|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
47-585 |
0e+00 |
|
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: 641.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 47 VPTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRV---GEGQFQPISWEQAF 123
Cdd:cd02755 1 VPSICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVgerGEGKFREASWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 124 QEIGSKLKELKEQYGPQSLVWLAHPELISPLEKHFMAAFGSPNYTGHGPTCYSSRNVAFEQMY---GGVPGVDYRNVRYY 200
Cdd:cd02755 81 QYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHESTCLASKNLAWKLVIdsfGGEVNPDFENARYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 201 IAFGRNLTGGIKNPDVQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAAYT 280
Cdd:cd02755 161 ILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFVEKYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 281 TGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAVDPGWHAVTgsqYGNSVQAGRAIAALNALLGNLGAR 360
Cdd:cd02755 241 NGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGTF---YSNSFQTRRAIAIINALLGNIDKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 361 GGLSLPPTIKlgspagimgpkppaataprwdgagsekwplnkdhgmiqtfpervkqdqPYPVKAVIIQHLNPVRSSTDSL 440
Cdd:cd02755 318 GGLYYAGSAK------------------------------------------------PYPIKALFIYRTNPFHSMPDRA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 441 AFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLMTVG---NKVLLRQPAIKPLFDNKGAEEIIAGIGRAAG 517
Cdd:cd02755 350 RLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGgpaPAVATRQRAIEPLYDTRPGWDILKELARRLG 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101271798 518 LseyfnftleqyndallgplgltqaqlartgvaeveaskpdyskLKTPSGKIELACPAFVKAGSTLTP 585
Cdd:cd02755 430 L-------------------------------------------FGTPSGKIELYSPILAKAGYDPLP 454
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-722 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 621.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 43 ETRVVPTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRV---GEGQFQPISW 119
Cdd:COG0243 20 GTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVgprGSGKFERISW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 120 EQAFQEIGSKLKELKEQYGPQSLVW--------LAHPElISPLEKHFMAAFGSPNYTGHGPTCYSSRNVAFEQMYG-GVP 190
Cdd:COG0243 100 DEALDLIAEKLKAIIDEYGPEAVAFytsggsagRLSNE-AAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGsDKG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 191 GV---DYRNVRYYIAFGRNL--TGGIKNPDVQKivAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVL 265
Cdd:COG0243 179 TVsyeDLEHADLIVLWGSNPaeNHPRLLRRLRE--AAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 266 INENLYDAAFVAAYTTGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAVdPGWHAvtgSQYGNSVQAGR 345
Cdd:COG0243 257 IEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVIL-WGMGL---QQHSNGTQTVR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 346 AIAALNALLGNLGARGGLSLPPTiklgspagimgpkppaataprwdgagsekwplnkdhgmiqtfPERVKQDQPYPVKAV 425
Cdd:COG0243 333 AIANLALLTGNIGKPGGGPFSLT------------------------------------------GEAILDGKPYPIKAL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 426 IIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLMTVG-NKVLLRQPAIKPLFDNKG 504
Cdd:COG0243 371 WVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 505 AEEIIAGIGRAAGLSEYFNF--TLEQYNDALL---GPLGLTQAQLARTGVAEVEASKPDY----SKLKTPSGKIELACPA 575
Cdd:COG0243 451 DWEIFAELAKRLGFEEAFPWgrTEEDYLRELLeatRGRGITFEELREKGPVQLPVPPEPAfrndGPFPTPSGKAEFYSET 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 576 FVKAGstlTPAWEPPL--VEPPDDS--FRLIQGHVPMHTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVAS 651
Cdd:COG0243 531 LALPP---LPRYAPPYegAEPLDAEypLRLITGRSRDQWHSTTYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVES 607
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101271798 652 KVGKVRVKARVTEAIHPEAVFLAHGFGcrvplRHLAYNRGANGGDLIPIMTAPVSGAAAQCETLVTVRKAG 722
Cdd:COG0243 608 DRGEVLARAKVTEGIRPGVVFAPHGWW-----YEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKAA 673
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
4-721 |
0e+00 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 598.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 4 QKITRRAFLKGSLAAGALATFG----GKLIPIEPAKAAAagqaETRVVPTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDP 79
Cdd:PRK15488 1 MSLSRRDFLKGAGAGCAACALGsllpGALAANEIAQLKG----KTKLTPSICEMCSTRCPIEARVVNGKNVFIQGNPKAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 80 QSGGRLCARGNAGTKTLYDPDRLKGPMKRVG---EGQFQPISWEQAFQEIGSKLKELKEQYGPQSLVWLAHPELISPLEK 156
Cdd:PRK15488 77 SFGTKVCARGGSGHSLLYDPQRIVKPLKRVGergEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSGSLSSHLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 157 HFMAAFGSPNYTGHGPTCYSSRNVAFEQMYGGVPGVDYRNVRYYIAFGRNLTGGIKNPDVQKIVAAKAE-GAHLVAVDPR 235
Cdd:PRK15488 157 HLATAFGSPNTFTHASTCPAGYAIAAKVMFGGKLKRDLANSKYIINFGHNLYEGINMSDTRGLMTAQMEkGAKLVVFEPR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 236 LSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAAYTTGFEELKKGVSGYTPAWAAGITGIEAGTISRIARE 315
Cdd:PRK15488 237 FSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 316 LAAAKPAAAVDPGwHAVTGSQygNSVQAGRAIAALNALLGNLGARGGL---------------SLPPTIKLGSPAGImgP 380
Cdd:PRK15488 317 LAAAAPHAIVDFG-HRATFTP--EEFDMRRAIFAANVLLGNIERKGGLyfgknasvynklageKVAPTLAKPGVKGM--P 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 381 KPpaaTAPRWDGAGSEKWPLNKDHGMIQTFPERVKQDQPYPVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMN 460
Cdd:PRK15488 392 KP---TAKRIDLVGEQFKYIAAGGGVVQSIIDATLTQKPYQIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 461 DTAYYAHYILPEATYLERYDPLMTVGNKV---LLRQPAIKPLFDNKGAEEIIAGIGRAAGLSEYFNF----TLEQY---- 529
Cdd:PRK15488 469 ESAAYADVVLPESTYLERDEEISDKSGKNpayALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYYPWqdmeTLQLYqvng 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 530 NDALLG------------PLGLTQAQLARTGVAEVEASKP--------DYSKLKTPSGKIELACPAFVKAGSTL-TPAWE 588
Cdd:PRK15488 549 DHALLKelkkkgyvsfgvPLLLREPKMVAKFVARYPNAKAvdedgtygSQLKFKTPSGKIELFSAKLEALAPGYgVPRYR 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 589 PPLVEPPDDSFrLIQGHVPMHTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHP 668
Cdd:PRK15488 629 DVALKKEDELY-FIQGKVAVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRP 707
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1101271798 669 EAVFLAHGFGCRVPLRHLAYNRGANGGDLIPIMTAPVSGAAAQcETLVTVRKA 721
Cdd:PRK15488 708 DTLFAYMGFGSKNKELTRATGKGIHCGNLLPHVTSPVSGTNVH-TTGVTLSKA 759
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
48-590 |
1.06e-113 |
|
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: 351.61 E-value: 1.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRV---GEGQFQPISWEQAFQ 124
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgerGENKWERISWDEALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 125 EIGSKLKELKEQYGPQSLV----------WLAHPELISplekhFMAAFGSPNYTGHGPTCYSSRNVA--FEQMYGGVPGV 192
Cdd:cd02759 81 EIAEKLAEIKAEYGPESIAtavgtgrgtmWQDSLFWIR-----FVRLFGSPNLFLSGESCYWPRDMAhaLTTGFGLGYDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 193 -DYRNVRYYIAFGRNLTggIKNPDVQ--KIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINEN 269
Cdd:cd02759 156 pDWENPECIVLWGKNPL--NSNLDLQghWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 270 LYDAAFVAAYTTGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKpaaavdPGWHAVTGS--QYGNSVQAGRAI 347
Cdd:cd02759 234 LYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAK------PACIQWGLAidQQKNGTQTSRAI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 348 AALNALLGNLGARGGLSLpptiklgspagimgpkppaataprwdgagsekwplnkdhgmiqtfpervkqdQPYPVKAVII 427
Cdd:cd02759 308 AILRAITGNLDVPGGNLL----------------------------------------------------IPYPVKMLIV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 428 QHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERyDPLMT---VGNKVLLRQPAIKPLFDNKG 504
Cdd:cd02759 336 FGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLER-PGLRGgfeAENFVQLRQKAVEPYGEAKS 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 505 AEEIIAGIGRAAGLSEyfnFTLEQYNDALLGPLGltqaqlaRTGVAeveaskpdysklkTPSGKIELACPAFVKAGSTLT 584
Cdd:cd02759 415 DYEIVLELGKRLGPEE---AEYYKYEKGLLRPDG-------QPGFN-------------TPTGKVELYSTMLEELGYDPL 471
|
....*.
