|
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 16129460 1 MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDK 80
Cdd:PRK09939 1 MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 81 QVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAA 160
Cdd:PRK09939 81 QVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 161 FLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKM 240
Cdd:PRK09939 161 FLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 241 IAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTV 320
Cdd:PRK09939 241 IAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 321 GFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGIC 400
Cdd:PRK09939 321 GFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGIC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 401 PLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPL 480
Cdd:PRK09939 401 PLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 481 TQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKNGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQ 560
Cdd:PRK09939 481 TQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 561 AALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNS 640
Cdd:PRK09939 561 AALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 641 KLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMAD 720
Cdd:PRK09939 641 KLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMAD 720
|
730 740 750
....*....|....*....|....*....|....*....
gi 16129460 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: 1264.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 11 AAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPD-PKHSASFDICENGAKAIAWEVTDKQVNASFFAE 89
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVsPQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 90 NTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYsDPNQVEFYTSGRTSNEAAFLYQLFARE 169
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSL-DPKQVAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 170 YGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQER 249
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 250 GLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASaagrPSLLDDEFIQTHTVGFDELRRDV 329
Cdd:TIGR01701 240 GLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQP----GSLIDHEFIANHTNGFDELRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 330 LNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQ 409
Cdd:TIGR01701 316 LQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 410 GDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHV 489
Cdd:TIGR01701 396 GDRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 490 ATKLNRSHLLTARHSYILPVLGRSEIDMQKNGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVA 569
Cdd:TIGR01701 476 ATKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 570 WEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAA-ERRWMTPSGKANFITSKGLLEDPSSAFNSKLVMATVR 648
Cdd:TIGR01701 556 WEILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAALcERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 649 SHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGkrSSRRMDRLKVVIYPMADRSLVTYFP 728
Cdd:TIGR01701 636 SHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDG--QKRKFDNLRIVFYDTPTGNAAAYYP 713
|
730 740 750
....*....|....*....|....*....|
gi 16129460 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: 968.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 46 GFDCPGCAWPDPKHS-ASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKP 124
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 125 LSWQQAFDEIGARLQSYsDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLE 204
Cdd:cd02767 81 ISWDEAFAEIAARLRAL-DPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 205 DFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTnSETQLASAYYNVRIGGDM 284
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 285 ALLKGMMRLLIERDDAasaagRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIIC 364
Cdd:cd02767 239 ALLNGMAKHLIERDDE-----PGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 365 YGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAA 444
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 445 IASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKNGAQA 524
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 525 VTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAVLPE-FADYNQRIRHPGG 603
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYEgFADFNQRGDQPGG 553
|
570 580
....*....|....*....|.
gi 16129460 604 FHLINAAAERRWMTPSGKANF 624
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQF 574
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
99-757 |
6.13e-150 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 453.15 E-value: 6.13e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 99 GDHELEAAGRLTQPLKYDAV--SDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSG----RTSNEAAFLYQLFARE 169
Cdd:COG0243 69 LDERLYSPDRLTYPMKRVGPrgSGKFERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsagRLSNEAAYLAQRFARA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 170 YGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINPLQE 248
Cdd:COG0243 149 LGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLReAAKKRGAKIVVIDPRRT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 249 RGlerftapqnpfemltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRD 328
Cdd:COG0243 229 ET------------------AAIADEWLPIRPGTDAALLLALAHVLIEEG----------LYDRDFLARHTVGFDELAAY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 329 VLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHsnv 408
Cdd:COG0243 281 VAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE--- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 409 qgdrtvGITEkpsaeflarlGERYgftpphapghaaiasmqaictgQARALICMGGNFALAMPD----REAsavpLTQLD 484
Cdd:COG0243 358 ------AILD----------GKPY----------------------PIKALWVYGGNPAVSAPDtnrvREA----LRKLD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 485 LAVHVATKLNRSHLLTArhsYILPVLGRSEIDMqkngaQAVTVEDsmSMIHASRGVLKPAGvMLKSECAVVAGIAQAALP 564
Cdd:COG0243 396 FVVVIDTFLTETARYAD---IVLPATTWLERDD-----IVTNSED--RRVHLSRPAVEPPG-EARSDWEIFAELAKRLGF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 565 QSVVAWEYLVEDY--DRIRNDIEAVLPeFADYNQRirhpGGFHLINA-----AAERRWMTPSGKANFiTSKGLLEDPSSA 637
Cdd:COG0243 465 EEAFPWGRTEEDYlrELLEATRGRGIT-FEELREK----GPVQLPVPpepafRNDGPFPTPSGKAEF-YSETLALPPLPR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 638 FNSK------------LVMATVRSHDQYNTTIYGmDDRYRGVFGqRDVVFMSAKQAKICRVKNGERVNLialtpdgkrSS 705
Cdd:COG0243 539 YAPPyegaepldaeypLRLITGRSRDQWHSTTYN-NPRLREIGP-RPVVEINPEDAAALGIKDGDLVRV---------ES 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129460 706 RR---------MDRLK--VVIYPMADRSLVTYFPESNH-MLTLDNHDPLSGIPGYKSIPVELEP 757
Cdd:COG0243 608 DRgevlarakvTEGIRpgVVFAPHGWWYEPADDKGGNVnVLTPDATDPLSGTPAFKSVPVRVEK 671
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
98-757 |
