|
Name |
Accession |
Description |
Interval |
E-value |
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
17-753 |
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: 983.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 17 PAGGWGALKATAIAVRTQMDTFDAPATLLRTNQPDGFDCPGCAWPDK-EHKSTFQFCENGAKAVTWEATSKRVTPAFLAA 95
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSpQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 96 NTVSSLLAKSDFELEGYGRLTHPLRYDRDSDTFRPVDWDEAFQRIGEVLRGLEPDQVEFYTSGRASNEAAYLFQLFAREY 175
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLDPKQVAFYTSGRTSNEAAYLYQLFARSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 176 GTNNFPDCSNMCHEATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLHELARRNVPIIVFNPLRERA 255
Cdd:TIGR01701 161 GSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 256 LERFADPQSVIEMATYGSTDIASTYFQVKAGGDAAALKGIAKHLLEMESE-RGDVLDRAFIAEHTQGFEDFAADIAQTRW 334
Cdd:TIGR01701 241 LERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAqPGSLIDHEFIANHTNGFDELRRHVLQLNW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 335 DEIERESGLSQAALKQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTV 414
Cdd:TIGR01701 321 NDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 415 GISEKPTPAFLNRLKEVFGFEPPSHHGHDAVQATQAMIDGRAKALICLGGNFAVAMPDHERGFPAMGSLDLSVHVGTKLN 494
Cdd:TIGR01701 401 GITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 495 RTHLLVGKETFIFPCLGRTELDVQATGRQSITVEDSMSMVHASSGKLKPASPLLRSEPAIVAGMAKATLPDTRVDWMTLV 574
Cdd:TIGR01701 481 RSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEILV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 575 EDYDRIRDLIEQTIPGFENYNARIRVPGGFRMPLPP-TQRLWPTATGKAMFSVFDGVHENASGEGEHVLRLITLRSHDQY 653
Cdd:TIGR01701 561 DTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLRSHDQF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 654 NTTIYALDDRYRGVFGRRDVLFMNEEDMAQSGLEHGDRVDIETALP-GNGQRLEDITVVAYNIAPGTVGAYYPEANVLVP 732
Cdd:TIGR01701 641 NTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGdGQKRKFDNLRIVFYDTPTGNAAAYYPEANPLLP 720
|
730 740
....*....|....*....|.
gi 1728610728 733 LDYLDKDSGTPSYKSVPVRIT 753
Cdd:TIGR01701 721 LDHHDPQSKTPEYKTIPVRLE 741
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
52-624 |
0e+00 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 933.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 52 GFDCPGCAWPD-KEHKSTFQFCENGAKAVTWEATSKRVTPAFLAANTVSSLLAKSDFELEGYGRLTHPLRYDRDSDTFRP 130
Cdd:cd02767 1 GFDCPGCAWGDpGQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 131 VDWDEAFQRIGEVLRGLEPDQVEFYTSGRASNEAAYLFQLFAREYGTNNFPDCSNMCHEATSVGLPRSIGIGKGTVSLDD 210
Cdd:cd02767 81 ISWDEAFAEIAARLRALDPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 211 FDKTELVISIGHNPATNHPRMMGTLHELARRNVPIIVFNPLRERALERFADPQSVIEMATyGSTDIASTYFQVKAGGDAA 290
Cdd:cd02767 161 FEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 291 ALKGIAKHLLEMESERGDVLDRAFIAEHTQGFEDFAADIAQTRWDEIERESGLSQAALKQVAEAYAKSNATIITYGMGIT 370
Cdd:cd02767 240 LLNGMAKHLIERDDEPGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 371 QHNKGTANVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGISEKPTPAFLNRLKEVFGFEPPSHHGHDAVQATQA 450
Cdd:cd02767 320 QHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDTVEAIEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 451 MIDGRAKALICLGGNFAVAMPDHERGFPAMGSLDLSVHVGTKLNRTHLLVGKETFIFPCLGRTELDVQATGRQSITVEDS 530
Cdd:cd02767 400 ALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQAVTVEDS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 531 MSMVHASSGKLKPASPLLRSEPAIVAGMAKATLPDTRVDWMTLVEDYDRIRDLIEQTIP-GFENYNARIRVPGGFRMPLP 609
Cdd:cd02767 480 MSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGGFHLPNG 559
|
570
....*....|....*
gi 1728610728 610 PTQRLWPTATGKAMF 624
Cdd:cd02767 560 ARERKFNTPSGKAQF 574
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
9-752 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 931.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 9 PGIRHYDGPAGGWGALKATAIAVRTQMDTFDAPATLLRTNQPDGFDCPGCAWPDKEHKSTFQFCENGAKAVTWEATSKRV 88
Cdd:PRK09939 3 KKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 89 TPAFLAANTVSSLLAKSDFELEGYGRLTHPLRYDRDSDTFRPVDWDEAFQRIGEVLRGL-EPDQVEFYTSGRASNEAAYL 167
Cdd:PRK09939 83 NASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYsDPNQVEFYTSGRTSNEAAFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 168 FQLFAREYGTNNFPDCSNMCHEATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLHELARRNVPIIV 247
Cdd:PRK09939 163 YQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 248 FNPLRERALERFADPQSVIEMATYGSTDIASTYFQVKAGGDAAALKGIAKHLLEME-----SERGDVLDRAFIAEHTQGF 322
Cdd:PRK09939 243 INPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaAGRPSLLDDEFIQTHTVGF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 323 EDFAADIAQTRWDEIERESGLSQAALKQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPL 402
Cdd:PRK09939 323 DELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 403 RGHSNVQGNRTVGISEKPTPAFLNRLKEVFGFEPPSHHGHDAVQATQAMIDGRAKALICLGGNFAVAMPDHERGFPAMGS 482
Cdd:PRK09939 403 RGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 483 LDLSVHVGTKLNRTHLLVGKETFIFPCLGRTELDVQATGRQSITVEDSMSMVHASSGKLKPASPLLRSEPAIVAGMAKAT 562
Cdd:PRK09939 483 LDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 563 LPDTRVDWMTLVEDYDRIRDLIEQTIPGFENYNARIRVPGGFRMPLPPTQRLWPTATGKAMFSVFDGVHENASGEGEHVL 642
Cdd:PRK09939 563 LPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 643 RLITLRSHDQYNTTIYALDDRYRGVFGRRDVLFMNEEDMAQSGLEHGDRVDIETALPG---NGQRLEDITVVAYNIAPGT 719
Cdd:PRK09939 643 VMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDgkrSSRRMDRLKVVIYPMADRS 722
|
730 740 750
....*....|....*....|....*....|...
