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Conserved domains on  [gi|1358904149|ref|WP_105700073|]
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FdhF/YdeP family oxidoreductase [Cronobacter dublinensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09939 super family cl32435
acid resistance putative oxidoreductase YdeP;
10-762 0e+00

acid resistance putative oxidoreductase YdeP;


The actual alignment was detected with superfamily member PRK09939:

Pssm-ID: 182156 [Multi-domain]  Cd Length: 759  Bit Score: 1087.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  10 IAPYGGSAGGWGALKAVADAIRGQMSVKQDVIALFKVNQPQGFDCPGCAWPDPQHASSFEFCENGAKAVSWEATSKRTTP 89
Cdd:PRK09939    5 IESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  90 EFFAAHPVSELWERSAFELEGEGRLTHPMKYDPKSDTYQPIEWDTAFREIGERLRSYDDPDSVEFYTSGRASNEAAFLWQ 169
Cdd:PRK09939   85 SFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 170 LFAREYGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAIN 249
Cdd:PRK09939  165 LFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAIN 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 250 PLRERGLERFTSPQSPIEMLSLSSTELASTYYKVRVGGDAAMLKGVMKILLSMHEEALATGEAGVLDEAFIREHTEGFDA 329
Cdd:PRK09939  245 PLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDE 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 330 LKADLDATDWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRG 409
Cdd:PRK09939  325 LRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 410 HSNVQGDRTVGITEIPPQSLLDSIERVFGFTPPQKHGHGAVAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLD 489
Cdd:PRK09939  405 HSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 490 LVVHMATKLNRSHLLLGRHNYILPVIGRTETDVQASGEQSITVEDSMSMVHASRGMLTPASPHLRSEPAIVAGLAKATLH 569
Cdd:PRK09939  485 LAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALP 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 570 DTVVDWDKMIGDYSFIRDAIEAVFPAFANFNERVKKPGGFRLRNAASERVWNTPSGKAQFKVMQGINEDPRSLKCHDLVL 649
Cdd:PRK09939  565 QSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVM 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 650 TTLRSHDQYNTTLYGLNDRYRGVTGRRDVLFINPDEAEKRELRVGDQVNITALDPDGNPTSRRMHNLTVVVIDMAPGSVG 729
Cdd:PRK09939  645 ATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLV 724
                         730       740       750
                  ....*....|....*....|....*....|...
gi 1358904149 730 AYYPEANVLVPLDSHDTQSGIPAYKSIPIAMER 762
Cdd:PRK09939  725 TYFPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
 
Name Accession Description Interval E-value
PRK09939 PRK09939
acid resistance putative oxidoreductase YdeP;
10-762 0e+00

acid resistance putative oxidoreductase YdeP;


Pssm-ID: 182156 [Multi-domain]  Cd Length: 759  Bit Score: 1087.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  10 IAPYGGSAGGWGALKAVADAIRGQMSVKQDVIALFKVNQPQGFDCPGCAWPDPQHASSFEFCENGAKAVSWEATSKRTTP 89
Cdd:PRK09939    5 IESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  90 EFFAAHPVSELWERSAFELEGEGRLTHPMKYDPKSDTYQPIEWDTAFREIGERLRSYDDPDSVEFYTSGRASNEAAFLWQ 169
Cdd:PRK09939   85 SFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 170 LFAREYGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAIN 249
Cdd:PRK09939  165 LFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAIN 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 250 PLRERGLERFTSPQSPIEMLSLSSTELASTYYKVRVGGDAAMLKGVMKILLSMHEEALATGEAGVLDEAFIREHTEGFDA 329
Cdd:PRK09939  245 PLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDE 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 330 LKADLDATDWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRG 409
Cdd:PRK09939  325 LRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 410 HSNVQGDRTVGITEIPPQSLLDSIERVFGFTPPQKHGHGAVAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLD 489
Cdd:PRK09939  405 HSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 490 LVVHMATKLNRSHLLLGRHNYILPVIGRTETDVQASGEQSITVEDSMSMVHASRGMLTPASPHLRSEPAIVAGLAKATLH 569
Cdd:PRK09939  485 LAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALP 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 570 DTVVDWDKMIGDYSFIRDAIEAVFPAFANFNERVKKPGGFRLRNAASERVWNTPSGKAQFKVMQGINEDPRSLKCHDLVL 649
Cdd:PRK09939  565 QSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVM 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 650 TTLRSHDQYNTTLYGLNDRYRGVTGRRDVLFINPDEAEKRELRVGDQVNITALDPDGNPTSRRMHNLTVVVIDMAPGSVG 729
Cdd:PRK09939  645 ATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLV 724
                         730       740       750
                  ....*....|....*....|....*....|...
gi 1358904149 730 AYYPEANVLVPLDSHDTQSGIPAYKSIPIAMER 762
Cdd:PRK09939  725 TYFPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
Fdhalpha-like TIGR01701
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ...
17-762 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: 1007.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  17 AGGWGALKAVADAIRGQMSVKQDVIALFKVNQPQGFDCPGCAWPD-PQHASSFEFCENGAKAVSWEATSKRTTPEFFAAH 95
Cdd:TIGR01701   2 AGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVsPQTLAGLEFCENGAKAIAWETTPRTIDPEFFAEH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  96 PVSELWERSAFELEGEGRLTHPMKYDPKSDTYQPIEWDTAFREIGERLRSYDdPDSVEFYTSGRASNEAAFLWQLFAREY 175
Cdd:TIGR01701  82 SVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLD-PKQVAFYTSGRTSNEAAYLYQLFARSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 176 GTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINPLRERG 255
Cdd:TIGR01701 161 GSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 256 LERFTSPQSPIEMLSLSSTELASTYYKVRVGGDAAMLKGVMKILLSMHEEAlatgEAGVLDEAFIREHTEGFDALKADLD 335
Cdd:TIGR01701 241 LERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQ----PGSLIDHEFIANHTNGFDELRRHVL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 336 ATDWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQG 415
Cdd:TIGR01701 317 QLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQG 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 416 DRTVGITEIPPQSLLDSIERVFGFTPPQKHGHGAVAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLDLVVHMA 495
Cdd:TIGR01701 397 DRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVA 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 496 TKLNRSHLLLGRHNYILPVIGRTETDVQASGEQSITVEDSMSMVHASRGMLTPASPHLRSEPAIVAGLAKATLHDTVVDW 575
Cdd:TIGR01701 477 TKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAW 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 576 DKMIGDYSFIRDAIEAVFPAFANFNERVKKPGGFRLRNAA-SERVWNTPSGKAQFKVMQGINEDPRSLKCHDLVLTTLRS 654
Cdd:TIGR01701 557 EILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLRS 636
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 655 HDQYNTTLYGLNDRYRGVTGRRDVLFINPDEAEKRELRVGDQVNITALDPDGNptSRRMHNLTVVVIDMAPGSVGAYYPE 734
Cdd:TIGR01701 637 HDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQ--KRKFDNLRIVFYDTPTGNAAAYYPE 714
                         730       740
                  ....*....|....*....|....*...
gi 1358904149 735 ANVLVPLDSHDTQSGIPAYKSIPIAMER 762
Cdd:TIGR01701 715 ANPLLPLDHHDPQSKTPEYKTIPVRLEA 742
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
51-629 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: 943.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  51 GFDCPGCAWPDP-QHASSFEFCENGAKAVSWEATSKRTTPEFFAAHPVSELWERSAFELEGEGRLTHPMKYDPKSDTYQP 129
Cdd:cd02767     1 GFDCPGCAWGDPgQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 130 IEWDTAFREIGERLRSYDdPDSVEFYTSGRASNEAAFLWQLFAREYGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELE 209
Cdd:cd02767    81 ISWDEAFAEIAARLRALD-PDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 210 DFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINPLRERGLERFTSPQSPIEMLSlSSTELASTYYKVRVGGDA 289
Cdd:cd02767   160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 290 AMLKGVMKILLSMHEEalatgEAGVLDEAFIREHTEGFDALKADLDATDWDHILKVSGMERKEIQNIARLYANAERTIIC 369
Cdd:cd02767   239 ALLNGMAKHLIERDDE-----PGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 370 YGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDRTVGITEIPPQSLLDSIERVFGFTPPQKHGHGA 449
Cdd:cd02767   314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 450 VAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLDLVVHMATKLNRSHLLLGRHNYILPVIGRTETDVQASGEQS 529
Cdd:cd02767   394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 530 ITVEDSMSMVHASRGMLTPASPHLRSEPAIVAGLAKATLHDTVVDWDKMIGDYSFIRDAIEAVFP-AFANFNERVKKPGG 608
Cdd:cd02767   474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGG 553
                         570       580
                  ....*....|....*....|.
gi 1358904149 609 FRLRNAASERVWNTPSGKAQF 629
Cdd:cd02767   554 FHLPNGARERKFNTPSGKAQF 574
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
17-765 1.93e-173

