER--TIICYgmGITQHEHGTQN 378
Cdd:cd02758 312 SWTN----ATHLVitvrvksALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRaaAVVHH--GGTMHSNGFYN 385
|
330
....*....|....*...
gi 485875156 379 VQQLVNLLLMKGNIGKPG 396
Cdd:cd02758 386 AYAIRMLNALIGNLNWKG 403
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
207-399 |
5.75e-20 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always 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. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 94.64 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 207 EKCDLVICIGHNP---------GTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTApqnpfemltnseTQLAsayyn 277
Cdd:cd02769 169 EHTELVVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPLRDDTAAELGA------------EWIA----- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 278 VRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVL--------NSEWKdiERISGLSQTQIA 349
Cdd:cd02769 232 IRPGTDVALMLALAHTLVTEG----------LHDKAFLARYTVGFDKFLPYLLgesdgvpkTPEWA--AAICGIPAETIR 299
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 485875156 350 ELADAYtAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGI 399
Cdd:cd02769 300 ELARRF-ASKRTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGF 348
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
108-417 |
3.69e-18 |
|
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: 88.92 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKY--DAVSDCYKPLSWQQAFDEIGARLQSYSDP--NQVEFYTSG--------RTSNEAAFLYQLFA------RE 169
Cdd:cd02770 59 RLKYPMKRvgKRGEGKFVRISWDEALDTIASELKRIIEKygNEAIYVNYGtgtyggvpAGRGAIARLLNLTGgylnyyGT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 170 YGSNNFPDcsnmcheptsvGLAASIGVGKGTVLLEDFEKCDLVICIGHNP--------GTNHprmltSLRALVKRGAKMI 241
Cdd:cd02770 139 YSWAQITT-----------ATPYTYGAAASGSSLDDLKDSKLVVLFGHNPaetrmgggGSTY-----YYLQAKKAGAKFI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 242 AINPlqergleRFtapqnpfemlTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVG 321
Cdd:cd02770 203 VIDP-------RY----------TDTAVTLADEWIPIRPGTDAALVAAMAYVMITEN----------LHDQAFLDRYCVG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 322 FDE------------LRRDVL---------NSEWKdiERISGLSQTQIAELADAYTAAERTIICYGMGITQHEHGTQNVQ 380
Cdd:cd02770 256 FDAehlpegappnesYKDYVLgtgydgtpkTPEWA--SEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAAR 333
|
330 340 350
....*....|....*....|....*....|....*..
gi 485875156 381 QLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGIT 417
Cdd:cd02770 334 AIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGK 370
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
108-521 |
1.28e-15 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 80.87 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKY--DAVSDCYKPLSWQQAFDEIGARL----QSYSdPNQVEFytSGRTSNEAAFLYQlFAREYGS-NNFPDCSN 180
Cdd:PRK15488 98 RIVKPLKRvgERGEGKWQEISWDEAYQEIAAKLnaikQQHG-PESVAF--SSKSGSLSSHLFH-LATAFGSpNTFTHAST 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 181 mChePTSVGLAASigVGKGTVLLEDFEKCDLVICIGHN--PGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApq 258
Cdd:PRK15488 174 -C--PAGYAIAAK--VMFGGKLKRDLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------RFSV-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 259 npfemltnsETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDV--LNSEWKd 336
Cdd:PRK15488 240 ---------VASKADEWHAIRPGTDLAVVLALCHVLIEEN----------LYDKAFVERYTSGFEELAASVkeYTPEWA- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 337 iERISGLSQTQIAELADA-YTAAERTIICYG--MGITQHEHGTQNVQQLVNLLLmkGNI--------GKPGAGICPLRGH 405
