|
Name |
Accession |
Description |
Interval |
E-value |
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
24-761 |
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: 979.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 24 AAGIPGVAATLRHSMAQMGVARTARTLRVINQRDGFDCPGCAWPEGrGEHRKAVEFCENGAKAVAEEATLRRVGREFFAS 103
Cdd:TIGR01701 2 AGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVS-PQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 104 HSVAELAERTDYWLGQQGRLTEPMVLRG--THYEPIGWDAAFALIAEHLRALStPDEAVFYTSGRTSNEAAFLYQLLVRS 181
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPgsDHYTPISWDDAYQEIAAKLNSLD-PKQVAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 182 YGTNNLPDCSNMCHESSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPLPEA 261
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 262 GLLRFKNPQN-VRGVVGRGTPLADQFLQIRLAGDQALFQAVGNLLLRWEDARPGTVVDRAFVERSTVDFDRYAEHVRALD 340
Cdd:TIGR01701 240 GLERFWIPQIpESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQPGSLIDHEFIANHTNGFDELRRHVLQLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 341 WEAVFAATGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPVRGHSNVQGDRT 420
Cdd:TIGR01701 320 WNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 421 MGIWEKMPEAFLSALESEFGVPVPRKHGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDTEVTEAALRQCELTVQVSTKL 500
Cdd:TIGR01701 400 MGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 501 NRSHVVPGRTALILPTLGRTERDKQASGEQFVTVEDSMSVVHRSRGRLDPASPHLRSEVAIICGLAQALFgPDHPVPWAR 580
Cdd:TIGR01701 480 NRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALL-PETPVAWEI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 581 FVEDYDRVRDHIANVVPGCADYNTRVRTPDGFVLPHAPRDAREFRgTESGKALFTANELTVLEVPPGR---LLLQTLRSH 657
Cdd:TIGR01701 559 LVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAALCERKFP-TPDGKANFIVIPLPEFRVPTGHefeLVLVTLRSH 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 658 DQYNTTIYGMDDRYRGVKDGRRVVFVNPDDLAALSIDDGALVDLVSEYAD-RERRAERFRVVAYPTARGCAATYFPEANN 736
Cdd:TIGR01701 638 DQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDgQKRKFDNLRIVFYDTPTGNAAAYYPEANP 717
|
730 740
....*....|....*....|....*
gi 1906445253 737 LVPLDSTAEVSNTPTSKSLVVRLEP 761
Cdd:TIGR01701 718 LLPLDHHDPQSKTPEYKTIPVRLEA 742
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
58-634 |
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: 875.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 58 GFDCPGCAWPEGrGEHRKAVEFCENGAKAVAEEATLRRVGREFFASHSVAELAERTDYWLGQQGRLTEPMVLRGT--HYE 135
Cdd:cd02767 1 GFDCPGCAWGDP-GQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGsdHYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 136 PIGWDAAFALIAEHLRALStPDEAVFYTSGRTSNEAAFLYQLLVRSYGTNNLPDCSNMCHESSGAALAQTTGIGKGSVTL 215
Cdd:cd02767 80 PISWDEAFAEIAARLRALD-PDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 216 ADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPLPEAGLLRFKNPQNVRGVVGRGTPLADQFLQIRLAGDQ 295
Cdd:cd02767 159 EDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLTGGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 296 ALFQAVGNLLLRWEDARPGtVVDRAFVERSTVDFDRYAEHVRALDWEAVFAATGLTHGEIEKFARTVADSKRMIVCWAMG 375
Cdd:cd02767 239 ALLNGMAKHLIERDDEPGN-VLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 376 LTQHRHAVATIREIANVVLVRGMIGKPGAGLCPVRGHSNVQGDRTMGIWEKMPEAFLSALESEFGVPVPRKHGYDTVEAI 455
Cdd:cd02767 318 ITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDTVEAI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 456 RAMRDGKAKVFMAVGGNFAAATPDTEVTEAALRQCELTVQVSTKLNRSHVVPGRTALILPTLGRTERDKQASGEQFVTVE 535
Cdd:cd02767 398 EAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQAVTVE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 536 DSMSVVHRSRGRLDPASPHLRSEVAIICGLAQALFGpDHPVPWARFVEDYDRVRDHIANVVP-GCADYNTRVRTPDGFVL 614
Cdd:cd02767 478 DSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLG-EAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGGFHL 556
|
570 580
....*....|....*....|
gi 1906445253 615 PHAPRDaREFRgTESGKALF 634
Cdd:cd02767 557 PNGARE-RKFN-TPSGKAQF 574
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
24-761 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 693.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 24 AAG----IPGVAATLRHsmaQMGVARTARTLRVINQRDGFDCPGCAWPEGRgeHRKAVEFCENGAKAVAEEATLRRVGRE 99
Cdd:PRK09939 11 AAGgwgaVKSVANAVRK---QMDIRQDVIAMFDMNKPEGFDCPGCAWPDPK--HSASFDICENGAKAIAWEVTDKQVNAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 100 FFASHSVAELAERTDYWLGQQGRLTEPMVLRGT--HYEPIGWDAAFALIAEHLRALSTPDEAVFYTSGRTSNEAAFLYQL 177
Cdd:PRK09939 86 FFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVsdCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 178 LVRSYGTNNLPDCSNMCHESSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNP 257
Cdd:PRK09939 166 FAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 258 LPEAGLLRFKNPQN-VRGVVGRGTPLADQFLQIRLAGDQALFQAVGNLLLRWEDA-----RPgTVVDRAFVERSTVDFDR 331
Cdd:PRK09939 246 LQERGLERFTAPQNpFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAasaagRP-SLLDDEFIQTHTVGFDE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 332 YAEHVRALDWEAVFAATGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPVRG 411
Cdd:PRK09939 325 LRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 412 HSNVQGDRTMGIWEKMPEAFLSALESEFGVPVPRKHGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDTEVTEAALRQCE 491
Cdd:PRK09939 405 HSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 492 LTVQVSTKLNRSHVVPGRTALILPTLGRTERDKQASGEQFVTVEDSMSVVHRSRGRLDPASPHLRSEVAIICGLAQALFg 571
Cdd:PRK09939 485 LAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAAL- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 572 PDHPVPWARFVEDYDRVRDHIANVVPGCADYNTRVRTPDGFVLPHAPRDAREFrgTESGKALFTANElTVLEVPP----G 647
Cdd:PRK09939 564 PQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWM--TPSGKANFITSK-GLLEDPSsafnS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 648 RLLLQTLRSHDQYNTTIYGMDDRYRGVKDGRRVVFVNPDDLAALSIDDGALVDLVSEYADRE---RRAERFRVVAYPTAR 724
Cdd:PRK09939 641 KLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKrssRRMDRLKVVIYPMAD 720
|
730 740 750
....*....|....*....|....*....|....*..