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 514.39  E-value: 1.93e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  17 AGGWGALKAVADAIRGQMSVkqdvialfkvnqpqgfdCPGCAwpdpqhassfEFCENGAKAVSWEATskRTTPEffAAHP 96
Cdd:COG0243     8 AAGAGAAALEAAGTKTVKTT-----------------CPGCG----------VGCGLGVKVEDGRVV--RVRGD--PDHP 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  97 VSELW-----ERSAFELEGEGRLTHPMKYDPK--SDTYQPIEWDTAFREIGERLRSYDD---PDSVEFYTSG----RASN 162
Cdd:COG0243    57 VNRGRlcakgAALDERLYSPDRLTYPMKRVGPrgSGKFERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsagRLSN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 163 EAAFLWQLFAREYGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLRE-VSKR 241
Cdd:COG0243   137 EAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKR 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 242 GATIVAINPLRERglerftspqspiemlslsSTELASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIR 321
Cdd:COG0243   217 GAKIVVIDPRRTE------------------TAAIADEWLPIRPGTDAALLLALAHVLI----------EEGLYDRDFLA 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 322 EHTEGFDALKADLDATDWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKG 401
Cdd:COG0243   269 RHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPG 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 402 AGICPLRGHsnvqgdrtvgiteippqslldsiervfgftppqkhghgavaaiqAMRDGK---AKALLCLGGNLAEAISDP 478
Cdd:COG0243   349 GGPFSLTGE--------------------------------------------AILDGKpypIKALWVYGGNPAVSAPDT 384
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 479 QVTFPAMRNLDLVVHMATKLNRSHLLlgrHNYILPVIGRTETDvqasgEQSITVEDsmSMVHASRGMLTPASpHLRSEPA 558
Cdd:COG0243   385 NRVREALRKLDFVVVIDTFLTETARY---ADIVLPATTWLERD-----DIVTNSED--RRVHLSRPAVEPPG-EARSDWE 453
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 559 IVAGLAKATLHDTVVDWDKMIGDYsfIRDAIEAVFPAFANFnERVKKPGGFRLRNAAS-----ERVWNTPSGKAQFKV-- 631
Cdd:COG0243   454 IFAELAKRLGFEEAFPWGRTEEDY--LRELLEATRGRGITF-EELREKGPVQLPVPPEpafrnDGPFPTPSGKAEFYSet 530
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 632 -----MQGINEDPRSLKC----HDLVLTTLRSHDQYNTTLYGlNDRYRGVTGRRdVLFINPDEAEKRELRVGDQVNItal 702
Cdd:COG0243   531 lalppLPRYAPPYEGAEPldaeYPLRLITGRSRDQWHSTTYN-NPRLREIGPRP-VVEINPEDAAALGIKDGDLVRV--- 605
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358904149 703 dpdgnpTSRR--MHNLTVVVIDMAPGSV----GAYYPEA-------NVLVPlDSHDTQSGIPAYKSIPIAMERVAE 765
Cdd:COG0243   606 ------ESDRgeVLARAKVTEGIRPGVVfaphGWWYEPAddkggnvNVLTP-DATDPLSGTPAFKSVPVRVEKAAA 674
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
113-505 3.48e-20

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 92.85  E-value: 3.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYDPKsDTYQPIEWDTAFREIGERLRSY-----DDPDSVEFYTSGRASNEAAFLWQLFAREYGTNNF---PDCS 184
Cdd:pfam00384   1 RLKYPMVRRGD-GKFVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 185 NMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPrMLGT--LREVSKRGATIVAINPLRERGLErftsp 262
Cdd:pfam00384  80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAP-ILNAriRKAALKGKAKVIVIGPRLDLTYA----- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 263 qspIEMLSLSStelastyykvrvGGDAAMLkgvmkiLLSMHeealatgeagvldeAFIREhtegfdaLKADLDAtdwdhi 342
Cdd:pfam00384 154 ---DEHLGIKP------------GTDLALA------LAGAH--------------VFIKE-------LKKDKDF------ 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 343 lkvsgmerkeiqniarlyanAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDrtVGIT 422
Cdd:pfam00384 186 --------------------APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASP--VGAL 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 423 EIppqslldsiervfGFTPPQKhghgAVAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLDLVV----HMATKL 498
Cdd:pfam00384 244 DL-------------GLVPGIK----SVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDKT 306

                  ....*...
gi 1358904149 499 -NRSHLLL 505
Cdd:pfam00384 307 aKYADVIL 314
 
Name Accession Description Interval E-value
PRK09939 PRK09939
acid resistance putative oxidoreductase YdeP;
10-762 0e+00

acid resistance putative oxidoreductase YdeP;


