|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
50-520 |
3.78e-132 |
|
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: 391.66 E-value: 3.78e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 50 ASLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAA---DGSFEAIDWDTAFS 126
Cdd:cd02755 2 PSICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGergEGKFREASWDEALQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 127 EIGAKVKDILAKNGPEALAIVQDPrPSGKEYSKRFINVLGSANIYTHGAACNSSKEAGFAQTIGT--GNFSVDFGNSKMV 204
Cdd:cd02755 82 YIASKLKEIKEQHGPESVLFGGHG-GCYSPFFKHFAAAFGSPNIFSHESTCLASKNLAWKLVIDSfgGEVNPDFENARYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 205 VFIGRSYGDGIRPSSVQSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQNA 284
Cdd:cd02755 161 ILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFVEKYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 285 VGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIARALAKAAPAAAVEASWRAAFGcahQNSFDTARAVTAVNALLGSWGAK 364
Cdd:cd02755 241 NGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGTFY---SNSFQTRRAIAIINALLGNIDKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 365 GGALltsspkagdidkqkFPSAPKPeakrvgdkeYPlapsgmgsnlavlqaaldgaMKGVFFYNSNAVQGYAQPKVWREG 444
Cdd:cd02755 318 GGLY--------------YAGSAKP---------YP--------------------IKALFIYRTNPFHSMPDRARLIKA 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527669108 445 LEKTDLVVTIDVQMSETALASDYVLPECTYLERMELPEFIGGKKHYVAMRTQVLEPIhPETKPCDEIFAGLAEACG 520
Cdd:cd02755 355 LKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAVATRQRAIEPL-YDTRPGWDILKELARRLG 429
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
31-524 |
2.34e-126 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 384.19 E-value: 2.34e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 31 GAWQAEAAHAEGsyeRKEGASLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRR 110
Cdd:COG0243 9 AGAGAAALEAAG---TKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 111 ---AADGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAI----VQDPRPSGKEY--SKRFINVLGSANIYTHGAACNSSK 181
Cdd:COG0243 86 vgpRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFytsgGSAGRLSNEAAylAQRFARALGTNNLDDNSRLCHESA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 182 EAGFAQTIGTGNFSV---DFGNSKMVVFIGRSYGDGiRPSSVQSL-AAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGT 257
Cdd:COG0243 166 VAGLPRTFGSDKGTVsyeDLEHADLIVLWGSNPAEN-HPRLLRRLrEAAKKRGAKIVVIDPRRTETAAIADEWLPIRPGT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 258 DLAFLLGICNVLIEEDLYDHEFVEQNAVGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIARALAKAApaaaveaswRAAF 337
Cdd:COG0243 245 DAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAK---------PAVI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 338 GCA-----HQNSFDTARAVTAVNALLGSWGAKGGALLtssPKAGDidkqkfpsapkpeakrvgdkeyplapsgmgsnlav 412
Cdd:COG0243 316 LWGmglqqHSNGTQTVRAIANLALLTGNIGKPGGGPF---SLTGE----------------------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 413 lqAALDGA---MKGVFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLERMELpeFIGGKKH 489
Cdd:COG0243 358 --AILDGKpypIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDI--VTNSEDR 433
|
490 500 510
....*....|....*....|....*....|....*
gi 2527669108 490 YVAMRTQVLEPIHpETKPCDEIFAGLAEACGVGEY 524
Cdd:COG0243 434 RVHLSRPAVEPPG-EARSDWEIFAELAKRLGFEEA 467
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
4-524 |
4.76e-110 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 344.34 E-value: 4.76e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 4 SVTRRTFLKGSAATAAlaatgagVCSL-----GAWQA-EAAHAEGSyeRKEGASLCNGCSSKCGLVATTLGGQLFTLRGS 77
Cdd:PRK15488 2 SLSRRDFLKGAGAGCA-------ACALgsllpGALAAnEIAQLKGK--TKLTPSICEMCSTRCPIEARVVNGKNVFIQGN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 78 dvhPYAK---GTICGRG-HGVAQIaYSDERLTQPMRRAA---DGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAIVQDp 150
Cdd:PRK15488 73 ---PKAKsfgTKVCARGgSGHSLL-YDPQRIVKPLKRVGergEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSK- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 151 rpSGKEYSK--RFINVLGSANIYTHGAACNSSKEAGFAQTIGtGNFSVDFGNSKMVVFIGRSYGDGIRPSSVQSLAAAA- 227
Cdd:PRK15488 148 --SGSLSSHlfHLATAFGSPNTFTHASTCPAGYAIAAKVMFG-GKLKRDLANSKYIINFGHNLYEGINMSDTRGLMTAQm 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 228 DKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQNAVGFEEFAAQAKEYTPAWAEQQCG 307
Cdd:PRK15488 225 EKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 308 VPAATIEEIARALAKAAPAAAVEASWRAAFGcahQNSFDTARAVTAVNALLGSWGAKGGALLTSSPK-----AGD----- 377
Cdd:PRK15488 305 VPADDIRRIARELAAAAPHAIVDFGHRATFT---PEEFDMRRAIFAANVLLGNIERKGGLYFGKNASvynklAGEkvapt 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 378 IDKQKFPSAPKPEAKRVG--DKEYPLAPSGMGSNLAVLQAALDG---AMKGVFFYNSNAVQGYAQPKVWREGLEKTDLVV 452
Cdd:PRK15488 382 LAKPGVKGMPKPTAKRIDlvGEQFKYIAAGGGVVQSIIDATLTQkpyQIKGWVMSRHNPMQTVTDRADVVKALKKLDLVV 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527669108 453 TIDVQMSETALASDYVLPECTYLERMELPEFIGGKKHYVAMRTQVLEPIHpETKPCDEIFAGLAEACGVGEY 524
Cdd:PRK15488 462 VCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYALRQRVVEPIG-DTKPSWQIFKELGEKMGLGQY 532
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
53-516 |
2.79e-74 |
|
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: 242.98 E-value: 2.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 53 CNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRA---ADGSFEAIDWDTAFSEIG 129
Cdd:cd02759 4 CPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgerGENKWERISWDEALDEIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 130 AKVKDILAKNGPEALAIVQDpRPSG-----KEYSKRFINVLGSANIYTHGAACNSSKEAGFAQTIGTGN--FSVDFGNSK 202
Cdd:cd02759 84 EKLAEIKAEYGPESIATAVG-TGRGtmwqdSLFWIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLgyDEPDWENPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 203 MVVFIGRsygDGIRPSSV---QSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEF 279
Cdd:cd02759 163 CIVLWGK---NPLNSNLDlqgHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKDF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 280 VEQNAVGFEEFAAQAKEYTPAWAEQQCGVPAatiEEIARALAKAAPAAAVEASWraAFGCAHQ-NSFDTARAVTAVNALL 358
Cdd:cd02759 240 VENWCYGFEELAERVQEYTPEKVAEITGVPA---EKIRKAARLYATAKPACIQW--GLAIDQQkNGTQTSRAIAILRAIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 359 GSWGAKGGALLTsspkagdidkqkfpsapkpeakrvgdkEYPLapsgmgsnlavlqaaldgamKGVFFYNSNAVQGYAQP 438
Cdd:cd02759 315 GNLDVPGGNLLI---------------------------PYPV--------------------KMLIVFGTNPLASYADT 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527669108 439 KVWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLERMELPEFIGGKKHyVAMRTQVLEPIHpETKPCDEIFAGLA 516