gi 1906445253 725 GCAATYFPEANNLVPLDSTAEVSNTPTSKSLVVRLEP 761
Cdd:PRK09939 721 RSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
21-761 |
1.22e-172 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 511.70 E-value: 1.22e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 21 KTFAAGIPGVAAtlrhsmAQMGVARTARTLrvinqrdgfdCPGCAwpegrgehrkavEFCENGAKAvaEEATLRRVGREf 100
Cdd:COG0243 4 RDFKAAGAGAAA------LEAAGTKTVKTT----------CPGCG------------VGCGLGVKV--EDGRVVRVRGD- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 101 fASHSVAEL-----AERTDYWLGQQGRLTEPMVLRG----THYEPIGWDAAFALIAEHLRALST---PDEAVFYTSG--- 165
Cdd:COG0243 53 -PDHPVNRGrlcakGAALDERLYSPDRLTYPMKRVGprgsGKFERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsa 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 166 -RTSNEAAFLYQLLVRSYGTNNLPDCSNMCHESSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSAL-E 243
Cdd:COG0243 132 gRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLrE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 244 AAKGNGAKIVAVNPLPEagllrfknpqnvrgvvgRGTPLADQFLQIRLAGDQALFQAVGNLLLRWEdarpgtVVDRAFVE 323
Cdd:COG0243 212 AAKKRGAKIVVIDPRRT-----------------ETAAIADEWLPIRPGTDAALLLALAHVLIEEG------LYDRDFLA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 324 RSTVDFDRYAEHVRALDWEAVFAATGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPG 403
Cdd:COG0243 269 RHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 404 AGLCPVRGhsnvqgdrtmgiwekmpeaflsalesefgvpvprkhgydtvEAIRAMRDGKAKVFMAVGGNFAAATPDTEVT 483
Cdd:COG0243 349 GGPFSLTG-----------------------------------------EAILDGKPYPIKALWVYGGNPAVSAPDTNRV 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 484 EAALRQCELTVQVSTKLNRSHVVpgrTALILPTLGRTERDkqasgEQFVTVEDSMsvVHRSRGRLDPASpHLRSEVAIIC 563
Cdd:COG0243 388 REALRKLDFVVVIDTFLTETARY---ADIVLPATTWLERD-----DIVTNSEDRR--VHLSRPAVEPPG-EARSDWEIFA 456
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 564 GLAQALfGPDHPVPWARFVEDYdrVRDHIANVVPGCADYNtRVRTPDGFVLPHAPRDAreFR-----GTESGKALFTANE 638
Cdd:COG0243 457 ELAKRL-GFEEAFPWGRTEEDY--LRELLEATRGRGITFE-ELREKGPVQLPVPPEPA--FRndgpfPTPSGKAEFYSET 530
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 639 LTVLEVP--------------PGRLLLQTLRSHDQYNTTIYGmDDRYRGVKdGRRVVFVNPDDLAALSIDDGALVDLVSE 704
Cdd:COG0243 531 LALPPLPryappyegaepldaEYPLRLITGRSRDQWHSTTYN-NPRLREIG-PRPVVEINPEDAAALGIKDGDLVRVESD 608
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906445253 705 YAdrerRAERFRVVAYPTARGCAATYF-----------PEANNLVPlDSTAEVSNTPTSKSLVVRLEP 761
Cdd:COG0243 609 RG----EVLARAKVTEGIRPGVVFAPHgwwyepaddkgGNVNVLTP-DATDPLSGTPAFKSVPVRVEK 671
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
121-761 |
2.73e-111 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 353.03 E-value: 2.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 121 GRLTEPMVLRGTHYEPIGWDAAFALIAEHLRALST---PDEAVFYTSGRTSNEAAFLYQLLVRSY-GTNNLPDCSNMCHE 196
Cdd:COG3383 60 DRLTTPLIRRGGEFREVSWDEALDLVAERLREIQAehgPDAVAFYGSGQLTNEENYLLQKLARGVlGTNNIDNNARLCMA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 197 SSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPlpeagllrfknpqnvrgvv 276
Cdd:COG3383 140 SAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 277 gRGTPL---ADQFLQIRLAGDQALFQAVGNLLLrWEDArpgtvVDRAFVERSTVDFDRYAEHVRALDWEAVFAATGLTHG 353
Cdd:COG3383 201 -RRTETarlADLHLQIKPGTDLALLNGLLHVII-EEGL-----VDEDFIAERTEGFEELKASVAKYTPERVAEITGVPAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 354 EIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPVRGHSNVQGDRTMGIwekMP----- 428
Cdd:COG3383 274 DIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGA---LPnvlpg 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 429 ------EAFLSALESEFGVP-VPRKHGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDTEVTEAALRQCELTVqVSTkln 501
Cdd:COG3383 351 yrdvtdPEHRAKVADAWGVPpLPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLV-VQD--- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 502 rshVVPGRTA----LILPTLGRTERDKqasgeqfvTVEDSMSVVHRSRGRLDPAsPHLRSEVAIICGLAQAL---FGPDH 574
Cdd:COG3383 427 ---IFLTETAeyadVVLPAASWAEKDG--------TFTNTERRVQRVRKAVEPP-GEARPDWEIIAELARRLgygFDYDS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 575 PvpwarfvEDydrVRDHIANVVPGCA--DYNtRVRTPDGFVLP----HAPRDAREFRG---TESGKALFTANELTVLEVP 645
Cdd:COG3383 495 P-------EE---VFDEIARLTPDYSgiSYE-RLEALGGVQWPcpseDHPGTPRLFTGrfpTPDGKARFVPVEYRPPAEL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 646 PGR---LLLQTLRSHDQYNT-TIYGMDDRYRGVkDGRRVVFVNPDDLAALSIDDGALVDLVSeyadreRRAErFRVVAYP 721
Cdd:COG3383 564 PDEeypLVLTTGRLLDQWHTgTRTRRSPRLNKH-APEPFVEIHPEDAARLGIKDGDLVRVSS------RRGE-VVLRARV 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1906445253 722 TAR---GCAATYF----PEANNLVPlDSTAEVSNTPTSKSLVVRLEP 761
Cdd:COG3383 636 TDRvrpGTVFMPFhwgeGAANALTN-DALDPVSKQPEYKACAVRVEK 681
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
122-759 |
7.63e-93 |
|
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: 304.39 E-value: 7.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGTHYEPIGWDAAFALIAEHLRALST---PDEAVFYTSGRTSNEAAFLYQLLVRS-YGTNNLPDCSNMCHES 197
Cdd:TIGR01591 53 RLTTPLIREGDKFREVSWDEAISYIAEKLKEIKEkygPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCHGP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 198 SGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPlpeagllrfknpqnvrgvvg 277
Cdd:TIGR01591 133 SVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-------------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 278 RGTPL---ADQFLQIRLAGDQALFQAVGNLLL--RWEDarpgtvvdRAFVERSTVDFDRYAEHVRALDWEAVFAATGLTH 352
Cdd:TIGR01591 193 RKTETakiADLHIPLKPGTDIALLNAMANVIIeeGLYD--------KAFIEKRTEGFEEFREIVKGYTPEYVEDITGVPA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 353 GEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPVRGHSNVQGDRTMGIWEKMP---- 428
Cdd:TIGR01591 265 DLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGALPDFLpgyq 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 429 ----EAFLSALESEFG-VPVPRKHGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDTEVTEAALRQCELTVQVSTKLNRS 503
Cdd:TIGR01591 345 pvsdEEVREKFAKAWGvVKLPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTET 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 504 ----HVVpgrtaliLPTlgrterdkQASGEQFVTVEDSMSVVHRSRGRLDPASpHLRSEVAIICGLAQALfgpdhPVPWa 579
Cdd:TIGR01591 425 akyaDVV-------LPA--------AAWLEKEGTFTNAERRIQRFFKAVEPKG-ESKPDWEIIQELANAL-----GLDW- 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 580 rFVEDYDRVRDHIANVVPGCA--------DYNTRVRTPDGFVLPHAPRDAREFRGTESGKALF-TANELTVLEVPPGR-- 648
Cdd:TIGR01591 483 -NYNHPQEIMDEIRELTPLFAgltyerldELGSLQWPCNDSDASPTSYLYKDKFATPDGKAKFiPLEWVAPIEEPDDEyp 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 649 LLLQTLRSHDQYNTTiyGMDDRYRGV--KDGRRVVFVNPDDLAALSIDDGALVDLVSEYADRERRAerfRVVAYPTARGC 726
Cdd:TIGR01591 562 LILTTGRVLTHYNVG--EMTRRVAGLrrLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRA---KVSDRVNKGAI 636
|
650 660 670
....*....|....*....|....*....|....*.