gi 1101271798 585 PAWEPP 590
Cdd:cd02759 472 PYYREP 477
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
44-678 |
1.47e-107 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 342.25 E-value: 1.47e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 44 TRVVPTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVGeGQFQPISWEQAF 123
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRG-GEFREVSWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 124 QEIGSKLKELKEQYGPQSLVWLAHPELisPLEKHFM------AAFGSPNYTGHGPTCYSSRNVAFEQMYG-GVPGVDYRN 196
Cdd:COG3383 83 DLVAERLREIQAEHGPDAVAFYGSGQL--TNEENYLlqklarGVLGTNNIDNNARLCMASAVAGLKQSFGsDAPPNSYDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 197 V---RYYIAFGRNLTGGikNPDV-QKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYD 272
Cdd:COG3383 161 IeeaDVILVIGSNPAEA--HPVLaRRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 273 AAFVAAYTTGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAvdpgWHAVTGSQYGNSVQAGRAIAALNA 352
Cdd:COG3383 239 EDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMI----LWGMGVNQHTQGTDNVNAIINLAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 353 LLGNLGARGGLSLPPTiklGSP----AGIMGPKPPAATAPRW--DGAGSEK----W---PLNKDHGMiqTFPERVKQDQP 419
Cdd:COG3383 315 ATGNIGRPGTGPFPLT---GQNnvqgGRDMGALPNVLPGYRDvtDPEHRAKvadaWgvpPLPDKPGL--TAVEMFDAIAD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 420 YPVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERyDPLMTvgN---KVLLRQPAI 496
Cdd:COG3383 390 GEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEK-DGTFT--NterRVQRVRKAV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 497 KPLFDNKGAEEIIAGIGRAAGlseyFNFTleqYND--------ALLGPL--GLTQAQLARTG-----VAEVEASKPDY-- 559
Cdd:COG3383 467 EPPGEARPDWEIIAELARRLG----YGFD---YDSpeevfdeiARLTPDysGISYERLEALGgvqwpCPSEDHPGTPRlf 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 560 -SKLKTPSGKielacpafvkagSTLTPAWEPPLVEPPDDS--FRLIQGHVPMHTHT--TTDNNSYLHAIMPENELWIHTS 634
Cdd:COG3383 540 tGRFPTPDGK------------ARFVPVEYRPPAELPDEEypLVLTTGRLLDQWHTgtRTRRSPRLNKHAPEPFVEIHPE 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1101271798 635 RAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFG 678
Cdd:COG3383 608 DAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMPFHWG 651
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
48-515 |
4.47e-102 |
|
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: 317.73 E-value: 4.47e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVGE-GQFQPISWEQAFQEI 126
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGrGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 127 GSKLKELKEQYGPQSLVWLA---HPELISPLEKHFMAAFGSPNYTGHGPTCYSSRNVAFEQMYGGVPGV---DYRNVRYY 200
Cdd:cd00368 81 AEKLKEIREKYGPDAIAFYGgggASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNtlaDIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 201 IAFGRNLTGGIkNPDVQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAminvlinenlydaafvaayt 280
Cdd:cd00368 161 LLWGSNPAETH-PVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA-------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 281 tgfeelkkgvsgytpAWAAGITGIEAGTISRIARELAAAKPAAAVdpGWHAVTgsQYGNSVQAGRAIAALNALLGNLGAR 360
Cdd:cd00368 220 ---------------EWAAEITGVPAETIRALAREFAAAKRAVIL--WGMGLT--QHTNGTQNVRAIANLAALTGNIGRP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 361 GGLSLPptiklgspagimgpkppaataprwdGAgsekwplnkdhgmiqtfpervkqdqpypvkaviiqhlNPVRSSTDSL 440
Cdd:cd00368 281 GGGLGP-------------------------GG-------------------------------------NPLVSAPDAN 298
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1101271798 441 AFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLMTVGNKVLLRQPAIKPLFDNKGAEEIIAGIGRA 515
Cdd:cd00368 299 RVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKR 373
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
49-674 |
2.30e-98 |
|
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: 317.87 E-value: 2.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 49 TLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVGeGQFQPISWEQAFQEIGS 128
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREG-DKFREVSWDEAISYIAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 129 KLKELKEQYGPQSLVWLAHP----ELISPLEKHFMAAFGSPNYTGHGPTCYSSRNVAFEQMYG-GVPGVDYR---NVRYY 200
Cdd:TIGR01591 80 KLKEIKEKYGPDSIGFIGSSrgtnEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGiGAMSNTISeieNADLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 201 IAFGRNLTGGikNPDV-QKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAAY 279
Cdd:TIGR01591 160 VIIGYNPAES--HPVVaQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFIEKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 280 TTGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAVdpgWH-AVTgsQYGNSVQAGRAIAALNALLGNLG 358
Cdd:TIGR01591 238 TEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAIL---WGmGVT--QHSQGVETVMALINLAMLTGNIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 359 ARGGLSLP---PTIKLGspAGIMG--PKPPAATAPRWDGAGSEK----W---PLNKDHGM-IQTFPERVKQDQpypVKAV 425
Cdd:TIGR01591 313 KPGGGVNPlrgQNNVQG--ACDMGalPDFLPGYQPVSDEEVREKfakaWgvvKLPAEPGLrIPEMIDAAADGD---VKAL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 426 IIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLMTVGNKVLLRQPAIKPLFDNKGA 505
Cdd:TIGR01591 388 YIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 506 EEIIAGIGRAAGLSEYFNFTLEQYND-ALLGPL--GLTQAQLARTGVAE--VEASKPDYS------KLKTPSGKielacp 574
Cdd:TIGR01591 468 WEIIQELANALGLDWNYNHPQEIMDEiRELTPLfaGLTYERLDELGSLQwpCNDSDASPTsylykdKFATPDGK------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 575 afvkaGSTLTPAWEPPLVEPPDDS-FRLIQGHVPMHTHT--TTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVAS 651
Cdd:TIGR01591 542 -----AKFIPLEWVAPIEEPDDEYpLILTTGRVLTHYNVgeMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKS 616
|
650 660
....*....|....*....|...
gi 1101271798 652 KVGKVRVKARVTEAIHPEAVFLA 674
Cdd:TIGR01591 617 RRGEITLRAKVSDRVNKGAIYIT 639
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
47-570 |
1.49e-97 |
|
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: 310.91 E-value: 1.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 47 VPTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVG-------EGQFQPISW 119
Cdd:cd02757 2 VPSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNprkgrdvDPKFVPISW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 120 EQAFQEIGSKLKELKEQYGPQS-LVWLAHPELISPLE-KHFMAAFGSPNYTGHGPTCYSSRNVAFEQMYGG--VPGVDYR 195
Cdd:cd02757 82 DEALDTIADKIRALRKENEPHKiMLHRGRYGHNNSILyGRFTKMIGSPNNISHSSVCAESEKFGRYYTEGGwdYNSYDYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 196 NVRYYIAFGRN-LTGGIKNPDVQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAA 274
Cdd:cd02757 162 NAKYILFFGADpLESNRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 275 FVAAYTTGFEELKKGVSG-----------------------YTPAWAAGITGIEAGTISRIARELAAAKPAaavdpgwhA 331
Cdd:cd02757 242 FVGDFVDGKNYFKAGETVdeesfkeksteglvkwwnlelkdYTPEWAAKISGIPAETIERVAREFATAAPA--------A 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 332 VTGSQYGNSVQ-----AGRAIAALNALLGNLGARGGLSlpptiklgspagimgpkppaatAPRWDGAgsekwplnkdhgm 406
Cdd:cd02757 314 AAFTWRGATMQnrgsyNSMACHALNGLVGSIDSKGGLC----------------------PNMGVPK------------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 407 IQTFPERVKqdqpypvkaviiqhlNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLMTVG 486
Cdd:cd02757 359 IKVYFTYLD---------------NPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQEN 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 487 N---KVLLRQPAIKPLFDNKGAEEIIAGIGR---AAGLSEYFNFTLEQYNDALLGplgltqaqlaRTGVAEVEaskpdyS 560
Cdd:cd02757 424 NlhpWLSIRQPVVKSLGEVREETEILIELAKkldPKGSDGMKRYAPGQFKDPETG----------KNNRWEFE------N 487
|
570
....*....|
gi 1101271798 561 KLKTPSGKIE 570
Cdd:cd02757 488 VFPTETGKFE 497
|
|
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
6-721 |
2.77e-97 |
|
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.
Pssm-ID: 274006 [Multi-domain] Cd Length: 797 Bit Score: 318.25 E-value: 2.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 6 ITRRAFLKGSLAAGALATFGGkLIPIEPAKAAAAGQAETR----VVPTLCEM-CGVKCGVLAHVRDGRVWRL-TGNPRDP 79
Cdd:TIGR02166 1 ISRRHFLKTSAALGGLAAASG-ALSLPFSVNAAAEATPTGpdekVVWSACTVnCGSRCPLRVHVKDGEITRIeTDNTGDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 80 QSGG---RLCARGNAGTKTLYDPDRLKGPMKRV---GEGQFQPISWEQAFQEIGSKLKELKEQYGPQSLVW--------- 144
Cdd:TIGR02166 80 EYGNhqvRACLRGRSMRRRVYNPDRLKYPMKRVgkrGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVnygtgttgg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 145 LAHPELISPLEKHFMAAF-GSPNYTGHgptcYSSRNV--AFEQMYG----GVPGVDYRNVRYYIAFGRNLT------GGI 211
Cdd:TIGR02166 160 TMSRSWPPTAVARLLNLCgGYLNQYGS----YSTAQIneAMPYTYGisadGSSLDDIENSKLVVMFGNNPAetrmsgGGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 212 KNPDVQkivAAKAEGAHLVAVDPRLSD-FAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAAYTTGFEE----- 285
Cdd:TIGR02166 236 TYYFLQ---ALEKSNARVIVIDPRYTDtVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEktlpa 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 286 ------------LKKGVSGY--TPAWAAGITGIEAGTISRIARELAAAKPAAAVDpGWhavtGSQ-YGNSVQAGRAIAAL 350
Cdd:TIGR02166 313 sapkngsykdyiLGEGADGTpkTPEWASKITGIPADTIIKLAREIGNAKPAFISQ-GW----GPQrHANGEQAARAIMML 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 351 NALLGNLGARGGLS--LPPTIKLGSPAGIMGPKPPAATAP--RWDGA---GSEKWPLnKDHgmiqtfpERVKQDQPYPVK 423
Cdd:TIGR02166 388 ALLTGNVGIKGGNNgaREGNYSLPFARMPELPNPVKTSIScfLWTDAidrGTEMTAI-KDG-------VRGKDKLDSNIK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 424 AV--------IIQHLNPVRSSTdslaFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLMTVGNK----VLL 491
Cdd:TIGR02166 460 FLwnyagnclINQHSDINRTHK----ILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASnmsyLIF 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 492 RQPAIKPLFDNKGAEEIIAGI------------GR--AAGLSEYFNFTLEqyNDALLGPL------GLTQAQLARTGVAE 551
Cdd:TIGR02166 536 MQKAIEPLFECKPIYDMLSEVakrlgveaefteGRtqEEWLEHLYAQTRA--ADPALPSFaelrkqGIYKAKSAPGPFVA 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 552 VEASK--PDYSKLKTPSGKIELACPAFVKAGST--------------LTPAWEPPLvEPPDDSF--RLIQGHVPMHTHTT 613
Cdd:TIGR02166 614 FEDFRrdPEANPLKTPSGKIEIYSERLAQIAHTwelpegdvitplpeYVPTFEGPD-DPLRKDFplQLTGFHYKGRTHST 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 614 TDNNSYLHAIMPEnELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGfGCRVPLRHlaynrGAN 693
Cdd:TIGR02166 693 YGNVDWLREAAPQ-ELWINPIDAQKRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQG-AWYQPDKN-----GID 765
|
810 820 830
....*....|....*....|....*....|..