gi 1728610728 720 VGAYYPEANVLVPLDYLDKDSGTPSYKSVPVRI 752
Cdd:PRK09939 723 LVTYFPESNHMLTLDNHDPLSGIPGYKSIPVEL 755
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
55-753 |
6.19e-171 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 507.46 E-value: 6.19e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 55 CPGCAWpdkehkstfqFCENGAKAVTWEATskRVTPAflAANTVSSLL-----AKSDFELEGYGRLTHPLRYD--RDSDT 127
Cdd:COG0243 28 CPGCGV----------GCGLGVKVEDGRVV--RVRGD--PDHPVNRGRlcakgAALDERLYSPDRLTYPMKRVgpRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 128 FRPVDWDEAFQRIGEVLRGLE----PDQVEFYTSG----RASNEAAYLFQLFAREYGTNNFPDCSNMCHEATSVGLPRSI 199
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIIdeygPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 200 GIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLHELARRN-VPIIVFNPLRERalerfadpqsviematygSTDIAS 278
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRgAKIVVIDPRRTE------------------TAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 279 TYFQVKAGGDAAALKGIAKHLLEMesergDVLDRAFIAEHTQGFEDFAADIAQTRWDEIERESGLSQAALKQVAEAYAKS 358
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEE-----GLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 359 NATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPLRGHsnvqgnrtvgisekptpaflnrlkevfgfepps 438
Cdd:COG0243 311 KPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE--------------------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 439 hhghdavqatqAMIDG---RAKALICLGGNFAVAMPDHERGFPAMGSLDLSVHVGTKLNRTHLLvgkETFIFPCLGRTEl 515
Cdd:COG0243 358 -----------AILDGkpyPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARY---ADIVLPATTWLE- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 516 dvqatgRQSITVEDSMSMVHASSGKLKPASpLLRSEPAIVAGMAKATLPDTRVDWMTLVEDYdrIRDLIEQTIPG---FE 592
Cdd:COG0243 423 ------RDDIVTNSEDRRVHLSRPAVEPPG-EARSDWEIFAELAKRLGFEEAFPWGRTEEDY--LRELLEATRGRgitFE 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 593 NYNARirvpGGFRMPLPPTQR-----LWPTATGKAMFSV-----------FDGVHENASGEGEHVLRLITLRSHDQYNTT 656
Cdd:COG0243 494 ELREK----GPVQLPVPPEPAfrndgPFPTPSGKAEFYSetlalpplpryAPPYEGAEPLDAEYPLRLITGRSRDQWHST 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 657 IYALdDRYRGVFGRRdVLFMNEEDMAQSGLEHGDRVDIETAlpgNGqRLEDITVVAYNIAPGTV----GAYYPEA----- 727
Cdd:COG0243 570 TYNN-PRLREIGPRP-VVEINPEDAAALGIKDGDLVRVESD---RG-EVLARAKVTEGIRPGVVfaphGWWYEPAddkgg 643
|
730 740
....*....|....*....|....*...
gi 1728610728 728 --NVLVPlDYLDKDSGTPSYKSVPVRIT 753
Cdd:COG0243 644 nvNVLTP-DATDPLSGTPAFKSVPVRVE 670
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
113-753 |
3.27e-115 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 363.43 E-value: 3.27e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 113 GRLTHPLRydRDSDTFRPVDWDEAFQRIGEVLRGLE----PDQVEFYTSGRASNEAAYLFQLFAREY-GTNNFPDCSNMC 187
Cdd:COG3383 60 DRLTTPLI--RRGGEFREVSWDEALDLVAERLREIQaehgPDAVAFYGSGQLTNEENYLLQKLARGVlGTNNIDNNARLC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 188 HEATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLHELARRNVPIIVFNPlRERALERFADpqsvie 267
Cdd:COG3383 138 MASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-RRTETARLAD------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 268 matygstdiasTYFQVKAGGDAAALKGIAKHLLEmeserGDVLDRAFIAEHTQGFEDFAADIAQTRWDEIERESGLSQAA 347
Cdd:COG3383 211 -----------LHLQIKPGTDLALLNGLLHVIIE-----EGLVDEDFIAERTEGFEELKASVAKYTPERVAEITGVPAED 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 348 LKQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGIseKPT------ 421
Cdd:COG3383 275 IREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGA--LPNvlpgyr 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 422 ----PAFLNRLKEVFGFEP-PSHHGHDAVQATQAMIDGRAKALICLGGNFAVAMPDHERGFPAMGSLDLSVHVGTKLNRT 496
Cdd:COG3383 353 dvtdPEHRAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTET 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 497 ----HLLVG------KE-TFIfpclgRTELDVQatgrqsitvedsmsmvhassgklkpaspllRSEPAIvagmakATLPD 565
Cdd:COG3383 433 aeyaDVVLPaaswaeKDgTFT-----NTERRVQ------------------------------RVRKAV------EPPGE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 566 TRVDWMTLVE---------DYDR---IRDLIEQTIPGFENYN-ARIRVPGGFRMPLPP-----TQRLW----PTATGKAM 623
Cdd:COG3383 472 ARPDWEIIAElarrlgygfDYDSpeeVFDEIARLTPDYSGISyERLEALGGVQWPCPSedhpgTPRLFtgrfPTPDGKAR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 624 FSVFDGVHENASGEGEHVLRLITLRSHDQYNT-TIYALDDRYRGVFGrRDVLFMNEEDMAQSGLEHGDRVDIETalpgng 702
Cdd:COG3383 552 FVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTgTRTRRSPRLNKHAP-EPFVEIHPEDAARLGIKDGDLVRVSS------ 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728610728 703 qRLEDITVVAY---NIAPGTVGAY--YPE--ANVLVPlDYLDKDSGTPSYKSVPVRIT 753
Cdd:COG3383 625 -RRGEVVLRARvtdRVRPGTVFMPfhWGEgaANALTN-DALDPVSKQPEYKACAVRVE 680
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
114-752 |
1.10e-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: 1.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRydRDSDTFRPVDWDEAFQRIGEVLRGLE----PDQVEFYTSGRASNEAAYLFQLFARE-YGTNNFPDCSNMCH 188
Cdd:TIGR01591 53 RLTTPLI--REGDKFREVSWDEAISYIAEKLKEIKekygPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 189 EATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLHELARRNVPIIVFNPlRERALERFADpqsviem 268
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-RKTETAKIAD------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 269 atygstdiasTYFQVKAGGDAAALKGIAKHLLEmesERgdVLDRAFIAEHTQGFEDFAADIAQTRWDEIERESGLSQAAL 348
Cdd:TIGR01591 203 ----------LHIPLKPGTDIALLNAMANVIIE---EG--LYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGVPADLI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 349 KQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVG-ISEKP------- 420
Cdd:TIGR01591 268 REAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGaLPDFLpgyqpvs 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 421 TPAFLNRLKEVFGFEP-PSHHGHDAVQATQAMIDGRAKALICLGGNFAVAMPDHERGFPAMGSLDLSVHVGTKLNRTHLL 499
Cdd:TIGR01591 348 DEEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 500 VgkeTFIFP--CLGRTELDVQATGRQsitvedsMSMVHassgklKPASPLLRSEP--AIVAGMAKAtlpdTRVDWMtlVE 575
Cdd:TIGR01591 428 A---DVVLPaaAWLEKEGTFTNAERR-------IQRFF------KAVEPKGESKPdwEIIQELANA----LGLDWN--YN 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 576 DYDRIRDLIEQTIPGFENYN-ARIRVPGGFRMPLP-----PTQRLWP----TATGKAMFSVFDGVHENASGEGEHVLRLI 645
Cdd:TIGR01591 486 HPQEIMDEIRELTPLFAGLTyERLDELGSLQWPCNdsdasPTSYLYKdkfaTPDGKAKFIPLEWVAPIEEPDDEYPLILT 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 646 TLRSHDQYNTTiyALDDRYRGVfgRRDV----LFMNEEDMAQSGLEHGDRVDIETalpgngqRLEDITV---VAYNIAPG 718
Cdd:TIGR01591 566 TGRVLTHYNVG--EMTRRVAGL--RRLSpepyVEINTEDAKKLGIKDGDLVKVKS-------RRGEITLrakVSDRVNKG 634
|
650 660 670
....*....|....*....|....*....|....*...