Cdd:cd02759 348 APVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAENF-VQLRQKAVEPYG-EAKSDYEIVLELG 423
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
51-518 |
9.08e-73 |
|
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: 235.69 E-value: 9.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAAD-GSFEAIDWDTAFSEIG 129
Cdd:cd00368 2 SVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGrGKFVPISWDEALDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 130 AKVKDILAKNGPEALAIVQDPRPSGKE--YSKRFINVLGSANIYTHGAACNSSKEAGFAQtIGTGNFSV---DFGNSKMV 204
Cdd:cd00368 82 EKLKEIREKYGPDAIAFYGGGGASNEEayLLQKLLRALGSNNVDSHARLCHASAVAALKA-FGGGAPTNtlaDIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 205 VFIGRSYGDGiRPSSVQSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGicnvlieedlydhefveqna 284
Cdd:cd00368 161 LLWGSNPAET-HPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA-------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 285 vgfeefaaqakeytpAWAEQQCGVPAATIEEIaralaKAAPAAAVEASWRAAFG-CAHQNSFDTARAVTAVNALLGSWGA 363
Cdd:cd00368 220 ---------------EWAAEITGVPAETIRAL-----AREFAAAKRAVILWGMGlTQHTNGTQNVRAIANLAALTGNIGR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 364 KGGAlltsspkagdidkqkfpsapkpeakrvgdkeyplapsgmgsnlavlqaaldgamkgvFFYNSNAVQGYAQPKVWRE 443
Cdd:cd00368 280 PGGG---------------------------------------------------------LGPGGNPLVSAPDANRVRA 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527669108 444 GLEKTDLVVTIDVQMSETALASDYVLPECTYLERmelPEFIGGKKHYVAMRTQVLEPIhPETKPCDEIFAGLAEA 518
Cdd:cd00368 303 ALKKLDFVVVIDIFMTETAAYADVVLPAATYLEK---EGTYTNTEGRVQLFRQAVEPP-GEARSDWEILRELAKR 373
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
56-524 |
5.22e-71 |
|
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: 235.22 E-value: 5.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 56 CSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAADGS--FEAIDWDTAFSEIGAKVK 133
Cdd:cd02766 8 CPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKGgqWERISWDEALDTIAAKLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 134 DILAKNGPEALA---------IVQDPRPSgkeyskRFINVLGSANiyTHGAACNSSKEAGFAQTIGT--GNFSVDFGNSK 202
Cdd:cd02766 88 EIKAEYGPESILpysyagtmgLLQRAARG------RFFHALGASE--LRGTICSGAGIEAQKYDFGAslGNDPEDMVNAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 203 MVVFIGRsygDGIRpSSVQSLA---AAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEF 279
Cdd:cd02766 160 LIVIWGI---NPAA-TNIHLMRiiqEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRDF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 280 VEQNAVGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIaralaKAAPAAAVEASWRAAFGCA-HQNSFDTARAVTAVNALL 358
Cdd:cd02766 236 LARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEEL-----ARLYGEAKPPSIRLGYGMQrYRNGGQNVRAIDALPALT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 359 GSWGAKGGalltsspkagdidkqkfpsapkpeakrvgdkeyplapsgmgsnlAVLQAALDGAMKGVFFYNSNAVQGYAQP 438
Cdd:cd02766 311 GNIGVPGG--------------------------------------------GAFYSNSGPPVKALWVYNSNPVAQAPDS 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 439 KVWREGLEKTDL-VVTIDVQMSETALASDYVLPECTYLERMELpeFIGGKKHYVAMRTQVLEPiHPETKPCDEIFAGLAE 517
Cdd:cd02766 347 NKVRKGLAREDLfVVVHDQFMTDTARYADIVLPATTFLEHEDV--YASYWHYYLQYNEPAIPP-PGEARSNTEIFRELAK 423
|
....*..
gi 2527669108 518 ACGVGEY 524
Cdd:cd02766 424 RLGFGEP 430
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
50-518 |
1.78e-68 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 228.86 E-value: 1.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 50 ASLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRA-------ADGSFEAIDWD 122
Cdd:cd02757 3 PSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgrdVDPKFVPISWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 123 TAFSEIGAKVKDILAKNGPEALAI-VQDPRPSGKEYSKRFINVLGSANIYTHGAACNSSKEAGFAQT-IGTGNFSVDFGN 200
Cdd:cd02757 83 EALDTIADKIRALRKENEPHKIMLhRGRYGHNNSILYGRFTKMIGSPNNISHSSVCAESEKFGRYYTeGGWDYNSYDYAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 201 SKMVVFIGRSYGDGIRPSS-VQSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEF 279
Cdd:cd02757 163 AKYILFFGADPLESNRQNPhAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKDF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 280 V----------------------EQNAVGF-EEFAAQAKEYTPAWAEQQCGVPAATIEEIaRALAKAAPAAAVEASWRAA 336
Cdd:cd02757 243 VgdfvdgknyfkagetvdeesfkEKSTEGLvKWWNLELKDYTPEWAAKISGIPAETIERV-AREFATAAPAAAAFTWRGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 337 fgCAHQNSFDTARAVTAVNALLGSWGAKGGALL-TSSPKagdidkqkfpsapkpeakrvgdkeyplapsgmgsnlavlqa 415
Cdd:cd02757 322 --TMQNRGSYNSMACHALNGLVGSIDSKGGLCPnMGVPK----------------------------------------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 416 aldgaMKGVFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLERMelpEFIGGKKH---YVA 492
Cdd:cd02757 359 -----IKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERW---DVMSQENNlhpWLS 430
|
490 500
....*....|....*....|....*.
gi 2527669108 493 MRTQVLEPIHpETKPCDEIFAGLAEA 518
Cdd:cd02757 431 IRQPVVKSLG-EVREETEILIELAKK 455
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
53-518 |
1.47e-67 |
|
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: 226.89 E-value: 1.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 53 CNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAaDGSFEAIDWDTAFSEIGAKV 132
Cdd:cd02762 4 CILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRR-GGSFEEIDWDEAFDEIAERL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 133 KDILAKNGPEALAIV----QDPRPSGKEYSKRFINVLGSANIYThgAACNSSKEAGFAQTIGTGNFSV----DFGNSKMV 204
Cdd:cd02762 83 RAIRARHGGDAVGVYggnpQAHTHAGGAYSPALLKALGTSNYFS--AATADQKPGHFWSGLMFGHPGLhpvpDIDRTDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 205 VFIGR----SYGD-GIRPSSVQSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEF 279
Cdd:cd02762 161 LILGAnplqSNGSlRTAPDRVLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAEGLTDRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 280 VEQNAVGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIaralaKAAPAAAVEASWRAAFGCAHQ-NSFDTARAVTAVNALL 358
Cdd:cd02762 241 LAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRL-----AREFAAAPSAAVYGRLGVQTQlFGTLCSWLVKLLNLLT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 359 GSWGAKGGALLTSSPkagdIDKQKFPSAPkpeAKRVGDKEYPL--APSGMG----SNLA-VLQAALDGAMKGVFFYNSNA 431
Cdd:cd02762 316 GNLDRPGGAMFTTPA----LDLVGQTSGR---TIGRGEWRSRVsgLPEIAGelpvNVLAeEILTDGPGRIRAMIVVAGNP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 432 VQGYAQPKVWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLERMEL----PEFIggkKHYVAMRTQVLEPIhPETKP 507
Cdd:cd02762 389 VLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHAtffnLEFP---RNAFRYRRPLFPPP-PGTLP 464
|
490
....*....|.