gi 1101271798 694 GGDLIPIMT----APVSGAAAQCETLVTVRKA 721
Cdd:TIGR02166 766 VGGCINTLTtqrpSPLAKGNPQHTNLVEVEKA 797
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
58-585 |
3.01e-88 |
|
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: 286.07 E-value: 3.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 58 CGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVG--EGQFQPISWEQAFQEIGSKLKELKE 135
Cdd:cd02766 12 CSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGrkGGQWERISWDEALDTIAAKLKEIKA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 136 QYGPQSLVWLAHPELISPLEKHFMAAFgsPNYTG----HGPTCYSSRNVAFEQMYGGVPGVDYR---NVRYYIAFGRNLT 208
Cdd:cd02766 92 EYGPESILPYSYAGTMGLLQRAARGRF--FHALGaselRGTICSGAGIEAQKYDFGASLGNDPEdmvNADLIVIWGINPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 209 ggIKNPDVQKIV-AAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAAYTTGFEELK 287
Cdd:cd02766 170 --ATNIHLMRIIqEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRDFLARHTEGFEELK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 288 KGVSGYTPAWAAGITGIEAGTISRIARELAAAKpaaavdP-----GWhavtGSQ-YGNSVQAGRAIAALNALLGNLGARG 361
Cdd:cd02766 248 AHLETYTPEWAAEITGVSAEEIEELARLYGEAK------PpsirlGY----GMQrYRNGGQNVRAIDALPALTGNIGVPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 362 GlslpptiklGSPAGIMGPkppaataprwdgagsekwplnkdhgmiqtfpervkqdqpyPVKAVIIQHLNPVRSSTDSLA 441
Cdd:cd02766 318 G---------GAFYSNSGP----------------------------------------PVKALWVYNSNPVAQAPDSNK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 442 FIEAL-KKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDpLMTVG--NKVLLRQPAIKPLFDNKGAEEIIAGIGRAAGL 518
Cdd:cd02766 349 VRKGLaREDLFVVVHDQFMTDTARYADIVLPATTFLEHED-VYASYwhYYLQYNEPAIPPPGEARSNTEIFRELAKRLGF 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1101271798 519 SE-YFNFTLEQYNDALLGP-----LGLTQAQLARTGVAEVEASKPDYSKLKTPSGKIELACPAFVKAGSTLTP 585
Cdd:cd02766 428 GEpPFEESDEEWLDQALDGtglplEGIDLERLLGPRKAGFPLVAWEDRGFPTPSGKFEFYSERAAKRGLPPLP 500
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
48-590 |
4.79e-81 |
|
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: 269.87 E-value: 4.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKcgvlAHVRDGRVWRLTGNPRDPQsggRLCARGNAGTKTLYDPDRLKGPMKRV-------------GEGQF 114
Cdd:cd02751 1 PTACHWGPFK----AHVKDGVIVRVEPDDTDQP---RPCPRGRSVRDRVYSPDRIKYPMKRVgwlgngpgsrelrGEGEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 115 QPISWEQAFQEIGSKLKELKEQYGPQSLV-----WLAHPELI--SPLEKHFMAAFGspNYTGHGPTcYSSRN--VAFEQM 185
Cdd:cd02751 74 VRISWDEALDLVASELKRIREKYGNEAIFggsygWASAGRLHhaQSLLHRFLNLIG--GYLGSYGT-YSTGAaqVILPHV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 186 YGGVPGVD--------YRNVRYYIAFGRNLT-------GGIKNPDVQKIVAAKAEGAHLVAVDPRLSDFA-YFADEWLPI 249
Cdd:cd02751 151 VGSDEVYEqgtswddiAEHSDLVVLFGANPLktrqgggGGPDHGSYYYLKQAKDAGVRFICIDPRYTDTAaVLAAEWIPI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 250 RPGTDLAMVLAMINVLINENLYDAAFVAAYTTGFEELKKGVSGY------TPAWAAGITGIEAGTISRIARELAAAKPAA 323
Cdd:cd02751 231 RPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGEsdgvpkTPEWAAEITGVPAETIRALAREIASKRTMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 324 AVdpGWhAVTGSQYGNsvQAGRAIAALNALLGNLGARGG----------LSLPPTIKLGSPAGIMGPKPPAATAP--RWd 391
Cdd:cd02751 311 AQ--GW-GLQRAHHGE--QPAWMLVTLAAMLGQIGLPGGgfgfgygysnGGGPPRGGAGGPGLPQGKNPVKDSIPvaRI- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 392 gagSEkwplnkdhgMIQTFPERVKQDQP---YP-VKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAH 467
Cdd:cd02751 385 ---AD---------ALLNPGKEFTANGKlktYPdIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYAD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 468 YILPEATYLERYDPLMT---VGNKVLLRQPAIKPLFDNKGAEEIIAGIGRAAGLSEYFNFTLEQ-------YN-----DA 532
Cdd:cd02751 453 IVLPATTSLERNDIGLTgnySNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEmewlehlYEetrakAA 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1101271798 533 LLGPLGLTQAQLARTGVAEVEASK------------PDYSKLKTPSGKIELACPAFvkAGSTLT-----PAWEPP 590
Cdd:cd02751 533 GPGPELPSFEEFWEKGIVRVPAAPkpfvafadfredPEANPLGTPSGKIEIYSETL--ADFGYDdcpghPTWIEP 605
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
48-523 |
1.66e-80 |
|
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: 265.62 E-value: 1.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVgEGQFQPISWEQAFQEIG 127
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRK-NGKFVEASWDEALSLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 128 SKLKELKEQYGPQSLVWLAHP----ELISPLEKHFMAAFGSPNYTG-----HGPTCYS-SRNVAFEQMYGGVPgvDYRNV 197
Cdd:cd02753 80 SRLKEIKDKYGPDAIAFFGSAkctnEENYLFQKLARAVGGTNNVDHcarlcHSPTVAGlAETLGSGAMTNSIA--DIEEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 198 RYYIAFGRNLTGGikNPDV-QKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFV 276
Cdd:cd02753 158 DVILVIGSNTTEA--HPVIaRRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEFI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 277 AAYTTGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAVdpgW-HAVTgsQYGNSVQAGRAIAALNALLG 355
Cdd:cd02753 236 EERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAIL---WgMGVT--QHSHGTDNVMALSNLALLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 356 NLGARGglslpptiklgspAGIMgpkpPAATAPRWDGAGsekwplnkDHGMIQTFpervkqdqpYP--VKAVIIQHLNPV 433
Cdd:cd02753 311 NIGRPG-------------TGVN----PLRGQNNVQGAC--------DMGALPNV---------LPgyVKALYIMGENPA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 434 RSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLMTVGNKVLLRQPAIKPLFDNKGAEEIIAGIG 513
Cdd:cd02753 357 LSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELA 436
|
490
....*....|.
gi 1101271798 514 RAAGL-SEYFN 523
Cdd:cd02753 437 NRLGYpGFYSH 447
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
54-590 |
2.00e-80 |
|
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: 268.42 E-value: 2.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 54 CGVKCGVLAHVRDGRVWRLTGNPRDPQSGG----RLCARGNAGTKTLYDPDRLKGPMKRVG---EGQFQPISWEQAFQEI 126
Cdd:cd02770 8 CGGRCPLKAHVKDGVITRIETDDTGDDDPGfhqiRACLRGRSQRKRVYNPDRLKYPMKRVGkrgEGKFVRISWDEALDTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 127 GSKLKELKEQYGPQSLVW------LAHPELISPLEKHFMAAFGSpnYTGHGPTcYSSRNVA------FEQMYGGVPGVDY 194
Cdd:cd02770 88 ASELKRIIEKYGNEAIYVnygtgtYGGVPAGRGAIARLLNLTGG--YLNYYGT-YSWAQITtatpytYGAAASGSSLDDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 195 RNVRYYIAFGRNLT-----GGIKNPDVQKivaAKAEGAHLVAVDPRLSDFAY-FADEWLPIRPGTDLAMVLAMINVLINE 268
Cdd:cd02770 165 KDSKLVVLFGHNPAetrmgGGGSTYYYLQ---AKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 269 NLYDAAFVAAYTTGFEE--LKKGVS------GY-----------TPAWAAGITGIEAGTISRIARELAAAKPAAAVDpGW 329
Cdd:cd02770 242 NLHDQAFLDRYCVGFDAehLPEGAPpnesykDYvlgtgydgtpkTPEWASEITGVPAETIRRLAREIATTKPAAILQ-GW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 330 havtGSQ-YGNSVQAGRAIAALNALLGNLGARGGL--SLPPTIKLGSPAGIMGPKPPAATAPrwdgagSEKWPLNKDHGM 406
Cdd:cd02770 321 ----GPQrHANGEQAARAIMMLAAMTGNVGIPGGNtgARPGGSAYNGAGLPAGKNPVKTSIP------CFMWTDAIERGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 407 IQT-FPERVKQDQPY--PVKAV--------IIQHlnpvrsSTDSLAfIEAL----KKLDLVVAIDIQMNDTAYYAHYILP 471
Cdd:cd02770 391 EMTaDDGGVKGADKLksNIKMIwnyagntlINQH------SDDNNT-TRALlddeSKCEFIVVIDNFMTPSARYADILLP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 472 EATYLERYDPLMT----VGNKVLLRQPAIKPLFDNKGAEEIIAGIGRAAGL----------SEYFNFTLEQYNDALLGPl 537
Cdd:cd02770 464 DTTELEREDIVLTsnagMMEYLIYSQKAIEPLYECKSDYEICAELAKRLGVedqftegkteQEWLEELYGQTRAKEPGL- 542
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1101271798 538 gLTQAQLARTGVAEVEASKP-----DYSK------LKTPSGKIELACPAFVKAGSTLT------------PAWEPP 590
Cdd:cd02770 543 -PTYEEFREKGIYRVPRALPfvafeDFREdpennpLKTPSGKIEIYSKALADMAKTLPegdeipaipkyvPAWEGP 617
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
48-577 |
4.10e-80 |
|
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: 265.41 E-value: 4.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVGeGQFQPISWEQAFQEIG 127
Cdd:cd02762 1 KRACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRG-GSFEEIDWDEAFDEIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 128 SKLKELKEQYGPQS-LVWL----AHPELISPLEKHFMAAFGSPNY---------TGHgptcyssrnVAFEQMYG---GVP 190
Cdd:cd02762 80 ERLRAIRARHGGDAvGVYGgnpqAHTHAGGAYSPALLKALGTSNYfsaatadqkPGH---------FWSGLMFGhpgLHP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 191 GVDYRNVRYYIAFGRN--LTGGIKN--PD-VQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVL 265
Cdd:cd02762 151 VPDIDRTDYLLILGANplQSNGSLRtaPDrVLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 266 INENLYDAAFVAAYTTGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAakpaaavdpgwhAVTGSQYG------- 338
Cdd:cd02762 231 LAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAA------------APSAAVYGrlgvqtq 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 339 -NSVQAGRAIAALNALLGNLGARGG--LSLPPTIKLGSPAG--IMGP--KPPAATAPRWDGagseKWPLNkdhgmiqTFP 411
Cdd:cd02762 299 lFGTLCSWLVKLLNLLTGNLDRPGGamFTTPALDLVGQTSGrtIGRGewRSRVSGLPEIAG----ELPVN-------VLA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 412 ERVKQDQPYPVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLER--YDPLMT--VGN 487
Cdd:cd02762 368 EEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKphATFFNLefPRN 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 488 KVLLRQPAIKPLFDNKGAEEIIAGIGRA--AGLSEYFnftleqYNDALLGPLGLtQAQLARTGVAEVEASKPD-YSKLKT 564
Cdd:cd02762 448 AFRYRRPLFPPPPGTLPEWEILARLVEAldAVLRAGF------YGERAGGTLLL-AALLERPSGVDLGPLTPRlWQRLRT 520
|
570
....*....|...