4.02e-105 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 336.86 E-value: 4.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 98 WGDHELEAAGRLTQPLKYDavSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREY-GSN 173
Cdd:COG3383 51 FGFEFVNSPDRLTTPLIRR--GGEFREVSWDEALDLVAERLREIQAehgPDAVAFYGSGQLTNEENYLLQKLARGVlGTN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 174 NFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleR 253
Cdd:COG3383 129 NIDNNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-------R 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 254 FTAPqnpfemltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSE 333
Cdd:COG3383 202 RTET-----------ARLADLHLQIKPGTDLALLNGLLHVIIEEG----------LVDEDFIAERTEGFEELKASVAKYT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 334 WKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRT 413
Cdd:COG3383 261 PERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 414 VGI--TEKP------SAEFLARLGERYGFTP-PHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
Cdd:COG3383 341 MGAlpNVLPgyrdvtDPEHRAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 485 LAVHVATKLNRshllTARHS-YILPVLGRSEidmqKNGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQAAl 563
Cdd:COG3383 421 FLVVQDIFLTE----TAEYAdVVLPAASWAE----KDG----TFTNTERRVQRVRKAVEPPG-EARPDWEIIAELARRL- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 564 pqsVVAWEYlvEDYDRIRNDIEAVLPEFA--DYnQRIRHPGGFHLINAAAER---------RWMTPSGKANFI--TSKGL 630
Cdd:COG3383 487 ---GYGFDY--DSPEEVFDEIARLTPDYSgiSY-ERLEALGGVQWPCPSEDHpgtprlftgRFPTPDGKARFVpvEYRPP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 631 LEDPSSAFNskLVMATVRSHDQYNT-TIYGMDDRYRGVFGqRDVVFMSAKQAKICRVKNGERVNLialtpdgkrSSRRMD 709
Cdd:COG3383 561 AELPDEEYP--LVLTTGRLLDQWHTgTRTRRSPRLNKHAP-EPFVEIHPEDAARLGIKDGDLVRV---------SSRRGE 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 16129460 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 |
4.23e-80 |
|
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: 270.11 E-value: 4.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARL---QSYSDPNQVEFYTSGRTSNEAAFLYQLFARE-YGSNNFPDCSNMCH 183
Cdd:TIGR01591 53 RLTTPLI--REGDKFREVSWDEAISYIAEKLkeiKEKYGPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 184 EPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTapqnpfem 263
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-------RKT-------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 264 ltnsET-QLASAYYNVRIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISG 342
Cdd:TIGR01591 196 ----ETaKIADLHIPLKPGTDIALLNAMANVIIEE----------GLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 343 LSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI--TEKP 420
Cdd:TIGR01591 262 VPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGAlpDFLP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 421 ------SAEFLARLGERYGFTP-PHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKL 493
Cdd:TIGR01591 342 gyqpvsDEEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 494 NRshllTARHS-YILPVLGRSEidmqKNGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQA-ALPqsvvaWE 571
Cdd:TIGR01591 422 TE----TAKYAdVVLPAAAWLE----KEG----TFTNAERRIQRFFKAVEPKG-ESKPDWEIIQELANAlGLD-----WN 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 572 YlvEDYDRIRNDIEAVLPEFADYN----------QRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSK 641
Cdd:TIGR01591 484 Y--NHPQEIMDEIRELTPLFAGLTyerldelgslQWPCNDSDASPTSYLYKDKFATPDGKAKFIPLEWVAPIEEPDDEYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 642 LVMATVRSHDQYNTTiyGMDDRYRGV--FGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKV-VIY-P 717
Cdd:TIGR01591 562 LILTTGRVLTHYNVG--EMTRRVAGLrrLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVNKgAIYiT 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 16129460 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 |
4.16e-76 |
|
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: 254.83 E-value: 4.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFARE-YGSNNFPDCSNMCH 183
Cdd:cd02753 54 RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 184 EPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTapqnpfEM 263
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-------RRT------EL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 264 ltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGL 343
Cdd:cd02753 199 -----ARFADLHLQLRPGTDVALLNAMAHVIIEEG----------LYDEEFIEERTEGFEELKEIVEKYTPEYAERITGV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 344 SQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGdrtvgitekpSAE 423
Cdd:cd02753 264 PAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQG----------ACD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 424 FlarlgeryGFTPPHAPGHaaiasmqaictgqARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRshllTARH 503
Cdd:cd02753 334 M--------GALPNVLPGY-------------VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTE----TAEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 504 S-YILPVLGRSEidmqKNGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQAA-LPqsvvaWEYL-VEDydrI 580
Cdd:cd02753 389 AdVVLPAASFAE----KDG----TFTNTERRVQRVRKAVEPPG-EARPDWEIIQELANRLgYP-----GFYShPEE---I 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129460 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 |
1.25e-63 |
|
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: 217.20 E-value: 1.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 103 LEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCS 179
Cdd:cd00368 49 LYSPDRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIREkygPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 180 NMCHEPTSVGLAAsIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGlerftapqn 259
Cdd:cd00368 129 RLCHASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTET--------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 260 pfemltnseTQLASAYYNVRIGGDMALLKGmmrllierddaasaagrpsllddefiqthtvgfdelrrdvlnsEWkdIER 339
Cdd:cd00368 199 ---------AAKADEWLPIRPGTDAALALA-------------------------------------------EW--AAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 340 ISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPlrghsnvqgdrtvgitek 419
Cdd:cd00368 225 ITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP------------------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 420 psaeflarlgerygftpphapghaaiasmqaictgqaralicmGGNFALAMPDREASAVPLTQLDLAVHVATKLNRshll 499
Cdd:cd00368 287 -------------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTE---- 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129460 500 TARHS-YILPVLGRSEidmqKNGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQA 561
Cdd:cd00368 320 TAAYAdVVLPAATYLE----KEG----TYTNTEGRVQLFRQAVEPPG-EARSDWEILRELAKR 373
|
|
| 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 16129460 642 LVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRssRRMDRLKVVIYPMADR 721
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQG--RIVRGFRVVEYDIPRG 78
|
90 100 110
....*....|....*....|....*....|....