gi 2527669108 508 CDEIFAGLAEA 518
Cdd:cd02762 465 EWEILARLVEA 475
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
51-522 |
2.34e-67 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 229.77 E-value: 2.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAaDGSFEAIDWDTAFSEIGA 130
Cdd:COG3383 9 TVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRR-GGEFREVSWDEALDLVAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 131 KVKDILAKNGPEALAIVQDPRPSGKEY---SKRFINVLGSANIYTHGAACNSSKEAGFAQTIGTGNFSV---DFGNSKMV 204
Cdd:COG3383 88 RLREIQAEHGPDAVAFYGSGQLTNEENyllQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNsydDIEEADVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 205 VFIG----RSYgdgirPSSVQSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFV 280
Cdd:COG3383 168 LVIGsnpaEAH-----PVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDEDFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 281 EQNAVGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIARALAKAApaaaveaswRAAFGCA-----HQNSFDTARAVTAVN 355
Cdd:COG3383 243 AERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAK---------RAMILWGmgvnqHTQGTDNVNAIINLA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 356 ALLGSWGAKGGAL--LTSSPK---AGDI--------DKQKF--PSAPKPEAKRVGDKEYPLAPsGMgSNLAVLQAALDGA 420
Cdd:COG3383 314 LATGNIGRPGTGPfpLTGQNNvqgGRDMgalpnvlpGYRDVtdPEHRAKVADAWGVPPLPDKP-GL-TAVEMFDAIADGE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 421 MKGVFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLERmelpefiggKKHY------VAMR 494
Cdd:COG3383 392 IKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEK---------DGTFtnterrVQRV 462
|
490 500
....*....|....*....|....*...
gi 2527669108 495 TQVLEPIhPETKPCDEIFAGLAEACGVG 522
Cdd:COG3383 463 RKAVEPP-GEARPDWEIIAELARRLGYG 489
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
50-524 |
4.18e-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: 210.55 E-value: 4.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 50 ASLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAADGSFEAIDWDTAFSEIG 129
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 130 AKVKDILAKNGPEALAIVQdprpSGK----EY---SKRFINVLGSANIYTHGAACNSSKEAGFAQTIG----TGNFSvDF 198
Cdd:cd02754 81 ERFKAIQAEYGPDSVAFYG----SGQllteEYyaaNKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGadgpPGSYD-DI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 199 GNSKMVVFIGRSYGDGiRPSSVQSL--AAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYD 276
Cdd:cd02754 156 EHADCFFLIGSNMAEC-HPILFRRLldRKKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLID 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 277 HEFVEQNAVGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIAralakaapaaaveaswrAAFGCA-------------HQN 343
Cdd:cd02754 235 RDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAA-----------------RLFGEArkvmslwtmgvnqSTQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 344 SFDTARAVTAVNALLGSWGAKGGAL--LTSSPKAG----------------DIDKQK--------FPSAPKPEAKRVGDK 397
Cdd:cd02754 298 GTAANNAIINLHLATGKIGRPGSGPfsLTGQPNAMggrevgglanllpghrSVNNPEhraevakfWGVPEGTIPPKPGLH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 398 EYPLapsgmgsnlavLQAALDGAMKGVFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDV-QMSETALASDYVLPECTYLE 476
Cdd:cd02754 378 AVEM-----------FEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEYADLVLPAASWGE 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2527669108 477 RmelpE--FIGGKKHYVAMRTQVLEPihPETKPCDEIFAGLAEACGVGEY 524
Cdd:cd02754 447 K----EgtMTNSERRVSLLRAAVEPP--GEARPDWWILADVARRLGFGEL 490
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
51-520 |
8.31e-61 |
|
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: 211.94 E-value: 8.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAADgSFEAIDWDTAFSEIGA 130
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGD-KFREVSWDEAISYIAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 131 KVKDILAKNGPEALAIVQDPRPSGKE-YS--KRFINVLGSANIYTHGAACNSSKEAGFAQTIGTGNFSVDFG---NSKMV 204
Cdd:TIGR01591 80 KLKEIKEKYGPDSIGFIGSSRGTNEEnYLlqKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISeieNADLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 205 VFIGRSYGDGiRPSSVQSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQNA 284
Cdd:TIGR01591 160 VIIGYNPAES-HPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFIEKRT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 285 VGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIaraLAKAAPAAAVEASWraAFGCA-HQNSFDTARAVTAVNALLGSWGA 363
Cdd:TIGR01591 239 EGFEEFREIVKGYTPEYVEDITGVPADLIREA---ARMYAKAGSAAILW--GMGVTqHSQGVETVMALINLAMLTGNIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 364 KGGALLtssPKAGDIDKQ------KFPSAPkPEAKRVGDKEY-----------PLaPSGMGSNLA-VLQAALDGAMKGVF 425
Cdd:TIGR01591 314 PGGGVN---PLRGQNNVQgacdmgALPDFL-PGYQPVSDEEVrekfakawgvvKL-PAEPGLRIPeMIDAAADGDVKALY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 426 FYNSNAVQGYAQPKVWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLERMElpEFIGGKKHyVAMRTQVLEPIHpET 505
Cdd:TIGR01591 389 IMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEG--TFTNAERR-IQRFFKAVEPKG-ES 464
|
490
....*....|....*
gi 2527669108 506 KPCDEIFAGLAEACG 520
Cdd:TIGR01591 465 KPDWEIIQELANALG 479
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
87-523 |
2.66e-53 |
|
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: 190.13 E-value: 2.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 87 ICGRGHGVAQIAYSDERLTQPMRRA-------------ADGSFEAIDWDTAFSEIGAKVKDILAKNGPEAL--------- 144
Cdd:cd02751 31 PCPRGRSVRDRVYSPDRIKYPMKRVgwlgngpgsrelrGEGEFVRISWDEALDLVASELKRIREKYGNEAIfggsygwas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 145 -AIVQDPRPSGKeyskRFINVLG----SANIYTHGAAcnsskEAGFAQTIGT-----GNFSVD--FGNSKMVVFIG---- 208
Cdd:cd02751 111 aGRLHHAQSLLH----RFLNLIGgylgSYGTYSTGAA-----QVILPHVVGSdevyeQGTSWDdiAEHSDLVVLFGanpl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 209 ---RSYGDGIRPSSVQSLAAAADKGTRIVIVDPRLNNSGI-FATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQNA 284
Cdd:cd02751 182 ktrQGGGGGPDHGSYYYLKQAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 285 VGFEEFAA--------QAKeyTPAWAEQQCGVPAATIEEIARALAKAAPAAAVEASW-RAAFGcaHQnsfdTARAVTAVN 355
Cdd:cd02751 262 VGFDEFKDyllgesdgVPK--TPEWAAEITGVPAETIRALAREIASKRTMIAQGWGLqRAHHG--EQ----PAWMLVTLA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 356 ALLG-----------SWGAKGGALLTSSPKAGDID-------KQKFPSAPKPEAKRVGDKEYplapSGMGSNLavlqaaL 417
Cdd:cd02751 334 AMLGqiglpgggfgfGYGYSNGGGPPRGGAGGPGLpqgknpvKDSIPVARIADALLNPGKEF----TANGKLK------T 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 418 DGAMKGVFFYNSNAV---QGYAQpkvWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLERMELPEFIGGKKHY-VAM 493
Cdd:cd02751 404 YPDIKMIYWAGGNPLhhhQDLNR---LIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNYSNRYlIAM 480
|
490 500 510
....*....|....*....|....*....|
gi 2527669108 494 RtQVLEPIHpETKPCDEIFAGLAEACGVGE 523
Cdd:cd02751 481 K-QAVEPLG-EARSDYEIFAELAKRLGVEE 508
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
51-477 |
1.14e-52 |
|
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: 186.65 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAaDGSFEAIDWDTAFSEIGA 130
Cdd:cd02753 2 TVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRK-NGKFVEASWDEALSLVAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 131 KVKDILAKNGPEALAIVQDPRPSGKE-YS-KRFI-NVLGSANIYTHGAACNSSKEAGFAQTIGTGNFSV---DFGNSKMV 204
Cdd:cd02753 81 RLKEIKDKYGPDAIAFFGSAKCTNEEnYLfQKLArAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNsiaDIEEADVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 205 VFIGRSYGDGiRPSSVQSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQNA 284
Cdd:cd02753 161 LVIGSNTTEA-HPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEFIEERT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 285 VGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIARALAKAApaaaveaswRAAFGCA-----HQNSFDTARAVTAVNALLG 359
Cdd:cd02753 240 EGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAK---------SAAILWGmgvtqHSHGTDNVMALSNLALLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 360 SWGAKGGALLtssPKAGDIDKQkfpsapkpeakrvgdkeyplAPSGMGsnlaVLQAALDGAMKGVFFYNSNAVQGYAQPK 439
Cdd:cd02753 311 NIGRPGTGVN---PLRGQNNVQ--------------------GACDMG----ALPNVLPGYVKALYIMGENPALSDPNTN 363
|
410 420 430
....*....|....*....|....*....|....*...