gi 1728610728 719 ----TVGAYYPEANVLVPLDyLDKDSGTPSYKSVPVRI 752
Cdd:TIGR01591 635 aiyiTMHFWDGAVNNLTTDD-LDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
114-410 |
1.39e-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: 1.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRydRDSDTFRPVDWDEAFQRIGEVLRGLE----PDQVEFYTSGRASNEAAYLFQLFARE-YGTNNFPDCSNMCH 188
Cdd:cd02753 54 RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKdkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 189 EATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLHELARRNVPIIVFNPLReralerfadpqsvIEM 268
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRR-------------TEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 269 AtygstDIASTYFQVKAGGDAAALKGIAKHLLEmeserGDVLDRAFIAEHTQGFEDFAADIAQTRWDEIERESGLSQAAL 348
Cdd:cd02753 199 A-----RFADLHLQLRPGTDVALLNAMAHVIIE-----EGLYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDI 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728610728 349 KQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPLRGHSNVQG 410
Cdd:cd02753 269 REAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQG 330
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
113-475 |
1.46e-65 |
|
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: 227.88 E-value: 1.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 113 GRLTHPLrYDRDSDTFRPVDWDEAFQRIGEVLRGLE----PDQVEFYTSGRASNEAAYLFQLFAREY-GTNNFPDCSNMC 187
Cdd:cd02754 53 ERLTRPL-LRRNGGELVPVSWDEALDLIAERFKAIQaeygPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSRLC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 188 HEATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLHE--LARRNVPIIVFNPLRERalerfadpqsv 265
Cdd:cd02754 132 MASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDrkKANPGAKIIVVDPRRTR----------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 266 iematygSTDIASTYFQVKAGGDAAALKGIAKHLLEMESergdvLDRAFIAEHTQGFEDFAADIAQTRWDEIERESGLSQ 345
Cdd:cd02754 201 -------TADIADLHLPIRPGTDLALLNGLLHVLIEEGL-----IDRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 346 AALKQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGisekptpAFL 425
Cdd:cd02754 269 ADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVG-------GLA 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728610728 426 NRLKEVFGFEPPSHH------------------GHDAVQATQAMIDGRAKALICLGGNFAVAMPDHER 475
Cdd:cd02754 342 NLLPGHRSVNNPEHRaevakfwgvpegtippkpGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANR 409
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
66-580 |
5.85e-65 |
|
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: 220.66 E-value: 5.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 66 KSTFQFCENGA--KAVTWEATSKRVTPAFLAANTVSSLLAKSDFELEG---YGRLTHPLRYDRDSDTFRPVDWDEAFQRI 140
Cdd:cd00368 1 PSVCPFCGVGCgiLVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGlysPDRLKYPLIRVGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 141 GEVLRGL----EPDQVEFYTSGRASNEAAYLFQLFAREYGTNNFPDCSNMCHEATSVGLPRsIGIGKGTVSLDDFDKTEL 216
Cdd:cd00368 81 AEKLKEIrekyGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKA-FGGGAPTNTLADIENADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 217 VISIGHNPATNHPRMMGTLHELARRNVPIIVFNPLRERalerfadpqsviematygSTDIASTYFQVKAGGDAAALKGia 296
Cdd:cd00368 160 ILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTE------------------TAAKADEWLPIRPGTDAALALA-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 297 khllemesergdvldrafiaehtqgfedfaadiaqtrwDEIERESGLSQAALKQVAEAYAKSNATIITYGMGITQHNKGT 376
Cdd:cd00368 220 --------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 377 ANVRLIADLLLMRGNIGKPGAGICPlrghsnvqgnrtvgisekptpaflnrlkevfgfeppshhghdavqatqamidgra 456
Cdd:cd00368 262 QNVRAIANLAALTGNIGRPGGGLGP------------------------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 457 kaliclGGNFAVAMPDHERGFPAMGSLDLSVHVGTKLNRTHLLvgkETFIFPCLGRTEldvqatgrqsitVEDSMSMVHA 536
Cdd:cd00368 287 ------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY---ADVVLPAATYLE------------KEGTYTNTEG 345
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1728610728 537 ssgklkpasPLLRSEPAIvagmakATLPDTRVDWMTLVEDYDRI 580
Cdd:cd00368 346 ---------RVQLFRQAV------EPPGEARSDWEILRELAKRL 374
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
642-752 |
6.46e-55 |
|
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: 184.02 E-value: 6.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 642 LRLITLRSHDQYNTTIYALDDRYRGVFGRRDVLFMNEEDMAQSGLEHGDRVDIETALP-GNGQRLEDITVVAYNIAPGTV 720
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGdGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 1728610728 721 GAYYPEANVLVPLDYLDKDSGTPSYKSVPVRI 752
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 ... |
114-451 |
1.42e-43 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 167.58 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRYDRDSDTFRPVDWDEAFQRIGEVLRGLE----------------PDQVEFYTSGRASNEAAYLFQLFAREYGT 177
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRdasfveknaagvvvnrPDSIAFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 178 NNFPDCSNMCHEATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHP-RMMGTLHELARRNVPIIVFNPlreral 256
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 257 eRFADPQSViematygstdiASTYFQVKAGGDAAALKGIAKHLLemesergdvldrafiaehtqgfedfaadiaqtRW-- 334