Pssm-ID: 182156 [Multi-domain]  Cd Length: 759  Bit Score: 1087.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  10 IAPYGGSAGGWGALKAVADAIRGQMSVKQDVIALFKVNQPQGFDCPGCAWPDPQHASSFEFCENGAKAVSWEATSKRTTP 89
Cdd:PRK09939    5 IESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  90 EFFAAHPVSELWERSAFELEGEGRLTHPMKYDPKSDTYQPIEWDTAFREIGERLRSYDDPDSVEFYTSGRASNEAAFLWQ 169
Cdd:PRK09939   85 SFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 170 LFAREYGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAIN 249
Cdd:PRK09939  165 LFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAIN 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 250 PLRERGLERFTSPQSPIEMLSLSSTELASTYYKVRVGGDAAMLKGVMKILLSMHEEALATGEAGVLDEAFIREHTEGFDA 329
Cdd:PRK09939  245 PLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDE 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 330 LKADLDATDWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRG 409
Cdd:PRK09939  325 LRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 410 HSNVQGDRTVGITEIPPQSLLDSIERVFGFTPPQKHGHGAVAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLD 489
Cdd:PRK09939  405 HSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 490 LVVHMATKLNRSHLLLGRHNYILPVIGRTETDVQASGEQSITVEDSMSMVHASRGMLTPASPHLRSEPAIVAGLAKATLH 569
Cdd:PRK09939  485 LAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALP 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 570 DTVVDWDKMIGDYSFIRDAIEAVFPAFANFNERVKKPGGFRLRNAASERVWNTPSGKAQFKVMQGINEDPRSLKCHDLVL 649
Cdd:PRK09939  565 QSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVM 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 650 TTLRSHDQYNTTLYGLNDRYRGVTGRRDVLFINPDEAEKRELRVGDQVNITALDPDGNPTSRRMHNLTVVVIDMAPGSVG 729
Cdd:PRK09939  645 ATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLV 724
                         730       740       750
                  ....*....|....*....|....*....|...
gi 1358904149 730 AYYPEANVLVPLDSHDTQSGIPAYKSIPIAMER 762
Cdd:PRK09939  725 TYFPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
Fdhalpha-like TIGR01701
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ...
17-762 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: 1007.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  17 AGGWGALKAVADAIRGQMSVKQDVIALFKVNQPQGFDCPGCAWPD-PQHASSFEFCENGAKAVSWEATSKRTTPEFFAAH 95
Cdd:TIGR01701   2 AGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVsPQTLAGLEFCENGAKAIAWETTPRTIDPEFFAEH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  96 PVSELWERSAFELEGEGRLTHPMKYDPKSDTYQPIEWDTAFREIGERLRSYDdPDSVEFYTSGRASNEAAFLWQLFAREY 175
Cdd:TIGR01701  82 SVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLD-PKQVAFYTSGRTSNEAAYLYQLFARSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 176 GTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINPLRERG 255
Cdd:TIGR01701 161 GSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 256 LERFTSPQSPIEMLSLSSTELASTYYKVRVGGDAAMLKGVMKILLSMHEEAlatgEAGVLDEAFIREHTEGFDALKADLD 335
Cdd:TIGR01701 241 LERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQ----PGSLIDHEFIANHTNGFDELRRHVL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 336 ATDWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQG 415
Cdd:TIGR01701 317 QLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQG 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 416 DRTVGITEIPPQSLLDSIERVFGFTPPQKHGHGAVAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLDLVVHMA 495
Cdd:TIGR01701 397 DRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVA 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 496 TKLNRSHLLLGRHNYILPVIGRTETDVQASGEQSITVEDSMSMVHASRGMLTPASPHLRSEPAIVAGLAKATLHDTVVDW 575
Cdd:TIGR01701 477 TKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAW 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 576 DKMIGDYSFIRDAIEAVFPAFANFNERVKKPGGFRLRNAA-SERVWNTPSGKAQFKVMQGINEDPRSLKCHDLVLTTLRS 654
Cdd:TIGR01701 557 EILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLRS 636
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 655 HDQYNTTLYGLNDRYRGVTGRRDVLFINPDEAEKRELRVGDQVNITALDPDGNptSRRMHNLTVVVIDMAPGSVGAYYPE 734
Cdd:TIGR01701 637 HDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQ--KRKFDNLRIVFYDTPTGNAAAYYPE 714
                         730       740
                  ....*....|....*....|....*...
gi 1358904149 735 ANVLVPLDSHDTQSGIPAYKSIPIAMER 762
Cdd:TIGR01701 715 ANPLLPLDHHDPQSKTPEYKTIPVRLEA 742
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
51-629 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: 943.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  51 GFDCPGCAWPDP-QHASSFEFCENGAKAVSWEATSKRTTPEFFAAHPVSELWERSAFELEGEGRLTHPMKYDPKSDTYQP 129
Cdd:cd02767     1 GFDCPGCAWGDPgQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 130 IEWDTAFREIGERLRSYDdPDSVEFYTSGRASNEAAFLWQLFAREYGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELE 209
Cdd:cd02767    81 ISWDEAFAEIAARLRALD-PDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 210 DFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINPLRERGLERFTSPQSPIEMLSlSSTELASTYYKVRVGGDA 289
Cdd:cd02767   160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 290 AMLKGVMKILLSMHEEalatgEAGVLDEAFIREHTEGFDALKADLDATDWDHILKVSGMERKEIQNIARLYANAERTIIC 369
Cdd:cd02767   239 ALLNGMAKHLIERDDE-----PGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 370 YGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDRTVGITEIPPQSLLDSIERVFGFTPPQKHGHGA 449
Cdd:cd02767   314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 450 VAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLDLVVHMATKLNRSHLLLGRHNYILPVIGRTETDVQASGEQS 529
Cdd:cd02767   394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 530 ITVEDSMSMVHASRGMLTPASPHLRSEPAIVAGLAKATLHDTVVDWDKMIGDYSFIRDAIEAVFP-AFANFNERVKKPGG 608
Cdd:cd02767   474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGG 553
                         570       580
                  ....*....|....*....|.
gi 1358904149 609 FRLRNAASERVWNTPSGKAQF 629
Cdd:cd02767   554 FHLPNGARERKFNTPSGKAQF 574
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
17-765 1.93e-173

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 514.39  E-value: 1.93e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  17 AGGWGALKAVADAIRGQMSVkqdvialfkvnqpqgfdCPGCAwpdpqhassfEFCENGAKAVSWEATskRTTPEffAAHP 96
Cdd:COG0243     8 AAGAGAAALEAAGTKTVKTT-----------------CPGCG----------VGCGLGVKVEDGRVV--RVRGD--PDHP 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  97 VSELW-----ERSAFELEGEGRLTHPMKYDPK--SDTYQPIEWDTAFREIGERLRSYDD---PDSVEFYTSG----RASN 162
Cdd:COG0243    57 VNRGRlcakgAALDERLYSPDRLTYPMKRVGPrgSGKFERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsagRLSN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 163 EAAFLWQLFAREYGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLRE-VSKR 241
Cdd:COG0243   137 EAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKR 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 242 GATIVAINPLRERglerftspqspiemlslsSTELASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIR 321
Cdd:COG0243   217 GAKIVVIDPRRTE------------------TAAIADEWLPIRPGTDAALLLALAHVLI----------EEGLYDRDFLA 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 322 EHTEGFDALKADLDATDWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKG 401
Cdd:COG0243   269 RHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPG 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 402 AGICPLRGHsnvqgdrtvgiteippqslldsiervfgftppqkhghgavaaiqAMRDGK---AKALLCLGGNLAEAISDP 478
Cdd:COG0243   349 GGPFSLTGE--------------------------------------------AILDGKpypIKALWVYGGNPAVSAPDT 384
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 479 QVTFPAMRNLDLVVHMATKLNRSHLLlgrHNYILPVIGRTETDvqasgEQSITVEDsmSMVHASRGMLTPASpHLRSEPA 558
Cdd:COG0243   385 NRVREALRKLDFVVVIDTFLTETARY---ADIVLPATTWLERD-----DIVTNSED--RRVHLSRPAVEPPG-EARSDWE 453
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 559 IVAGLAKATLHDTVVDWDKMIGDYsfIRDAIEAVFPAFANFnERVKKPGGFRLRNAAS-----ERVWNTPSGKAQFKV-- 631
Cdd:COG0243   454 IFAELAKRLGFEEAFPWGRTEEDY--LRELLEATRGRGITF-EELREKGPVQLPVPPEpafrnDGPFPTPSGKAEFYSet 530
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 632 -----MQGINEDPRSLKC----HDLVLTTLRSHDQYNTTLYGlNDRYRGVTGRRdVLFINPDEAEKRELRVGDQVNItal 702
Cdd:COG0243   531 lalppLPRYAPPYEGAEPldaeYPLRLITGRSRDQWHSTTYN-NPRLREIGPRP-VVEINPEDAAALGIKDGDLVRV--- 605
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358904149 703 dpdgnpTSRR--MHNLTVVVIDMAPGSV----GAYYPEA-------NVLVPlDSHDTQSGIPAYKSIPIAMERVAE 765
Cdd:COG0243   606 ------ESDRgeVLARAKVTEGIRPGVVfaphGWWYEPAddkggnvNVLTP-DATDPLSGTPAFKSVPVRVEKAAA 674
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
103-765 1.09e-112

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 357.27  E-value: 1.09e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 103 RSAFE-LEGEGRLTHPMKYdpKSDTYQPIEWDTAFREIGERLRSYDD---PDSVEFYTSGRASNEAAFLWQLFAREY-GT 177
Cdd:COG3383    50 RFGFEfVNSPDRLTTPLIR--RGGEFREVSWDEALDLVAERLREIQAehgPDAVAFYGSGQLTNEENYLLQKLARGVlGT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 178 NNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINPLRergle 257
Cdd:COG3383   128 NNIDNNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRR----- 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 258 rftspqspIEMlslssTELASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGFDALKADLDAT 337
Cdd:COG3383   203 --------TET-----ARLADLHLQIKPGTDLALLNGLLHVII----------EEGLVDEDFIAERTEGFEELKASVAKY 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 338 DWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDR 417
Cdd:COG3383   260 TPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGR 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 418 TVGI--TEIP-PQSLLDS-----IERVFGFTP-PQKHGHGAVAAIQAMRDGKAKALLCLGGNLaeAISDPQVTF--PAMR 486
Cdd:COG3383   340 DMGAlpNVLPgYRDVTDPehrakVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENP--AVSDPDANHvrEALE 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 487 NLDLVVHMAtklnrshlllgrhnyilpvIGRTET----DV----QASGEQSITVEDSMSMVHASRGMLTPAsPHLRSEPA 558
Cdd:COG3383   418 KLEFLVVQD-------------------IFLTETaeyaDVvlpaASWAEKDGTFTNTERRVQRVRKAVEPP-GEARPDWE 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 559 IVAGLAKATLHDtvVDWDkmigDYSFIRDAIEAVFPAFANFN-ERVKKPGGFRLRNAASER---------VWNTPSGKAQ 628
Cdd:COG3383   478 IIAELARRLGYG--FDYD----SPEEVFDEIARLTPDYSGISyERLEALGGVQWPCPSEDHpgtprlftgRFPTPDGKAR 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 629 FKVMQGINEDPRSLKCHDLVLTTLRSHDQYNT-TLYGLNDRYRGVTGrRDVLFINPDEAEKRELRVGDQVNItaldpdgn 707
Cdd:COG3383   552 FVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTgTRTRRSPRLNKHAP-EPFVEIHPEDAARLGIKDGDLVRV-------- 622
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358904149 708 pTSRRMHNLTVVVID--MAPGSVGAY--YPE--ANVLVPlDSHDTQSGIPAYKSIPIAMERVAE 765
Cdd:COG3383   623 -SSRRGEVVLRARVTdrVRPGTVFMPfhWGEgaANALTN-DALDPVSKQPEYKACAVRVEKVAE 684
Fdh-alpha TIGR01591
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ...
113-760 1.35e-89