gi 1101271798 565 PSGKIELACPAFV 577
Cdd:cd02762 521 PDGRIHLAPPELL 533
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
54-590 |
1.86e-76 |
|
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: 256.64 E-value: 1.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 54 CGVKCGVLAHVRDGRVWRLTgnPRDPQSG--GRLCARGNAGTKTLYDPDRLKGPMKRV---GEGQFQPISWEQAFQEIGS 128
Cdd:cd02765 8 CGGRCPLKCHVRDGKIVKVE--PNEWPDKtyKRGCTRGLSHLQRVYSPDRLKYPMKRVgerGEGKFERITWDEALDTIAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 129 KLKELKEQYGPQSLVWLAHPELISPLEKHFMAAFGSpnyTGHGPTCYS---------SRNVAFEQMYGGVPGVDYRNVRY 199
Cdd:cd02765 86 KLTEAKREYGGKSILWMSSSGDGAILSYLRLALLGG---GLQDALTYGidtgvgqgfNRVTGGGFMPPTNEITDWVNAKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 200 YIAFGRNLTGGiKNPDVQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAAY 279
Cdd:cd02765 163 IIIWGSNILET-QFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEAFLKSN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 280 T--------------------------------------------------------------TGFEELKKGVSGYTPAW 297
Cdd:cd02765 242 TsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhTVLTALREQAASYPPKA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 298 AAGITGIEAGTISRIARELAAAKPAAavdpGWHAVTGSQYGNSVQAGRAIAALNALLGNLGARGGLslpptiklgspagi 377
Cdd:cd02765 322 AAEICGLEEAIIETLAEWYATGKPSG----IWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG-------------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 378 mgpkppaataprwdgagsekwplnkdHGMIqtfpervkqdqpypvKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDI 457
Cdd:cd02765 384 --------------------------VGQI---------------KFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVDI 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 458 QMNDTAYYAHYILPEATYLERYDPLMTVGNK--VLLRQPAIKPLFDNKGAEEIIAGIGRAAGLSEYFNFTLEQYNDALL- 534
Cdd:cd02765 423 FHTPTVRYADIVLPAAHWFEVEDLLVRYTTHphVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFPKTPEDYVRAFMn 502
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1101271798 535 --GP--LGLTQAQLARTGVAEVEA--SKPDYS----KLKTPSGKIELACPAFvKAGSTLTPAWEPP 590
Cdd:cd02765 503 sdDPalDGITWEALKEEGIIMRLAtpEDPYVAyldqKFGTPSGKLEFYNEAA-PELEEALPLPEEP 567
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
48-525 |
8.97e-74 |
|
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: 249.45 E-value: 8.97e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVGEGQFQPISWEQAFQEIG 127
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 128 SKLKELKEQYGPQSLVWLA----HPELISPLEKHFMAAFGSPNYTGHGPTCYSSRNVAFEQMYG--GVPGV--DYRNVRY 199
Cdd:cd02754 81 ERFKAIQAEYGPDSVAFYGsgqlLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGadGPPGSydDIEHADC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 200 YIAFGRNL--TGGIKNPDVQKIVAAkAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVA 277
Cdd:cd02754 161 FFLIGSNMaeCHPILFRRLLDRKKA-NPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDRDFID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 278 AYTTGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAVdpgWhaVTG-SQYGNSVQAGRAIAALNALLGN 356
Cdd:cd02754 240 AHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSL---W--TMGvNQSTQGTAANNAIINLHLATGK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 357 LGARGG--LSLP--PTIKLGSPAGIMGPKPP-----------AATAPRWDGAGSEKWPLNKDHGMIQtfPERVKQDQpyp 421
Cdd:cd02754 315 IGRPGSgpFSLTgqPNAMGGREVGGLANLLPghrsvnnpehrAEVAKFWGVPEGTIPPKPGLHAVEM--FEAIEDGE--- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 422 VKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDI-QMNDTAYYAHYILPEATYLERYDplmTVGN---KVLLRQPAIK 497
Cdd:cd02754 390 IKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEYADLVLPAASWGEKEG---TMTNserRVSLLRAAVE 466
|
490 500
....*....|....*....|....*...
gi 1101271798 498 PLFDNKGAEEIIAGIGRAAGLSEYFNFT 525
Cdd:cd02754 467 PPGEARPDWWILADVARRLGFGELFPYT 494
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-523 |
1.59e-72 |
|
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: 248.98 E-value: 1.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 49 TLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRVGE---GQFQPISWEQAFQE 125
Cdd:cd02763 2 TTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPrgsGQFEEIEWEEAFSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 126 IGSKLKELKeQYGPQSLVWLAHPELISPLEKHFMAAFGSPNYTGHGPTCysSRNVAFEQMY--GG----VPGVDYRNVRY 199
Cdd:cd02763 82 ATKRLKAAR-ATDPKKFAFFTGRDQMQALTGWFAGQFGTPNYAAHGGFC--SVNMAAGGLYsiGGsfweFGGPDLEHTKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 200 YIAFGrNLTGGIKNPDVQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAAY 279
Cdd:cd02763 159 FMMIG-VAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 280 TTGFEelkkgVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAVD-P-GW------------------HAVTG-SQYG 338
Cdd:cd02763 238 TNAAE-----LVDYTPEWVEKITGIPADTIRRIAKELGVTARDQPIElPiAWtdvwgrkhekitgrpvsfHAMRGiAAHS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 339 NSVQAGRAIAALNALLGNLGARGGLSLPPTIKLGSPAGIMGPKPPAATAP---------------------------RWD 391
Cdd:cd02763 313 NGFQTIRALFVLMMLLGTIDRPGGFRHKPPYPRHIPPLPKPPKIPSADKPftplygpplgwpaspddllvdedgnplRID 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 392 GAGSEKWPLNKdHGMIQTFPERVKQDQPYPVKAVIIQHLNPV-RSSTDSLAFIEALK--------KLDLVVAIDIQMNDT 462
Cdd:cd02763 393 KAYSWEYPLAA-HGCMQNVITNAWRGDPYPIDTLMIYMANMAwNSSMNTPEVREMLTdkdasgnyKIPFIIVCDAFYSEM 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101271798 463 AYYAHYILPEATYLERYDPLMTV--------GNKVLLRQPAIKPLFDNKGAEEIIAGIGRAAGLSEYFN 523
Cdd:cd02763 472 VAFADLVLPDTTYLERHDAMSLLdrpiseadGPVDAIRVPIVEPKGDVKPFQEVLIELGTRLGLPGFTN 540
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
1-676 |
3.84e-66 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 234.15 E-value: 3.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 1 MLEQKITRRAFLKgSLAAGALATFGGKL-IPI----EPAKAAAAGQAETRVVPTLCEM-CGVKCGVLAHVRDGRV-WRLT 73
Cdd:PRK14990 9 VLAAEVSRRGLVK-TTAIGGLAMASSALtLPFsriaHAVDSAIPTKSDEKVIWSACTVnCGSRCPLRMHVVDGEIkYVET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 74 GNPRDPQSGG----RLCARGNAGTKTLYDPDRLKGPMKRVG---EGQFQPISWEQAFQEIGSKLKELKEQYGPQSLV--- 143
Cdd:PRK14990 88 DNTGDDNYDGlhqvRACLRGRSMRRRVYNPDRLKYPMKRVGargEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlny 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 144 ------------WLAHPELISPLekhFMAAFGSPNYTGHgptcYSSRNVA--FEQMYGG-----VPGvDYRNVRYYIAFG 204
Cdd:PRK14990 168 gtgtlggtmtrsWPPGNTLVARL---MNCCGGYLNHYGD----YSSAQIAegLNYTYGGwadgnSPS-DIENSKLVVLFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 205 RN-----LTGGIKNPDVQKivAAKAEGAHLVAVDPRLSDF-AYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAA 278
Cdd:PRK14990 240 NNpgetrMSGGGVTYYLEQ--ARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 279 YTTGFEE-----------------LKKGVSGY--TPAWAAGITGIEAGTISRIARELaAAKPAAAVDPGWhavtGSQ-YG 338
Cdd:PRK14990 318 YCVGYDEktlpasapknghykayiLGEGPDGVakTPEWASQITGVPADKIIKLAREI-GSTKPAFISQGW----GPQrHA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 339 NSVQAGRAIAALNALLGNLGARGG--------LSLP----PTIKlgspagimGPKPPAATAPRWDGA---GSEKWPLNKD 403
Cdd:PRK14990 393 NGEIATRAISMLAILTGNVGINGGnsgaregsYSLPfvrmPTLE--------NPIQTSISMFMWTDAierGPEMTALRDG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 404 HGMIQTFPERVKQDQPYPVKAVIIQHLNPVRSSTdslaFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLM 483
Cdd:PRK14990 465 VRGKDKLDVPIKMIWNYAGNCLINQHSEINRTHE----ILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFAL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 484 --TVGNK--VLLRQPAIKPLFDNKGAEEIIAGIGRAAGLSEYFN----------FTLEQYNDALlgPLGLTQAQLARTGV 549
Cdd:PRK14990 541 daSCGNMsyVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTegrtqeewmrHLYAQSREAI--PELPTFEEFRKQGI 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 550 AEVEASK------------PDYSKLKTPSGKIELACPAFVKAGSTltpaWEPP---LVEP----------------PDDS 598
Cdd:PRK14990 619 FKKRDPQghhvaykafredPQANPLTTPSGKIEIYSQALADIAAT----WELPegdVIDPlpiytpgfesyqdplnKQYP 694
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101271798 599 FRLIQGHVPMHTHTTTDNNSYLHAIMpENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHG 676
Cdd:PRK14990 695 LQLTGFHYKSRVHSTYGNVDVLKAAC-RQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEG 771
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
48-518 |
3.17e-65 |
|
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: 229.92 E-value: 3.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRD--GRVWRLTGNP-----RDPQ----------------------SGGRLCARGNAGTKTLYD 98
Cdd:cd02758 1 YSSCLGCWTQCGIRVRVDKetGKVLRIAGNPyhplnTAPSlpyntplkeslylslvgenglkARATACARGNAGLQYLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 99 PDRLKGPMKRVG---EGQFQPISWEQAFQEIGSKLK--------ELKEQYGPQSLVWLAHPEL----------------I 151
Cdd:cd02758 81 PYRVLQPLKRVGprgSGKWKPISWEQLIEEVVEGGDlfgeghveGLKAIRDLDTPIDPDHPDLgpkanqllytfgrdegR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 152 SPLEKHFM-AAFGSPNYTGHGPTC---YSSRNVAFEQMYGGVPGV--DYRNVRYYIAFGRNL--TGGIKNPDVQKIVAAK 223
Cdd:cd02758 161 TPFIKRFAnQAFGTVNFGGHGSYCglsYRAGNGALMNDLDGYPHVkpDFDNAEFALFIGTSPaqAGNPFKRQARRLAEAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 224 AEGA-HLVAVDPRLSDFAYFADE---WLPIRPGTDLAMVLAMINVLINENLYDAAFV------AAYT------------- 280