gi 16129460 722 SLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVEL 755
Cdd:cd02787 79 CLAAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
103-561 |
3.13e-50 |
|
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: 185.12 E-value: 3.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 103 LEAAGRLTQPLkYDAVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREY-GSNNFPDC 178
Cdd:cd02754 49 LNGPERLTRPL-LRRNGGELVPVSWDEALDLIAERFKAIQAeygPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 179 SNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSL--RALVKRGAKMIAINPlqergleRFTA 256
Cdd:cd02754 128 SRLCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLldRKKANPGAKIIVVDP-------RRTR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 257 PqnpfemltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKD 336
Cdd:cd02754 201 T-----------ADIADLHLPIRPGTDLALLNGLLHVLIEEG----------LIDRDFIDAHTEGFEELKAFVADYTPEK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 337 IERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVG- 415
Cdd:cd02754 260 VAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGg 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 416 ----------ITEKPSAEFLARL-GERYGFTPPhAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
Cdd:cd02754 340 lanllpghrsVNNPEHRAEVAKFwGVPEGTIPP-KPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLE 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129460 485 LAVhVATKLNRSHllTARHS-YILPVLGRSEidmqKNGaqavTVEDSMSMIHASRGVLKPAGvMLKSECAVVAGIAQA 561
Cdd:cd02754 419 FVV-VQDAFADTE--TAEYAdLVLPAASWGE----KEG----TMTNSERRVSLLRAAVEPPG-EARPDWWILADVARR 484
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
108-410 |
8.84e-40 |
|
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: 156.02 E-value: 8.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVE---------------FYTSGRTSNEAAFLYQLFAREYGS 172
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRDASFVEknaagvvvnrpdsiaFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 173 NNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHP-RMLTSLRALVKRGAKMIAINPlqergl 251
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 252 eRFTApqnpfemlTNSEtqlASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrPsllddefiqthtvgfdelrrdvln 331
Cdd:cd02752 208 -RFTR--------TAAK---ADLYVPIRSGTDIAFLGGMINYIIRYT--------P------------------------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 332 sewKDIERISGLSQTQIAELADAYAAAER-----TIIcYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHS 406
Cdd:cd02752 244 ---EEVEDICGVPKEDFLKVAEMFAATGRpdkpgTIL-YAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHS 319
|
....
gi 16129460 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 |
3.96e-31 |
|
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: 128.67 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKYDAvsDCYKPLSWQQAFDEIGARL---QSYSDPNQVEFYTSGRTSNEAA-------FLYQLFAREYGSNNFPD 177
Cdd:cd02762 54 RLRTPMRRRG--GSFEEIDWDEAFDEIAERLraiRARHGGDAVGVYGGNPQAHTHAggayspaLLKALGTSNYFSAATAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 178 csNMCHEPTSVGLAASigvgKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTS------LRALVKRGAKMIAINPlqergl 251
Cdd:cd02762 132 --QKPGHFWSGLMFGH----PGLHPVPDIDRTDYLLILGANPLQSNGSLRTApdrvlrLKAAKDRGGSLVVIDP------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 252 erftapqnpfemlTNSET-QLASAYYNVRIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVL 330
Cdd:cd02762 200 -------------RRTETaKLADEHLFVRPGTDAWLLAAMLAVLLAE----------GLTDRRFLAEHCDGLDEVRAALA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 331 NSEWKDIERISGLSQTQIAELADAYAAAeRTIICYG-MGITQHEHGTQNvQQLVNLL-LMKGNIGKPGAGIC-----PLR 403
Cdd:cd02762 257 EFTPEAYAPRCGVPAETIRRLAREFAAA-PSAAVYGrLGVQTQLFGTLC-SWLVKLLnLLTGNLDRPGGAMFttpalDLV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 404 GHSnvqGDRTVGITEKPSAefLARLGERYGFTPPhapghAAIAsmQAICT---GQARALICMGGNFALAMPDREASAVPL 480
Cdd:cd02762 335 GQT---SGRTIGRGEWRSR--VSGLPEIAGELPV-----NVLA--EEILTdgpGRIRAMIVVAGNPVLSAPDGARLEAAL 402
|
410 420 430
....*....|....*....|....*....|....*
gi 16129460 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 |
2.71e-25 |
|
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: 110.09 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKY--DAVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFY-TSGRTSNEAAFLYQL-FAREYGSNNFPDCSN 180