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: 295.91  E-value: 1.35e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYdpKSDTYQPIEWDTAFREIGERLRSYD---DPDSVEFYTSGRASNEAAFLWQLFARE-YGTNNFPDCSNMCH 188
Cdd:TIGR01591  53 RLTTPLIR--EGDKFREVSWDEAISYIAEKLKEIKekyGPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 189 EPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINPlRERGLERFtspqspiem 268
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-RKTETAKI--------- 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 269 lslsstelASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGFDALKADLDATDWDHILKVSGM 348
Cdd:TIGR01591 201 --------ADLHIPLKPGTDIALLNAMANVII----------EEGLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGV 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 349 ERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDRTVG-ITEIPP- 426
Cdd:TIGR01591 263 PADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGaLPDFLPg 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 427 ------QSLLDSIERVFGFTP-PQKHGHGAVAAIQAMRDGKAKALLCLGGNLaeAISDPQV--TFPAMRNLDLVVHMATK 497
Cdd:TIGR01591 343 yqpvsdEEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDP--LQSDPNTskVRKALEKLELLVVQDIF 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 498 LNRSHLLLgrhNYILPvigrtetdVQASGEQSITVEDSMSMVHASRGMLTPASpHLRSEPAIVAGLAKAtlhdtvVDWDK 577
Cdd:TIGR01591 421 MTETAKYA---DVVLP--------AAAWLEKEGTFTNAERRIQRFFKAVEPKG-ESKPDWEIIQELANA------LGLDW 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 578 MIGDYSFIRDAIEAVFPAFANFN-ERVKKPGgfrlrnaASERVWN----------------TPSGKAQFKVMQGINEDPR 640
Cdd:TIGR01591 483 NYNHPQEIMDEIRELTPLFAGLTyERLDELG-------SLQWPCNdsdasptsylykdkfaTPDGKAKFIPLEWVAPIEE 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 641 SLKCHDLVLTTLRSHDQYNT-TLYGLNDRYRGVTGRRDVLfINPDEAEKRELRVGDQVNITAldPDGNPTSR-RMHNLTV 718
Cdd:TIGR01591 556 PDDEYPLILTTGRVLTHYNVgEMTRRVAGLRRLSPEPYVE-INTEDAKKLGIKDGDLVKVKS--RRGEITLRaKVSDRVN 632
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 1358904149 719 VVIDMAPgsVGAYYPEANVLVPLDShDTQSGIPAYKSIPIAM 760
Cdd:TIGR01591 633 KGAIYIT--MHFWDGAVNNLTTDDL-DPISGTPEYKYTAVRI 671
MopB_Formate-Dh-H cd02753
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
103-629 1.32e-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: 256.37  E-value: 1.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 103 RSAFE-LEGEGRLTHPMKYdpKSDTYQPIEWDTAFREIGERLRSYDD---PDSVEFYTSGRASNEAAFLWQLFARE-YGT 177
Cdd:cd02753    43 RFGFDfVNSKDRLTKPLIR--KNGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAvGGT 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 178 NNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINPLRergle 257
Cdd:cd02753   121 NNVDHCARLCHSPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRR----- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 258 rftspqspIEMlslssTELASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGFDALKADLDAT 337
Cdd:cd02753   196 --------TEL-----ARFADLHLQLRPGTDVALLNAMAHVII----------EEGLYDEEFIEERTEGFEELKEIVEKY 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 338 DWDHILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDR 417
Cdd:cd02753   253 TPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGAC 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 418 TVGiteippqslldsiervfgftppqkhghgavaAIQAMRDGKAKALLCLGGNLaeAISDP--QVTFPAMRNLDLVVHMA 495
Cdd:cd02753   333 DMG-------------------------------ALPNVLPGYVKALYIMGENP--ALSDPntNHVRKALESLEFLVVQD 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 496 TKLNRSHLLLgrhNYILPVIgrtetdvqASGEQSITVEDSMSMVHASRGMLTPASpHLRSEPAIVAGLAKATLHDtvvdw 575
Cdd:cd02753   380 IFLTETAELA---DVVLPAA--------SFAEKDGTFTNTERRVQRVRKAVEPPG-EARPDWEIIQELANRLGYP----- 442
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358904149 576 dkmiGDYSF---IRDAIEAVFPAFANFN-ERVKKPGGFRLrNAASE----------RVWNTPSGKAQF 629
Cdd:cd02753   443 ----GFYSHpeeIFDEIARLTPQYAGISyERLERPGGLQW-PCPDEdhpgtpilhtERFATPDGKARF 505
Molybdopterin-Binding cd00368
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
95-566 7.31e-70

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: 234.14  E-value: 7.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  95 HPVSE--LWERSAFELEG---EGRLTHPMKYDPKSDTYQPIEWDTAFREIGERLRSYDD---PDSVEFYTSGRASNEAAF 166
Cdd:cd00368    31 HPVNEgrLCDKGRAGLDGlysPDRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIREkygPDAIAFYGGGGASNEEAY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 167 LWQLFAREYGTNNFPDCSNMCHEPTSVGLPEsIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIV 246
Cdd:cd00368   111 LLQKLLRALGSNNVDSHARLCHASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLI 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 247 AINPLRERglerftspqspiemlslsSTELASTYYKVRVGGDAAMLKGvmkillsmhEEAlatgeagvldeafirehteg 326
Cdd:cd00368   190 VIDPRRTE------------------TAAKADEWLPIRPGTDAALALA---------EWA-------------------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 327 fdalkadldatdwdhiLKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICP 406
Cdd:cd00368   223 ----------------AEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 407 lrghsnvqgdrtvgiteippqslldsiervfgftppqkhghgavaaiqamrdgkakallclGGNLAEAISDPQVTFPAMR 486
Cdd:cd00368   287 -------------------------------------------------------------GGNPLVSAPDANRVRAALK 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 487 NLDLVVHMATKLNRSHLLlgrHNYILPVIGRTETDvqasGeqsiTVEDSMSMVHASRGMLTPAsPHLRSEPAIVAGLAKA 566
Cdd:cd00368   306 KLDFVVVIDIFMTETAAY---ADVVLPAATYLEKE----G----TYTNTEGRVQLFRQAVEPP-GEARSDWEILRELAKR 373
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
108-492 4.94e-58

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: 207.46  E-value: 4.94e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 108 LEGEGRLTHPMkYDPKSDTYQPIEWDTAFREIGERLRS---YDDPDSVEFYTSGRASNEAAFLWQLFAREY-GTNNFPDC 183
Cdd:cd02754    49 LNGPERLTRPL-LRRNGGELVPVSWDEALDLIAERFKAiqaEYGPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTN 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 184 SNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSK--RGATIVAINPLRERglerfts 261
Cdd:cd02754   128 SRLCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKanPGAKIIVVDPRRTR------- 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 262 pqspiemlslsSTELASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGFDALKADLDATDWDH 341
Cdd:cd02754   201 -----------TADIADLHLPIRPGTDLALLNGLLHVLI----------EEGLIDRDFIDAHTEGFEELKAFVADYTPEK 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 342 ILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDRTVGI 421
Cdd:cd02754   260 VAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGG 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 422 T--------EIPPQSLLDSIERVFGFTP---PQKHGHGAVAAIQAMRDGKAKALLCLGGNlaeaisdPQVTFP------- 483
Cdd:cd02754   340 LanllpghrSVNNPEHRAEVAKFWGVPEgtiPPKPGLHAVEMFEAIEDGEIKALWVMCTN-------PAVSLPnanrvre 412