gi 1906445253 727 AAT---YFPEANNLVPLDSTaEVSNTPTSKSLVVRL 759
Cdd:TIGR01591 637 YITmhfWDGAVNNLTTDDLD-PISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
122-634 |
6.78e-76 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 254.45 E-value: 6.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGTHYEPIGWDAAFALIAEHLRALS---TPDEAVFYTSGRTSNEAAFLYQLLVRS-YGTNNLPDCSNMCHES 197
Cdd:cd02753 54 RLTKPLIRKNGKFVEASWDEALSLVASRLKEIKdkyGPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCHSP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 198 SGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPlpeagllrfknpqnvrgvvg 277
Cdd:cd02753 134 TVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-------------------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 278 RGTPL---ADQFLQIRLAGDQALFQAVGNLLLRwEDarpgtVVDRAFVERSTVDFDRYAEHVRALDWEAVFAATGLTHGE 354
Cdd:cd02753 194 RRTELarfADLHLQLRPGTDVALLNAMAHVIIE-EG-----LYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAED 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 355 IEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPVRGHSNVQGDRTMGiweKMPEAFlsa 434
Cdd:cd02753 268 IREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG---ALPNVL--- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 435 lesefgvPvprkhGYdtveaIRAMrdgkakvfMAVGGNFAAATPDTEVTEAALRQCE-LTVQvstklnrsHVVPGRTA-- 511
Cdd:cd02753 342 -------P-----GY-----VKAL--------YIMGENPALSDPNTNHVRKALESLEfLVVQ--------DIFLTETAel 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 512 --LILPTlgrterdkQASGEQFVTVEDSMSVVHRSRGRLDPASpHLRSEVAIICGLAQALFGPDHpvpwarfvedYDRVR 589
Cdd:cd02753 389 adVVLPA--------ASFAEKDGTFTNTERRVQRVRKAVEPPG-EARPDWEIIQELANRLGYPGF----------YSHPE 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906445253 590 ---DHIANVVP--GCADYNtRVRTPDGFVLP------------HAPRDArefrgTESGKALF 634
Cdd:cd02753 450 eifDEIARLTPqyAGISYE-RLERPGGLQWPcpdedhpgtpilHTERFA-----TPDGKARF 505
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
121-569 |
1.14e-61 |
|
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: 211.80 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 121 GRLTEPMVLRG--THYEPIGWDAAFALIAEHLRALST---PDEAVFYTSGRTSNEAAFLYQLLVRSYGTNNLPDCSNMCH 195
Cdd:cd00368 53 DRLKYPLIRVGgrGKFVPISWDEALDEIAEKLKEIREkygPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 196 ESSGAALAQTtGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPLPEagllrfknpqnvrgv 275
Cdd:cd00368 133 ASAVAALKAF-GGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRT--------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 276 vgRGTPLADQFLQIRLAGDQALFQAvgnlllrwedarpgtvvdrafverstvdfDRYAEHvraldweavfaaTGLTHGEI 355
Cdd:cd00368 197 --ETAAKADEWLPIRPGTDAALALA-----------------------------EWAAEI------------TGVPAETI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 356 EKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPvrghsnvqgdrtmgiwekmpeaflsal 435
Cdd:cd00368 234 RALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP--------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 436 esefgvpvprkhgydtveairamrdgkakvfmavGGNFAAATPDTEVTEAALRQCELTVQVSTKLNRSHvvpgRTA-LIL 514
Cdd:cd00368 287 ----------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETA----AYAdVVL 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1906445253 515 PTLGRTERDkqasgeqfVTVEDSMSVVHRSRGRLDPAsPHLRSEVAIICGLAQAL 569
Cdd:cd00368 329 PAATYLEKE--------GTYTNTEGRVQLFRQAVEPP-GEARSDWEILRELAKRL 374
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
117-569 |
3.54e-61 |
|
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: 215.94 E-value: 3.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 117 LGQQGRLTEPMVLR-GTHYEPIGWDAAFALIAEHLRALST---PDEAVFYTSGRTSNEAAFLYQLLVRSY-GTNNLPDCS 191
Cdd:cd02754 49 LNGPERLTRPLLRRnGGELVPVSWDEALDLIAERFKAIQAeygPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 192 NMCHESSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAK--GNGAKIVAVNPlpeagllrfknp 269
Cdd:cd02754 129 RLCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKkaNPGAKIIVVDP------------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 270 qnvrgvvgRGTP---LADQFLQIRLAGDQALFQAVGNLLLrWEDArpgtvVDRAFVERSTVDFDRYAEHVRALDWEAVFA 346
Cdd:cd02754 197 --------RRTRtadIADLHLPIRPGTDLALLNGLLHVLI-EEGL-----IDRDFIDAHTEGFEELKAFVADYTPEKVAE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 347 ATGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPVRGHSNVQGDRTMG---- 422
Cdd:cd02754 263 ITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGglan 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 423 -----IWEKMPE--AFLSALeseFGVPV---PRKHGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDTEVTEAALRQCEL 492
Cdd:cd02754 343 llpghRSVNNPEhrAEVAKF---WGVPEgtiPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEF 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906445253 493 TVqVSTKLNRShvVPGRTA-LILPTLGRTERDkqasGeqfvTVEDSMSVVHRSRGRLDPAsPHLRSEVAIICGLAQAL 569
Cdd:cd02754 420 VV-VQDAFADT--ETAEYAdLVLPAASWGEKE----G----TMTNSERRVSLLRAAVEPP-GEARPDWWILADVARRL 485
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
649-759 |
3.72e-50 |
|
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: 170.92 E-value: 3.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 649 LLLQTLRSHDQYNTTIYGMDDRYRGVKDGRRVVFVNPDDLAALSIDDGALVDLVSEYAD-RERRAERFRVVAYPTARGCA 727
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDgQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 1906445253 728 ATYFPEANNLVPLDSTAEVSNTPTSKSLVVRL 759
Cdd:cd02787 81 AAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
122-428 |
3.12e-38 |
|
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: 151.40 E-value: 3.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRG--THYEPIGWDAAFALIAEHLRALST---------------PDEAVFYTSGRTSNEAAFLYQLLVRSYGT 184
Cdd:cd02752 54 RLKYPMYRAPgsGKWEEISWDEALDEIARKMKDIRDasfveknaagvvvnrPDSIAFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 185 NNLPDCSNMCHESSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHP-RMLSALEAAKGNGAKIVAVNPlpeagl 263
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 264 lRFKnpqnvrgvvgRGTPLADQFLQIRLAGDQALFQAVGNLLLRWEdarPGTVVDRAFVerSTVDFDRYAEhvraldwea 343
Cdd:cd02752 208 -RFT----------RTAAKADLYVPIRSGTDIAFLGGMINYIIRYT---PEEVEDICGV--PKEDFLKVAE--------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 344 VFAATGlthgeiekfartvADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPVRGHSNVQGDRTMGI 423
Cdd:cd02752 263 MFAATG-------------RPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGL 329
|
....*.