Cdd:cd02752 208 -RFTRTAAK-----------ADLYVPIRSGTDIAFLGGMINYII--------------------------------RYtp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 335 DEIERESGLSQAALKQVAEAYAKSN----ATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPLRGHSNVQG 410
Cdd:cd02752 244 EEVEDICGVPKEDFLKVAEMFAATGrpdkPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1728610728 411 NRTVGISEKPTPAFLNrlkevfGFEPPShHGHDAVQATQAM 451
Cdd:cd02752 324 ATDLGLLSHNLPGYLG------GQNPNS-SFPNANKVRRAL 357
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-496 |
1.28e-30 |
|
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: 127.13 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRydRDSDTFRPVDWDEAFQRIGEVLRGLE----PDQVEFYTSGRASNE---AAYLFQLFAREYGTNNFPDCS-- 184
Cdd:cd02762 54 RLRTPMR--RRGGSFEEIDWDEAFDEIAERLRAIRarhgGDAVGVYGGNPQAHThagGAYSPALLKALGTSNYFSAATad 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 185 NMCHEATSVGLPRSigigKGTVSLDDFDKTELVISIGHNPATNHPRMM------GTLHELARRNVPIIVFNPLRERALER 258
Cdd:cd02762 132 QKPGHFWSGLMFGH----PGLHPVPDIDRTDYLLILGANPLQSNGSLRtapdrvLRLKAAKDRGGSLVVIDPRRTETAKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 259 fadpqsviematygstdiASTYFQVKAGGDAAALKGIAKHLLEmesERgdVLDRAFIAEHTQGFEDFAADIAQTRWDEIE 338
Cdd:cd02762 208 ------------------ADEHLFVRPGTDAWLLAAMLAVLLA---EG--LTDRRFLAEHCDGLDEVRAALAEFTPEAYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 339 RESGLSQAALKQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGIC-----PLRGHSnvqGNRT 413
Cdd:cd02762 265 PRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFttpalDLVGQT---SGRT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 414 VGISEKPTPafLNRLKEVFGFEPPShhghdaVQATQAMIDG--RAKALICLGGNFAVAMPDHERGFPAMGSLDLSVHVGT 491
Cdd:cd02762 342 IGRGEWRSR--VSGLPEIAGELPVN------VLAEEILTDGpgRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDV 413
|
....*
gi 1728610728 492 KLNRT 496
Cdd:cd02762 414 YMTET 418
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
114-399 |
6.89e-30 |
|
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: 124.28 E-value: 6.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRYD-RDSDTFRPVDWDEAFQRIGEVLR------GLEPDQVEFYTSGRASNEAAYLFQLFAREYGTNNF-PDCSN 185
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKeikaeyGPESILPYSYAGTMGLLQRAARGRFFHALGASELRgTICSG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 186 MCHEATSVGLPRSIGigkgtVSLDDFDKTELVISIGHNPATNHPRMMGTLHELARRNVPIIVFNPLRERALERfadpqsv 265
Cdd:cd02766 135 AGIEAQKYDFGASLG-----NDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAAR------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 266 iematygstdiASTYFQVKAGGDAA-ALkGIAKHLLEMESergdvLDRAFIAEHTQGFEDFAADIAQTRWDEIERESGLS 344
Cdd:cd02766 203 -----------ADLHIQIRPGTDGAlAL-GVAKVLFREGL-----YDRDFLARHTEGFEELKAHLETYTPEWAAEITGVS 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1728610728 345 QAALKQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGI 399
Cdd:cd02766 266 AEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
114-489 |
6.19e-24 |
|
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: 105.85 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRY--DRDSDTFRPVDWDEAFQRIGEVLRGLE----PDQVEFYtSGRASNEAAYLFQLFAREYGTNNFPdcsNMC 187
Cdd:cd02759 54 RLLYPLKRvgERGENKWERISWDEALDEIAEKLAEIKaeygPESIATA-VGTGRGTMWQDSLFWIRFVRLFGSP---NLF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 188 HEATSVGLPRS-----IGIGKGTVSLDDFDKTELVISIGHNPA-TNHPRMMGTLHELARRNVPIIVFNPLRERALERfad 261
Cdd:cd02759 130 LSGESCYWPRDmahalTTGFGLGYDEPDWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAAR--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 262 pqsviematygstdiASTYFQVKAGGDAAALKGIAKHLLEMEsergdVLDRAFIAEHTQGFEDFAADIAQTRWDEIERES 341
Cdd:cd02759 207 ---------------ADLWLPIRPGTDAALALGMLNVIINEG-----LYDKDFVENWCYGFEELAERVQEYTPEKVAEIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 342 GLSQAALKQVAEAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGicplrghsnvqgnrtvgisekpt 421
Cdd:cd02759 267 GVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGN----------------------- 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728610728 422 paflnrlkevFGFEPPshhghdavqatqamidgrAKALICLGGNFAVAMPDHERGFPAMGSLDLSVHV 489
Cdd:cd02759 324 ----------LLIPYP------------------VKMLIVFGTNPLASYADTAPVLEALKALDFIVVV 363
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
113-487 |
1.87e-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: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 113 GRLTHPLR--YDRDSDTFRPVDWDEAFQRIGEVLRGLEPDQV-EFYTSGRASNEAAYLFQLFAREYGTNNFPDCSNMCHE 189
Cdd:cd02755 54 DRLKKPLIrvGERGEGKFREASWDEALQYIASKLKEIKEQHGpESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHESTCLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 190 ATSVGLpRSIGIGKGTVSLDDFDKTELVISIGHN--PATNHPRMMGTLheLARRN-VPIIVFNPlreraleRFAdpqsvi 266
Cdd:cd02755 134 SKNLAW-KLVIDSFGGEVNPDFENARYIILFGRNlaEAIIVVDARRLM--KALENgAKVVVVDP-------RFS------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 267 EMATygstdIASTYFQVKAGGDAAALKGIAKHLLemeSErgDVLDRAFIAEHTQGFEDFAADIAQTRWDEIERESGLSQA 346
Cdd:cd02755 198 ELAS-----KADEWIPIKPGTDLAFVLALIHVLI---SE--NLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPAD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 347 ALKQVAE--AYAKSNATIITYGMGITQHNKgTANVRLIADLLLMRGNIGKPGaGICPlrghsnvqgnrtvgiSEKPTPaf 424