Cdd:cd02759 54 RLLYPLKRvgERGENKWERISWDEALDEIAEKLAEIKAeygPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 181 MCHEPTSVGLAASIGVGkGTVLLEDFEKCDLVICIGHNPG-TNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApqn 259
Cdd:cd02759 134 SCYWPRDMAHALTTGFG-LGYDEPDWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDP-------RLTW--- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 260 pfemltnsETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDV--LNSEWkdI 337
Cdd:cd02759 203 --------LAARADLWLPIRPGTDAALALGMLNVIINEG----------LYDKDFVENWCYGFEELAERVqeYTPEK--V 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 338 ERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGicplrghsnvqgdrtvgit 417
Cdd:cd02759 263 AEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGN------------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 418 ekpsaeflaRLGerygftpPHAPghaaiasmqaictgqaRALICMGGNFALAMPDREASAVPLTQLDLAVHVatklNRSH 497
Cdd:cd02759 324 ---------LLI-------PYPV----------------KMLIVFGTNPLASYADTAPVLEALKALDFIVVV----DLFM 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 498 LLTARHS-YILPVLGRSEIDmqkngaqavtvedsmsmihasrgvlkpaGVMLKSECAVVAGIAQAAlpqsvvaweylVED 576
Cdd:cd02759 368 TPTAMLAdIVLPVAMSLERP----------------------------GLRGGFEAENFVQLRQKA-----------VEP 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129460 577 YDRIRNDIEAVLpEFAdynQRIrHPGGFHlinaaaERRWMT----PSGKANFITSKGLLEDPSSAF 638
Cdd:cd02759 409 YGEAKSDYEIVL-ELG---KRL-GPEEAE------YYKYEKgllrPDGQPGFNTPTGKVELYSTML 463
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
108-508 |
1.43e-23 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 103.25 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKYDAVSDcYKPLSWQQAFDEIGARLQSY-----SDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNF---PDCS 179
Cdd:pfam00384 1 RLKYPMVRRGDGK-FVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 180 NMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINPlqergleRFTApq 258
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRkAALKGKAKVIVIGP-------RLDL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 259 npfemltnsetQLASAYYNVRIGGDMALLKGMMRLLIErddaasaagrpSLLDDEFIQThtvgfdelrrdvlnsewkdie 338
Cdd:pfam00384 151 -----------TYADEHLGIKPGTDLALALAGAHVFIK-----------ELKKDKDFAP--------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 339 risglsqtqiaeladayaaaeRTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVqgdrtvgite 418
Cdd:pfam00384 188 ---------------------KPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA---------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 419 kpsAEFLARLGErygftpPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAV----HVATKln 494
Cdd:pfam00384 237 ---ASPVGALDL------GLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDK-- 305
|
410
....*....|....*
gi 16129460 495 rshllTARHS-YILP 508
Cdd:pfam00384 306 -----TAKYAdVILP 315
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
107-522 |
3.05e-22 |
|
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: 100.45 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 107 GRLTQPLKYDAV--SDCYKPLSWQQAFDEIGARLQSYSD--PNQVEFYTSGRTSNEAAFlyQLFAREYGSNNFPDCSNMC 182
Cdd:cd02755 54 DRLKKPLIRVGErgEGKFREASWDEALQYIASKLKEIKEqhGPESVLFGGHGGCYSPFF--KHFAAAFGSPNIFSHESTC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 183 HEPTSVGLAASIGVGkGTVLLEDFEKCDLVICIGHN--PGTNHPRMLTSLRALvKRGAKMIAINPlqergleRFtapqnp 260
Cdd:cd02755 132 LASKNLAWKLVIDSF-GGEVNPDFENARYIILFGRNlaEAIIVVDARRLMKAL-ENGAKVVVVDP-------RF------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 261 femltnSET-QLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLN--SEWkdI 337
Cdd:cd02755 197 ------SELaSKADEWIPIKPGTDLAFVLALIHVLISEN----------LYDAAFVEKYTNGFELLKAHVKPytPEW--A 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 338 ERISGLSQTQIAELADAYAAAERTIICY-G-MGI-TQHEHGTQNVQQLVNLLLmkGNIGKPGaGICplrghsnvqgdrtv 414
Cdd:cd02755 259 AQITDIPADTIRRIAREFAAAAPHAVVDpGwRGTfYSNSFQTRRAIAIINALL--GNIDKRG-GLY-------------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 415 gitekpsaeflarlgerygFTPPHAPghaaiasmqaictGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLN 494
Cdd:cd02755 322 -------------------YAGSAKP-------------YPIKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPS 369
|
410 420 430
....*....|....*....|....*....|.