gi 1906445253 424 -WEKMP 428
Cdd:cd02752 330 lSHNLP 335
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
122-496 |
3.89e-29 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 121.64 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMvlRGTH------YEPIGWDAAFALIAEHLRALS---TPDEAVFY-TSGRTSNEAAFLYQL-LVRSYGTNNLPDC 190
Cdd:cd02759 54 RLLYPL--KRVGergenkWERISWDEALDEIAEKLAEIKaeyGPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 191 SNMCHESSGAALAQTTGIGKGSVTlADLEQADLIVVVGQNPG-TNHPRMLSALEAAKGNGAKIVAVNPlpeagllrfknp 269
Cdd:cd02759 132 GESCYWPRDMAHALTTGFGLGYDE-PDWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDP------------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 270 qnvrgvvgRGTPLA---DQFLQIRLAGDQALFQAVGNLLLRWEdarpgtVVDRAFVERSTVDFDRYAEHVRALDWEAVFA 346
Cdd:cd02759 199 --------RLTWLAaraDLWLPIRPGTDAALALGMLNVIINEG------LYDKDFVENWCYGFEELAERVQEYTPEKVAE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 347 ATGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLcpvrghsnvqgdrtmgiwek 426
Cdd:cd02759 265 ITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL-------------------- 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 427 mpeaflsalesefGVPVPrkhgydtveaIRAMrdgkakvfMAVGGNFAAATPDTEVTEAALRQCELTVQV 496
Cdd:cd02759 325 -------------LIPYP----------VKML--------IVFGTNPLASYADTAPVLEALKALDFIVVV 363
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
122-611 |
4.88e-28 |
|
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: 118.89 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMV---LRGTHYEPIGWDAAFALIAEHLRAL--STPDEAVFYTS-----GRTSNEA-AFLYQLLvrsyGTNNL--P 188
Cdd:cd02766 55 RLLTPLKrvgRKGGQWERISWDEALDTIAAKLKEIkaEYGPESILPYSyagtmGLLQRAArGRFFHAL----GASELrgT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 189 DCSnmcheSSGAAlAQTTGIG-KGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPLPeagllrfk 267
Cdd:cd02766 131 ICS-----GAGIE-AQKYDFGaSLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYR-------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 268 npqnvrgvvGRGTPLADQFLQIRLAGDQALFQAVGNLLLRWEDarpgtvVDRAFVERSTVDFDRYAEHVRALDWEAVFAA 347
Cdd:cd02766 197 ---------TATAARADLHIQIRPGTDGALALGVAKVLFREGL------YDRDFLARHTEGFEELKAHLETYTPEWAAEI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 348 TGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGlcpvrghsnvqgdrtmgiwekm 427
Cdd:cd02766 262 TGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGG---------------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 428 peaflsALESEFGVPVprkhgydtveairamrdgkaKVFMAVGGNFAAATPDT-EVTEAALRQCELTVQVSTKLNRShvv 506
Cdd:cd02766 320 ------AFYSNSGPPV--------------------KALWVYNSNPVAQAPDSnKVRKGLAREDLFVVVHDQFMTDT--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 507 pGRTA-LILPTLGRTERdkqasgEQFVTvedsmSVVHRSRGRLDPASPHL---RSEVAIICGLAQALFGPDHPVPWAR-- 580
Cdd:cd02766 371 -ARYAdIVLPATTFLEH------EDVYA-----SYWHYYLQYNEPAIPPPgeaRSNTEIFRELAKRLGFGEPPFEESDee 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1906445253 581 -------------FVEDYDRVRDHIANVVPGCADYNTRVRTPDG 611
Cdd:cd02766 439 wldqaldgtglplEGIDLERLLGPRKAGFPLVAWEDRGFPTPSG 482
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
110-618 |
4.99e-28 |
|
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: 119.42 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 110 AERTDYWLGQQGRLTEPMVLRGTHYEPIGWDAAFALIAEHLRALST---PDEAVFYTSGRTSNEAA-------FLYQLLV 179
Cdd:cd02762 42 AAALGDYQNDPDRLRTPMRRRGGSFEEIDWDEAFDEIAERLRAIRArhgGDAVGVYGGNPQAHTHAggayspaLLKALGT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 180 RSYGTNNLPDcsNMCHEssgAALAQTTGIGkGSVTLADLEQADLIVVVGQNPGTNHPRMLSA------LEAAKGNGAKIV 253
Cdd:cd02762 122 SNYFSAATAD--QKPGH---FWSGLMFGHP-GLHPVPDIDRTDYLLILGANPLQSNGSLRTApdrvlrLKAAKDRGGSLV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 254 AVNPlpeagllrfknpqnvrgVVGRGTPLADQFLQIRLAGDQALFQAVGNLLLRWEDarpgtvVDRAFVERSTVDFDRYA 333
Cdd:cd02762 196 VIDP-----------------RRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAEGL------TDRRFLAEHCDGLDEVR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 334 EHVRALDWEAVFAATGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLCPV---- 409
Cdd:cd02762 253 AALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFTTpald 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 410 ---------RGHSNVQgDRTMGIWEKMPEAFLSALESEFGVPVPRKhgydtveaIRAMrdgkakvfMAVGGNFAAATPDT 480
Cdd:cd02762 333 lvgqtsgrtIGRGEWR-SRVSGLPEIAGELPVNVLAEEILTDGPGR--------IRAM--------IVVAGNPVLSAPDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 481 EVTEAALRQCELTVQVSTKLNRShvvpGRTA-LILPTLGRTERDKQasgeQFVTVEDSMSVVHRSRgRLDPASPHLRSEV 559
Cdd:cd02762 396 ARLEAALGGLEFMVSVDVYMTET----TRHAdYILPPASQLEKPHA----TFFNLEFPRNAFRYRR-PLFPPPPGTLPEW 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906445253 560 AIICGLAQAL-----FGPDHpvPWARFVEDYDRVRDHIANVVPGCADYN--TRVRTPDGFVLPHAP 618
Cdd:cd02762 467 EILARLVEALdavlrAGFYG--ERAGGTLLLAALLERPSGVDLGPLTPRlwQRLRTPDGRIHLAPP 530
|
|
| 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 ... |
122-614 |
4.14e-23 |
|
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: 103.24 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGTHYEPIGWDAAFALIAEHLRALStpDEAVFYTSGRTSNEAAFLYQLLVRSY-GTNNLPdcsnmcHESSGA 200
