|
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
|
|
|