gi 2527669108 440 VWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLER 477
Cdd:cd02753 364 HVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEK 401
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
51-516 |
5.53e-50 |
|
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: 182.34 E-value: 5.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAAD---GSFEAIDWDTAFSE 127
Cdd:cd02763 2 TTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPrgsGQFEEIEWEEAFSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 128 IGAKVKDILAKNgPEALAIVQDpRPSGKEYSKRFINVLGSANIYTHGAACNSSKEAGFAQTIGtGNF----SVDFGNSKM 203
Cdd:cd02763 82 ATKRLKAARATD-PKKFAFFTG-RDQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIG-GSFwefgGPDLEHTKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 204 VVFIGRSYGDGIRPSSVqSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQN 283
Cdd:cd02763 159 FMMIGVAEDHHSNPFKI-GIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 284 AVgfeefAAQAKEYTPAWAEQQCGVPAATIEEIARALAKAAPAAAVEA--SWRAAFG-------------------CAHQ 342
Cdd:cd02763 238 TN-----AAELVDYTPEWVEKITGIPADTIRRIAKELGVTARDQPIELpiAWTDVWGrkhekitgrpvsfhamrgiAAHS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 343 NSFDTARAVTAVNALLGSWGAKGGALLTS--------SPK-AGDIDKQK-----------FPSAP-------KPEAKRVg 395
Cdd:cd02763 313 NGFQTIRALFVLMMLLGTIDRPGGFRHKPpyprhippLPKpPKIPSADKpftplygpplgWPASPddllvdeDGNPLRI- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 396 DK----EYPLAPSGMGSNlaVLQAALDG---AMKGVFFYNSNAVQGYAQ--PKVWR-------EGLEKTDLVVTIDVQMS 459
Cdd:cd02763 392 DKayswEYPLAAHGCMQN--VITNAWRGdpyPIDTLMIYMANMAWNSSMntPEVREmltdkdaSGNYKIPFIIVCDAFYS 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527669108 460 ETALASDYVLPECTYLER------MELP--EFIGGKKhyvAMRTQVLEPIHpETKPCDEIFAGLA 516
Cdd:cd02763 470 EMVAFADLVLPDTTYLERhdamslLDRPisEADGPVD---AIRVPIVEPKG-DVKPFQEVLIELG 530
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
51-481 |
5.08e-46 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 171.76 E-value: 5.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVA--TTLGGQLFTLRGSDVHPY---------------------------AKGTICGRGHGVAQIAYSD 101
Cdd:cd02758 2 SSCLGCWTQCGIRVrvDKETGKVLRIAGNPYHPLntapslpyntplkeslylslvgenglkARATACARGNAGLQYLYDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 102 ERLTQPMRRAA---DGSFEAIDWDTAFSEI----------------GAKVKDILAKN-----GPEALAI-VQDPRPSGKE 156
Cdd:cd02758 82 YRVLQPLKRVGprgSGKWKPISWEQLIEEVveggdlfgeghveglkAIRDLDTPIDPdhpdlGPKANQLlYTFGRDEGRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 157 Y-SKRFI-NVLGSANIYTHGAACNSSKEAGFAQTIGT--GNFSV--DFGNSKMVVFIGRS---YGDGIRPSSVQSLAAAA 227
Cdd:cd02758 162 PfIKRFAnQAFGTVNFGGHGSYCGLSYRAGNGALMNDldGYPHVkpDFDNAEFALFIGTSpaqAGNPFKRQARRLAEART 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 228 DKGTRIVIVDPRLNNSGIFATD---WVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQ---------------NAV---- 285
Cdd:cd02758 242 EGNFKYVVVDPVLPNTTSAAGEnirWVPIKPGGDGALAMAMIRWIIENERYNAEYLSIpskeaakaagepswtNAThlvi 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 286 ------GFEEFAAQAKEYTPA-WAEQqCGVPAATIEEIARALAKAAPaaaveaswRAAF----GCAHQNSFDTARAVTAV 354
Cdd:cd02758 322 tvrvksALQLLKEEAFSYSLEeYAEI-CGVPEAKIIELAKEFTSHGR--------AAAVvhhgGTMHSNGFYNAYAIRML 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 355 NALLGSWGAKGGALLTSSP-----KAGDIDKQKFPSAPKP----------------EAKRVGDKE----------YPLAP 403
Cdd:cd02758 393 NALIGNLNWKGGLLMSGGGfadnsAGPRYDFKKFFGEVKPwgvpidrskkayektsEYKRKVAAGenpypakrpwYPLTP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 404 SGMGSnlaVLQAALDG---AMKGVFFYNSNAVqgYAQP---KVWREGL---EKTDLVVTIDVQMSETALASDYVLPECTY 474
Cdd:cd02758 473 ELYTE---VIASAAEGypyKLKALILWMANPV--YGAPglvKQVEEKLkdpKKLPLFIAIDAFINETSAYADYIVPDTTY 547
|
....*..