Cdd:cd02771 54 RLTQPLIRRGGTLVPVSWNEALDVAAARLKEAK--DKVGGIGSPRASNESNYALQKLVGAVlGTNNVD------HRARRL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 201 ALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRM-LSALEAAKGNGAKIVAVNPLPEagllrFKNPQNVRGVVGRG 279
Cdd:cd02771 126 IAEILRNGPIYIPSLRDIESADAVLVLGEDLTQTAPRIaLALRQAARRKAVELAALSGIPK-----WQDAAVRNIAQGAK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 280 TPLAdqflqirlagdqalfqAVGNLLLRWEDARPGTVVDrafverSTVDFDRYAEHV-RALDWEAVFAATGLTHGEIEKF 358
Cdd:cd02771 201 SPLF----------------IVNALATRLDDIAAESIRA------SPGGQARLGAALaRAVDASAAGVSGLAPKEKAARI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 359 ARTVADSKRMIVCWAMGLtqhrHAVATIREIANVVLVRGMIGKpGAGLCPVRGHSNVQGdrtmgiwekmpeafLSALESE 438
Cdd:cd02771 259 AARLTGAKKPLIVSGTLS----GSLELIKAAANLAKALKRRGE-NAGLTLAVEEGNSPG--------------LLLLGGH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 439 FGVPvprkhGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDTEVtEAALRQCELTVQVSTKLNRshvVPGRTALILPTLG 518
Cdd:cd02771 320 VTEP-----GLDLDGALAALEDGSADALIVLGNDLYRSAPERRV-EAALDAAEFVVVLDHFLTE---TAERADVVLPAAS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 519 RTErdkqASGeQFVTVEDSMSVVHRSRGrlDPASPhLRSEVAIICGLAQALFGPDHPVPWARFvedydrvrDHIANVVPG 598
Cdd:cd02771 391 FAE----KSG-TFVNYEGRAQRFFKAYD--DPAGD-ARSDWRWLHALAAKLGGKLVPSDAAIL--------DEIIALVPG 454
|
490
....*....|....*.
gi 1906445253 599 CADYNTRVRTPDGFVL 614
Cdd:cd02771 455 KAPVGGHLYGGDPGVT 470
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
122-523 |
5.71e-22 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 98.24 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGT-HYEPIGWDAAFALIAEHLRALST---PDEA--VFYTSGRTSNEAAFLYQLLVRSYG---TNNLPDCSN 192
Cdd:pfam00384 1 RLKYPMVRRGDgKFVRVSWDEALDLIAKKLKRIIKkygPDAIaiNGGSGGLTDVESLYALKKLLNRLGsknGNTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 193 MCHESSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPrMLSALE--AAKGNGAKIVAVNPlpeagllrFKNPQ 270
Cdd:pfam00384 81 LCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAP-ILNARIrkAALKGKAKVIVIGP--------RLDLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 271 nvrgvvgrgtpLADQFLQIRLAGDQALFQAVGNLLlrwedarpgtvvdrafverstvdfdryaehvraldweavfaatgl 350
Cdd:pfam00384 152 -----------YADEHLGIKPGTDLALALAGAHVF--------------------------------------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 351 thgeIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGlcpVRGHSNVQGDRtmgiwekmpeA 430
Cdd:pfam00384 176 ----IKELKKDKDFAPKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG---WNGLNILQGAA----------S 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 431 FLSALEsefgvpVPRKHGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDTEVTEAALRQCELTV----QVSTKL-NRSHV 505
Cdd:pfam00384 239 PVGALD------LGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDKTaKYADV 312
|
410
....*....|....*...
gi 1906445253 506 vpgrtalILPTLGRTERD 523
Cdd:pfam00384 313 -------ILPAAAYTEKN 323
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
121-570 |
1.83e-21 |
|
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: 98.14 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 121 GRLTEPMV---LRGT-HYEPIGWDAAFALIAEHLRAL--STPDEAVFYTSGRTSNEAAFlyQLLVRSYGTNNLPDCSNMC 194
Cdd:cd02755 54 DRLKKPLIrvgERGEgKFREASWDEALQYIASKLKEIkeQHGPESVLFGGHGGCYSPFF--KHFAAAFGSPNIFSHESTC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 195 HESSGAALAQTTGIGKGSVtLADLEQADLIVVVGQN--PGTNHPRMlSALEAAKGNGAKIVAVNP-LPEAgllrfknpqn 271
Cdd:cd02755 132 LASKNLAWKLVIDSFGGEV-NPDFENARYIILFGRNlaEAIIVVDA-RRLMKALENGAKVVVVDPrFSEL---------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 272 vrgvvgrgTPLADQFLQIRLAGDQALFQAVGNLLLRwEDarpgtVVDRAFVERSTVDFDRYAEHVRA--LDWEAvfAATG 349
Cdd:cd02755 200 --------ASKADEWIPIKPGTDLAFVLALIHVLIS-EN-----LYDAAFVEKYTNGFELLKAHVKPytPEWAA--QITD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 350 LTHGEIEKFARTVADSKRMIV-------CWAMGLTQHRHAVATIreiaNVVLvrGMIGKPGaGLCPVRGHSnvqgdrtmg 422
Cdd:cd02755 264 IPADTIRRIAREFAAAAPHAVvdpgwrgTFYSNSFQTRRAIAII----NALL--GNIDKRG-GLYYAGSAK--------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 423 iwekmpeaflsalesefgvPVPrkhgydtveairamrdgkAKVFMAVGGNFAAATPDTEVTEAALRQCELTVQVStklnr 502
Cdd:cd02755 328 -------------------PYP------------------IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAID----- 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906445253 503 shVVPGRTAL----ILPTLGRTERD-----KQASGEQFVTvedsmsvvhrsRGRLDPASPHLRSEVAIICGLAQALF 570
Cdd:cd02755 366 --ILPSDTALyadvILPEATYLERDepfsdKGGPAPAVAT-----------RQRAIEPLYDTRPGWDILKELARRLG 429
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
122-267 |
1.40e-20 |
|
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: 94.66 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGTHYEPIGWDAAFALIAEHLRAlSTPDEAVFYTSGRTSNEAAFLYQLLVRSYGTNNLpDCSNMCHESSGAA 201
Cdd:cd02768 54 RLTQPLIKKGGKLVPVSWEEALKTVAEGLKA-VKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNI-DHRLRQSDLPADN 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906445253 202 LAQTTGIgkGSVTLADLEQADLIVVVGQNPGTNHPRMLSAL-EAAKGNGAKIVAVNPLPEAGLLRFK 267
Cdd:cd02768 132 RLRGNYL--FNTSIAEIEEADAVLLIGSNLRKEAPLLNARLrKAVKKKGAKIAVIGPKDTDLIADLT 196
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
81-417 |
3.86e-15 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 78.35 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 81 ENGAKAVAEEATlrRVGREFFAsHSVAElaertdywlgqqGRLTEPMVlrgtHYEPIGWDAAFALIAEHLRALSTPdeaV 160