gi 16129460 495 rSHLLTArhSYILP---VLGRSEIDMQKNGA 522
Cdd:cd02755 370 -DTALYA--DVILPeatYLERDEPFSDKGGP 397
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
108-399 |
4.35e-22 |
|
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: 100.40 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKYD-AVSDCYKPLSWQQAFDEIGARLQSYSDPNQVE-----FYTSGRTSNEAAFLYQLFAREYGSNNF-PDCSN 180
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKEIKAEYGPEsilpySYAGTMGLLQRAARGRFFHALGASELRgTICSG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 181 MCHEPTSVGLAASIGVgkgtvLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERglerfTApqnp 260
Cdd:cd02766 135 AGIEAQKYDFGASLGN-----DPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTA-----TA---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 261 femltnsetQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERI 340
Cdd:cd02766 201 ---------ARADLHIQIRPGTDGALALGVAKVLFREG----------LYDRDFLARHTEGFEELKAHLETYTPEWAAEI 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129460 341 SGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGI 399
Cdd:cd02766 262 TGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
122-412 |
3.08e-20 |
|
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: 95.37 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 122 YKPLSWQQAFDEIGARLQSYSDpnqvefyTSGrtsNEAaflyqLFAREYG---SNNFPDCSNMCHE-------------P 185
Cdd:cd02751 73 FVRISWDEALDLVASELKRIRE-------KYG---NEA-----IFGGSYGwasAGRLHHAQSLLHRflnliggylgsygT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 186 TSVGLAA--------SIGVGKGTVLLED-FEKCDLVICIGHNPGTN--------HPRMLTSLRALVKRGAKMIAINPLQE 248
Cdd:cd02751 138 YSTGAAQvilphvvgSDEVYEQGTSWDDiAEHSDLVVLFGANPLKTrqgggggpDHGSYYYLKQAKDAGVRFICIDPRYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 249 RGLERFTAPQNPfemltnsetqlasayynVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRD 328
Cdd:cd02751 218 DTAAVLAAEWIP-----------------IRPGTDVALMLAMAHTLITED----------LHDQAFLARYTVGFDEFKDY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 329 VL--------NSEWKdiERISGLSQTQIAELADAYAAAeRTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGIC 400
Cdd:cd02751 271 LLgesdgvpkTPEWA--AEITGVPAETIRALAREIASK-RTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFG 347
|
330
....*....|..
gi 16129460 401 PLRGHSNVQGDR 412
Cdd:cd02751 348 FGYGYSNGGGPP 359
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
108-396 |
8.67e-17 |
|
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: 84.70 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKYDAV--SDCYKPLSWQQAFDEI--GARL---------------QSYSDPNQVEF--------YTSGRTSNEAA 160
Cdd:cd02758 83 RVLQPLKRVGPrgSGKWKPISWEQLIEEVveGGDLfgeghveglkairdlDTPIDPDHPDLgpkanqllYTFGRDEGRTP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 161 FLYQLFAREYGSNNFPDCSNMCHEPTSVG-LAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMltslralvKRGAK 239
Cdd:cd02758 163 FIKRFANQAFGTVNFGGHGSYCGLSYRAGnGALMNDLDGYPHVKPDFDNAEFALFIGTSPAQAGNPF--------KRQAR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 240 MIAiNPLQERGLERFTApqNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERD------------DAASAAGRP 307
Cdd:cd02758 235 RLA-EARTEGNFKYVVV--DPVLPNTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENErynaeylsipskEAAKAAGEP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 308 SLLDdefiQTHTV-------GFDELRRDVLNSEWKDIERISGLSQTQIAELAdayaaaeRTIICYGM-------GITQHE 373
Cdd:cd02758 312 SWTN----ATHLVitvrvksALQLLKEEAFSYSLEEYAEICGVPEAKIIELA-------KEFTSHGRaaavvhhGGTMHS 380
|
330 340
....*....|....*....|...
gi 16129460 374 HGTQNVQQLVNLLLMKGNIGKPG 396
Cdd:cd02758 381 NGFYNAYAIRMLNALIGNLNWKG 403
|
|
| 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 16129460 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARLQSySDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFpDCSNMCHEPTS 187
Cdd:cd02768 54 RLTQPLI--KKGGKLVPVSWEEALKTVAEGLKA-VKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNI-DHRLRQSDLPA 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129460 188 VGLAASIGVGkgTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINPLQERGLERFTAP 257
Cdd:cd02768 130 DNRLRGNYLF--NTSIAEIEEADAVLLIGSNLRKEAPLLNARLRkAVKKKGAKIAVIGPKDTDLIADLTYP 198
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
207-399 |
2.11e-15 |
|
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: 80.00 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 207 EKCDLVICIGHNP---------GTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTApqnpfemltnseTQLAsayyn 277
Cdd:cd02769 169 EHTELVVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPLRDDTAAELGA------------EWIA----- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 278 VRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVL--------NSEWKdiERISGLSQTQIA 349
Cdd:cd02769 232 IRPGTDVALMLALAHTLVTEG----------LHDKAFLARYTVGFDKFLPYLLgesdgvpkTPEWA--AAICGIPAETIR 299
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16129460 350 ELADAYAAAeRTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGI 399
Cdd:cd02769 300 ELARRFASK-RTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGF 348
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
108-417 |
3.32e-14 |
|
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: 76.21 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKY--DAVSDCYKPLSWQQAFDEIGARLQSYSDP--NQVEFYTSG--------RTSNEAAFLYQLFA------RE 169
Cdd:cd02770 59 RLKYPMKRvgKRGEGKFVRISWDEALDTIASELKRIIEKygNEAIYVNYGtgtyggvpAGRGAIARLLNLTGgylnyyGT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 170 YGSNNFPDcsnmcheptsvGLAASIGVGKGTVLLEDFEKCDLVICIGHNP--------GTNHprmltSLRALVKRGAKMI 241
Cdd:cd02770 139 YSWAQITT-----------ATPYTYGAAASGSSLDDLKDSKLVVLFGHNPaetrmgggGSTY-----YYLQAKKAGAKFI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 242 AINPlqergleRFtapqnpfemlTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVG 321
Cdd:cd02770 203 VIDP-------RY----------TDTAVTLADEWIPIRPGTDAALVAAMAYVMITEN----------LHDQAFLDRYCVG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 322 FDE------------LRRDVL---------NSEWKdiERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQ 380
Cdd:cd02770 256 FDAehlpegappnesYKDYVLgtgydgtpkTPEWA--SEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAAR 333
|
330 340 350
....*....|....*....|....*....|....*..