gi 2527669108 475 LERMELP 481
Cdd:cd02758 548 YESWGFS 554
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
55-524 |
2.50e-45 |
|
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: 167.66 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 55 GCSSKCGLVATTLGGQLFTLRGSDV--HPYAKgtICGRGHGVAQIAYSDERLTQPMRRA---ADGSFEAIDWDTAFSEIG 129
Cdd:cd02765 7 NCGGRCPLKCHVRDGKIVKVEPNEWpdKTYKR--GCTRGLSHLQRVYSPDRLKYPMKRVgerGEGKFERITWDEALDTIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 130 AKVKDILAKNGPEALAIVQDprpSGKEYSKRFI-NVLGSANIY-THGAACNSSKEAGFAQTIGTGNF-----SVDFGNSK 202
Cdd:cd02765 85 DKLTEAKREYGGKSILWMSS---SGDGAILSYLrLALLGGGLQdALTYGIDTGVGQGFNRVTGGGFMpptneITDWVNAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 203 MVVFIGRSygdgIRPSSVQSLA---AAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEF 279
Cdd:cd02765 162 TIIIWGSN----ILETQFQDAEfflDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 280 VEQNA--------------------------------------------------------------VGFEEFAAQAKEY 297
Cdd:cd02765 238 LKSNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhTVLTALREQAASY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 298 TPAWAEQQCGVPAATIEEIARALAKAAPAAAveaswRAAFGCAH-QNSFDTARAVTAVNALLGSWGAKGGALltsspkag 376
Cdd:cd02765 318 PPKAAAEICGLEEAIIETLAEWYATGKPSGI-----WGFGGVDRyYHSHVFGRTAAILAALTGNIGRVGGGV-------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 377 didkqkfpsapkpeakrvgdkeyplapsgmgsnlavlqaaldGAMKGVFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDV 456
Cdd:cd02765 385 ------------------------------------------GQIKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVDI 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527669108 457 QMSETALASDYVLPECTYLE-RMELPEFIggKKHYVAMRTQVLEPIHpETKPCDEIFAGLAEACGVGEY 524
Cdd:cd02765 423 FHTPTVRYADIVLPAAHWFEvEDLLVRYT--THPHVLLQQKAIEPLF-ESKSDFEIEKGLAERLGLGDY 488
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
88-516 |
9.62e-43 |
|
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: 158.25 E-value: 9.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 88 CGRGHGVAQIAYSDERLTQPMRRAA---DGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAIVQdPRPSGKEYSK----R 160
Cdd:cd02750 51 CQRGASFSWYLYSPDRVKYPLKRVGargEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFS-PIPAMSMVSYaagsR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 161 FINVLGSANIytHGAACNSSKEAGFAQTIG--TGNF-SVDFGNSKMVVFIGrSYGDGIRPSSVQSLAAAADKGTRIVIVD 237
Cdd:cd02750 130 FASLIGGVSL--SFYDWYGDLPPGSPQTWGeqTDVPeSADWYNADYIIMWG-SNVPVTRTPDAHFLTEARYNGAKVVVVS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 238 PRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFV-EQNAVGFeefaaqaKEYTPAWAEQQCGVPAATIEEI 316
Cdd:cd02750 207 PDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLkEYTDLPF-------LVYTPAWQEAITGVPRETVIRL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 317 ARALAKAAPAAAVEaswraAFGCAHQ-NSFDTARAVTAVNALLGSWGAKGGalltsspkagdidkqkfpsapkpeakrvG 395
Cdd:cd02750 280 AREFATNGRSMIIV-----GAGINHWyHGDLCYRALILLLALTGNEGKNGG----------------------------G 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 396 DKEYplapsgmgsnlavlqaalDGAMKGVFFYNSNAVQGYAQPKVWREG--LEKTDLVVTIDVQMSETALASDYVLPECT 473
Cdd:cd02750 327 WAHY------------------VGQPRVLFVWRGNLFGSSGKGHEYFEDapEGKLDLIVDLDFRMDSTALYSDIVLPAAT 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2527669108 474 YLERMELPEFIGgkkH-YVAMRTQVLEPIHpETKPCDEIFAGLA 516
Cdd:cd02750 389 WYEKHDLSTTDM---HpFIHPFSPAVDPLW-EAKSDWEIFKALA 428
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
88-523 |
9.11e-42 |
|
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: 158.25 E-value: 9.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 88 CGRGHGVAQIAYSDERLTQPMRR---AADGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAI-----VQDPRPSGKEYSK 159
Cdd:cd02770 44 CLRGRSQRKRVYNPDRLKYPMKRvgkRGEGKFVRISWDEALDTIASELKRIIEKYGNEAIYVnygtgTYGGVPAGRGAIA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 160 RFINVLG----------SANI-----YTHGAAcnsskeagfaqtiGTGNFSVDFGNSKMVVFIG------RSYGDGirps 218
Cdd:cd02770 124 RLLNLTGgylnyygtysWAQIttatpYTYGAA-------------ASGSSLDDLKDSKLVVLFGhnpaetRMGGGG---- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 219 SVQSLAAAADKGTRIVIVDPRLNNSGI-FATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQNAVGF-----EEFAA 292
Cdd:cd02770 187 STYYYLQAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFdaehlPEGAP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 293 QAKEY--------------TPAWAEQQCGVPAATI----EEIARAlakaapaaaveaswRAAFGCA------HQNSFDTA 348
Cdd:cd02770 267 PNESYkdyvlgtgydgtpkTPEWASEITGVPAETIrrlaREIATT--------------KPAAILQgwgpqrHANGEQAA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 349 RAVTAVNALLGSWGAKGGAL-----LTSSPKAGdidkqkFPSAPKPEAKRVGDKEYPLA---PSGMGSNLAVLQAA--LD 418
Cdd:cd02770 333 RAIMMLAAMTGNVGIPGGNTgarpgGSAYNGAG------LPAGKNPVKTSIPCFMWTDAierGEEMTADDGGVKGAdkLK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 419 GAMKGVFFYNSNAVQGYAQP-----KVWREGLEKTDLVVTIDVQMSETALASDYVLPECTYLERMELPEF-IGGKKHYVA 492
Cdd:cd02770 407 SNIKMIWNYAGNTLINQHSDdnnttRALLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTsNAGMMEYLI 486
|
490 500 510
....*....|....*....|....*....|.
gi 2527669108 493 MRTQVLEPIHpETKPCDEIFAGLAEACGVGE 523
Cdd:cd02770 487 YSQKAIEPLY-ECKSDYEICAELAKRLGVED 516
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
51-476 |
2.24e-39 |
|
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: 151.78 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAA-DGSFEAIDWDTAFSEIG 129
Cdd:cd02752 2 TICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPgSGKWEEISWDEALDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 130 AKVKDI------------LAKNGPEALAIVQDPRPSGKE--YSKRFINVLGSANIYTHGAACNSSKEAGFAQTIGTG--- 192
Cdd:cd02752 82 RKMKDIrdasfveknaagVVVNRPDSIAFLGSAKLSNEEcyLIRKFARALGTNNLDHQARIUHSPTVAGLANTFGRGamt 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 193 NFSVDFGNSKMVVFIGRSYGDGiRPSSVQSLAAAADK-GTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIe 271
Cdd:cd02752 162 NSWNDIKNADVILVMGGNPAEA-HPVSFKWILEAKEKnGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYII- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 272 edlydhefveqnavgfeefaaqakEYTPAWAEQQCGVPAATIEEIARALAKAAPAAAVEASWRAAFGCAHQNSFDTARAV 351
Cdd:cd02752 240 ------------------------RYTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 352 TAVNALLGSWGAKGG---ALLTSSPKAGDIDkqkfpsapkpeakrvgdkeyplapsgmgsnLAVLQAALDGAMKGVffyn 428
Cdd:cd02752 296 CILQLLLGNIGVAGGgvnALRGHSNVQGATD------------------------------LGLLSHNLPGYLGGQ---- 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527669108 429 sNAVQGYAQPKVWREGLEKTDLVVTIDVQMSETALASD-------------YVLPECTYLE 476