Cdd:cd02758 241 TEGNfKYVVVDPVLPNTTSAAGEnirWVPIKPGGDGALAMAMIRWIIENERYNAEYLsipskeAAKAagepswtnathlv 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 281 ------TGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAVDpgwhAVTGSQYGNSVQAGRAIAALNALL 354
Cdd:cd02758 321 itvrvkSALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVV----HHGGTMHSNGFYNAYAIRMLNALI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 355 GNLGARGGLSLP--PTIKLGSPAGIMGPKPPAATAPRWDGAGSEKWPLNKDhgmiQTFPERVKQDQ-------------- 418
Cdd:cd02758 397 GNLNWKGGLLMSggGFADNSAGPRYDFKKFFGEVKPWGVPIDRSKKAYEKT----SEYKRKVAAGEnpypakrpwypltp 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 419 --------------PYPVKAVIIQHLNPVRSSTDSLA-FIEALK---KLDLVVAIDIQMNDTAYYAHYILPEATYLER-- 478
Cdd:cd02758 473 elyteviasaaegyPYKLKALILWMANPVYGAPGLVKqVEEKLKdpkKLPLFIAIDAFINETSAYADYIVPDTTYYESwg 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1101271798 479 ------YDPLMTVGnkvlLRQPAIKPLFDNKG------AEEIIAGIGRAAGL 518
Cdd:cd02758 553 fstpwgGVPTKAST----ARWPVIAPLTEKTAnghpvsMESFLIDLAKALGL 600
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
54-515 |
4.13e-65 |
|
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: 222.96 E-value: 4.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 54 CGVKCGVLAHVRDGRVWRLT-------GNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRV---GEGQFQPISWEQAF 123
Cdd:cd02750 12 CTGSCSWNVYVKNGIVTREEqatdypeTPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVgarGEGKWKRISWDEAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 124 QEIGSKLKELKEQYGPQSLVWLAHPELISPLEK----HFMAAFGSPnyTGHGPTCYSSRNVAFEQMYGGVPGV----DYR 195
Cdd:cd02750 92 ELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYaagsRFASLIGGV--SLSFYDWYGDLPPGSPQTWGEQTDVpesaDWY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 196 NVRYYIAFGRNLTGgIKNPDVQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAF 275
Cdd:cd02750 170 NADYIIMWGSNVPV-TRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 276 VAAYTtgfeELKKGVsgYTPAWAAGITGIEAGTISRIARELAAAKPAaavdpgwHAVTG---SQYGNSVQAGRAIAALNA 352
Cdd:cd02750 249 LKEYT----DLPFLV--YTPAWQEAITGVPRETVIRLAREFATNGRS-------MIIVGagiNHWYHGDLCYRALILLLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 353 LLGNLGARGGLslpptiklgspagimgpkppAATaprWDGagsekWPlnkdhgmiqtfpervkqdqpypvKAVIIQHLNP 432
Cdd:cd02750 316 LTGNEGKNGGG--------------------WAH---YVG-----QP-----------------------RVLFVWRGNL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 433 VRSSTDSLAFIEA--LKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDPLMTVGNK-VLLRQPAIKPLFDNKGAEEII 509
Cdd:cd02750 345 FGSSGKGHEYFEDapEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPfIHPFSPAVDPLWEAKSDWEIF 424
|
....*.
gi 1101271798 510 AGIGRA 515
Cdd:cd02750 425 KALAKK 430
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
599-720 |
4.94e-56 |
|
The MopB_CT_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. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 187.10 E-value: 4.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 599 FRLIQGHVPMHTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFG 678
Cdd:cd02778 2 FRLIYGKSPVHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGFG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1101271798 679 CRVPLRHLAYNRGANGGDLIPIMTAPVSGAAAQCETLVTVRK 720
Cdd:cd02778 82 HWAPALSRAYGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
48-533 |
6.86e-47 |
|
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: 178.24 E-value: 6.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAH-VRDGRVWRLTGNPRDPQSG---GRLCARGNAGTKTLYDPDRLKGPMKRVGEGQ-------FQP 116
Cdd:cd02760 1 PTYCYNCVAGPDFMAVkVVDGVATEIEPNFAAEDIHparGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKKgrnedpgFVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 117 ISWEQAFQEIGSKLKELKE------QYGPQSLVWLAH---PELISPLEKHFMAAFGSPNYT---GHGPTCyssrnVAFEQ 184
Cdd:cd02760 81 ISWDEALDLVAAKLRRVREkglldeKGLPRLAATFGHggtPAMYMGTFPAFLAAWGPIDFSfgsGQGVKC-----VHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 185 MYGGV------PGVDYRNVRYYIAFGRNLTGGIKNPDVQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMV 258
Cdd:cd02760 156 LYGEFwhraftVAADTPLANYVISFGSNVEASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 259 LAMINVLINE---NLYDAAFVAAYT------------------------------------------------------- 280
Cdd:cd02760 236 FAMIHVMVHEqglGKLDVPFLRDRTsspylvgpdglylrdaatgkplvwdersgravpfdtrgavpavagdfavdgavsv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 281 ---------------TGFEELKKGVSGYTPAWAAGITGIEAGTISRIARE-LAAAKPAAAVDPGWH-------AVT---G 334
Cdd:cd02760 316 daddetaihqgvegtTAFTMLVEHMRKYTPEWAESICDVPAATIRRIAREfLENASIGSTIEVDGVtlpyrpvAVTlgkS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 335 SQYG-NSVQAGRAIAALNALLGNLGARGGlSLPPTIKLGSPA------------GIMGP------KPPAATAPRWDGAGS 395
Cdd:cd02760 396 VNNGwGAFECCWARTLLATLVGALEVPGG-TLGTTVRLNRPHddrlasvkpgedGFMAQgfnptdKEHWVVKPTGRNAHR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 396 EKWPLNKDHGMIQ-------------TFPERVKQDQPYPVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDT 462
Cdd:cd02760 475 TLVPIVGNSAWSQalgptqlawmflrEVPLDWKFELPTLPDVWFNYRTNPAISFWDTATLVDNIAKFPFTVSFAYTEDET 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 463 AYYAHYILPEATYLERYDPLMTVGNK----------VLLRQPAIKPLFDNKGAEEIIAGIGRAAGLseyfnftLEQYNDA 532
Cdd:cd02760 555 NWMADVLLPEATDLESLQMIKVGGTKfveqfwehrgVVLRQPAVEPQGEARDFTWISTELAKRTGL-------LADYNAA 627
|
.
gi 1101271798 533 L 533
Cdd:cd02760 628 L 628
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
62-571 |
1.07e-45 |
|
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: 172.45 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 62 AHVRDGRVWRLTGNPRDPQSGGRLcargNAGTKTLYDPDRLKGPMKRV--------------GEGQFQPISWEQAFQEIG 127
Cdd:cd02769 11 ARVKDGRIVGVRPFEEDPDPSPLL----DGVPDAVYSPTRIKYPMVRRgwlekgpgsdrslrGKEEFVRVSWDEALDLVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 128 SKLKELKEQYGPQSLV-----W-----LAHPeliSPLEKHFMAAFGspNYTGHGPTcYSS--RNVAFEQMYGGVPGVDYR 195
Cdd:cd02769 87 AELKRVRKTYGNEAIFggsygWssagrFHHA---QSLLHRFLNLAG--GYVGSVGD-YSTgaAQVILPHVVGSMEVYTEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 196 ---------NVRYYIAFGRNLtggIKNPDVQKIV-----------AAKAEGAHLVAVDPRLSDFA-YFADEWLPIRPGTD 254
Cdd:cd02769 161 qtswpviaeHTELVVAFGADP---LKNAQIAWGGipdhqaysylkALKDRGIRFISISPLRDDTAaELGAEWIAIRPGTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 255 LAMVLAMINVLINENLYDAAFVAAYTTGFEELKKGVSGY------TPAWAAGITGIEAGTISRIARELAAAKPAAAVdpG 328
Cdd:cd02769 238 VALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGEsdgvpkTPEWAAAICGIPAETIRELARRFASKRTMIMA--G 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 329 WhAVTGSQYGNsvQAGRAIAALNALLGNLGARGG---LSLPPTIKLGSPAGimGPKPPAAtaPRWDGAGSEKWPLNKDHG 405
Cdd:cd02769 316 W-SLQRAHHGE--QPHWMAVTLAAMLGQIGLPGGgfgFGYHYSNGGGPPRG--AAPPPAL--PQGRNPVSSFIPVARIAD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 406 MI----QTFP---ERVKqdqpYP-VKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLE 477
Cdd:cd02769 389 MLlnpgKPFDyngKKLT----YPdIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 478 RYDPLMTVGNKVLL--RQpAIKPLFDNKGAEEIIAGIGRAAGLSEYFNFTLE---------QYNDALLGPLGLTQ---AQ 543
Cdd:cd02769 465 RNDIGGSGDNRYIVamKQ-VVEPVGEARDDYDIFADLAERLGVEEQFTEGRDemewlrhlyEESRAQAAARGVEMpsfDE 543
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1101271798 544 LARTGVAEVEA------------SKPDYSKLKTPSGKIEL 571
Cdd:cd02769 544 FWAQGYVELPIpeadfvrladfrEDPEANPLGTPSGRIEI 583
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
8-557 |
5.71e-42 |
|
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: 160.35 E-value: 5.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 8 RRAFLK---GSLAAGALATFGGKLIPIEPAKAAAAGQAETRVVPTLCEMC--GVKCGVLAHVRDGRVWRLTGNPRDPQSG 82
Cdd:cd02764 1 RRGFLKlmgASLAMASAAACRYPVEKIVPYVIWPENIVPGETVYYATSLVpaGEGQGVLVKTVDGRPIKIEGNPDHPASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 83 GRLCARGNAGTKTLYDPDRLKGPMKRVGEGQFQPISWEQAFQEIGSKLKELKeqyGPQSLVWLAhPELISPLEKHFMAAF 162
Cdd:cd02764 81 GGTSARAQASVLSLYDPDRAQGPLRRGIDGAYVASDWADFDAKVAEQLKAVK---DGGKLAVLS-GNVNSPTTEALIGDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 163 -----GSPNYTgHGPTCYSSRNVAFEQMYGG--VPGVDYRNVRYYIAFGRNLTG----GIKNpdVQKIVAAKAEGAH--- 228
Cdd:cd02764 157 lkkypGAKHVV-YDPLSAEDVNEAWQASFGKdvVPGYDFDKAEVIVSIDADFLGswisAIRH--RHDFAAKRRLGAEepm 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 229 --LVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINenlydaafVAAYTTGFEELKKGVSGYTPAWAAGITGIEA 306
Cdd:cd02764 234 srLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIK--------KGAGSSLPDFFRALNLAFKPAKVAELTVDLD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 307 GTISRIARELAAAKPAAavdpgwhAVTGSQYGNSVQAGRAIA--ALNALLGNLGArgglSLPPTiklgspagimGPKPPA 384
Cdd:cd02764 306 KALAALAKALAAAGKSL-------VVAGSELSQTAGADTQVAvnALNSLLGNDGK----TVDHA----------RPIKGG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 385 ataprwdgagsekwPLNKDHGMIqTFPERVKQDQpypVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAY 464
Cdd:cd02764 365 --------------ELGNQQDLK-ALASRINAGK---VSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAM 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 465 YAHYILPEATYLERYDPLMTVGNKVLLRQPAIKPLFDNKGAEEIIAGigrAAGLSEYFNFTLEQYNDALLGPLGLTQ-AQ 543
Cdd:cd02764 427 LCDWVAPMSHGLESWGDAETPDGTYSICQPVIAPLFDTRSAQESLLL---ALGGSLGGYEKLRRYTSWIKAAIGDRSwEQ 503
|
570
....*....|....