gi 16129460 381 QLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGIT 417
Cdd:cd02770 334 AIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGK 370
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
108-341 |
1.38e-13 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 74.32 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKY--DAVSDCYKPLSWQQAFDEIGARL----QSYSdPNQVEFytSGRTSNEAAFLYQlFAREYGS-NNFPDCSN 180
Cdd:PRK15488 98 RIVKPLKRvgERGEGKWQEISWDEAYQEIAAKLnaikQQHG-PESVAF--SSKSGSLSSHLFH-LATAFGSpNTFTHAST 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 181 mChePTSVGLAASigVGKGTVLLEDFEKCDLVICIGHN--PGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApq 258
Cdd:PRK15488 174 -C--PAGYAIAAK--VMFGGKLKRDLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------RFSV-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 259 npfemltnsETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDV--LNSEW-- 334
Cdd:PRK15488 240 ---------VASKADEWHAIRPGTDLAVVLALCHVLIEEN----------LYDKAFVERYTSGFEELAASVkeYTPEWae 300
|
250
....*....|....
gi 16129460 335 -------KDIERIS 341
Cdd:PRK15488 301 aisdvpaDDIRRIA 314
|
|
| 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 ... |
108-317 |
5.02e-13 |
|
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: 72.04 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARLQSYSDpnQVEFYTSGRTSNEAAFLYQLFAREY-GSNNFpDCSNMCHept 186
Cdd:cd02771 54 RLTQPLI--RRGGTLVPVSWNEALDVAAARLKEAKD--KVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRARRL--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 187 svgLAASIGVGKG-TVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIA----INPLQERGLERFT-APQNP 260
Cdd:cd02771 126 ---IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAalsgIPKWQDAAVRNIAqGAKSP 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 261 FEMLTNSETQL---ASAYYNVRIGGDMALLKGMMRLLierddAASAAGRPSLLDDEFIQT 317
Cdd:cd02771 203 LFIVNALATRLddiAAESIRASPGGQARLGAALARAV-----DASAAGVSGLAPKEKAAR 257
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
108-319 |
2.12e-10 |
|
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: 64.08 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPL--KYDAVSDCYKPLSWQQAFDEIGARLQSY--SDPNQVEFYTsGRTSNEAafLYQLFAREYGSNNFPDCSNMCh 183
Cdd:cd02763 54 RLTKPLlrKGPRGSGQFEEIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFC- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 184 eptSVGLAASIGVGKGTVLLE----DFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQerglerftapqn 259
Cdd:cd02763 130 ---SVNMAAGGLYSIGGSFWEfggpDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVR------------ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 260 pfemltNSETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHT 319
Cdd:cd02763 195 ------TGYAAIADEWVPIKPGTDGAFILALAHELLKAG----------LIDWEFLKRYT 238
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
123-410 |
5.10e-08 |
|
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: 55.80 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 123 KPLSWQQAFDEIGARLQSYSDPnqvEFYTSGRTSNEA-AFLYQLfaREYGSNNFPDCSNMCHEPTSVGLAASiGVgKGTV 201
Cdd:cd02761 52 KPVSLEEAIEKAAEILKEAKRP---LFYGLGTTVCEAqRAGIEL--AEKLGAIIDHAASVCHGPNLLALQDS-GW-PTTT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 202 LLEDFEKCDLVICIGHNPGTNHPRMLtSLRALVKRGAkmiainpLQERGLERFTApqnpfemltnsetqlasayynVRIG 281
Cdd:cd02761 125 LGEVKNRADVIVYWGTNPMHAHPRHM-SRYSVFPRGF-------FREGGREDRTL---------------------IVVD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 282 GdmallkgmmrllieRDDAASAAGrpslldDEFIQT---HTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAA 358
Cdd:cd02761 176 P--------------RKSDTAKLA------DIHLQIdpgSDYELLAALRALLRGAGLVPDEVAGIPAETILELAERLKNA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16129460 359 ERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKpgAGICPLRGHSNVQG 410
Cdd:cd02761 236 KFGVIFWGLGLLPSRGAHRNIEAAIRLVKALNEYTK--FALLPLRGHYNVRG 285
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
103-246 |
2.83e-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: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 103 LEAAGRLTQPL-KYDAVsdcYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFP-- 176
Cdd:cd02772 49 LNSEDRLTKPMiKKDGQ---WQEVDWETALEYVAEGLSAIIKkhgADQIGALASPHSTLEELYLLQKLARGLGSDNIDhr 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129460 177 ----DCSNMCHEPTSVGLAASIgvgkgtvllEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPL 246
Cdd:cd02772 126 lrqsDFRDDAKASGAPWLGMPI---------AEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPA 190
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
108-404 |
6.68e-07 |
|
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: 52.83 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLK------YDAVSDCYKPLSWQQAFDEIGARLQSYSDPN-QVEF-YTSGRTSNEAAFLYQLFAREYGSNNFPDCS 179
Cdd:cd02757 56 RILYPMKrtnprkGRDVDPKFVPISWDEALDTIADKIRALRKENePHKImLHRGRYGHNNSILYGRFTKMIGSPNNISHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 180 NMCHEPTSVGLAAS-IGVGKGTVlleDFEKCDLVICIGHNP-GTNHP-----RMLTSLRAlvkrGAKMIAINPlqergle 252
Cdd:cd02757 136 SVCAESEKFGRYYTeGGWDYNSY---DYANAKYILFFGADPlESNRQnphaqRIWGGKMD----QAKVVVVDP------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 253 RFTA----PQNPFEMLTNSETQLASAYYNVRIGGDmALLKGMMRLLIE-RDDAasAAGRPsLLDDEFIQTHTVGFDELrr 327
Cdd:cd02757 202 RLSNtaakADEWLPIKPGEDGALALAIAHVILTEG-LWDKDFVGDFVDgKNYF--KAGET-VDEESFKEKSTEGLVKW-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 328 dvLNSEWKD-----IERISGLSQTQIAELADAYAAAERTIICY-GMGITQHEHGTQNVQQLVNLLLMKGNIGKPGaGICP 401
Cdd:cd02757 276 --WNLELKDytpewAAKISGIPAETIERVAREFATAAPAAAAFtWRGATMQNRGSYNSMACHALNGLVGSIDSKG-GLCP 352
|
...
gi 16129460 402 LRG 404
Cdd:cd02757 353 NMG 355
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
649-749 |
7.09e-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: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 649 SHDQYNTTIYGMDDRYRGVFGqRDVVFMSAKQAKICRVKNGERVNLIalTPDGK-----RSSRRMDRlKVVIYPMADRSL 723
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAP-EPVVEINPEDAAALGIKDGDLVRVE--SRRGSvvlraKVTDGVPP-GVVFLPHGWGHR 76
|
90 100
....*....|....*....|....*.
gi 16129460 724 VTYFPESNHmLTLDNHDPLSGIPGYK 749
Cdd:cd02775 77 GGRGGNANV-LTPDALDPPSGGPAYK 101
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
266-399 |
3.95e-06 |
|
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: 50.01 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 266 NSETQLASAYYNVRIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTvgfdELRRDVLNSEWKdiERISGLSQ 345
Cdd:cd02750 210 SPSAKHADLWVPIKPGTDAALALAMAHVIIKE----------KLYDEDYLKEYT----DLPFLVYTPAWQ--EAITGVPR 273
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 16129460 346 TQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGI 399
Cdd:cd02750 274 ETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGW 327
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
309-399 |
5.01e-06 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 50.05 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 309 LLDDEFIQTHTVGFDELRRDVL--------NSEWKdiERISGLSQTQIAELADAYAAaERTIICYGMGITQHEHGTQNVQ 380
Cdd:PRK15102 299 LYDKKFIDNYCLGFEQFLPYLLgekdgvpkTPEWA--EKICGIDAETIRELARQMAK-GRTQIIAGWCIQRQQHGEQPYW 375
|
90
....*....|....*....
gi 16129460 381 QLVNLLLMKGNIGKPGAGI 399
Cdd:PRK15102 376 MGAVLAAMLGQIGLPGGGI 394
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
642-752 |
5.57e-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: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 642 LVMATVRSHDQYNTTIYGMDDRYRGVFgQRDVVFMSAKQAKICRVKNGERVNLialtpdgkRSSRRMDRLKVVIYP-MAD 720
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLVEV--------TSRRGSVVVRAKVTDrVRP 71
|
90 100 110
....*....|....*....|....*....|....*....