                  ....*....
gi 1358904149 484 AMRNLDLVV 492
Cdd:cd02754   413 ALERLEFVV 421
MopB_CT_ydeP cd02787
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ...
647-758 3.88e-51

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: 174.00  E-value: 3.88e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 647 LVLTTLRSHDQYNTTLYGLNDRYRGVTGRRDVLFINPDEAEKRELRVGDQVNITALDPDGNPtsRRMHNLTVVVIDMAPG 726
Cdd:cd02787     1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQG--RIVRGFRVVEYDIPRG 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1358904149 727 SVGAYYPEANVLVPLDSHDTQSGIPAYKSIPI 758
Cdd:cd02787    79 CLAAYYPEGNVLVPLDHRDPQSKTPAYKSVPV 110
MopB_Formate-Dh-Na-like cd02752
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
95-415 1.93e-41

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: 161.41  E-value: 1.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  95 HPVSE---------LWERsafeLEGEGRLTHPMKYDPKSDTYQPIEWDTAFREIGERLRSYDD---------------PD 150
Cdd:cd02752    31 HPVNRgslcpkgaaLRDF----VHSPKRLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRDasfveknaagvvvnrPD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 151 SVEFYTSGRASNEAAFLWQLFAREYGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHP- 229
Cdd:cd02752   107 SIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPv 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 230 RMLGTLREVSKRGATIVAINPlrergleRFTSPQSpiemlslssteLASTYYKVRVGGDAAMLKGVMKILLSMHEEALAT 309
Cdd:cd02752   187 SFKWILEAKEKNGAKLIVVDP-------RFTRTAA-----------KADLYVPIRSGTDIAFLGGMINYIIRYTPEEVED 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 310 gEAGVLDEAFIRehtegfdalkadldatdwdhilkvsgmerkeiqnIARLYANAER-----TIIcYGMGITQHQYGTQNV 384
Cdd:cd02752   249 -ICGVPKEDFLK----------------------------------VAEMFAATGRpdkpgTIL-YAMGWTQHTVGSQNI 292
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1358904149 385 QQIANLLLLRGNIGKKGAGICPLRGHSNVQG 415
Cdd:cd02752   293 RAMCILQLLLGNIGVAGGGVNALRGHSNVQG 323
MopB_1 cd02762
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
113-566 2.99e-37

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: 147.16  E-value: 2.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYDPksDTYQPIEWDTAFREIGERLRSY---DDPDSVEFYTSGRASNEAA-------FLWQLFAREYGTNNFPD 182
Cdd:cd02762    54 RLRTPMRRRG--GSFEEIDWDEAFDEIAERLRAIrarHGGDAVGVYGGNPQAHTHAggayspaLLKALGTSNYFSAATAD 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 183 csNMCHEPTSVGLPESigvgKGTVELEDFDHCDLVLCIGHNPGTNH------PRMLGTLREVSKRGATIVAINPLRERgl 256
Cdd:cd02762   132 --QKPGHFWSGLMFGH----PGLHPVPDIDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKDRGGSLVVIDPRRTE-- 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 257 erftspqspiemlslsSTELASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGFDALKADLDA 336
Cdd:cd02762   204 ----------------TAKLADEHLFVRPGTDAWLLAAMLAVLL----------AEGLTDRRFLAEHCDGLDEVRAALAE 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 337 TDWDHILKVSGMERKEIQNIARLYANAeRTIICYG-MGITQHQYGTQNvQQIANLL-LLRGNIGKKGAGICPL------- 407
Cdd:cd02762   258 FTPEAYAPRCGVPAETIRRLAREFAAA-PSAAVYGrLGVQTQLFGTLC-SWLVKLLnLLTGNLDRPGGAMFTTpaldlvg 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 408 ------RGHSNVQgDRTVG----ITEIPPQSLLDSIERVfgftppqkhghgavaaiqamRDGKAKALLCLGGNLAEAISD 477
Cdd:cd02762   336 qtsgrtIGRGEWR-SRVSGlpeiAGELPVNVLAEEILTD--------------------GPGRIRAMIVVAGNPVLSAPD 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 478 PQVTFPAMRNLDLVVHMATKLNRShlllGRH-NYILPVIGRTETDVqASGeqsITVEDSMSMVHASRGMLtPASPHLRSE 556
Cdd:cd02762   395 GARLEAALGGLEFMVSVDVYMTET----TRHaDYILPPASQLEKPH-ATF---FNLEFPRNAFRYRRPLF-PPPPGTLPE 465
                         490
                  ....*....|
gi 1358904149 557 PAIVAGLAKA 566
Cdd:cd02762   466 WEILARLVEA 475
MopB_3 cd02766
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ...
113-404 1.48e-31

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: 129.68  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYD-PKSDTYQPIEWDTAFREIGERLRSYDDPDSVE-----FYTSGRASNEAAFLWQLFAREYGTNNFpdcSNM 186
Cdd:cd02766    55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKEIKAEYGPEsilpySYAGTMGLLQRAARGRFFHALGASELR---GTI 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 187 CHEPTSVGLPESIGVGKGtVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINPLRERglerftspqspi 266
Cdd:cd02766   132 CSGAGIEAQKYDFGASLG-NDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTA------------ 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 267 emlslsSTELASTYYKVRVGGDAAMLKGVMKILLSMheealatgeaGVLDEAFIREHTEGFDALKADLDATDWDHILKVS 346
Cdd:cd02766   199 ------TAARADLHIQIRPGTDGALALGVAKVLFRE----------GLYDRDFLARHTEGFEELKAHLETYTPEWAAEIT 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358904149 347 GMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGI 404
Cdd:cd02766   263 GVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
MopB_Acetylene-hydratase cd02759
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ...
113-404 5.33e-26

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: 112.40  E-value: 5.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMK-YDPK-SDTYQPIEWDTAFREIGERLRSY---DDPDSVEFY-TSGRASNEA-AFLWQLFAREYGTNNFPDCSN 185
Cdd:cd02759    54 RLLYPLKrVGERgENKWERISWDEALDEIAEKLAEIkaeYGPESIATAvGTGRGTMWQdSLFWIRFVRLFGSPNLFLSGE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 186 MCHEPTSVGLPESIGVGKGTVELeDFDHCDLVLCIGHNPGTNHPRMLG-TLREVSKRGATIVAINPLRerglerftspqs 264
Cdd:cd02759   134 SCYWPRDMAHALTTGFGLGYDEP-DWENPECIVLWGKNPLNSNLDLQGhWLVAAMKRGAKLIVVDPRL------------ 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 265 piemlslssTELAS---TYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGFDALKADLDATDWDH 341
Cdd:cd02759   201 ---------TWLAAradLWLPIRPGTDAALALGMLNVII----------NEGLYDKDFVENWCYGFEELAERVQEYTPEK 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358904149 342 ILKVSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGI 404
Cdd:cd02759   262 VAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL 324
MopB_Thiosulfate-R-like cd02755
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ...
111-492 2.13e-23

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: 103.92  E-value: 2.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 111 EGRLTHPMK-YDPKSD-TYQPIEWDTAFREIGERLRSY---DDPDSVEFyTSGRASNEAAFlwQLFAREYGTNNFPDCSN 185
Cdd:cd02755    53 PDRLKKPLIrVGERGEgKFREASWDEALQYIASKLKEIkeqHGPESVLF-GGHGGCYSPFF--KHFAAAFGSPNIFSHES 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 186 MCHEPTSVGLPESIGVGkGTVELEDFDHCDLVLCIGHN--PGTNHPRM--LGTLREvskRGATIVAINPlrergleRFTs 261
Cdd:cd02755   130 TCLASKNLAWKLVIDSF-GGEVNPDFENARYIILFGRNlaEAIIVVDArrLMKALE---NGAKVVVVDP-------RFS- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 262 pqspiEMLSLsstelASTYYKVRVGGDAAMLKGVMKILLSmheEALatgeagvLDEAFIREHTEGFDALKADLDATDWDH 341
Cdd:cd02755   198 -----ELASK-----ADEWIPIKPGTDLAFVLALIHVLIS---ENL-------YDAAFVEKYTNGFELLKAHVKPYTPEW 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 342 ILKVSGMERKEIQNIARLYANAERTIICY-GMGITQHQYGTQNVQQIANLLLLRGNIGKKGagicplrghsnvqgdrtvg 420
Cdd:cd02755   258 AAQITDIPADTIRRIAREFAAAAPHAVVDpGWRGTFYSNSFQTRRAIAIINALLGNIDKRG------------------- 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358904149 421 iteippqslldsiervfGFTPPQKHghgavaaiqamRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLDLVV 492
Cdd:cd02755   319 -----------------GLYYAGSA-----------KPYPIKALFIYRTNPFHSMPDRARLIKALKNLDLVV 362
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
113-505 3.48e-20