gi 1101271798 544 LARTGVAEVEASKP 557
Cdd:cd02764 504 ALRDGVAADVNVSA 517
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
48-520 |
1.34e-41 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 161.41 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYDPDRLKGPMKRV-GEGQFQPISWEQAFQEI 126
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRApGSGKWEEISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 127 GSKLKELKEQ------------YGPQSLVWLAHPELISP---LEKHFMAAFGSpNYT------GHGPTCYSsrnVAFEQM 185
Cdd:cd02752 81 ARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSNEecyLIRKFARALGT-NNLdhqariUHSPTVAG---LANTFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 186 YGGVPG--VDYRNVRYYIAFGRNltgGIKNPDV--QKIVAAKA-EGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLA 260
Cdd:cd02752 157 RGAMTNswNDIKNADVILVMGGN---PAEAHPVsfKWILEAKEkNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 261 MINVLINenlydaafvaayttgfeelkkgvsgYTPAWAAGITGIEAGTISRIARELAAAKPAAAVDPGWHAVTGSQYGNS 340
Cdd:cd02752 234 MINYIIR-------------------------YTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 341 VQAGRAIAALNALLGNLGARGGlslpPTIKLGSPAGIMGpkppaATaprwdgagsekwplnkDHGMIQTfpervkqDQPY 420
Cdd:cd02752 289 SQNIRAMCILQLLLGNIGVAGG----GVNALRGHSNVQG-----AT----------------DLGLLSH-------NLPG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 421 PVKAViiqhlNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAH-------------YILPEATYLERYDPLMTVGN 487
Cdd:cd02752 337 YLGGQ-----NPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGSITNSGR 411
|
490 500 510
....*....|....*....|....*....|...
gi 1101271798 488 KVLLRQPAIKPLFDNKGAEEIIAGIGRAAGLSE 520
Cdd:cd02752 412 WLQWRYKVVEPPGEAKSDGDILVELAKRLGFLY 444
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
5-680 |
2.40e-41 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 162.86 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 5 KITRRAFLKGSLAAGALATFG-----------------------------------------GKLIPiEPakaaaagqaE 43
Cdd:PRK14991 2 DKTRRQLLKGGLAAGGLAAFAagysdtakraakgllngtsgkptrdrihgnsltpeyrvdaqGQLQP-NP---------Q 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 44 TRVVPTLCEMCGVKCGVLAHV--RDGRVWRLTGNPRDPQS------------------------GGR--LCARGNAGTKT 95
Cdd:PRK14991 72 QRVANTQCLGCWTQCGVRVRVdnATNKILRIAGNPYHPLStdhhidmstpvkeafeslsgesglEGRstACARGNAMLEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 96 LYDPDRLKGPMKRVG---EGQFQPISWEQAFQEI-------------GskLKELKE----------QYGP---QSLVWLA 146
Cdd:PRK14991 152 LDSPYRVLQPLKRVGkrgSGKWQRISFEQLVEEVveggdlfgeghvdG--LRAIRDldtpidaknpEYGPkanQLLVTNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 147 HPELISPLEKHFMA-AFGSPNYTGHGPTC---YSSRNVAF----EQMYGGVPgvDYRNVRYYIAFGRNlTGGIKNP---D 215
Cdd:PRK14991 230 SDEGRDAFIKRFAFnSFGTRNFGNHGSYCglaYRAGSGALmgdlDKNPHVKP--DWDNVEFALFIGTS-PAQSGNPfkrQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 216 VQKIVAAKAEGA-HLVAVDPRL----SDFAYFADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVA------------- 277
Cdd:PRK14991 307 ARQLANARTRGNfEYVVVAPALplssSLAAGDNNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYLAqpgvaamqaagea 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 278 -----------------------------------------------------------------------------AYT 280
Cdd:PRK14991 387 swtnathlviadpghprygqflrasdlglpfegeargdgedtlvvdaadgelvpatqaqparlfveqyvtladgqrvRVK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 281 TGFEELKKGVSGYTPAWAAGITGIEAGTISRIARELAAAKPAAAVDPgwHAvtGSQYGNSVQAGRAIAALNALLGNLGAR 360
Cdd:PRK14991 467 SSLQLLKEAARKLSLAEYSEQCGVPEAQIIALAEEFTSHGRKAAVIS--HG--GTMSGNGFYNAWAIMMLNALIGNLNLK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 361 GGLSLPPtiklgspagimGPKPPAATAPRWDGAGSE-------------KWPLNKDhgmiQTFPERVKQDQ--------- 418
Cdd:PRK14991 543 GGVVVGG-----------GKFPGFGDGPRYNLASFAgkvkpkgvslsrsKFPYEKS----SEYRRKVEAGQspypakapw 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 419 -------------------PYPVKAVIIQHLNPVRSSTDSLAFIEAL----KKLDLVVAIDIQMNDTAYYAHYILPEATY 475
Cdd:PRK14991 608 ypfvaglltemltaalegyPYPLKAWINHMSNPIYGVPGLRAVIEEKlkdpKKLPLFISIDAFINETTALADYIVPDTHT 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 476 LERYD---PLMTVGNK-VLLRQPAIKPLFDnKGAEE--------IIA--------GIGRAA---------GLSEYFNFTL 526
Cdd:PRK14991 688 YESWGftaPWGGVPTKaSTARWPVVEPRTA-KTADGqpvcmesfLIAvakrlqlpGFGDNAikdaqgnthPLNRAEDFYL 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 527 EQY-NDALLGPLGL---TQAQLARTGVA----EVEAS-KPDYSK----LKTPSGKIELACPAFvkAGSTLTPAWEPPLV- 592
Cdd:PRK14991 767 RGAaNIAYLGKTPVadaSDEDIALTGVSrilpALQATlKPDEVRrvafIYARGGRFAPAESAY--DEERMGNRWKKPLQi 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 593 -----------------------EPPddsfRLIQGhVPMHTHTTTDN-------------NSY------LHAIMPENELW 630
Cdd:PRK14991 845 wnedvaaarhsmtgerysgcptwYPP----RLADG-TPLREQFPESQwplllisfksnlmSSMsiasprLRQVKPANPVA 919
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|
gi 1101271798 631 IHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFGCR 680
Cdd:PRK14991 920 LNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHGYGHR 969
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
101-503 |
3.04e-39 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 148.70 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 101 RLKGPMKRVGEGQFQPISWEQAFQEIGSKLKELKEQYGPQSLVWLAHPELISPLE-----KHFMAAFGSPN--YTGHGPT 173
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGGLTDVEslyalKKLLNRLGSKNgnTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 174 CYSSRNVAF--EQMYGGVPGVDYRNV---RYYIAFGRNL--TGGIKNPDVQKivAAKAEGAHLVAVDPRLSdfAYFADEW 246
Cdd:pfam00384 81 LCTAAAAAFgsDLRSNYLFNSSIADIenaDLILLIGTNPreEAPILNARIRK--AALKGKAKVIVIGPRLD--LTYADEH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 247 LPIRPGTDLAMVLAMINVLINENLYDAAFvaayttgfeelkkgvsgytpawaagitgieagtisriarelaaaKPAAAVD 326
Cdd:pfam00384 157 LGIKPGTDLALALAGAHVFIKELKKDKDF--------------------------------------------APKPIII 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 327 PGWHAVTGSqygNSVQAGRAIAALNALLGNLGARGGLSLPPTIklgspagimgpkppAATAPRWDGAGSEkwPLNKDHGM 406
Cdd:pfam00384 193 VGAGVLQRQ---DGEAIFRAIANLADLTGNIGRPGGGWNGLNI--------------LQGAASPVGALDL--GLVPGIKS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 407 IqtfpERVKQDQPYPVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMND-TAYYAHYILPEATYLERYDPLMTV 485
Cdd:pfam00384 254 V----EMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDkTAKYADVILPAAAYTEKNGTYVNT 329
|
410
....*....|....*...