Cdd:COG1029 25 EGGKIVVVKNAC--AIGAAKFE-RAVSD------------HRITSPRI----RGKEVSLEEAIDKAAEILANAKRP---L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 161 FYTSGRTSNEAA-FLYQLLVRSYGTnnLPDCSNMCHESSGAALaQTTGIGkgSVTLADLEQ-ADLIVVVGQNPGTNHPRM 238
Cdd:COG1029 83 IYGLSSTDCEAMrAGLALAERVGAV--VDNTASVCHGPSLLAL-QDVGWP--TCTLGEVKNrADVIIYWGCNPVHAHPRH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 239 LSAleaakgngakiVAVNPlpeAGLLRfKNPQNVRGVV---GRGTP---LADQFLQIRLAGDQALFQAVgNLLLRWEDAR 312
Cdd:COG1029 158 MSR-----------YSVFP---RGFFT-PKGRKDRTVIvvdPRPTDtakVADLHLQVKPGRDYEVLSAL-RALVRGKELS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 313 PGTVvdrafverstvdfdryaehvraldweavfaaTGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANv 392
Cdd:COG1029 222 PEEV-------------------------------AGIPVEDLEELAERLKNAKYGVIFWGMGLTQSPGKHLNVDAAIE- 269
|
330 340
....*....|....*....|....*
gi 1906445253 393 vLVRGMIGKPGAGLCPVRGHSNVQG 417
Cdd:COG1029 270 -LVRDLNRYTKFSILPLRGHYNVAG 293
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
116-423 |
2.43e-14 |
|
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: 76.50 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 116 WLGQQGRLTEpmvLRGT-HYEPIGWDAAFALIAEHLRALSTP--DEAVFYTSG---------RTSNEAAFLYQLL---VR 180
Cdd:cd02751 57 WLGNGPGSRE---LRGEgEFVRISWDEALDLVASELKRIREKygNEAIFGGSYgwasagrlhHAQSLLHRFLNLIggyLG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 181 SYGTnnlpdcsnmchESSGA---ALAQTTG---IGKGSVTLAD-LEQADLIVVVGQNPGTN--------HPRMLSALEAA 245
Cdd:cd02751 134 SYGT-----------YSTGAaqvILPHVVGsdeVYEQGTSWDDiAEHSDLVVLFGANPLKTrqgggggpDHGSYYYLKQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 246 KGNGAKIVAVNPLpeagllrfknpqNVRGVVGrgtpLADQFLQIRLAGDQALFQAVGNLLLrWEDArpgtvVDRAFVERS 325
Cdd:cd02751 203 KDAGVRFICIDPR------------YTDTAAV----LAAEWIPIRPGTDVALMLAMAHTLI-TEDL-----HDQAFLARY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 326 TVDFDRYAEHVRALD--------WEAvfAATGLTHGEIEKFARTVADSKRMIVCwAMGLTQHRHAVATIREIANVVLVRG 397
Cdd:cd02751 261 TVGFDEFKDYLLGESdgvpktpeWAA--EITGVPAETIRALAREIASKRTMIAQ-GWGLQRAHHGEQPAWMLVTLAAMLG 337
|
330 340
....*....|....*....|....*.
gi 1906445253 398 MIGKPGAGLCPVRGHSNVQGDRTMGI 423
Cdd:cd02751 338 QIGLPGGGFGFGYGYSNGGGPPRGGA 363
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
122-417 |
3.50e-14 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 76.21 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGT----HYEPIGWDAAFALIAEHLRALSTP--DEAVFYTSG--------RTSNEAAFLYQLL---VRSYGT 184
Cdd:cd02770 59 RLKYPMKRVGKrgegKFVRISWDEALDTIASELKRIIEKygNEAIYVNYGtgtyggvpAGRGAIARLLNLTggyLNYYGT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 185 NnlpdcsnmcheSSG---AALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNhpRMLSALEA-----AKGNGAKIVAVN 256
Cdd:cd02770 139 Y-----------SWAqitTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAET--RMGGGGSTyyylqAKKAGAKFIVID 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 257 PlpeagllrfKNPQNVRGvvgrgtpLADQFLQIRLAGDQALFQAVGNLLLrWEDarpgtVVDRAFVERSTVDFDR----- 331
Cdd:cd02770 206 P---------RYTDTAVT-------LADEWIPIRPGTDAALVAAMAYVMI-TEN-----LHDQAFLDRYCVGFDAehlpe 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 332 -------YAEHV---------RALDWEAvfAATGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLV 395
Cdd:cd02770 264 gappnesYKDYVlgtgydgtpKTPEWAS--EITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAM 341
|
330 340
....*....|....*....|..
gi 1906445253 396 RGMIGKPGAGLCPVRGHSNVQG 417
Cdd:cd02770 342 TGNVGIPGGNTGARPGGSAYNG 363
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
122-539 |
4.12e-12 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 69.93 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMvLRGTH--------YEPIGWDAAFALIAEHL-RALST--PDEAVFYTSGR-TSNE---AAFLYQLLVRSygtNN 186
Cdd:PRK13532 97 RLTQPL-LRMKDgkydkegeFTPVSWDQAFDVMAEKFkKALKEkgPTAVGMFGSGQwTIWEgyaASKLMKAGFRS---NN 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 187 LPDCSNMCHESSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHP--------RMLSALEAAkgngakiVAVnpl 258
Cdd:PRK13532 173 IDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPilwsrvtdRRLSNPDVK-------VAV--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 259 peagLLRFKNpqnvrgvvgRGTPLADQFLQIRLAGDQALFQAVGNLLLRwEDArpgtvVDRAFVERSTV----------- 327
Cdd:PRK13532 243 ----LSTFEH---------RSFELADNGIIFTPQTDLAILNYIANYIIQ-NNA-----VNWDFVNKHTNfrkgatdigyg 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 328 -----------------------DFDRYAEHVRALDWEAVFAATGLTHGEIEKFARTVADSKRMIVC-WAMGLTQHRHAV 383
Cdd:PRK13532 304 lrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVSfWTMGFNQHTRGV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 384 ATIREIANVVLVRGMIGKPGAGLCPVRGHSNVQGD-RTMG-----------------------IWeKMPEaflsalesef 439
Cdd:PRK13532 384 WANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGTaREVGtfshrlpadmvvtnpkhreiaekIW-KLPE---------- 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 440 GVpVPRKHGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDT-EVTEAALRQCELTVQVstklnrSHVVPGRTA----LIL 514
Cdd:PRK13532 453 GT-IPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNInEERLPGWRNPDNFIVV------SDPYPTVSAlaadLIL 525
|
490 500 510
....*....|....*....|....*....|....