Cdd:PRK15488 300 -EAISDVPADDIRRIARElAAAAPHAIVDFGhrATFTPEEFDMRRAIFAANVLL--GNIerkgglyfGKNASVYNKLAGE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 406 SNVQGDRTVGITE--KPSAEFLARLGERYGFTppyAPGHAAIASM-QAICTG---QARALICMGGNFALAMPDREASAVP 479
Cdd:PRK15488 377 KVAPTLAKPGVKGmpKPTAKRIDLVGEQFKYI---AAGGGVVQSIiDATLTQkpyQIKGWVMSRHNPMQTVTDRADVVKA 453
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 485875156 480 LTQLDLAVHVATKLNRShllTARHSYILP---VLGRSEIDMQKSG 521
Cdd:PRK15488 454 LKKLDLVVVCDVYLSES---AAYADVVLPestYLERDEEISDKSG 495
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
108-257 |
1.45e-15 |
|
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: 79.25 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARLQSySDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFpDCSNMCHEPTS 187
Cdd:cd02768 54 RLTQPLI--KKGGKLVPVSWEEALKTVAEGLKA-VKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNI-DHRLRQSDLPA 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 485875156 188 VGLAASIGVGkgTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINPLQERGLERFTAP 257
Cdd:cd02768 130 DNRLRGNYLF--NTSIAEIEEADAVLLIGSNLRKEAPLLNARLRkAVKKKGAKIAVIGPKDTDLIADLTYP 198
|
|
| 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 ... |
108-477 |
7.07e-14 |
|
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: 74.73 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARLQSYSDpnQVEFYTSGRTSNEAAFLYQLFAREY-GSNNFpDCSNMCHept 186
Cdd:cd02771 54 RLTQPLI--RRGGTLVPVSWNEALDVAAARLKEAKD--KVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRARRL--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 187 svgLAASIGVGKG-TVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIA----INPLQERGLERFT-APQNP 260
Cdd:cd02771 126 ---IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAalsgIPKWQDAAVRNIAqGAKSP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 261 FEMLTNSETQL---ASAYYNVRIGGDMALLKGMMRLLierddAASAAGRPSLLDDEFIQThtvgfdelrrdvlnsewkdi 337
Cdd:cd02771 203 LFIVNALATRLddiAAESIRASPGGQARLGAALARAV-----DASAAGVSGLAPKEKAAR-------------------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 338 erisglsqtqiaeLADAYTAAERTIICYGmgitQHEHGTQNVQQLVNLLLMKGNIGKpGAGICPLRGHSNVQGdrtvgit 417
Cdd:cd02771 258 -------------IAARLTGAKKPLIVSG----TLSGSLELIKAAANLAKALKRRGE-NAGLTLAVEEGNSPG------- 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 418 ekpsaefLARLGerygfTPPYAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASA 477
Cdd:cd02771 313 -------LLLLG-----GHVTEPGLDLDGALAALEDGSADALIVLGNDLYRSAPERRVEA 360
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
108-396 |
8.08e-13 |
|
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: 71.79 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPL--KYDAVSDCYKPLSWQQAFDEIGARLQSY--SDPNQVEFYTsGRTSNEAafLYQLFAREYGSNNFPDCSNMCh 183
Cdd:cd02763 54 RLTKPLlrKGPRGSGQFEEIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFC- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 184 eptSVGLAASIGVGKGTVLLE----DFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQerglerftapqn 259
Cdd:cd02763 130 ---SVNMAAGGLYSIGGSFWEfggpDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVR------------ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 260 pfemltNSETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTvgfdelrrdvlNSEW----- 334
Cdd:cd02763 195 ------TGYAAIADEWVPIKPGTDGAFILALAHELLKAG----------LIDWEFLKRYT-----------NAAElvdyt 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 335 -KDIERISGLSQTQIAELAD--AYTAAERTII-------CYGM----------------GITQHEHGTQNVQQLVNLLLM 388
Cdd:cd02763 248 pEWVEKITGIPADTIRRIAKelGVTARDQPIElpiawtdVWGRkhekitgrpvsfhamrGIAAHSNGFQTIRALFVLMML 327
|
....*...