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 92.85  E-value: 3.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYDPKsDTYQPIEWDTAFREIGERLRSY-----DDPDSVEFYTSGRASNEAAFLWQLFAREYGTNNF---PDCS 184
Cdd:pfam00384   1 RLKYPMVRRGD-GKFVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 185 NMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPrMLGT--LREVSKRGATIVAINPLRERGLErftsp 262
Cdd:pfam00384  80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAP-ILNAriRKAALKGKAKVIVIGPRLDLTYA----- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 263 qspIEMLSLSStelastyykvrvGGDAAMLkgvmkiLLSMHeealatgeagvldeAFIREhtegfdaLKADLDAtdwdhi 342
Cdd:pfam00384 154 ---DEHLGIKP------------GTDLALA------LAGAH--------------VFIKE-------LKKDKDF------ 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 343 lkvsgmerkeiqniarlyanAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDrtVGIT 422
Cdd:pfam00384 186 --------------------APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASP--VGAL 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 423 EIppqslldsiervfGFTPPQKhghgAVAAIQAMRDGKAKALLCLGGNLAEAISDPQVTFPAMRNLDLVV----HMATKL 498
Cdd:pfam00384 244 DL-------------GLVPGIK----SVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDKT 306

                  ....*...
gi 1358904149 499 -NRSHLLL 505
Cdd:pfam00384 307 aKYADVIL 314
MopB_DMSOR-like cd02751
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
113-626 6.14e-19

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: 91.52  E-value: 6.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMK---YDPK---------SDTYQPIEWDTAFREIGERLRSYDDpdsvefyTSGrasNEAAFL----WQLFAReyg 176
Cdd:cd02751    47 RIKYPMKrvgWLGNgpgsrelrgEGEFVRISWDEALDLVASELKRIRE-------KYG---NEAIFGgsygWASAGR--- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 177 tnnFPDCSNMCH------------------EPTSVGLPESIG---VGKGTVELED-FDHCDLVLCIGHNPGTN------- 227
Cdd:cd02751   114 ---LHHAQSLLHrflnliggylgsygtystGAAQVILPHVVGsdeVYEQGTSWDDiAEHSDLVVLFGANPLKTrqggggg 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 228 -HPRMLGTLREVSKRGATIVAINPLRERGLErftspqspiemlslsstELASTYYKVRVGGDAAMLKGVMKILLSmheEA 306
Cdd:cd02751   191 pDHGSYYYLKQAKDAGVRFICIDPRYTDTAA-----------------VLAAEWIPIRPGTDVALMLAMAHTLIT---ED 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 307 LatgeagvLDEAFIREHTEGFDALKADLDATDwDHILK-------VSGMERKEIQNIARLYANaERTIICYGMGITQHQY 379
Cdd:cd02751   251 L-------HDQAFLARYTVGFDEFKDYLLGES-DGVPKtpewaaeITGVPAETIRALAREIAS-KRTMIAQGWGLQRAHH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 380 GTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGDRTVGI-------------TEIPPQSLLDSIERvfgftPPQKHG 446
Cdd:cd02751   322 GEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAggpglpqgknpvkDSIPVARIADALLN-----PGKEFT 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 447 HGAvaaiQAMRDGKAKALLCLGGN----------LAEAISDPQvTF--------PAMRNLDLVVHMATKLNRSHLLLGrH 508
Cdd:cd02751   397 ANG----KLKTYPDIKMIYWAGGNplhhhqdlnrLIKALRKDE-TIvvhdifwtASARYADIVLPATTSLERNDIGLT-G 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 509 NYilpvigrtetdvqasgeqsitvedSMSMVHASRGMLTP---AsphlRSEPAIVAGLAKA-------TLHDTVVDWDKM 578
Cdd:cd02751   471 NY------------------------SNRYLIAMKQAVEPlgeA----RSDYEIFAELAKRlgveeefTEGRDEMEWLEH 522
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358904149 579 IGDYSFIRDAIEAV-FPAFANFNERvkkpGGFRLRNAASERVW-------------NTPSGK 626
Cdd:cd02751   523 LYEETRAKAAGPGPeLPSFEEFWEK----GIVRVPAAPKPFVAfadfredpeanplGTPSGK 580
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
113-435 9.92e-19

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: 90.84  E-value: 9.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYDPK--SDTYQPIEWDTAFREIGERLRSYDD---PDSVEF-YTSG------RASNEAAFLWQLFA------RE 174
Cdd:cd02770    59 RLKYPMKRVGKrgEGKFVRISWDEALDTIASELKRIIEkygNEAIYVnYGTGtyggvpAGRGAIARLLNLTGgylnyyGT 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 175 YGTNNFPDcsnmcheptsvGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNhpRMLGT-----LREVSKRGATIVAIN 249
Cdd:cd02770   139 YSWAQITT-----------ATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAET--RMGGGgstyyYLQAKKAGAKFIVID 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 250 PlrergleRFTSpqspiemlslSSTELASTYYKVRVGGDAAMLKGVMKILLSmheEALatgeagvLDEAFIREHTEGFDA 329
Cdd:cd02770   206 P-------RYTD----------TAVTLADEWIPIRPGTDAALVAAMAYVMIT---ENL-------HDQAFLDRYCVGFDA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 330 ------------LKADLDATDWDHILK-------VSGMERKEIQNIARLYANAERTIICYGMGITQHQYGTQNVQQIANL 390
Cdd:cd02770   259 ehlpegappnesYKDYVLGTGYDGTPKtpewaseITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMML 338
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358904149 391 LLLRGNIGKKGAGICPLRGHSNVQGDRTVGI-----TEIPPQSLLDSIER 435
Cdd:cd02770   339 AAMTGNVGIPGGNTGARPGGSAYNGAGLPAGknpvkTSIPCFMWTDAIER 388
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 ...
108-521 1.25e-15

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: 80.13  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 108 LEGEGRLTHPMKYdpKSDTYQPIEWDTAFREIGERLRSYDDpdSVEFYTSGRASNEAAFLWQLFAREY-GTNNFpDCSNM 186
Cdd:cd02771    49 VNSRDRLTQPLIR--RGGTLVPVSWNEALDVAAARLKEAKD--KVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRAR 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 187 CHeptsvgLPESIGVGKG-TVELEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRGATIVAINP-----LRERGLERFT 260
Cdd:cd02771   124 RL------IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSgipkwQDAAVRNIAQ 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 261 SPQSPIEMLSLSSTEL----ASTYYKVrVGGDAAMLKGVmkillsmhEEALATGEAGVLDEAFIrehtegfdalkadlda 336
Cdd:cd02771   198 GAKSPLFIVNALATRLddiaAESIRAS-PGGQARLGAAL--------ARAVDASAAGVSGLAPK---------------- 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 337 tdwdhilkvsgmerKEIQNIARLYANAERTIICYGmgitQHQYGTQNVQQIANLLLLRGNIGkKGAGICPLRGHSNVQGd 416
Cdd:cd02771   253 --------------EKAARIAARLTGAKKPLIVSG----TLSGSLELIKAAANLAKALKRRG-ENAGLTLAVEEGNSPG- 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 417 rtvgiteippqsLLDsiervfGFTPPQKHGHGAVAAIQAMRDGKAKALLCLGGNLAEAISDPQVTfPAMRNLDLVV---H 493
Cdd:cd02771   313 ------------LLL------LGGHVTEPGLDLDGALAALEDGSADALIVLGNDLYRSAPERRVE-AALDAAEFVVvldH 373
                         410       420
                  ....*....|....*....|....*....
gi 1358904149 494 MATK-LNRSHLllgrhnyILPVIGRTETD 521
Cdd:cd02771   374 FLTEtAERADV-------VLPAASFAEKS 395
MopB_NADH-Q-OR-NuoG2 cd02768
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ...
103-266 1.10e-13