Cdd:cd02752 342 -NPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYE 401
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
91-524 |
1.25e-36 |
|
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: 143.56 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 91 GHGVAQIAYSDERLTQPMRRAA--------------DGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAivqdprpsGKE 156
Cdd:cd02769 34 LDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrslrgKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIF--------GGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 157 YS--------------KRFINVLG----SANIYTHGAAcnsskeagfaQTIG---TGNFSVDFG----------NSKMVV 205
Cdd:cd02769 106 YGwssagrfhhaqsllHRFLNLAGgyvgSVGDYSTGAA----------QVILphvVGSMEVYTEqqtswpviaeHTELVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 206 FIGrsyGDGIRPSSVQS-----------LAAAADKGTRIVIVDP-RLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEED 273
Cdd:cd02769 176 AFG---ADPLKNAQIAWggipdhqaysyLKALKDRGIRFISISPlRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 274 LYDHEFVEQNAVGFEEFAA--------QAKeyTPAWAEQQCGVPAATIEEIarALAKAAPAAAVEASW---RAAFGcaHQ 342
Cdd:cd02769 253 LHDKAFLARYTVGFDKFLPyllgesdgVPK--TPEWAAAICGIPAETIREL--ARRFASKRTMIMAGWslqRAHHG--EQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 343 nsfdTARAVTAVNALLGSWGAKGG--ALLTSSPKAGDIDKQKFPSAPKPEAKRVGDKEYPLApsgmgsnlAVLQAALD-G 419
Cdd:cd02769 327 ----PHWMAVTLAAMLGQIGLPGGgfGFGYHYSNGGGPPRGAAPPPALPQGRNPVSSFIPVA--------RIADMLLNpG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 420 amkGVFFYNSnavQGYAQPKV----W---------------REGLEKTDLVVTIDVQMSETALASDYVLPECTYLERMEL 480
Cdd:cd02769 395 ---KPFDYNG---KKLTYPDIklvyWaggnpfhhhqdlnrlIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDI 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2527669108 481 pEFIGGKKHYVAMRtQVLEPIHpETKPCDEIFAGLAEACGVGEY 524
Cdd:cd02769 469 -GGSGDNRYIVAMK-QVVEPVG-EARDDYDIFADLAERLGVEEQ 509
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
88-523 |
1.26e-35 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 141.70 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 88 CGRGHGVAQIAYSDERLTQPMRRAA---DGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAI----------VQDPRPSG 154
Cdd:PRK14990 104 CLRGRSMRRRVYNPDRLKYPMKRVGargEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLnygtgtlggtMTRSWPPG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 155 KEYSKRFINVLGsANIYTHGAACNSSKEAGFAQTIG---TGNFSVDFGNSKMVVFIG------RSYGDGIRPSSVQslaA 225
Cdd:PRK14990 184 NTLVARLMNCCG-GYLNHYGDYSSAQIAEGLNYTYGgwaDGNSPSDIENSKLVVLFGnnpgetRMSGGGVTYYLEQ---A 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 226 AADKGTRIVIVDPRLNNSGIFATD-WVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQNAVGFEEFAAQA--------KE 296
Cdd:PRK14990 260 RQKSNARMIIIDPRYTDTGAGREDeWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEKTLPAsapknghyKA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 297 Y-----------TPAWAEQQCGVPAATIEEIaRALAKAAPAAAVEASWRAAfgcAHQNSFDTARAVTAVNALLGSWGAKG 365
Cdd:PRK14990 340 YilgegpdgvakTPEWASQITGVPADKIIKL-AREIGSTKPAFISQGWGPQ---RHANGEIATRAISMLAILTGNVGING 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 366 GallTSSPKAGD--IDKQKFPSAPKPEAKRVGDKEYPLAPSgMGSNLAVLQAA------LDGAMKGVFFYNSNA-VQGYA 436
Cdd:PRK14990 416 G---NSGAREGSysLPFVRMPTLENPIQTSISMFMWTDAIE-RGPEMTALRDGvrgkdkLDVPIKMIWNYAGNClINQHS 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 437 QPKVWREGLE---KTDLVVTIDVQMSETALASDYVLPECTYLERMELP-EFIGGKKHYVAMRTQVLEPiHPETKPCDEIF 512
Cdd:PRK14990 492 EINRTHEILQddkKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFAlDASCGNMSYVIFNDQVIKP-RFECKTIYEMT 570
|
490
....*....|.
gi 2527669108 513 AGLAEACGVGE 523
Cdd:PRK14990 571 SELAKRLGVEQ 581
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
103-518 |
3.04e-35 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 135.22 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 103 RLTQPMRRAADGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAIVQDPRP--SGKEY--SKRFINVLGSANIYTHGaaCN 178
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGGltDVESLyaLKKLLNRLGSKNGNTED--HN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 179 SSKEAGFAQTIGTGNFS--------VDFGNSKMVVFIGRSYGDGIRPSSVQSLAAAADKGTRIVIVDPRLNnsGIFATDW 250
Cdd:pfam00384 79 GDLCTAAAAAFGSDLRSnylfnssiADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLD--LTYADEH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 251 VSIKPGTDLAFLLGICNVLIEEDLYDhefveqnavgfeefaaqaKEYTPAwaeqqcgvpAATIeeiaralakaapaaave 330
Cdd:pfam00384 157 LGIKPGTDLALALAGAHVFIKELKKD------------------KDFAPK---------PIII----------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 331 ASWRAAFgcaHQNSFDTARAVTAVNALLGSWGAKGG--ALLTSSPKAgdidkqkfpsapkpeAKRVGDKEYPLAPSGMGS 408
Cdd:pfam00384 193 VGAGVLQ---RQDGEAIFRAIANLADLTGNIGRPGGgwNGLNILQGA---------------ASPVGALDLGLVPGIKSV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 409 NLAvlQAALDGAMKGVFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDVQM-SETALASDYVLPECTYLERMELpefiggk 487
Cdd:pfam00384 255 EMI--NAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGT------- 325
|
410 420 430
....*....|....*....|....*....|....*.
gi 2527669108 488 khYVAM--RTQVLEPIHP---ETKPCDEIFAGLAEA 518
Cdd:pfam00384 326 --YVNTegRVQSTKQAVPppgEAREDWKILRALSEV 359
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
103-470 |
2.10e-27 |
|
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: 115.87 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 103 RLTQPMR-RAADGSFEAIDWDTAFSEIGAKVKDILakngPEALAIVQDPRPSGKEY--SKRFINVLGSANIYTHGAACNS 179
Cdd:cd02767 64 RLTYPMRyDAGSDHYRPISWDEAFAEIAARLRALD----PDRAAFYTSGRASNEAAylYQLFARAYGTNNLPDCSNMCHE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 180 SKEAGFAQTIGTGNFSV---DFGNSKMVVFIGRSYGDGiRPSSVQSLAAAADKGTRIVIVDP-----------------R 239
Cdd:cd02767 140 PSSVGLKKSIGVGKGTVsleDFEHTDLIFFIGQNPGTN-HPRMLHYLREAKKRGGKIIVINPlrepglerfanpqnpesM 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 240 LNNSGIFATDWVSIKPGTDLAFLLGICNVLIEED-----LYDHEFVEQNAVGFEEFAAQAKEYTpaWA--EQQCGVPAAT 312
Cdd:cd02767 219 LTGGTKIADEYFQVRIGGDIALLNGMAKHLIERDdepgnVLDHDFIAEHTSGFEEYVAALRALS--WDeiERASGLSREE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 313 IEEIaralakaapAAAVEASWRAAFGCA-----HQNSFDTARAVtaVNALL--GSWGAKGGALltsSPKAGDIDKQKFPS 385
Cdd:cd02767 297 IEAF---------AAMYAKSERVVFVWGmgitqHAHGVDNVRAI--VNLALlrGNIGRPGAGL---MPIRGHSNVQGDRT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 386 A-----PKPEAKRVGDKEYPLAPS---GMgSNLAVLQAALDGAMKGVFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDVQ 457
Cdd:cd02767 363 MgitekPFPEFLDALEEVFGFTPPrdpGL-DTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATK 441
|
410
....*....|....*.