gi 1101271798 486 GNKVLLRQPAIKPLFDNK 503
Cdd:pfam00384 330 EGRVQSTKQAVPPPGEAR 347
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
6-664 |
4.40e-27 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 117.46 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 6 ITRRAFLKGSLAAGALATFGGKLIPIEPAKAAAAGQAETrvvPTLCEMCGVKCGVL-AHVRDGRV-----WRLTGNPRDP 79
Cdd:PRK15102 1 ASRRRFLKGLGGLSAAGMLGPSLLTPRSALAAQAAAAET---TKEWILTGSHWGAFrAKVKNGRFveakpFELDKYPTKM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 80 QSGGRlcargnagtKTLYDPDRLKGPMKRV--------------GEGQFQPISWEQAFQEIGSKLKELKEQYGPQSLV-- 143
Cdd:PRK15102 78 INGIK---------GHVYNPSRIRYPMVRLdwlrkrhksdtsqrGDNRFVRVSWDEALDLFYEELERVQKTYGPSALHtg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 144 ---WLAHPELIS---------PLEKHFMAAFGspNY-TGHG----PTCYSSRNVaFEQmyGGVPGVDYRNVRYYIAFG-- 204
Cdd:PRK15102 149 qtgWQSTGQFHSatghmqraiGMHGNSVGTVG--DYsTGAGqvilPYVLGSTEV-YEQ--GTSWPLILENSKTIVLWGsd 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 205 --RNLTGGIKNPD------VQKIVAAKAEGA-HLVAVDPRLSDF-AYFADEWLPIRPGTDLAMVLAMINVLINENLYDAA 274
Cdd:PRK15102 224 pvKNLQVGWNCEThesyayLAQLKEKVAKGEiNVISIDPVVTKTqNYLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 275 FVAAYTTGFEELKKGVSG------YTPAWAAGITGIEAGTISRIARELAAAKPAAAVdpGWhAVTGSQYGNsvQAGRAIA 348
Cdd:PRK15102 304 FIDNYCLGFEQFLPYLLGekdgvpKTPEWAEKICGIDAETIRELARQMAKGRTQIIA--GW-CIQRQQHGE--QPYWMGA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 349 ALNALLGNLG-ARGGLSLP--------PTIKLGSPAGI-----MGPKPP---------AATAP--RWDGAGSEKWPLNKD 403
Cdd:PRK15102 379 VLAAMLGQIGlPGGGISYGhhysgigvPSSGGAIPGGFpgnldTGQKPKhdnsdykgySSTIPvaRFIDAILEPGKTINW 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 404 HGMIQTFPervkqdqpyPVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLERYDpLM 483
Cdd:PRK15102 459 NGKKVTLP---------PLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERND-ID 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 484 TVGNK----VLLRQPAIKPLFDNKGAEEIIAGIGRAAGLSEYFNFTLEQ-------YNDALLGPLGLTQ----AQLARTG 548
Cdd:PRK15102 529 QYGSYsnrgIIAMKKVVEPLFESRSDFDIFRELCRRFGREKEYTRGMDEmgwlkrlYQECKQQNKGKFHmpefDEFWKKG 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 549 VAEVEASK-----------PDYSKLKTPSGKIELACPAFVKAGStltpawepplveppDDSfrliQGHvPM------HTH 611
Cdd:PRK15102 609 YVEFGEGQpwvrhadfredPELNPLGTPSGLIEIYSRKIADMGY--------------DDC----QGH-PMwfekieRSH 669
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101271798 612 TTTDNNSY------------LHAIMPENE-------------LWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTE 664
Cdd:PRK15102 670 GGPGSDKYplwlqsvhpdkrLHSQLCESEelretytvqgrepVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSD 747
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
606-711 |
7.88e-24 |
|
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: 96.23 E-value: 7.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 606 VPMHTHTTTDNNS-YLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFGCRvplr 684
Cdd:cd02775 1 LRDHFHSGTRTRNpWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHR---- 76
|
90 100
....*....|....*....|....*..
gi 1101271798 685 hlaYNRGANGGDLIPIMTAPVSGAAAQ 711
Cdd:cd02775 77 ---GGRGGNANVLTPDALDPPSGGPAY 100
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
5-313 |
5.28e-22 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 101.51 E-value: 5.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 5 KITRRAFLKGSlAAGALATFGGKLIPIEPAKAAAAGQAETRVVPTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGR 84
Cdd:PRK13532 2 KLSRRDFMKAN-AAAAAAAAAGLSLPAVANAVVGSAQTAIKWDKAPCRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 85 LCARGNAGTKTLYDPDRLKGPMKRV--GE----GQFQPISWEQAFQEIGSKLKE-LKEQyGP---------QSLVWLAHP 148
Cdd:PRK13532 81 NCIKGYFLSKIMYGKDRLTQPLLRMkdGKydkeGEFTPVSWDQAFDVMAEKFKKaLKEK-GPtavgmfgsgQWTIWEGYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 149 ELispleKHFMAAFGSPNYTGHGPTCYSSRNVAFEQMYggvpGVD-----YRNVRYYIAF-------------------G 204
Cdd:PRK13532 160 AS-----KLMKAGFRSNNIDPNARHCMASAVVGFMRTF----GIDepmgcYDDIEAADAFvlwgsnmaemhpilwsrvtD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 205 RNLTggikNPDVQkivaakaegahlVAVdprLSDFAY----FADEWLPIRPGTDLAMVLAMINVLINENLYDAAFVAAYT 280
Cdd:PRK13532 231 RRLS----NPDVK------------VAV---LSTFEHrsfeLADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNKHT 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1101271798 281 ---TG-------------------------------FEELKKGVSGYTPAWAAGITGIEAGTISRIA 313
Cdd:PRK13532 292 nfrKGatdigyglrpthplekaaknpgtagksepisFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLA 358
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
599-710 |
1.20e-21 |
|
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: 90.41 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 599 FRLIQGHVPMHTHTTTDNNSYLHAIMPENE-LWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGF 677
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEvVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|...
gi 1101271798 678 GCRvplrhlayNRGANGGDLIPIMTAPVSGAAA 710
Cdd:pfam01568 81 WYE--------PRGGNANALTDDATDPLSGGPE 105
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
44-98 |
9.32e-21 |
|
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: 86.15 E-value: 9.32e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1101271798 44 TRVVPTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYD 98
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
44-98 |
1.38e-17 |
|
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: 76.95 E-value: 1.38e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1101271798 44 TRVVPTLCEMCGVKCGVLAHVRDGRVWRLTGNPRDPQSGGRLCARGNAGTKTLYD 98
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
610-710 |
3.53e-17 |
|
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: 78.87 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 610 THTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFGcrvplrHLAYn 689
Cdd:cd02780 13 NSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEHGYG------HWAY- 85
|
90 100
....*....|....*....|.
gi 1101271798 690 rganGGDLIPIMTAPVSGAAA 710
Cdd:cd02780 86 ----GAVASTIDGKDLPGDAW 102
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
101-478 |
7.31e-17 |
|
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: 84.28 E-value: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 101 RLKGPM-KRVGEGQFQPISWEQAFQEIGSKLKELKeqygPQSLVWLAHPEliSPLEKHFMA-----AFGSPNYTGHGPTC 174
Cdd:cd02767 64 RLTYPMrYDAGSDHYRPISWDEAFAEIAARLRALD----PDRAAFYTSGR--ASNEAAYLYqlfarAYGTNNLPDCSNMC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 175 YSSRNVAFEQMYG-GVPGV---DYRNVRYYIAFGRNLtgGIKNPDVQK-IVAAKAEGAHLVAVDPR----LSDFA----- 240
Cdd:cd02767 138 HEPSSVGLKKSIGvGKGTVsleDFEHTDLIFFIGQNP--GTNHPRMLHyLREAKKRGGKIIVINPLrepgLERFAnpqnp 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 241 --------YFADEWLPIRPGTDLAMVLAMINVLI-----NENLYDAAFVAAYTTGFEELKKGVSgyTPAWA--AGITGIE 305
Cdd:cd02767 216 esmltggtKIADEYFQVRIGGDIALLNGMAKHLIerddePGNVLDHDFIAEHTSGFEEYVAALR--ALSWDeiERASGLS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 306 AGTISRIARELAAAKPAAAVdpgW-HAVTgsQYGNSVQAGRAIAALNALLGNLGARGGLSLPptIKLGSP---AGIMG-- 379
Cdd:cd02767 294 REEIEAFAAMYAKSERVVFV---WgMGIT--QHAHGVDNVRAIVNLALLRGNIGRPGAGLMP--IRGHSNvqgDRTMGit 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 380 PKPPAATAPRWdgagSEKW--PLNKDHGM--IQTFpERVKQDQpypVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVVAI 455
Cdd:cd02767 367 EKPFPEFLDAL----EEVFgfTPPRDPGLdtVEAI-EAALEGK---VKAFISLGGNFAEAMPDPAATEEALRRLDLTVHV 438
|
410 420
....*....|....*....|....*.
gi 1101271798 456 DIQMNDTAYY---AHYILPEATYLER 478
Cdd:cd02767 439 ATKLNRSHLVhgeEALILPCLGRTEI 464
|
|
| 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 ... |
48-477 |
2.33e-16 |
|
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: 82.44 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTGnpRDPQS--GGRLCARGNAGTKTLYDPDRLKGPMKRVGeGQFQPISWEQAFQE 125
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVEN--RYNGAvnHYFLCDRGRFGYGYVNSRDRLTQPLIRRG-GTLVPVSWNEALDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 126 IGSKLKELKEQYGpqslvwlahpELISP---LEKHFMAAFGSPNYTGHGPTCYSSRNVAFEQM-YGGVPGVDYRNVRYYI 201
Cdd:cd02771 78 AAARLKEAKDKVG----------GIGSPrasNESNYALQKLVGAVLGTNNVDHRARRLIAEILrNGPIYIPSLRDIESAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 202 A---FGRNLTGgiKNPDVQKIV--AAKAEGAHLvAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLineNLYDAAFV 276
Cdd:cd02771 148 AvlvLGEDLTQ--TAPRIALALrqAARRKAVEL-AALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRL---DDIAAESI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 277 AAYTTGFEELKKGVSGYTPAWAAGITGIEAG-TISRIARELAAAKPAAAVdPGwhavTGSQYGNSVQAGRAIAalnALLG 355
Cdd:cd02771 222 RASPGGQARLGAALARAVDASAAGVSGLAPKeKAARIAARLTGAKKPLIV-SG----TLSGSLELIKAAANLA---KALK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 356 NLGARGGLSLpptikLGSPAGIMGPKPPAAtAPRWDGAGSEkwplnkdhGMIQTFpERVKqdqpypVKAVIIQHLNPVRS 435
Cdd:cd02771 294 RRGENAGLTL-----AVEEGNSPGLLLLGG-HVTEPGLDLD--------GALAAL-EDGS------ADALIVLGNDLYRS 352
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1101271798 436 STDSlAFIEALKKLDLVVAIDIQMNDTAYYAHYILPEATYLE 477
Cdd:cd02771 353 APER-RVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAE 393
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
599-721 |
2.89e-16 |
|
The MopB_CT_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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 75.48 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 599 FRLIQGHVPMHTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFG 678
Cdd:cd02785 4 LACIQRHSRFRVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQGWW 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1101271798 679 CRvplrhlaYNRGANGGDLI-----PIMTAPVSGAAAQCETLVTVRKA 721
Cdd:cd02785 84 SR-------YFQEGSLQDLTspfvnPVHEYIYGPNSAFYDTLVEVRKA 124
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
599-676 |
3.40e-15 |
|
The MopB_CT_DmsA-EC CD 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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 72.32 E-value: 3.40e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101271798 599 FRLIQGHVPMHTHTTTDNNSYLHAIMPeNELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHG 676
Cdd:cd02794 3 LQLIGWHYKRRTHSTFDNVPWLREAFP-QEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQG 79
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
48-477 |
1.03e-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: 76.55 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTgnPRDPQS--GGRLCARGNAGTKTLYDPDRLKGPMKRVGeGQFQPISWEQAFQE 125
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRIL--PRENEAinEEWISDKGRFGYDGLNSRQRLTQPLIKKG-GKLVPVSWEEALKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 126 IGSKLKElkeqYGPQSLVWLAHPelISPLE-----KHFMAAFGSPNytghgptcyssrnvafeqmyggvpgVDYRNVRY- 199
Cdd:cd02768 78 VAEGLKA----VKGDKIGGIAGP--RADLEslfllKKLLNKLGSNN-------------------------IDHRLRQSd 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 200 YIAFGRNLTGGIKNPDVQKIVAAKAegAHLVAVDPRlsdfayfaDEwLPIrpgtdlaMVLAMINVLINENLYDAAFVAAY 279
Cdd:cd02768 127 LPADNRLRGNYLFNTSIAEIEEADA--VLLIGSNLR--------KE-APL-------LNARLRKAVKKKGAKIAVIGPKD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 280 TTGFEELKKGVSgYTPAW-AAGITGIEAGTISRIARELAAAKPAAAVdpgwhavtgsqYGNSVQAGRAIAALNAlLGNLG 358
Cdd:cd02768 189 TDLIADLTYPVS-PLGASlATLLDIAEGKHLKPFAKSLKKAKKPLII-----------LGSSALRKDGAAILKA-LANLA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 359 ArgglslpptiKLGSPAGIMGPKPPAATAPRWDGAGSekwplnKDHGmiqtfperVKQDQPYPVKAVIIQHLNPVRSSTD 438
Cdd:cd02768 256 A----------KLGTGAGLWNGLNVLNSVGARLGGAG------LDAG--------LALLEPGKAKLLLLGEDELDRSNPP 311
|
410 420 430
....*....|....*....|....*....|....*....