gi 485875156 389 KGNIGKPG 396
Cdd:cd02763 328 LGTIDRPG 335
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
123-410 |
4.29e-12 |
|
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: 68.90 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 123 KPLSWQQAFDEIGARLQSYSDPnqvEFYTSGRTSNEA-AFLYQLfaREYGSNNFPDCSNMCHEPTSVGLAASiGVgKGTV 201
Cdd:cd02761 52 KPVSLEEAIEKAAEILKEAKRP---LFYGLGTTVCEAqRAGIEL--AEKLGAIIDHAASVCHGPNLLALQDS-GW-PTTT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 202 LLEDFEKCDLVICIGHNPGTNHPRMLtSLRALVKRGAkmiainpLQERGLERFTApqnpfemltnsetqlasayynVRIG 281
Cdd:cd02761 125 LGEVKNRADVIVYWGTNPMHAHPRHM-SRYSVFPRGF-------FREGGREDRTL---------------------IVVD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 282 GdmallkgmmrllieRDDAASAAGrpslldDEFIQT---HTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYTAA 358
Cdd:cd02761 176 P--------------RKSDTAKLA------DIHLQIdpgSDYELLAALRALLRGAGLVPDEVAGIPAETILELAERLKNA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 485875156 359 ERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKpgAGICPLRGHSNVQG 410
Cdd:cd02761 236 KFGVIFWGLGLLPSRGAHRNIEAAIRLVKALNEYTK--FALLPLRGHYNVRG 285
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
108-404 |
3.77e-09 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 59.76 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLK------YDAVSDCYKPLSWQQAFDEIGARLQSYSDPN-QVEF-YTSGRTSNEAAFLYQLFAREYGSNNFPDCS 179
Cdd:cd02757 56 RILYPMKrtnprkGRDVDPKFVPISWDEALDTIADKIRALRKENePHKImLHRGRYGHNNSILYGRFTKMIGSPNNISHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 180 NMCHEPTSVGLAAS-IGVGKGTVlleDFEKCDLVICIGHNP-GTNHP-----RMLTSLRAlvkrGAKMIAINPlqergle 252
Cdd:cd02757 136 SVCAESEKFGRYYTeGGWDYNSY---DYANAKYILFFGADPlESNRQnphaqRIWGGKMD----QAKVVVVDP------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 253 RFTA----PQNPFEMLTNSETQLASAYYNVRIGGDmALLKGMMRLLIE-RDDAasAAGRPsLLDDEFIQTHTVGFDELrr 327
Cdd:cd02757 202 RLSNtaakADEWLPIKPGEDGALALAIAHVILTEG-LWDKDFVGDFVDgKNYF--KAGET-VDEESFKEKSTEGLVKW-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 328 dvLNSEWKD-----IERISGLSQTQIAELADAYTAAERTIICY-GMGITQHEHGTQNVQQLVNLLLMKGNIGKPGaGICP 401
Cdd:cd02757 276 --WNLELKDytpewAAKISGIPAETIERVAREFATAAPAAAAFtWRGATMQNRGSYNSMACHALNGLVGSIDSKG-GLCP 352
|
...
gi 485875156 402 LRG 404
Cdd:cd02757 353 NMG 355
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
309-399 |
6.06e-09 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 59.68 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 309 LLDDEFIQTHTVGFDELRRDVL--------NSEWKdiERISGLSQTQIAELADAyTAAERTIICYGMGITQHEHGTQNVQ 380
Cdd:PRK15102 299 LYDKKFIDNYCLGFEQFLPYLLgekdgvpkTPEWA--EKICGIDAETIRELARQ-MAKGRTQIIAGWCIQRQQHGEQPYW 375
|
90
....*....|....*....
gi 485875156 381 QLVNLLLMKGNIGKPGAGI 399
Cdd:PRK15102 376 MGAVLAAMLGQIGLPGGGI 394
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
266-399 |
9.00e-09 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 58.48 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 266 NSETQLASAYYNVRIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTvgfdELRRDVLNSEWKdiERISGLSQ 345
Cdd:cd02750 210 SPSAKHADLWVPIKPGTDAALALAMAHVIIKE----------KLYDEDYLKEYT----DLPFLVYTPAWQ--EAITGVPR 273
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 485875156 346 TQIAELADAYTAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGI 399
Cdd:cd02750 274 ETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGW 327
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
103-246 |
3.09e-07 |
|
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: 53.51 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 103 LEAAGRLTQPL-KYDAVsdcYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFP-- 176
Cdd:cd02772 49 LNSEDRLTKPMiKKDGQ---WQEVDWETALEYVAEGLSAIIKkhgADQIGALASPHSTLEELYLLQKLARGLGSDNIDhr 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485875156 177 ----DCSNMCHEPTSVGLAASIgvgkgtvllEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPL 246
Cdd:cd02772 126 lrqsDFRDDAKASGAPWLGMPI---------AEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPA 190
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
122-426 |
5.18e-07 |
|