Cdd:cd02755 268 TIRRIARefAAAAPHAVVDPGWRGTFYSNS-FQTRRAIAIINALLGNIDKRG-GLYY---------------AGSAKP-- 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728610728 425 lnrlkevfgfeppshhghdavqatqamidGRAKALICLGGNFAVAMPDHERGFPAMGSLDLSV 487
Cdd:cd02755 329 -----------------------------YPIKALFIYRTNPFHSMPDRARLIKALKNLDLVV 362
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
114-492 |
4.21e-21 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 95.54 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLrYDRDSDTFRPVDWDEAFQRIGEVLRGLEPD------QVEFYTSGRASNEAAYLFQLFAREYGTNNF---PDCS 184
Cdd:pfam00384 1 RLKYPM-VRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 185 NMCHEATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLH-ELARRNVPIIVFNPLREralerfadpq 263
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRkAALKGKAKVIVIGPRLD---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 264 sviemATYGSTDIAstyfqVKAGGDAAALKGIAKhllemesergdvldrAFIAEhtqgfedfaadiaqtrwdeieresgl 343
Cdd:pfam00384 150 -----LTYADEHLG-----IKPGTDLALALAGAH---------------VFIKE-------------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 344 sqaaLKqvaeaYAKSNAT--IITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGICPLRghsNVQGNRTvgisekPT 421
Cdd:pfam00384 179 ----LK-----KDKDFAPkpIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGAAS------PV 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728610728 422 PAFlnrlkeVFGFEPPShhghDAVQATQAMIDGRAKALICLGGNFAVAMPDHERGFPAMGSLDLSV----HVGTK 492
Cdd:pfam00384 241 GAL------DLGLVPGI----KSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDK 305
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
123-432 |
1.60e-18 |
|
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: 89.98 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 123 RDSDTFRPVDWDEAFQRIG-EVLRglepdqvefyTSGRASNEAaylfqLFAREYG---TNNFPDCSNMCH---------- 188
Cdd:cd02751 68 RGEGEFVRISWDEALDLVAsELKR----------IREKYGNEA-----IFGGSYGwasAGRLHHAQSLLHrflnliggyl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 189 --------EATSVGLPRSIG---IGKGTVSLDD-FDKTELVISIGHNPATNhpRM---MGTLH-------ELARRNVPII 246
Cdd:cd02751 133 gsygtystGAAQVILPHVVGsdeVYEQGTSWDDiAEHSDLVVLFGANPLKT--RQgggGGPDHgsyyylkQAKDAGVRFI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 247 VFNPLRERALERFADpqsviematygstdiasTYFQVKAGGDAAALKGIAKHLLemeSErgDVLDRAFIAEHTQGFEDFA 326
Cdd:cd02751 211 CIDPRYTDTAAVLAA-----------------EWIPIRPGTDVALMLAMAHTLI---TE--DLHDQAFLARYTVGFDEFK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 327 A------D-IAQT-RWdeIERESGLSQAALKQVAEAYAkSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAG 398
Cdd:cd02751 269 DyllgesDgVPKTpEW--AAEITGVPAETIRALAREIA-SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGG 345
|
330 340 350
....*....|....*....|....*....|....
gi 1728610728 399 ICPLRGHSNVQGNRTVGISEKPTPAFLNRLKEVF 432
Cdd:cd02751 346 FGFGYGYSNGGGPPRGGAGGPGLPQGKNPVKDSI 379
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-396 |
7.50e-17 |
|
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: 84.88 E-value: 7.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPL--RYDRDSDTFRPVDWDEAF----QRIGEVlRGLEPDQVEFYTsGRASNEAayLFQLFAREYGTNNFPDCSNMC 187
Cdd:cd02763 54 RLTKPLlrKGPRGSGQFEEIEWEEAFsiatKRLKAA-RATDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 188 HEATSVGLPRSIGIGKGTVSLDDFDKTELVISIGhnPATNH---PRMMGtLHELARRNVPIIVFNPLReralerfadpqs 264
Cdd:cd02763 130 SVNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIG--VAEDHhsnPFKIG-IQKLKRRGGKFVAVNPVR------------ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 265 viematYGSTDIASTYFQVKAGGDAAALKGIAKHLLEmeserGDVLDRAFIAEHTQGFE------DFAADIAQTRWDEIE 338
Cdd:cd02763 195 ------TGYAAIADEWVPIKPGTDGAFILALAHELLK-----AGLIDWEFLKRYTNAAElvdytpEWVEKITGIPADTIR 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728610728 339 RESG-LSQAALKQVAE-------AYAKSNATIIT-----YGM-GITQHNKGTANVRLIADLLLMRGNIGKPG 396
Cdd:cd02763 264 RIAKeLGVTARDQPIElpiawtdVWGRKHEKITGrpvsfHAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
112-398 |
1.87e-16 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 83.79 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 112 YG--RLTHPL------RYDRDSDtFRPVDWDEAF----QRIGEVLRGLEPDQVEFYTSGRASNEAAYLFQ-LFAREYGTN 178
Cdd:PRK13532 93 YGkdRLTQPLlrmkdgKYDKEGE-FTPVSWDQAFdvmaEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASkLMKAGFRSN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 179 NFPDCSNMCHEATSVGLPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPrmmgtlhelarrnvpiIVFNPLRERaleR 258
Cdd:PRK13532 172 NIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHP----------------ILWSRVTDR---R 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 259 FADPQS-VIEMATYG--STDIASTYFQVKAGGDAAALKGIAKHLLEmeserGDVLDRAFIAEHT---QG----------- 321
Cdd:PRK13532 233 LSNPDVkVAVLSTFEhrSFELADNGIIFTPQTDLAILNYIANYIIQ-----NNAVNWDFVNKHTnfrKGatdigyglrpt 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 322 --------------------FEDFAADIAQTRWDEIERESGLSQAALKQVAEAYAKSNATIITY-GMGITQHNKGT-ANv 379
Cdd:PRK13532 308 hplekaaknpgtagksepisFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVSFwTMGFNQHTRGVwAN- 386
|
330
....*....|....*....