gi 2527669108 458 MSETAL---ASDYVLP 470
Cdd:cd02767 442 LNRSHLvhgEEALILP 457
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
51-500 |
3.32e-26 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 113.14 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFT-----LRGSDVHPyAKGTICGRGHGVAQIAYSDERLTQPMRRA-------ADGSFEA 118
Cdd:cd02760 2 TYCYNCVAGPDFMAVKVVDGVATeiepnFAAEDIHP-ARGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkkgrnEDPGFVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 119 IDWDTAFSEIGAKV-----KDILAKNG-PEALAIVQDPRPSGKEYSK--RFINVLGSANIYT---HGAACNSSK--EAGF 185
Cdd:cd02760 81 ISWDEALDLVAAKLrrvreKGLLDEKGlPRLAATFGHGGTPAMYMGTfpAFLAAWGPIDFSFgsgQGVKCVHSEhlYGEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 186 AQTigtgNFSV--DFGNSKMVVFIGRSYGDGIRPSSVQSLAAAADKGTRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLL 263
Cdd:cd02760 161 WHR----AFTVaaDTPLANYVISFGSNVEASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 264 GICNVLIEE---DLYDHEFVE---------------------------------------QNAV---------------- 285
Cdd:cd02760 237 AMIHVMVHEqglGKLDVPFLRdrtsspylvgpdglylrdaatgkplvwdersgravpfdtRGAVpavagdfavdgavsvd 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 286 ---------------GFEEFAAQAKEYTPAWAEQQCGVPAATIEEIARALAKAAPAAAVEA------SWRAAFGCA---- 340
Cdd:cd02760 317 addetaihqgvegttAFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFLENASIGSTIEvdgvtlPYRPVAVTLgksv 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 341 --HQNSFDTARAVTAVNALLGSWGAKGGALLTS------------SPKAGD----------IDKQKFPSAPKPEAKR--- 393
Cdd:cd02760 397 nnGWGAFECCWARTLLATLVGALEVPGGTLGTTvrlnrphddrlaSVKPGEdgfmaqgfnpTDKEHWVVKPTGRNAHrtl 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 394 ---VGDKEYPLApsgMG-SNLAVL---QAALDGAMKG------VFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDVQMSE 460
Cdd:cd02760 477 vpiVGNSAWSQA---LGpTQLAWMflrEVPLDWKFELptlpdvWFNYRTNPAISFWDTATLVDNIAKFPFTVSFAYTEDE 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2527669108 461 TALASDYVLPECTYLERMELPEFIGGK------KHY-VAMRTQVLEP 500
Cdd:cd02760 554 TNWMADVLLPEATDLESLQMIKVGGTKfveqfwEHRgVVLRQPAVEP 600
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
51-501 |
1.26e-24 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 107.19 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGcSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRAADGSFEAIDWDTAfseiGA 130
Cdd:cd02764 48 SLVPA-GEGQGVLVKTVDGRPIKIEGNPDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGIDGAYVASDWADF----DA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 131 KVKDILAKN-GPEALAIVQDP--RPSGKEYSKRFINVLGSANIYTHGAacNSSKEAGFAQTIGTGNFSV---DFGNSKMV 204
Cdd:cd02764 123 KVAEQLKAVkDGGKLAVLSGNvnSPTTEALIGDFLKKYPGAKHVVYDP--LSAEDVNEAWQASFGKDVVpgyDFDKAEVI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 205 VFIGRSY-GDGIRPSSVQSLAAAADKG------TRIVIVDPRLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEEDlydh 277
Cdd:cd02764 201 VSIDADFlGSWISAIRHRHDFAAKRRLgaeepmSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKG---- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 278 efveQNAVGFEEFAAQAKEYTPAWAEQQCGVPAATIEEIARALAKAAPAAAVEASWRAAFGCAhqnsfDTARAVTAVNAL 357
Cdd:cd02764 277 ----AGSSLPDFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAGKSLVVAGSELSQTAGA-----DTQVAVNALNSL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 358 LGSWGAkggALLTSSPKAGDidkqkfpsapkpeakrvgdkeyplaPSGMGSNLAVLQAAL-DGAMKGVFFYNSNAVqgYA 436
Cdd:cd02764 348 LGNDGK---TVDHARPIKGG-------------------------ELGNQQDLKALASRInAGKVSALLVYDVNPV--YD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 437 QPKVWR--EGLEKTDLVVTIDVQMSETALASDYVLPECTYLER---MELPEfiggkKHYvAMRTQVLEPI 501
Cdd:cd02764 398 LPQGLGfaKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESwgdAETPD-----GTY-SICQPVIAPL 461
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
51-471 |
5.29e-21 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 96.99 E-value: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVA--TTLGGQLFTLRGSDVHPYA--------------------------KGTICGRGHGVAQIAYSDE 102
Cdd:PRK14991 77 TQCLGCWTQCGVRVrvDNATNKILRIAGNPYHPLStdhhidmstpvkeafeslsgesglegRSTACARGNAMLEQLDSPY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 103 RLTQPMRRAA---DG-----SFE----------------------AI-DWDT----AFSEIGAKVKDILAKN-GPEAlai 146
Cdd:PRK14991 157 RVLQPLKRVGkrgSGkwqriSFEqlveevveggdlfgeghvdglrAIrDLDTpidaKNPEYGPKANQLLVTNaSDEG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 147 vQDPrpsgkeYSKRFI-NVLGSANIYTHGAACnsskeaGFAQTIGTGNF----------SVDFGNSKMVVFIGRSYGDGI 215
Cdd:PRK14991 234 -RDA------FIKRFAfNSFGTRNFGNHGSYC------GLAYRAGSGALmgdldknphvKPDWDNVEFALFIGTSPAQSG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 216 RPSSVQS--LAAAADKGT-RIVIVDPRLNNSGIFATD----WVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQ------ 282
Cdd:PRK14991 301 NPFKRQArqLANARTRGNfEYVVVAPALPLSSSLAAGdnnrWLPIRPGTDSALAMGMIRWIIDNQRYNADYLAQpgvaam 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 283 ---------NAV-------------------------------------------------------------------- 285
Cdd:PRK14991 381 qaageaswtNAThlviadpghprygqflrasdlglpfegeargdgedtlvvdaadgelvpatqaqparlfveqyvtladg 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 286 -------GFEEFAAQAKEYTPAWAEQQCGVPAATIEEIARALAKAAPaaaveaswRAAF----GCAHQNSFDTARAVTAV 354
Cdd:PRK14991 461 qrvrvksSLQLLKEAARKLSLAEYSEQCGVPEAQIIALAEEFTSHGR--------KAAVishgGTMSGNGFYNAWAIMML 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 355 NALLGSWGAKGGALLTSS--PKAGD---IDKQKFPSAPKP----------------EAKR---VGDKEYPL------APS 404
Cdd:PRK14991 533 NALIGNLNLKGGVVVGGGkfPGFGDgprYNLASFAGKVKPkgvslsrskfpyekssEYRRkveAGQSPYPAkapwypFVA 612
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527669108 405 GMGSNLavLQAALDG---AMKGVFFYNSNAVqgYAQPKvWREGLE-------KTDLVVTIDVQMSETALASDYVLPE 471
Cdd:PRK14991 613 GLLTEM--LTAALEGypyPLKAWINHMSNPI--YGVPG-LRAVIEeklkdpkKLPLFISIDAFINETTALADYIVPD 684
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
93-520 |
4.45e-16 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 81.64 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 93 GVAQIAYSDERLTQPMRRA--------------ADGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAIVQ-DPRPSGKEY 157
Cdd:PRK15102 80 GIKGHVYNPSRIRYPMVRLdwlrkrhksdtsqrGDNRFVRVSWDEALDLFYEELERVQKTYGPSALHTGQtGWQSTGQFH 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 158 S-----KRFI----NVLGSANIYTHGAAcnsskeagfaQTI-------------GTgNFSVDFGNSKMVVFIGrsyGDGI 215
Cdd:PRK15102 160 SatghmQRAIgmhgNSVGTVGDYSTGAG----------QVIlpyvlgstevyeqGT-SWPLILENSKTIVLWG---SDPV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 216 RPSSV--------------QSLAAAADKGTRIVIVDPRLNNSGIF-ATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFV 280
Cdd:PRK15102 226 KNLQVgwncethesyaylaQLKEKVAKGEINVISIDPVVTKTQNYlGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 281 EQNAVGFEEFA--------AQAKeyTPAWAEQQCGVPAATIEEIARALAKAAPaaaveaswRAAFGCA-----HQNSFDT 347