gi 1101271798 439 SLAfieALKKLDLVVAIDIQMNDTAYYAHYILPEATYLE 477
Cdd:cd02768 312 AAV---ALAAADAFVVYQGHHGDTGAQADVILPAAAFTE 347
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
609-673 |
5.80e-14 |
|
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: 68.69 E-value: 5.80e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1101271798 609 HTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFL 673
Cdd:cd00508 17 HTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFM 81
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
609-673 |
7.30e-13 |
|
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. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 65.72 E-value: 7.30e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1101271798 609 HTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFL 673
Cdd:cd02790 17 HTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFM 81
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
608-720 |
2.73e-12 |
|
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: 64.17 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 608 MHTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFGcrvplrHLA 687
Cdd:cd02792 16 FHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIPYHWG------GMG 89
|
90 100 110
....*....|....*....|....*....|...
gi 1101271798 688 YNRGANGGDLIPIMTAPVSGAAAQCETLVTVRK 720
Cdd:cd02792 90 LVIGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
607-721 |
6.68e-12 |
|
The MopB_CT_2 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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239184 [Multi-domain] Cd Length: 156 Bit Score: 64.02 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 607 PMHT-HTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFGCRVP--- 682
Cdd:cd02783 11 PMAMyHSWGSQNAWLRQIHTRNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTETVEPGTVWTWNAIGKRPGawg 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1101271798 683 -------------LRHLAYNRGANGGDLIPIMTA-PVSGAAAQCETLVTVRKA 721
Cdd:cd02783 91 lkpdapesvkgflLNHLINDSLPPPGDAKRISNSdPVTGQAAWFDLRVRIVKA 143
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
599-676 |
1.03e-11 |
|
The MopB_CT_DMSOR-like 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. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 62.60 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 599 FRLIQGHVPMHTHTTTDNNSYLHAIMPEN---ELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAH 675
Cdd:cd02777 3 LQLISPHPKRRLHSQLDNVPWLREAYKVKgrePVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALPE 82
|
.
gi 1101271798 676 G 676
Cdd:cd02777 83 G 83
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
92-471 |
7.81e-10 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 62.37 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 92 GTKTLYDPDRLKGPMK-RVGEGQFQPISWEQAFQEIGSKLKELKEQYGPQSLVWLAHPELISPLEKHFMAAFGSPNYTGH 170
Cdd:PRK09939 99 GDHELEAAGRLTQPLKyDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDC 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 171 GPTCYSSRNVAFEQMYGGVPGV----DYRNVRYYIAFGRNltGGIKNPD-VQKIVAAKAEGAHLVAVDPR----LSDF-- 239
Cdd:PRK09939 179 SNMCHEPTSVGLAASIGVGKGTvlleDFEKCDLVICIGHN--PGTNHPRmLTSLRALVKRGAKMIAINPLqergLERFta 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 240 ------------AYFADEWLPIRPGTDLAMVLAMINVLINEN----------LYDAAFVAAYTTGFEELKKGVSGYTPAW 297
Cdd:PRK09939 257 pqnpfemltnseTQLASAYYNVRIGGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 298 AAGITGIEAGTISRIARELAAAKPAAAVdpgwHAVTGSQYGNSVQAGRAIAALNALLGNLGARGGLSLP----PTIKLGS 373
Cdd:PRK09939 337 IERISGLSQTQIAELADAYAAAERTIIC----YGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPlrghSNVQGDR 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 374 PAGIMgPKPPAATAPRWDGAGSEKWPLNKDHGMIQTFpERVKQDQpypVKAVIIQHLNPVRSSTDSLAFIEALKKLDLVV 453
Cdd:PRK09939 413 TVGIT-EKPSAEFLARLGERYGFTPPHAPGHAAIASM-QAICTGQ---ARALICMGGNFALAMPDREASAVPLTQLDLAV 487
|
410 420
....*....|....*....|..
gi 1101271798 454 AIDIQMND----TAYYAhYILP 471
Cdd:PRK09939 488 HVATKLNRshllTARHS-YILP 508
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
607-710 |
1.14e-09 |
|
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: 56.93 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 607 PMHTHTTTDNNSYLH----------AIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHG 676
Cdd:cd02781 3 PLILTTGARSYYYFHsehrqlpslrELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHG 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 1101271798 677 --FGCRVPLRHLAYNR-GANGGDLIPI-MTAPVSGAAA 710
Cdd:cd02781 83 wwYPEREAGEPALGGVwESNANALTSDdWNDPVSGSSP 120
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
609-707 |
5.49e-09 |
|
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: 54.50 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 609 HTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFGCRvplrhLAY 688
Cdd:cd02791 17 HTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFVPMHWGDQ-----FGR 91
|
90
....*....|....*....
gi 1101271798 689 NRGANGgdLIPIMTAPVSG 707
Cdd:cd02791 92 SGRVNA--LTLDATDPVSG 108
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
616-721 |
6.68e-09 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 54.71 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 616 NNSYLHAIM------PENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFGCRVP-LRHLAY 688
Cdd:cd02782 16 NNSWLHNDPrlvkgrNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYPgVSGAGS 95
|
90 100 110
....*....|....*....|....*....|....
gi 1101271798 689 NRGANGGDLI-PIMTAPVSGAAAQCETLVTVRKA 721
Cdd:cd02782 96 RPGVNVNDLTdDTQRDPLSGNAAHNGVPVRLARV 129
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
193-268 |
7.91e-09 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 59.06 E-value: 7.91e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101271798 193 DYRNVRYYIAFGRN--LTggiKNPDVQKIVAAKAEGAHLVAVDPRLSDFAYFADEWLPIRPGTDLAMVLAMINVLINE 268
Cdd:COG5013 246 DWYNSGYLIMWGSNvpQT---RTPDAHFMTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKE 320
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
48-166 |
2.64e-07 |
|
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: 53.51 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWRLTgnPRDPQS--GGRLCARGNAGTKTLYDPDRLKGPMKRVGeGQFQPISWEQAFQE 125
Cdd:cd02772 1 KSVSPHDALGSNLVVHVKNNKVMRVV--PRENEAinECWLSDRDRFSYEGLNSEDRLTKPMIKKD-GQWQEVDWETALEY 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1101271798 126 IGSKLKELKEQYGPQSLVWLAHPEliSPLE-----KHFMAAFGSPN 166
Cdd:cd02772 78 VAEGLSAIIKKHGADQIGALASPH--STLEelyllQKLARGLGSDN 121
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
599-718 |
3.22e-05 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 43.81 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 599 FRLIQGHVPMHTHTTTDNNSYLHAIMPENELWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHGFg 678
Cdd:cd02786 3 LRLITPPAHNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGGW- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1101271798 679 crvPLRHLAYNRGANGgdLIPIMTAPVSGAAAQCETLVTV 718
Cdd:cd02786 82 ---WREHSPDGRGVNA--LTSARLTDLGGGSTFHDTRVEV 116
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
599-705 |
1.62e-04 |
|
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. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 42.36 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101271798 599 FRLIQGHVPMHTHTTTDNNSY---LHAIMPEneLWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAH 675
Cdd:cd02776 2 LNYLTPHGKWSIHSTYRDNLLmlrLQRGGPV--VWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYH 79
|
90 100 110
....*....|....*....|....*....|..
gi 1101271798 676 GFG--CRVPLRHLAYNRGANGGDLIPIMTAPV 705
Cdd:cd02776 80 AQErhVNVPGSKLTGKRGGIHNSVTRVRIKPT 111
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
629-676 |
5.94e-04 |
|
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.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 40.31 E-value: 5.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1101271798 629 LWIHTSRAGKLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVFLAHG 676
Cdd:cd02793 35 IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLPTG 82
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
101-168 |
9.45e-04 |
|
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: 42.25 E-value: 9.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1101271798 101 RLKGPMKRvGEGQFQPISWEQAFQEIGSKLKELKeqygPQSLVWLAHPelISPLE-----KHFMAAFGSPNYT 168
Cdd:cd02773 53 RLDKPYIR-KNGKLKPATWEEALAAIAKALKGVK----PDEIAAIAGD--LADVEsmvalKDLLNKLGSENLA 118
|
|
| TAT_signal |
pfam10518 |
TAT (twin-arginine translocation) pathway signal sequence; |
5-26 |
9.94e-04 |
|
TAT (twin-arginine translocation) pathway signal sequence;
Pssm-ID: 463131 [Multi-domain] Cd Length: 26 Bit Score: 36.97 E-value: 9.94e-04
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
638-672 |
1.10e-03 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 39.45 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*
gi 1101271798 638 KLGIKTGDLVEVASKVGKVRVKARVTEAIHPEAVF 672
Cdd:COG1153 42 KLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVF 76
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
48-124 |
2.74e-03 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 41.08 E-value: 2.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101271798 48 PTLCEMCGVKCGVLAHVRDGRVWR-LTGNprDPQSGGR-LCARGNAGTKTLYDPDRLKGPMKRVGEGQFQPISWEQAFQ 124
Cdd:PRK07860 225 PSVCEHCASGCAQRTDHRRGKVLRrLAGD--DPEVNEEwNCDKGRWAFTYATQPDRITTPLVRDEDGELEPASWSEALA 301
|
|
| |