gi 16129460 721 RSLVTYF--PESNH-----MLTLDNHDPLSGIPGYKSIP 752
Cdd:pfam01568 72 GVVFMPFgwWYEPRggnanALTDDATDPLSGGPEFKTCA 110
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
98-256 |
8.38e-05 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 46.09 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 98 WGDHELEAAGRLTQPLKYDAvSDCYKPLSWQQAFDEIGARLQSYSDPnqVEFYTSGRTSNEAAFLYQLFAR-EYGSNNFp 176
Cdd:PRK07860 268 WAFTYATQPDRITTPLVRDE-DGELEPASWSEALAVAARGLAAARGR--VGVLVGGRLTVEDAYAYAKFARvALGTNDI- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 177 DCSNMCHEPTSVG-LAASI-GVGKGtVLLEDFEKCDLVICIGHNPGTNHPRMLTSLR-ALVKRGAKMIAINPLQERGLER 253
Cdd:PRK07860 344 DFRARPHSAEEADfLAARVaGRGLG-VTYADLEKAPAVLLVGFEPEEESPIVFLRLRkAARKHGLKVYSIAPFATRGLEK 422
|
...
gi 16129460 254 FTA 256
Cdd:PRK07860 423 MGG 425
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
300-405 |
1.64e-04 |
|
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: 45.17 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 300 AASAAGRPSLLddeFIQ----THTVGFDELRRDVL--NSEW-KDIERISGLSQTQIAELAD------AYAAAERTIICYG 366
Cdd:cd02756 287 AEAAAGKDRVL---HLQvnpgTDTALANAIARYIYesLDEVlAEAEQITGVPRAQIEKAADwiakpkEGGYRKRVMFEYE 363
|
90 100 110
....*....|....*....|....*....|....*....
gi 16129460 367 MGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGH 405
Cdd:cd02756 364 KGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCVRQGGH 402
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
122-426 |
2.15e-04 |
|
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: 44.78 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 122 YKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSgrtSNEAAFLYQLFAREYGSNnfpdcsnmchEPTSVGLAASIGVGK 198
Cdd:cd02765 71 FERITWDEALDTIADKLTEAKReygGKSILWMSS---SGDGAILSYLRLALLGGG----------LQDALTYGIDTGVGQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 199 GTVLL------------EDFEKCDLVICIGHNPGTNHprmLTSLRALVK---RGAKMIAINPLQerglerftapqnpfem 263
Cdd:cd02765 138 GFNRVtgggfmpptneiTDWVNAKTIIIWGSNILETQ---FQDAEFFLDareNGAKIVVIDPVY---------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 264 ltNSETQLASAYYNVRIGGDMALLKGMMRLLIERD-------DAASAAG-----------RPSLLDDEFIQTHTVGFDEL 325
Cdd:cd02765 199 --STTAAKADQWVPIRPGTDPALALGMINYILEHNwydeaflKSNTSAPflvredngtllRQADVTATPAEDGYVVWDTN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 326 RRDV-----------LNSEW-----------------------KDIERISGLSQTQIAELADAYAAAERTIICYGMGITQ 371
Cdd:cd02765 277 SDSPepvaatninpaLEGEYtingvkvhtvltalreqaasyppKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDR 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129460 372 HEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRG----HSNVQG---DRTVGITEKPSAEFLA 426
Cdd:cd02765 357 YYHSHVFGRTAAILAALTGNIGRVGGGVGQIKFmyfmGSNFLGnqpDRDRWLKVMKNLDFIV 418
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
108-245 |
3.08e-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: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 108 RLTQPLKYDavSDCYKPLSWQQAFDEIGARLQSySDPNQVEFYTSGRTSNEAAF-LYQLFAREygsnnfpDCSNMCHEPT 186
Cdd:cd02773 53 RLDKPYIRK--NGKLKPATWEEALAAIAKALKG-VKPDEIAAIAGDLADVESMVaLKDLLNKL-------GSENLACEQD 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129460 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 |
6.76e-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: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 642 LVMATVRSHDQYNTTiyGMDDRYRG--VFGQRDVVFMSAKQAKICRVKNGERVNLialtpdgkrSSRRMdrlKVVIYPMA 719
Cdd:cd02790 5 LVLTTGRVLYHYHTG--TMTRRAEGldAIAPEEYVEINPEDAKRLGIEDGEKVRV---------SSRRG---SVEVRARV 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 16129460 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 |
3.21e-03 |
|
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: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 642 LVMATVRSHDQYNT-----TIYGMDDRYRGVFgqrdvVFMSAKQAKICRVKNGERVNLIalTPDGK-----RSSRRMdRL 711
Cdd:cd00508 5 LVLTTGRLLEHWHTgtmtrRSPRLAALAPEPF-----VEIHPEDAARLGIKDGDLVRVS--SRRGSvvvraRVTDRV-RP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 16129460 712 KVVIYPMADRSLVTyfPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
Cdd:cd00508 77 GTVFMPFHWGGEVS--GGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
673-757 |
4.30e-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: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129460 673 VVFMSAKQAKICRVKNGERVNLialtpdgkrSSRRMD---RLKV--------VIYPMADRSLVTYFPESNHmLTLDNHDP 741
Cdd:cd02791 36 YVEIHPEDAARLGLKEGDLVRV---------TSRRGEvvlRVRVtdrvrpgeVFVPMHWGDQFGRSGRVNA-LTLDATDP 105
|
90
....*....|....*.
gi 16129460 742 LSGIPGYKSIPVELEP 757
Cdd:cd02791 106 VSGQPEFKHCAVRIEK 121
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