Cdd:PRK15102 306 DNYCLGFEQFLpyllgekdGVPK--TPEWAEKICGIDAETIRELARQMAKGRT--------QIIAGWCiqrqqHGEQPYW 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 348 ARAVTAvnALLGSWGAKGGALLTSspkagdidkQKFPSAPKPEAKRVgdkeyplAPSGMGSNLAVLQAALdgamkgvffY 427
Cdd:PRK15102 376 MGAVLA--AMLGQIGLPGGGISYG---------HHYSGIGVPSSGGA-------IPGGFPGNLDTGQKPK---------H 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 428 NSNAVQGYA-------------QP---------KV---------------W---------REGLEKTDLVVTIDVQMSET 461
Cdd:PRK15102 429 DNSDYKGYSstipvarfidailEPgktinwngkKVtlpplkmmifsgtnpWhrhqdrnrmKEAFRKLETVVAIDNQWTAT 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527669108 462 ALASDYVLPECTYLERMELPEFiG--GKKHYVAMRtQVLEPIHpETKPCDEIFAGLAEACG 520
Cdd:PRK15102 509 CRFADIVLPACTQFERNDIDQY-GsySNRGIIAMK-KVVEPLF-ESRSDFDIFRELCRRFG 566
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
103-470 |
1.66e-15 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 79.70 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 103 RLTQPMR-RAADGSFEAIDWDTAFSEIGAKVKdilAKNGPEALAIVQDPRPSGKE--YSKRFINVLGSANIYTHGAACNS 179
Cdd:PRK09939 108 RLTQPLKyDAVSDCYKPLSWQQAFDEIGARLQ---SYSDPNQVEFYTSGRTSNEAafLYQLFAREYGSNNFPDCSNMCHE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 180 SKEAGFAQTIGTGNFSV---DFGNSKMVVFIGRSYGDGiRPSSVQSLAAAADKGTRIVIVDP------------------ 238
Cdd:PRK09939 185 PTSVGLAASIGVGKGTVlleDFEKCDLVICIGHNPGTN-HPRMLTSLRALVKRGAKMIAINPlqerglerftapqnpfem 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 239 RLNNSGIFATDWVSIKPGTDLAFLLGICNVLIEED----------LYDHEFVEQNAVGFEEFAAQAKEYTPAWAEQQCGV 308
Cdd:PRK09939 264 LTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 309 PAATIEEIARALAKAAPAAaveaswrAAFGCA-HQNSFDTARAVTAVNALL--GSWGAKGGALLTSSPKAGDIDKQKFPS 385
Cdd:PRK09939 344 SQTQIAELADAYAAAERTI-------ICYGMGiTQHEHGTQNVQQLVNLLLmkGNIGKPGAGICPLRGHSNVQGDRTVGI 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 386 APKPEAK---RVGDKeYPLAPSGMGSNLAV--LQAALDGAMKGVFFYNSNAVQGYAQPKVWREGLEKTDLVVTIDVQMSE 460
Cdd:PRK09939 417 TEKPSAEflaRLGER-YGFTPPHAPGHAAIasMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNR 495
|
410
....*....|...
gi 2527669108 461 TALAS---DYVLP 470
Cdd:PRK09939 496 SHLLTarhSYILP 508
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
4-315 |
1.21e-14 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 76.86 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 4 SVTRRTFLKGSAATAALAATGAGVCSLGAWQAEAAHAEGSYERkegaSLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYA 83
Cdd:PRK13532 2 KLSRRDFMKANAAAAAAAAAGLSLPAVANAVVGSAQTAIKWDK----APCRFCGTGCGVLVGTKDGRVVATQGDPDAPVN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 84 KGTICGRGHGVAQIAYSDERLTQPMRR------AADGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAIV---QDPRPSG 154
Cdd:PRK13532 78 RGLNCIKGYFLSKIMYGKDRLTQPLLRmkdgkyDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFgsgQWTIWEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 155 KEYSKRFINVLGSANIYTHGAACNSSKEAGFAQTIG----TGNFSvDFGNSKMVVFIGrsygdgirpssvqslAAAADKG 230
Cdd:PRK13532 158 YAASKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGidepMGCYD-DIEAADAFVLWG---------------SNMAEMH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 231 ----TRivIVDPRLNNSGI--------------FATDWVSIKPGTDLAFLLGICNVLIEEDLYDHEFVEQNAV------- 285
Cdd:PRK13532 222 pilwSR--VTDRRLSNPDVkvavlstfehrsfeLADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNKHTNfrkgatd 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2527669108 286 ---------------------------GFEEFAAQAKEYTPAWAEQQCGVPAATIEE 315
Cdd:PRK13532 300 igyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQ 356
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
99-238 |
1.28e-08 |
|
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: 56.98 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 99 YSDERLTQPMRRaADGSFEAIDWDTAFSEIGAKVKDILAKNGPEALAIVQDPRPSGKEYS--KRFINVLGSANIYTHGAA 176
Cdd:cd02772 50 NSEDRLTKPMIK-KDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYllQKLARGLGSDNIDHRLRQ 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527669108 177 CNSSKEAGFAQTIGTGNFSVDFGNSKMVVFIGRSygdgIR---PSSVQSLAAAADKGTRIVIVDP 238
Cdd:cd02772 129 SDFRDDAKASGAPWLGMPIAEISELDRVLVIGSN----LRkehPLLAQRLRQAVKKGAKLSAINP 189
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
51-100 |
1.49e-08 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 51.10 E-value: 1.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYS 100
Cdd:smart00926 6 TVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
81-314 |
2.06e-07 |
|
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: 53.64 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 81 PYAKGTICGRGHGVAQIAYS------DERLTQPMRRAAdGSFEAIDWDTAFSEIGAKVKDILAKNGPE--ALAIVQDPRP 152
Cdd:cd02756 89 PVNSGNYSTRGGTNAERIWSpdnrvgETRLTTPLVRRG-GQLQPTTWDDAIDLVARVIKGILDKDGNDdaVFASRFDHGG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 153 SGKEY------SKRFINVLGSANIYTH-----GAACNSSKEAGfaqtIGTGNFS-VDFGNSKMVVFIG-RSYG------- 212
Cdd:cd02756 168 GGGGFennwgvGKFFFMALQTPFVRIHnrpayNSEVHATREMG----VGELNNSyEDARLADTIVLWGnNPYEtqtvyfl 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 213 ----DGIRPSSVQSLAAAADKG-----TRIVIVDPRLNNS-----GIFATDWV---SIKPGTDLAFLLGICNVLIEedly 275
Cdd:cd02756 244 nhwlPNLRGATVSEKQQWFPPGepvppGRIIVVDPRRTETvhaaeAAAGKDRVlhlQVNPGTDTALANAIARYIYE---- 319
|
250 260 270
....*....|....*....|....*....|....*....
gi 2527669108 276 dhefveqnavGFEEFAAQAKEYTpawaeqqcGVPAATIE 314
Cdd:cd02756 320 ----------SLDEVLAEAEQIT--------GVPRAQIE 340
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
51-100 |
1.17e-05 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 42.67 E-value: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYS 100
Cdd:pfam04879 6 TICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| 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 ... |
51-170 |
2.68e-05 |
|
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: 46.61 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527669108 51 SLCNGCSSKCGLVATTLGGQLFTLRGSDVHPYAKGTICGRGHGVAQIAYSDERLTQPMRRaADGSFEAIDWDTAFSeiga 130
Cdd:cd02771 2 SICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR-RGGTLVPVSWNEALD---- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2527669108 131 KVKDILAKNGPEALAIVQdPRPSGKE---YSKRFINVLGSANI 170
Cdd:cd02771 77 VAAARLKEAKDKVGGIGS-PRASNESnyaLQKLVGAVLGTNNV 118
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
99-170 |
1.25e-04 |
|
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: 44.20 E-value: 1.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527669108 99 YSDERLTQPMRRAaDGSFEAIDWDTAFseigAKVKDILAKNGPEALAIVQDPRPSGKE--YSKRFINVLGSANI 170
Cdd:cd02768 50 NSRQRLTQPLIKK-GGKLVPVSWEEAL----KTVAEGLKAVKGDKIGGIAGPRADLESlfLLKKLLNKLGSNNI 118
|
|
| |