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: 53.25 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 122 YKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSgrtSNEAAFLYQLFAREYGSNnfpdcsnmchEPTSVGLAASIGVGK 198
Cdd:cd02765 71 FERITWDEALDTIADKLTEAKReygGKSILWMSS---SGDGAILSYLRLALLGGG----------LQDALTYGIDTGVGQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 199 GTVLL------------EDFEKCDLVICIGHNPGTNHprmLTSLRALVK---RGAKMIAINPLQerglerftapqnpfem 263
Cdd:cd02765 138 GFNRVtgggfmpptneiTDWVNAKTIIIWGSNILETQ---FQDAEFFLDareNGAKIVVIDPVY---------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 264 ltNSETQLASAYYNVRIGGDMALLKGMMRLLIERD-------DAASAAG-----------RPSLLDDEFIQTHTVGFDEL 325
Cdd:cd02765 199 --STTAAKADQWVPIRPGTDPALALGMINYILEHNwydeaflKSNTSAPflvredngtllRQADVTATPAEDGYVVWDTN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 326 RRDV-----------LNSEW-----------------------KDIERISGLSQTQIAELADAYTAAERTIICYGMGITQ 371
Cdd:cd02765 277 SDSPepvaatninpaLEGEYtingvkvhtvltalreqaasyppKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDR 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485875156 372 HEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRG----HSNVQG---DRTVGITEKPSAEFLA 426
Cdd:cd02765 357 YYHSHVFGRTAAILAALTGNIGRVGGGVGQIKFmyfmGSNFLGnqpDRDRWLKVMKNLDFIV 418
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
649-749 |
6.56e-07 |
|
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: 48.08 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 649 SHDQYNTTIYGMDDRYRGVFGqRDVVFMSAKQAKICRVKNGERVNLIalTPDGK-----RSSRRMDRlKVVIYPMADRSL 723
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAP-EPVVEINPEDAAALGIKDGDLVRVE--SRRGSvvlraKVTDGVPP-GVVFLPHGWGHR 76
|
90 100
....*....|....*....|....*.
gi 485875156 724 VTYFPESNHmLTLDNHDPLSGIPGYK 749
Cdd:cd02775 77 GGRGGNANV-LTPDALDPPSGGPAYK 101
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
108-398 |
7.79e-07 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 52.59 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPL------KYDAVSDcYKPLSWQQAFDEIGARLQSY---SDPNQVEFYTSGR-TSNEAAFLYQLFAREYGSNNFPD 177
Cdd:PRK13532 97 RLTQPLlrmkdgKYDKEGE-FTPVSWDQAFDVMAEKFKKAlkeKGPTAVGMFGSGQwTIWEGYAASKLMKAGFRSNNIDP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 178 CSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSL--RALVKRGAKMIAINPLQERGLErft 255
Cdd:PRK13532 176 NARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVtdRRLSNPDVKVAVLSTFEHRSFE--- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 256 apqnpfemltnsetqLASAYYNVRIGGDMALLKGMMRLLIERDDaasaagrpslLDDEFIQTHTV--------------- 320
Cdd:PRK13532 253 ---------------LADNGIIFTPQTDLAILNYIANYIIQNNA----------VNWDFVNKHTNfrkgatdigyglrpt 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 321 -------------------GFDELRRDVLNSEWKDIERISGLSQTQIAELADAYTAAERTIICY-GMGITQHEHGTQNVQ 380
Cdd:PRK13532 308 hplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVSFwTMGFNQHTRGVWANN 387
|
330
....*....|....*...
gi 485875156 381 QLVNLLLMKGNIGKPGAG 398
Cdd:PRK13532 388 LVYNIHLLTGKISTPGNG 405
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
300-405 |
4.06e-06 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 50.17 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 300 AASAAGRPSLLddeFIQ----THTVGFDELRRDVL--NSEW-KDIERISGLSQTQIAELAD------AYTAAERTIICYG 366
Cdd:cd02756 287 AEAAAGKDRVL---HLQvnpgTDTALANAIARYIYesLDEVlAEAEQITGVPRAQIEKAADwiakpkEGGYRKRVMFEYE 363
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90 100 110
....*....|....*....|....*....|....*....
gi 485875156 367 MGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGH 405
Cdd:cd02756 364 KGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCVRQGGH 402
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| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
642-752 |
5.36e-05 |
|
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: 43.03 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 642 LVMATVRSHDQYNTTIYGMDDRYRGVFgQRDVVFMSAKQAKICRVKNGERVNLialtpdgkRSSRRMDRLKVVIYP-MAD 720
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLVEV--------TSRRGSVVVRAKVTDrVRP 71
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90 100 110
....*....|....*....|....*....|....*....