gi 1906445253 515 PT---------LGRTERDKQASGEQFVTVEDSMS 539
Cdd:PRK13532 526 PTamwvekegaYGNAERRTQFWRQQVKAPGEAKS 559
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
122-417 |
4.57e-11 |
|
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: 65.43 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVlrgtHYEPIGWDAAFALIAEHLRALSTPdeaVFYTSGRTSNEA-AFLYQLLVRSYGTnnLPDCSNMCHESSGA 200
Cdd:cd02761 43 RITTPRI----DGKPVSLEEAIEKAAEILKEAKRP---LFYGLGTTVCEAqRAGIELAEKLGAI--IDHAASVCHGPNLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 201 ALAQTtgiGKGSVTLADLE-QADLIVVVGQNPGTNHPRMLSAleaakgngakiVAVNPlpeAGLLRFKNPQNvRGVV--- 276
Cdd:cd02761 114 ALQDS---GWPTTTLGEVKnRADVIVYWGTNPMHAHPRHMSR-----------YSVFP---RGFFREGGRED-RTLIvvd 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 277 GRGTP---LADQFLQIRLAGDQALFQAVGNLLlrwedARPGTVVDRafverstvdfdryaehvraldweavfaATGLTHG 353
Cdd:cd02761 176 PRKSDtakLADIHLQIDPGSDYELLAALRALL-----RGAGLVPDE---------------------------VAGIPAE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906445253 354 EIEKFARTVADSKRMIVCWAMGLTQHRHAvatIREIANVV-LVRGMIGKPGAGLCPVRGHSNVQG 417
Cdd:cd02761 224 TILELAERLKNAKFGVIFWGLGLLPSRGA---HRNIEAAIrLVKALNEYTKFALLPLRGHYNVRG 285
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
204-406 |
4.90e-10 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 62.34 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 204 QTTGIGKGSVTLADLEQADLIVVVGQNPgtNHPRMLSA--LEAAKGNGAKIVAVNPlpeagllRFkNPQnvrgvvgrgTP 281
Cdd:cd02750 154 QTWGEQTDVPESADWYNADYIIMWGSNV--PVTRTPDAhfLTEARYNGAKVVVVSP-------DY-SPS---------AK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 282 LADQFLQIRLAGDQALFQAVGNLLLRwedarpGTVVDRAFVERSTvDFDRYaehVRALDWEAvfAATGLTHGEIEKFART 361
Cdd:cd02750 215 HADLWVPIKPGTDAALALAMAHVIIK------EKLYDEDYLKEYT-DLPFL---VYTPAWQE--AITGVPRETVIRLARE 282
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1906445253 362 VADSKR-MIVCWAmGLTQHRHAVATIREIANVVLVRGMIGKPGAGL 406
Cdd:cd02750 283 FATNGRsMIIVGA-GINHWYHGDLCYRALILLLALTGNEGKNGGGW 327
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
122-403 |
6.63e-10 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 62.54 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGTH----YEPIGWDAAFALIAEHLRAL--STPDEAVFYTsGRTSNEAafLYQLLVRSYGTNNLPDCSNMCH 195
Cdd:cd02763 54 RLTKPLLRKGPRgsgqFEEIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFCS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 196 ESSGAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPlpeagllrfknpqnVRGV 275
Cdd:cd02763 131 VNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNP--------------VRTG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 276 VGrgtPLADQFLQIRLAGDQALFQAVGNLLLRWEdarpgtVVDRAFVERST-----VDFDRyaehvraldwEAVFAATGL 350
Cdd:cd02763 197 YA---AIADEWVPIKPGTDGAFILALAHELLKAG------LIDWEFLKRYTnaaelVDYTP----------EWVEKITGI 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906445253 351 THGEIEKFARTVADSKR-----MIVCW-------------------AM-GLTQHRHAVATIREIANVVLVRGMIGKPG 403
Cdd:cd02763 258 PADTIRRIAKELGVTARdqpieLPIAWtdvwgrkhekitgrpvsfhAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
117-258 |
1.18e-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: 61.22 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 117 LGQQGRLTEPMVLRGTHYEPIGWDAAFALIAEHLRALST---PDEAVFYTSGRTSNEAAFLYQLLVRSYGTNNLPDCSNM 193
Cdd:cd02772 49 LNSEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKkhgADQIGALASPHSTLEELYLLQKLARGLGSDNIDHRLRQ 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906445253 194 CHESSGAALAQTTGIGkgsVTLADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPL 258
Cdd:cd02772 129 SDFRDDAKASGAPWLG---MPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPA 190
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
118-412 |
1.29e-09 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 61.73 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 118 GQQGRLTEPMVLRGTHYEPIGWDAAFALIAEHLRAL---STPDEAVFYT--------SGRTSNEAA---FLYQLLVRSYG 183
Cdd:cd02756 113 VGETRLTTPLVRRGGQLQPTTWDDAIDLVARVIKGIldkDGNDDAVFASrfdhggggGGFENNWGVgkfFFMALQTPFVR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 184 TNNLPDCSNMCHESSGAalaqttGIGKGSVTLADLEQADLIVVVGQNP---GTNH--PRMLSALEAAKgNGAKIVAVNPL 258
Cdd:cd02756 193 IHNRPAYNSEVHATREM------GVGELNNSYEDARLADTIVLWGNNPyetQTVYflNHWLPNLRGAT-VSEKQQWFPPG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 259 P--EAGLLRFKNPQNVRGV-VGRGTPLADQFL--QIRLAGDQALFQAVGnlllrwedarpgtvvdrAFVERSTVDFDRYA 333
Cdd:cd02756 266 EpvPPGRIIVVDPRRTETVhAAEAAAGKDRVLhlQVNPGTDTALANAIA-----------------RYIYESLDEVLAEA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 334 EHVraldweavfaaTGLTHGEIEKFARTVADSK------RMIVCWAMGLTQHRHAVATIREIANVVLVRGMIGKPGAGLC 407
Cdd:cd02756 329 EQI-----------TGVPRAQIEKAADWIAKPKeggyrkRVMFEYEKGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCV 397
|
....*
gi 1906445253 408 PVRGH 412
Cdd:cd02756 398 RQGGH 402
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
649-754 |
3.13e-09 |
|
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: 54.97 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 649 LLLQTLRSHDQYNTTIYGMDDRYRGvKDGRRVVFVNPDDLAALSIDDGALVDLVSEYADRERRAERFRVVayptARGCAA 728
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLA-KPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRV----RPGVVF 75
|
90 100 110
....*....|....*....|....*....|....