gi 1728610728 380 RLIADLLLMRGNIGKPGAG 398
Cdd:PRK13532 387 NLVYNIHLLTGKISTPGNG 405
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
642-749 |
3.49e-16 |
|
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: 75.00 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 642 LRLITLRSHDQYNTTIYALDDRYRGVFgRRDVLFMNEEDMAQSGLEHGDRVDIETAlpgNGqRLEDITVVAYNIAPGTVG 721
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLVEVTSR---RG-SVVVRAKVTDRVRPGVVF 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 1728610728 722 AYYPE--------ANVLVPlDYLDKDSGTPSYKSVP 749
Cdd:pfam01568 76 MPFGWwyeprggnANALTD-DATDPLSGGPEFKTCA 110
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
109-231 |
1.97e-14 |
|
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: 75.78 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 109 LEGYGRLTHPLRydRDSDTFRPVDWDEAFQRIGEVLRGLEPDQVEFYTSGRASNEAAYLFQLFAREYGTNNFpDCSNMCH 188
Cdd:cd02768 49 LNSRQRLTQPLI--KKGGKLVPVSWEEALKTVAEGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNI-DHRLRQS 125
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1728610728 189 EATSVGLPRSIGIgkGTVSLDDFDKTELVISIGHNPATNHPRM 231
Cdd:cd02768 126 DLPADNRLRGNYL--FNTSIAEIEEADAVLLIGSNLRKEAPLL 166
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
649-746 |
2.17e-13 |
|
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: 66.57 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 649 SHDQYNTTIYALDDRYRGVFgRRDVLFMNEEDMAQSGLEHGDRVDIETAlpgnGQRLEDITVVAYNIAPGTVGAYYP--- 725
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELA-PEPVVEINPEDAAALGIKDGDLVRVESR----RGSVVLRAKVTDGVPPGVVFLPHGwgh 75
|
90 100
....*....|....*....|....*..
gi 1728610728 726 ------EANVLVPlDYLDKDSGTPSYK 746
Cdd:cd02775 76 rggrggNANVLTP-DALDPPSGGPAYK 101
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
114-417 |
8.87e-13 |
|
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: 71.58 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHP--LRY------DRDSDTFRPVDWDEAFQRIGEVLRGLepdqVEFYtsgraSNEAAYLfqlfarEYGT-------- 177
Cdd:cd02770 53 RVYNPdrLKYpmkrvgKRGEGKFVRISWDEALDTIASELKRI----IEKY-----GNEAIYV------NYGTgtyggvpa 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 178 --NNFPDCSNMC------HEATSVG-----LPRSIGIGKGTVSLDDFDKTELVISIGHNPATNHPRMMGTLHELA---RR 241
Cdd:cd02770 118 grGAIARLLNLTggylnyYGTYSWAqittaTPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLqakKA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 242 NVPIIVFNPlreraleRFADpqSVIEMatygstdiASTYFQVKAGGDAAALKGIAkhlLEMESErgDVLDRAFIAEHTQG 321
Cdd:cd02770 198 GAKFIVIDP-------RYTD--TAVTL--------ADEWIPIRPGTDAALVAAMA---YVMITE--NLHDQAFLDRYCVG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 322 F------------EDFAADIAQTRWDEIERE-------SGLSQAALKQVAEAYAKSNATIITYGMGITQHNKGTANVRLI 382
Cdd:cd02770 256 FdaehlpegappnESYKDYVLGTGYDGTPKTpewaseiTGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAI 335
|
330 340 350
....*....|....*....|....*....|....*
gi 1728610728 383 ADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGIS 417
Cdd:cd02770 336 MMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGK 370
|
|
| 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 ... |
114-297 |
3.15e-12 |
|
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: 69.34 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRydRDSDTFRPVDWDEAFQRIGEVLRGLEpDQVEFYTSGRASNEAAYLFQLFAREY-GTNNFpDCSnmcheats 192
Cdd:cd02771 54 RLTQPLI--RRGGTLVPVSWNEALDVAAARLKEAK-DKVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHR-------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 193 vGLPRSIGIGKG----TVSLDDFDKTELVISIGHNPATNHPRMMGTLHELARRNVPIIVF--------NPLRERALERFA 260
Cdd:cd02771 122 -ARRLIAEILRNgpiyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAAlsgipkwqDAAVRNIAQGAK 200
|
170 180 190
....*....|....*....|....*....|....*..
gi 1728610728 261 DPQSVIEMATYGSTDIASTYFQVKAGGDAAALKGIAK 297
Cdd:cd02771 201 SPLFIVNALATRLDDIAAESIRASPGGQARLGAALAR 237
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
114-366 |
3.72e-11 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 66.61 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRY--DRDSDTFRPVDWDEAFQRIGEVLRGLE----PDQVEFytSGRASNEAAYLFQlFAREYGTnnfPDCsnMC 187
Cdd:PRK15488 98 RIVKPLKRvgERGEGKWQEISWDEAYQEIAAKLNAIKqqhgPESVAF--SSKSGSLSSHLFH-LATAFGS---PNT--FT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 188 HEATSvglPRSIGI-GKGTVSLD---DFDKTELVISIGHN--PATNHPRMMGTLHELARRNVPIIVFNPlreraleRFad 261
Cdd:PRK15488 170 HASTC---PAGYAIaAKVMFGGKlkrDLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------RF-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 262 pqSVieMAtygstDIASTYFQVKAGGDAAALKGIAkHLLEMEsergDVLDRAFIAEHTQGFEDFAADIAQTRWDEIERES 341
Cdd:PRK15488 238 --SV--VA-----SKADEWHAIRPGTDLAVVLALC-HVLIEE----NLYDKAFVERYTSGFEELAASVKEYTPEWAEAIS 303
|
250 260
....*....|....*....|....*.
gi 1728610728 342 GLSQAALKQVA-EAYAKSNATIITYG 366
Cdd:PRK15488 304 DVPADDIRRIArELAAAAPHAIVDFG 329
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
123-399 |
9.02e-10 |
|
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: 61.90 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 123 RDSDTFRPVDWDEAFQRIGEVLRglepdqvefYTSGRASNEAaylfqLFAREYG---TNNFPDCSNMCHE---------- 189
Cdd:cd02769 68 RGKEEFVRVSWDEALDLVAAELK---------RVRKTYGNEA-----IFGGSYGwssAGRFHHAQSLLHRflnlaggyvg 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 190 --------ATSVGLPRSIG-----IGKGTvSLDDF-DKTELVISIGHNPATN----------HpRMMGTLHELARRNVPI 245
Cdd:cd02769 134 svgdystgAAQVILPHVVGsmevyTEQQT-SWPVIaEHTELVVAFGADPLKNaqiawggipdH-QAYSYLKALKDRGIRF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 246 IVFNPLRERALERFAdpqsviematygstdiaSTYFQVKAGGDAAALKGIAKHLLEMesergDVLDRAFIAEHTQGFEDF 325
Cdd:cd02769 212 ISISPLRDDTAAELG-----------------AEWIAIRPGTDVALMLALAHTLVTE-----GLHDKAFLARYTVGFDKF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 326 AA------D-IAQT-RW-DEIereSGLSQAALKQVAEAYAkSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPG 396
Cdd:cd02769 270 LPyllgesDgVPKTpEWaAAI---CGIPAETIRELARRFA-SKRTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPG 345
|
...