gi 485875156 721 RSLVTYF--PESNH-----MLTLDNHDPLSGIPGYKSIP 752
Cdd:pfam01568 72 GVVFMPFgwWYEPRggnanALTDDATDPLSGGPEFKTCA 110
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| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
98-256 |
9.52e-05 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 46.09 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 98 WGDHELEAAGRLTQPLKYDAvSDCYKPLSWQQAFDEIGARLQSYSDPnqVEFYTSGRTSNEAAFLYQLFAR-EYGSNNFp 176
Cdd:PRK07860 268 WAFTYATQPDRITTPLVRDE-DGELEPASWSEALAVAARGLAAARGR--VGVLVGGRLTVEDAYAYAKFARvALGTNDI- 343
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 177 DCSNMCHEPTSVG-LAASI-GVGKGtVLLEDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINPLQERGLER 253
Cdd:PRK07860 344 DFRARPHSAEEADfLAARVaGRGLG-VTYADLEKAPAVLLVGFEPEEESPIVFLRLRkAARKHGLKVYSIAPFATRGLEK 422
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...
gi 485875156 254 FTA 256
Cdd:PRK07860 423 MGG 425
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| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
108-245 |
3.33e-04 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase 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 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 Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 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: 239174 [Multi-domain] Cd Length: 375 Bit Score: 43.79 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 108 RLTQPLKYDavSDCYKPLSWQQAFDEIGARLQSySDPNQVEFYTSGRTSNEAAF-LYQLFAREygsnnfpDCSNMCHEPT 186
Cdd:cd02773 53 RLDKPYIRK--NGKLKPATWEEALAAIAKALKG-VKPDEIAAIAGDLADVESMVaLKDLLNKL-------GSENLACEQD 122
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485875156 187 SVGLAASIgvgKGTVLL----EDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINP 245
Cdd:cd02773 123 GPDLPADL---RSNYLFnttiAGIEEADAVLLVGTNPRFEAPVLNARIRkAWLHGGLKVGVIGP 183
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| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
642-757 |
7.23e-04 |
|
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. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 39.91 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 642 LVMATVRSHDQYNTTiyGMDDRYRG--VFGQRDVVFMSAKQAKICRVKNGERVNLialtpdgkrSSRRMdrlKVVIYPMA 719
Cdd:cd02790 5 LVLTTGRVLYHYHTG--TMTRRAEGldAIAPEEYVEINPEDAKRLGIEDGEKVRV---------SSRRG---SVEVRARV 70
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90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 485875156 720 DRSL------VTY-FPESN-HMLTLDNHDPLSGIPGYKSIPVELEP 757
Cdd:cd02790 71 TDRVpegvvfMPFhFAEAAaNLLTNAALDPVAKIPEFKVCAVRVEK 116
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| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
642-757 |
3.18e-03 |
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This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 38.26 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 642 LVMATVRSHDQYNT-----TIYGMDDRYRGVFgqrdvVFMSAKQAKICRVKNGERVNLIalTPDGK-----RSSRRMdRL 711
Cdd:cd00508 5 LVLTTGRLLEHWHTgtmtrRSPRLAALAPEPF-----VEIHPEDAARLGIKDGDLVRVS--SRRGSvvvraRVTDRV-RP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 485875156 712 KVVIYPMADRSLVTyfPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
Cdd:cd00508 77 GTVFMPFHWGGEVS--GGAANALTNDALDPVSGQPEFKACAVRIEK 120
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| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
673-757 |
4.05e-03 |
|
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. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 37.94 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485875156 673 VVFMSAKQAKICRVKNGERVNLialtpdgkrSSRRMD---RLKV--------VIYPMADRSLVTYFPESNHmLTLDNHDP 741
Cdd:cd02791 36 YVEIHPEDAARLGLKEGDLVRV---------TSRRGEvvlRVRVtdrvrpgeVFVPMHWGDQFGRSGRVNA-LTLDATDP 105
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90
....*....|....*.
gi 485875156 742 LSGIPGYKSIPVELEP 757
Cdd:cd02791 106 VSGQPEFKHCAVRIEK 121
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