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: 73.47  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 103 RSAFE-LEGEGRLTHPMKydPKSDTYQPIEWDTAFREIGERLRSYDdPDSVEFYTSGRASNEAAFLWQLFAREYGTNNFp 181
Cdd:cd02768    43 RFGYDgLNSRQRLTQPLI--KKGGKLVPVSWEEALKTVAEGLKAVK-GDKIGGIAGPRADLESLFLLKKLLNKLGSNNI- 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 182 DCSN-MCHEPTSVGLPESIGVGkgtVELEDFDHCDLVLCIGHNPGTNHPRMLGTLRE-VSKRGATIVAINPLRERGLERF 259
Cdd:cd02768   119 DHRLrQSDLPADNRLRGNYLFN---TSIAEIEEADAVLLIGSNLRKEAPLLNARLRKaVKKKGAKIAVIGPKDTDLIADL 195

                  ....*..
gi 1358904149 260 TSPQSPI 266
Cdd:cd02768   196 TYPVSPL 202
MopB_DMSOR-BSOR-TMAOR cd02769
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
212-404 3.14e-12

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: 69.98  E-value: 3.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 212 DHCDLVLCIGHNP---------GTNHPRMLGTLREVSKRGATIVAINPLRERGLErftspqspiemlslsstELASTYYK 282
Cdd:cd02769   169 EHTELVVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPLRDDTAA-----------------ELGAEWIA 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 283 VRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGFDALKADLDATDwDHILK-------VSGMERKEIQN 355
Cdd:cd02769   232 IRPGTDVALMLALAHTLV----------TEGLHDKAFLARYTVGFDKFLPYLLGES-DGVPKtpewaaaICGIPAETIRE 300
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1358904149 356 IARLYAnAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKKGAGI 404
Cdd:cd02769   301 LARRFA-SKRTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGF 348
PRK15488 PRK15488
thiosulfate reductase PhsA; Provisional
113-492 4.42e-12

thiosulfate reductase PhsA; Provisional


Pssm-ID: 237973 [Multi-domain]  Cd Length: 759  Bit Score: 69.70  E-value: 4.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYDPK--SDTYQPIEWDTAFREIGERLRSYDD---PDSVEFytSGRASNEAAFLWQlFAREYGTnnfPDCsnMC 187
Cdd:PRK15488   98 RIVKPLKRVGErgEGKWQEISWDEAYQEIAAKLNAIKQqhgPESVAF--SSKSGSLSSHLFH-LATAFGS---PNT--FT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 188 HEPTSvglPESIGVGKGTV---ELE-DFDHCDLVLCIGHN--PGTNHPRMLGTLREVSKRGATIVAINPlrergleRFts 261
Cdd:PRK15488  170 HASTC---PAGYAIAAKVMfggKLKrDLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------RF-- 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 262 pqspiemlSLSSTElASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGFDALKADLDATDWDH 341
Cdd:PRK15488  238 --------SVVASK-ADEWHAIRPGTDLAVVLALCHVLI----------EENLYDKAFVERYTSGFEELAASVKEYTPEW 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 342 ILKVSGMERKEIQNIAR-LYANAERTIICYG--MGITQHQYGTQNVQQIANLLLlrGNI--------GKKGAGICPLRGH 410
Cdd:PRK15488  299 AEAISDVPADDIRRIAReLAAAAPHAIVDFGhrATFTPEEFDMRRAIFAANVLL--GNIerkgglyfGKNASVYNKLAGE 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 411 SNVQGDRTVGITEIPPQSL--LDSIERVFGFTppqKHGHGAVAAI-QAMRDGKA---KALLCLGGNLAEAISDPQVTFPA 484
Cdd:PRK15488  377 KVAPTLAKPGVKGMPKPTAkrIDLVGEQFKYI---AAGGGVVQSIiDATLTQKPyqiKGWVMSRHNPMQTVTDRADVVKA 453

                  ....*...
gi 1358904149 485 MRNLDLVV 492
Cdd:PRK15488  454 LKKLDLVV 461
MopB_2 cd02763
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
113-401 5.84e-12

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: 69.09  E-value: 5.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYDPK--SDTYQPIEWDTAFREIGERLRSY--DDPDSVEFYTsGRASNEAafLWQLFAREYGTNNFPDCSNMCH 188
Cdd:cd02763    54 RLTKPLLRKGPrgSGQFEEIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFCS 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 189 EPTSVGLPESIGVGKGTVELEDFDHCDLVLCIG----HNpgtNHPRMLGtLREVSKRGATIVAINPLRErglerftspqs 264
Cdd:cd02763   131 VNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGvaedHH---SNPFKIG-IQKLKRRGGKFVAVNPVRT----------- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 265 piemlslSSTELASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTEGfdalkADLDATDWDHILK 344
Cdd:cd02763   196 -------GYAAIADEWVPIKPGTDGAFILALAHELL----------KAGLIDWEFLKRYTNA-----AELVDYTPEWVEK 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 345 VSGMERKEIQNIAR------LYANAERTII---CYGM----------------GITQHQYGTQNVQQIANLLLLRGNIGK 399
Cdd:cd02763   254 ITGIPADTIRRIAKelgvtaRDQPIELPIAwtdVWGRkhekitgrpvsfhamrGIAAHSNGFQTIRALFVLMMLLGTIDR 333

                  ..
gi 1358904149 400 KG 401
Cdd:cd02763   334 PG 335
Molydop_binding pfam01568
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ...
647-757 1.42e-11

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: 61.91  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 647 LVLTTLRSHDQYNTTLYGLNDRYRGVtGRRDVLFINPDEAEKRELRVGDQVNItaldpdgnpTSRRMHNLTVVVID--MA 724
Cdd:pfam01568   1 LYLITGRVLGQYHSQTRTRRVLRLAK-PEPEVVEIHPEDAAALGIKDGDLVEV---------TSRRGSVVVRAKVTdrVR 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1358904149 725 PGSVGAYYPE--------ANVLVPLDShDTQSGIPAYKSIP 757
Cdd:pfam01568  71 PGVVFMPFGWwyeprggnANALTDDAT-DPLSGGPEFKTCA 110
MopB_CT cd02775
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ...
654-754 2.42e-10

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: 58.10  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 654 SHDQYNTTLYGLNDRYRGVTgRRDVLFINPDEAEKRELRVGDQVNItaldpdgnpTSRRMHNLTVVVID--MAPGSVGAY 731
Cdd:cd02775     1 LRDHFHSGTRTRNPWLRELA-PEPVVEINPEDAAALGIKDGDLVRV---------ESRRGSVVLRAKVTdgVPPGVVFLP 70
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1358904149 732 YP---------EANVLVPLDSHDTqSGIPAYK 754
Cdd:cd02775    71 HGwghrggrggNANVLTPDALDPP-SGGPAYK 101
MopB_NDH-1_NuoG2 cd02772
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ...
97-251 1.69e-09

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: 60.83  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  97 VSELW--ERSAFELEG---EGRLTHPMKydPKSDTYQPIEWDTAFREIGERL---RSYDDPDSVEFYTSGRASNEAAFLW 168
Cdd:cd02772    33 INECWlsDRDRFSYEGlnsEDRLTKPMI--KKDGQWQEVDWETALEYVAEGLsaiIKKHGADQIGALASPHSTLEELYLL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 169 QLFAREYGTNNFP------DCSNMCHEPTSVGLPESIgvgkgtvelEDFDHCDLVLCIGHNPGTNHPRMLGTLREVSKRG 242
Cdd:cd02772   111 QKLARGLGSDNIDhrlrqsDFRDDAKASGAPWLGMPI---------AEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKG 181

                  ....*....
gi 1358904149 243 ATIVAINPL 251
Cdd:cd02772   182 AKLSAINPA 190
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
110-489 4.55e-09