gi 1728610728 397 AGI 399
Cdd:cd02769 346 GGF 348
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
105-405 |
1.16e-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: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 105 SDFELEGYGRLTHPLRydRDSDTFRPVDWDEAFQRIGEVLRGL-----EPDQVEFYTS-------GRASNEAAYLFQL-- 170
Cdd:cd02756 108 SPDNRVGETRLTTPLV--RRGGQLQPTTWDDAIDLVARVIKGIldkdgNDDAVFASRFdhgggggGFENNWGVGKFFFma 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 171 ----FAReygTNNFPDCSNMCHEAtsvglpRSIGIGKGTVSLDDFDKTELVISIGHNP---ATNH------PRMMG-TLH 236
Cdd:cd02756 186 lqtpFVR---IHNRPAYNSEVHAT------REMGVGELNNSYEDARLADTIVLWGNNPyetQTVYflnhwlPNLRGaTVS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 237 ELARRNVP--------IIVFNPLRE---RALERFADPQSVIematygstdiastYFQVKAGGDAAALKGIAKHLLEMESE 305
Cdd:cd02756 257 EKQQWFPPgepvppgrIIVVDPRRTetvHAAEAAAGKDRVL-------------HLQVNPGTDTALANAIARYIYESLDE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 306 rgdVLDRAfiaehtqgfedfaadiaqtrwdeiERESGLSQAALKQVAEAYAKSNA------TIITYGMGITQHNKGTANV 379
Cdd:cd02756 324 ---VLAEA------------------------EQITGVPRAQIEKAADWIAKPKEggyrkrVMFEYEKGIIWGNDNYRPI 376
|
330 340
....*....|....*....|....*.
gi 1728610728 380 RLIADLLLMRGNIGKPGAGICPLRGH 405
Cdd:cd02756 377 YSLVNLAIITGNIGRPGTGCVRQGGH 402
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
113-410 |
1.70e-09 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 60.63 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 113 GRLTHPLRYdrdsdtFRPVDWDEAFQRIGEVLRglEPDQVEFYTSGRASNEAAYLFQLFAREYGTNnFPDCSNMCHEATS 192
Cdd:COG1029 50 HRITSPRIR------GKEVSLEEAIDKAAEILA--NAKRPLIYGLSSTDCEAMRAGLALAERVGAV-VDNTASVCHGPSL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 193 VGLPRSigiGKGTVSLddfdkTE------LVISIGHNPATNHPRMM--------GTLHELARRNVPIIVFNPlreraleR 258
Cdd:COG1029 121 LALQDV---GWPTCTL-----GEvknradVIIYWGCNPVHAHPRHMsrysvfprGFFTPKGRKDRTVIVVDP-------R 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 259 FADpqsviematygSTDIASTYFQVKAGGDAAALkgiakhllemesergDVLdRAFIAehtqGFEDFAADIAqtrwdeie 338
Cdd:COG1029 186 PTD-----------TAKVADLHLQVKPGRDYEVL---------------SAL-RALVR----GKELSPEEVA-------- 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728610728 339 resGLSQAALKQVAEAYAKSNATIITYGMGITQHNKGTANVR----LIADLllmrGNIGKpgAGICPLRGHSNVQG 410
Cdd:COG1029 227 ---GIPVEDLEELAERLKNAKYGVIFWGMGLTQSPGKHLNVDaaieLVRDL----NRYTK--FSILPLRGHYNVAG 293
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
273-399 |
3.83e-08 |
|
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: 56.56 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 273 STDIASTYFQVKAGGDAAALKGIAKHLLEmeserGDVLDRAFIAEHTqgfeDFAADIAQTRWdeIERESGLSQAALKQVA 352
Cdd:cd02750 212 SAKHADLWVPIKPGTDAALALAMAHVIIK-----EKLYDEDYLKEYT----DLPFLVYTPAW--QEAITGVPRETVIRLA 280
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1728610728 353 EAYAKSNATIITYGMGITQHNKGTANVRLIADLLLMRGNIGKPGAGI 399
Cdd:cd02750 281 REFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGW 327
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
642-753 |
3.94e-07 |
|
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: 49.43 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 642 LRLITLRSHDQYNT-----TIYALDDRYRGVFgrrdvLFMNEEDMAQSGLEHGDRVDIETAlpgNGQrledITVVA---Y 713
Cdd:cd00508 5 LVLTTGRLLEHWHTgtmtrRSPRLAALAPEPF-----VEIHPEDAARLGIKDGDLVRVSSR---RGS----VVVRArvtD 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1728610728 714 NIAPGTVGAYY--------PEANVLVPlDYLDKDSGTPSYKSVPVRIT 753
Cdd:cd00508 73 RVRPGTVFMPFhwggevsgGAANALTN-DALDPVSGQPEFKACAVRIE 119
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
673-752 |
9.00e-07 |
|
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: 48.46 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 673 VLFMNEEDMAQSGLEHGDRVDIETAlpgNGqRLEDITVVAYNIAPGTV----GAYYPE---------------ANVLVPL 733
Cdd:cd02781 34 VAEINPETAAKLGIADGDWVWVETP---RG-RARQKARLTPGIRPGVVraehGWWYPEreagepalggvwesnANALTSD 109
|
90
....*....|....*....