gi 1906445253 729 TYFPE--------ANNLVPlDSTAEVSNTPTSKS 754
Cdd:pfam01568 76 MPFGWwyeprggnANALTD-DATDPLSGGPEFKT 108
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
122-257 |
6.93e-09 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 58.43 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGTHYEPIGWDAAFALIAEHLRAlSTPDEAVFYTSGRTSNEAAFLYQLLVRSYGtnnlpdCSNMCHESSGAA 201
Cdd:cd02773 53 RLDKPYIRKNGKLKPATWEEALAAIAKALKG-VKPDEIAAIAGDLADVESMVALKDLLNKLG------SENLACEQDGPD 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906445253 202 LAQ--------TTGIgkgsvtlADLEQADLIVVVGQNPGTNHPrMLSAL--EAAKGNGAKIVAVNP 257
Cdd:cd02773 126 LPAdlrsnylfNTTI-------AGIEEADAVLLVGTNPRFEAP-VLNARirKAWLHGGLKVGVIGP 183
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
122-489 |
7.84e-09 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 59.30 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGTH----YEPIGWDAAFALIAEHLRALSTP--DEAVFYTSGRTSNEAAFLYqlLVRSYGTNNLpdcsnMCH 195
Cdd:PRK15488 98 RIVKPLKRVGERgegkWQEISWDEAYQEIAAKLNAIKQQhgPESVAFSSKSGSLSSHLFH--LATAFGSPNT-----FTH 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 196 ESS---GAALAQTTGIGkGSVTLaDLEQADLIVVVGQN--PGTNHPRMLSALEAAKGNGAKIVAVNPlpeagllRFKnpq 270
Cdd:PRK15488 171 ASTcpaGYAIAAKVMFG-GKLKR-DLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------RFS--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 271 nvrgVVGRGtplADQFLQIRLAGDQALFQAVGNLLLRwEDarpgtVVDRAFVERSTVDFDRYAEHVRAL--DWEAVFaaT 348
Cdd:PRK15488 239 ----VVASK---ADEWHAIRPGTDLAVVLALCHVLIE-EN-----LYDKAFVERYTSGFEELAASVKEYtpEWAEAI--S 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 349 GLTHGEIEKFARTVAD-SKRMIVCWAmgltqHRhAVATIREI--------ANVvlvrgMIGkpgaglcpvrghsNVQgdR 419
Cdd:PRK15488 304 DVPADDIRRIARELAAaAPHAIVDFG-----HR-ATFTPEEFdmrraifaANV-----LLG-------------NIE--R 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906445253 420 TMGIWEKMPEAFLSALESEFGVPV---PRKHGYDTVEAIRAMRDGKAKVFMAVGGNFAAATPDtevteAALRQ 489
Cdd:PRK15488 358 KGGLYFGKNASVYNKLAGEKVAPTlakPGVKGMPKPTAKRIDLVGEQFKYIAAGGGVVQSIID-----ATLTQ 425
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
218-405 |
7.23e-08 |
|
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: 55.73 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 218 LEQADLIVVVGQNP---------GTNHPRMLSALEAAKGNGAKIVAVNPLpeagllRFKNPQnvrgvvgrgtPLADQFLQ 288
Cdd:cd02769 168 AEHTELVVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPL------RDDTAA----------ELGAEWIA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 289 IRLAGDQALFQAVGNLLLRwEDArpgtvVDRAFVERSTVDFDRYAEHVRALD--------WEAvfAATGLTHGEIEKFAR 360
Cdd:cd02769 232 IRPGTDVALMLALAHTLVT-EGL-----HDKAFLARYTVGFDKFLPYLLGESdgvpktpeWAA--AICGIPAETIRELAR 303
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1906445253 361 TVADSKRMIVCwAMGLTQHRHAVATIREIANVVLVRGMIGKPGAG 405
Cdd:cd02769 304 RFASKRTMIMA-GWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGG 347
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
122-461 |
2.42e-07 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 54.26 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGTH----YEPIGWDAAFALIAEHLRAL--STPDEAVFYTSGRTSneaafLYQLLVRSY--GTNNLPDCSNM 193
Cdd:PRK14990 119 RLKYPMKRVGARgegkFERISWEEAYDIIATNMQRLikEYGNESIYLNYGTGT-----LGGTMTRSWppGNTLVARLMNC 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 194 C---------HESS--GAALAQTTGIGKGSVTLADLEQADLIVVVGQNPGTNhpRMLSA-----LEAAKG-NGAKIVAVN 256
Cdd:PRK14990 194 CggylnhygdYSSAqiAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGET--RMSGGgvtyyLEQARQkSNARMIIID 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 257 PlpeagllRFKNPqnvrgvvgrGTPLADQFLQIRLAGDQALFQAVGNLLLRwEDarpgtVVDRAFVERSTVDFDR----- 331
Cdd:PRK14990 272 P-------RYTDT---------GAGREDEWIPIRPGTDAALVNGLAYVMIT-EN-----LVDQPFLDKYCVGYDEktlpa 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 332 -------YAEHV---------RALDWEAVFaaTGLTHGEIEKFARTVADSKRMIVCWAMGLTQHRHAVATIREIANVVLV 395
Cdd:PRK14990 330 sapknghYKAYIlgegpdgvaKTPEWASQI--TGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAIL 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906445253 396 RGMIGKPGaglcpvrGHSNVQGDRTMGIWEKMPeaflsALESEFGVPVPRKHGYDTVE---AIRAMRDG 461
Cdd:PRK14990 408 TGNVGING-------GNSGAREGSYSLPFVRMP-----TLENPIQTSISMFMWTDAIErgpEMTALRDG 464
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
122-326 |
3.09e-07 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 53.64 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 122 RLTEPMVLRGT----HYEPIGWDAAFALIAEHLRALST---PDEAVFYTSgrtSNEAAFLYQLLVRSYGTNNLPDCSNMC 194
Cdd:cd02765 55 RLKYPMKRVGErgegKFERITWDEALDTIADKLTEAKReygGKSILWMSS---SGDGAILSYLRLALLGGGLQDALTYGI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 195 HESSGAALAQTTGIGKGSVT--LADLEQADLIVVVGQNPGTNHPRMLSALEAAKGNGAKIVAVNPlpeagllRFKNPQNV 272
Cdd:cd02765 132 DTGVGQGFNRVTGGGFMPPTneITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDP-------VYSTTAAK 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906445253 273 rgvvgrgtplADQFLQIRLAGDQALFQAVGNLLLR--WedarpgtvVDRAFVERST 326
Cdd:cd02765 205 ----------ADQWVPIRPGTDPALALGMINYILEhnW--------YDEAFLKSNT 242
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
119-263 |
7.89e-04 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 43.01 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 119 QQGRLTEPMVlRGTH--YEPIGWDAAFALIAEHLRALStpDEAVFYTSGRTSNEAAFLYQLLVR-SYGTNNLpDCSNMCH 195
Cdd:PRK07860 275 QPDRITTPLV-RDEDgeLEPASWSEALAVAARGLAAAR--GRVGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPH 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445253 196 ESSGAALAQTTGIGKG-SVTLADLEQADLIVVVGQNPGTNHPRMLSAL-EAAKGNGAKIVAVNPLPEAGL 263
Cdd:PRK07860 351 SAEEADFLAARVAGRGlGVTYADLEKAPAVLLVGFEPEEESPIVFLRLrKAARKHGLKVYSIAPFATRGL 420
|
|
| |