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 59.91  E-value: 4.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 110 GEGRLTHPM------KYDPKSDtYQPIEWDTAFREIGERLRSY---DDPDSVEFYTSGRASneaafLWQ------LFARE 174
Cdd:PRK13532   94 GKDRLTQPLlrmkdgKYDKEGE-FTPVSWDQAFDVMAEKFKKAlkeKGPTAVGMFGSGQWT-----IWEgyaaskLMKAG 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 175 YGTNNFPDCSNMCHEPTSVGLPESIGVGKGTVELEDFDHCDLVLCIGHNPGTNHPrMLGTlrEVSKRgativainplrer 254
Cdd:PRK13532  168 FRSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHP-ILWS--RVTDR------------- 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 255 gleRFTSPQSPIEMLSL---SSTELASTYYKVRVGGDAAMLKGVMKILLsmheealatgEAGVLDEAFIREHTE------ 325
Cdd:PRK13532  232 ---RLSNPDVKVAVLSTfehRSFELADNGIIFTPQTDLAILNYIANYII----------QNNAVNWDFVNKHTNfrkgat 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 326 ----------------------------GFDALKADLDATDWDHILKVSGMERKEIQNIARLYANAERTIICY-GMGITQ 376
Cdd:PRK13532  299 digyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVSFwTMGFNQ 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 377 HQYGTQNVQQIANLLLLRGNIGKKGAGICPLRGHSNVQGD-RTVG-------------------ITE----IPPQsllds 432
Cdd:PRK13532  379 HTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGTaREVGtfshrlpadmvvtnpkhreIAEkiwkLPEG----- 453
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358904149 433 iervfgfTPPQKHGHGAVAAIQAMRDGKAKAL--LClGGNLAEAISDPQVTFPAMRNLD 489
Cdd:PRK13532  454 -------TIPPKPGYHAVAQDRMLKDGKLNAYwvMC-NNNMQAGPNINEERLPGWRNPD 504
MopB_FmdB-FwdB cd02761
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ...
128-415 1.83e-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: 57.34  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 128 QPIEWDTAFREIGERLRSYDDPdsvEFYTSGRASNEAAFLWQLFAREYGTNnFPDCSNMCHEPTSVGLPESiGVgKGTVE 207
Cdd:cd02761    52 KPVSLEEAIEKAAEILKEAKRP---LFYGLGTTVCEAQRAGIELAEKLGAI-IDHAASVCHGPNLLALQDS-GW-PTTTL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 208 LEDFDHCDLVLCIGHNPGTNHPRML--------GTLREVSKRGATIVAINPlrergleRFTSpqspiemlslsSTELAST 279
Cdd:cd02761   126 GEVKNRADVIVYWGTNPMHAHPRHMsrysvfprGFFREGGREDRTLIVVDP-------RKSD-----------TAKLADI 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 280 YYKVRVGGDAAMLKGVMkillsmheeALATGEAGVLDEafirehtegfdalkadldatdwdhilkVSGMERKEIQNIARL 359
Cdd:cd02761   188 HLQIDPGSDYELLAALR---------ALLRGAGLVPDE---------------------------VAGIPAETILELAER 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358904149 360 YANAERTIICYGMGITQHQYGTQNVQQIANLLLLRGNIGKkgAGICPLRGHSNVQG 415
Cdd:cd02761   232 LKNAKFGVIFWGLGLLPSRGAHRNIEAAIRLVKALNEYTK--FALLPLRGHYNVRG 285
MopB_Tetrathionate-Ra cd02758
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ...
113-401 3.52e-07

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: 53.89  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 113 RLTHPMKYDPK--SDTYQPIEWDTAFREI---------GER--LRSYDDPDSV------EF--------YTSGRASNEAA 165
Cdd:cd02758    83 RVLQPLKRVGPrgSGKWKPISWEQLIEEVveggdlfgeGHVegLKAIRDLDTPidpdhpDLgpkanqllYTFGRDEGRTP 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 166 FLWQLFAREYGTNNFPDCSNMCheptsvGLPESIGVGKGTVELE-------DFDHCDLVLCIGHNPGTNHPRMlgtlrev 238
Cdd:cd02758   163 FIKRFANQAFGTVNFGGHGSYC------GLSYRAGNGALMNDLDgyphvkpDFDNAEFALFIGTSPAQAGNPF------- 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 239 sKRGATIVAiNPLRERGLERFTSpqSPIEMLSLSSTELASTYYKVRVGGDAAMLKGVM-----------KILLSMHEEAL 307
Cdd:cd02758   230 -KRQARRLA-EARTEGNFKYVVV--DPVLPNTTSAAGENIRWVPIKPGGDGALAMAMIrwiienerynaEYLSIPSKEAA 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 308 -ATGEAGVLDEAF---IREHTEGFDALKADLDATDWDHILKVSGMERKEIQNIARLYANAER--TIICYgmGITQHQYGT 381
Cdd:cd02758   306 kAAGEPSWTNATHlviTVRVKSALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRaaAVVHH--GGTMHSNGF 383
                         330       340
                  ....*....|....*....|
gi 1358904149 382 QNVQQIANLLLLRGNIGKKG 401
Cdd:cd02758   384 YNAYAIRMLNALIGNLNWKG 403
MopB_CT_Fdh-Nap-like cd00508
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ...
645-762 1.82e-06

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: 47.50  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 645 HDLVLTTLRSHDQYNTtlyglndryRGVTGR---------RDVLFINPDEAEKRELRVGDQVNITaldpdgnptSRRMHN 715
Cdd:cd00508     3 YPLVLTTGRLLEHWHT---------GTMTRRsprlaalapEPFVEIHPEDAARLGIKDGDLVRVS---------SRRGSV 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358904149 716 LTVVVID--MAPGSVGAYY--------PEANVLVPLDShDTQSGIPAYKSIPIAMER 762
Cdd:cd00508    65 VVRARVTdrVRPGTVFMPFhwggevsgGAANALTNDAL-DPVSGQPEFKACAVRIEK 120
MopB_CT_Acetylene-hydratase cd02781
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ...
645-762 6.74e-05

The MopB_CT_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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239182 [Multi-domain]  Cd Length: 130  Bit Score: 43.07  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 645 HDLVLTTlrshdqYNTTLYGLNDRYRGVTGRRD-----VLFINPDEAEKRELRVGDQVNITAldPDGnptsrRMHNLTVV 719
Cdd:cd02781     2 YPLILTT------GARSYYYFHSEHRQLPSLRElhpdpVAEINPETAAKLGIADGDWVWVET--PRG-----RARQKARL 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358904149 720 VIDMAPGSV----GAYYPE---------------ANVLVPLDSHDTQSGIPAYKSIPIAMER 762
Cdd:cd02781    69 TPGIRPGVVraehGWWYPEreagepalggvwesnANALTSDDWNDPVSGSSPLRSMLCKIYK 130
MopB_CT_1 cd02782
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
646-763 1.65e-03

The MopB_CT_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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239183 [Multi-domain]  Cd Length: 129  Bit Score: 39.30  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 646 DLVLTTLRSHDQYNTTLYglndRYRGVTGRRD--VLFINPDEAEKRELRVGDQVNITaldpdgnpTSRRMHNLTV-VVID 722
Cdd:cd02782     4 FLLLIGRRHLRSNNSWLH----NDPRLVKGRNrcTLRIHPDDAAALGLADGDKVRVT--------SAAGSVEAEVeVTDD 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358904149 723 MAPGSV------GAYYP-----------EANVLVPLDSHDTQSGIPAYKSIPIAMERV 763
Cdd:cd02782    72 MMPGVVslphgwGHDYPgvsgagsrpgvNVNDLTDDTQRDPLSGNAAHNGVPVRLARV 129
PRK07860 PRK07860
NADH dehydrogenase subunit G; Validated
97-258 2.74e-03

NADH dehydrogenase subunit G; Validated


Pssm-ID: 236118 [Multi-domain]  Cd Length: 797  Bit Score: 41.08  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149  97 VSELWE----RSAFEL-EGEGRLTHPMKYDpKSDTYQPIEWDTAFREIGERLRSYDDpdSVEFYTSGRASNEAAFLWQLF 171
Cdd:PRK07860  257 VNEEWNcdkgRWAFTYaTQPDRITTPLVRD-EDGELEPASWSEALAVAARGLAAARG--RVGVLVGGRLTVEDAYAYAKF 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358904149 172 AR-EYGTNNFpDCSNMCHEPTSVGLPESIGVGKG-TVELEDFDHCDLVLCIGHNPGTNHPRMLGTLRE-VSKRGATIVAI 248
Cdd:PRK07860  334 ARvALGTNDI-DFRARPHSAEEADFLAARVAGRGlGVTYADLEKAPAVLLVGFEPEEESPIVFLRLRKaARKHGLKVYSI 412
                         170
                  ....*....|
gi 1358904149 249 NPLRERGLER 258
Cdd:PRK07860  413 APFATRGLEK 422
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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