gi 1728610728 734 DYLDKDSGTPSYKSVPVRI 752
Cdd:cd02781 110 DWNDPVSGSSPLRSMLCKI 128
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
128-410 |
1.51e-06 |
|
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: 51.18 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 128 FRPVDWDEAFQRIGEVLRglEPDQVEFYTSGRASNEA-AYLFQLfaREYGTNNFPDCSNMCHEATSVGLPRSigiGKGTV 206
Cdd:cd02761 51 GKPVSLEEAIEKAAEILK--EAKRPLFYGLGTTVCEAqRAGIEL--AEKLGAIIDHAASVCHGPNLLALQDS---GWPTT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 207 SLDDF-DKTELVISIGHNPATNHPRMMgtlhelARRNVPiivfnplrERALERFADPQS----VIEMATYGSTDIASTYF 281
Cdd:cd02761 124 TLGEVkNRADVIVYWGTNPMHAHPRHM------SRYSVF--------PRGFFREGGREDrtliVVDPRKSDTAKLADIHL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 282 QVKAGGDaaalkgiakhllemesergdvldrafiaehtqgFEDFAADIAQTRWDEIERES--GLSQAALKQVAEAYAKSN 359
Cdd:cd02761 190 QIDPGSD---------------------------------YELLAALRALLRGAGLVPDEvaGIPAETILELAERLKNAK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1728610728 360 ATIITYGMGITQ----HNKGTANVRLIADLllmrGNIGKpgAGICPLRGHSNVQG 410
Cdd:cd02761 237 FGVIFWGLGLLPsrgaHRNIEAAIRLVKAL----NEYTK--FALLPLRGHYNVRG 285
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
673-752 |
3.62e-06 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 46.77 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 673 VLFMNEEDMAQSGLEHGDRVDIETalpgngqrlEDITVV-----AYNIAPGTV----GayyPEANVLVPLDylDKDSGTP 743
Cdd:COG1153 32 VCELNPEDMKKLGIKEGDKVKVTS---------EYGEVVvkakeSEDLHPGLVfipmG---PWANAVVPPE--THSTGMP 97
|
....*....
gi 1728610728 744 SYKSVPVRI 752
Cdd:COG1153 98 DFKGVPVEV 106
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
104-224 |
7.24e-06 |
|
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: 48.80 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 104 KSDFELEG--YGRLTHPlrYDRDSDTFRPVDWDEAFQRIGEVLRGLEPDQVEFYTSGRASNEAAYLFQLFAREYGtnnfp 181
Cdd:cd02773 41 KTRFAYDGlkRQRLDKP--YIRKNGKLKPATWEEALAAIAKALKGVKPDEIAAIAGDLADVESMVALKDLLNKLG----- 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1728610728 182 dCSNMCHEATSVGLP---RSIGIGKGTVSldDFDKTELVISIGHNP 224
Cdd:cd02773 114 -SENLACEQDGPDLPadlRSNYLFNTTIA--GIEEADAVLLVGTNP 156
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
676-753 |
1.77e-05 |
|
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. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 44.52 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 676 MNEEDMAQSGLEHGDRVDIETAlpgNGqRLEDITVVAYNIAPGTVGAYY----------PEANVLVPLDYlDKDSGTPSY 745
Cdd:cd02792 39 ISPELAAERGIKNGDMVWVSSP---RG-KIKVKALVTDRVKPHEVGIPYhwggmglvigDSANTLTPYVG-DPNTQTPEY 113
|
....*...
gi 1728610728 746 KSVPVRIT 753
Cdd:cd02792 114 KAFLVNIE 121
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
618-721 |
3.63e-05 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 47.30 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 618 ATGKAMFSVFDgvhenasgEGEHVLRLITLRSHDQYNTTIYAldDRYRGVFGRRDVLfMNEEDMAQSGLEHGDRVDIETa 697
Cdd:PRK14991 873 ADGTPLREQFP--------ESQWPLLLISFKSNLMSSMSIAS--PRLRQVKPANPVA-LNPQDAARLGIQHGDRVRIST- 940
|
90 100
....*....|....*....|....
gi 1728610728 698 lPGnGQRLEDITVVAyNIAPGTVG 721
Cdd:PRK14991 941 -PG-GSVVAQASVLN-GVMPGVIA 961
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
114-302 |
1.52e-04 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 45.32 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 114 RLTHPLRYDRDsDTFRPVDWDEAFQRIGEVLRGLEpDQVEFYTSGRASNEAAYLFQLFAR-EYGTNNFpDCSNMCH---E 189
Cdd:PRK07860 278 RITTPLVRDED-GELEPASWSEALAVAARGLAAAR-GRVGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPHsaeE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 190 ATSVGlPRSIGIGKGtVSLDDFDKTELVISIGHNPATNHPrmmgtlhelarrnvpiIVFNPLRERALERFADPQSVIEMA 269
Cdd:PRK07860 355 ADFLA-ARVAGRGLG-VTYADLEKAPAVLLVGFEPEEESP----------------IVFLRLRKAARKHGLKVYSIAPFA 416
|
170 180 190
....*....|....*....|....*....|...
gi 1728610728 270 TYGSTDIASTYFQVKAGGDAAALKGIAKHLLEM 302
Cdd:PRK07860 417 TRGLEKMGGTLLRTAPGGEAAALDALATGAPDV 449
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
642-724 |
2.22e-04 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 41.90 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 642 LRLITLRSHdqYNTTIYALDDRYRGvFGRRDVLFMNEEDMAQSGLEHGDRVDIETalPGNgqRLEDITVVAYNIAPGTVG 721
Cdd:cd02780 3 FILVTFKSN--LNSHRSANAPWLKE-IKPENPVWINPEDAAKLGIKTGDRVRVVT--PGG--SVVGKAKVTEGVRPGVVA 75
|
...
gi 1728610728 722 AYY 724
Cdd:cd02780 76 IEH 78
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|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
676-752 |
3.31e-04 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), 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 superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 40.49 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 676 MNEEDMAQSGLEHGDRVDIETalpgngqrlEDITVVAY-----NIAPGTVgaYYPE---ANVLVPLDYLdkDSGTPSYKS 747
Cdd:cd02789 35 INPEDYKLLGKPEGDKVKVTS---------EFGEVVVFakeneGVPEGMV--FIPMgpwANVVVDPYTD--STGSPIFKG 101
|
....*
gi 1728610728 748 VPVRI 752
Cdd:cd02789 102 VPVYI 106
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
673-753 |
8.79e-03 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 36.78 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728610728 673 VLFMNEEDMAQSGLEHGDRVDIETAlpgNGQ-----RLEDItvvaynIAPGTV---------GAYYPEANVLVpLDYLDK 738
Cdd:cd02791 36 YVEIHPEDAARLGLKEGDLVRVTSR---RGEvvlrvRVTDR------VRPGEVfvpmhwgdqFGRSGRVNALT-LDATDP 105
|
90
....*....|....*
gi 1728610728 739 DSGTPSYKSVPVRIT 753
Cdd:cd02791 106 VSGQPEFKHCAVRIE 120
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