|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
7-534 |
0e+00 |
|
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: 678.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 7 SACPLNCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQN---GEFVRISWEQALDE 83
Cdd:cd02766 2 SVCPLDCPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGrkgGQWERISWDEALDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 84 IADKLREIKETSETTAVLHsHDYANNGLLKALDQR-FFNGYGGVTEIVGSICWGSGIEAQSWDFGRSYGHGPLDIYNSKH 162
Cdd:cd02766 82 IAAKLKEIKAEYGPESILP-YSYAGTMGLLQRAARgRFFHALGASELRGTICSGAGIEAQKYDFGASLGNDPEDMVNADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 163 VVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDETFISEHS 242
Cdd:cd02766 161 IVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRDFLARHT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 243 VGFDDVKELLKTVSLEEFIVKTETSMEDLEYLAGLYAD-GPVSTFMGLGMQRYKNGGGTIRWIDALVAASGNVGIKGGGA 321
Cdd:cd02766 241 EGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEaKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 322 NFGNVQigesfaktkltlpelkttsrsfsmmtqaeevltaadPAIEMIIVTCGNPLTQVPNTNKVRQ-AFEKVPMTVAID 400
Cdd:cd02766 321 FYSNSG------------------------------------PPVKALWVYNSNPVAQAPDSNKVRKgLAREDLFVVVHD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 401 SIMTDTAELCDYVLPTATVFEEEDIYYsSMYHHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGE-LFEYSTQEFLEMG 479
Cdd:cd02766 365 QFMTDTARYADIVLPATTFLEHEDVYA-SYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEpPFEESDEEWLDQA 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 806801541 480 LSSLEAEDVTLERLKEKGHLPLPVKQVPWDDYQFLTPSGKFEFTSSLAEQKGFSG 534
Cdd:cd02766 444 LDGTGLPLEGIDLERLLGPRKAGFPLVAWEDRGFPTPSGKFEFYSERAAKRGLPP 498
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
1-667 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 579.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 1 MSKVHQSACPlNCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMK----KQNGEFVRIS 76
Cdd:COG0243 20 GTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKrvgpRGSGKFERIS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 77 WEQALDEIADKLREIKETSETTAVLHSHDYANNGLLKA----LDQRFFNGYG--GVTEiVGSICWGSGIEAQSWDFGRSY 150
Cdd:COG0243 99 WDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNeaayLAQRFARALGtnNLDD-NSRLCHESAVAGLPRTFGSDK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 151 GHGPL-DIYNSKHVVVWGRNVSRTNMHLYHHLQQ-VKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLI 228
Cdd:COG0243 178 GTVSYeDLEHADLIVLWGSNPAENHPRLLRRLREaAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 229 EMGRTDETFISEHSVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLAGLYAD-GPVSTFMGLGMQRYKNGGGTIRWIDAL 307
Cdd:COG0243 258 EEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATaKPAVILWGMGLQQHSNGTQTVRAIANL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 308 VAASGNVGIKGGGANFGNvqigesfaktkltlpelkttsrsfsmmtqAEEVLTAADPAIEMIIVTCGNPLTQVPNTNKVR 387
Cdd:COG0243 338 ALLTGNIGKPGGGPFSLT-----------------------------GEAILDGKPYPIKALWVYGGNPAVSAPDTNRVR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 388 QAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIYYSSmYHHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGEL 467
Cdd:COG0243 389 EALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNS-EDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 468 F--EYSTQEFLEMGLSSLEAEDVTLERLKEKGHLPLPVKQVP--WDDYQFLTPSGKFEFTSSLAEqkgFSGSLQLNVPEE 543
Cdd:COG0243 468 FpwGRTEEDYLRELLEATRGRGITFEELREKGPVQLPVPPEPafRNDGPFPTPSGKAEFYSETLA---LPPLPRYAPPYE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 544 SVfhnEELAGKYPYTLLSIHPQRSNHSQH--VPFIEKLQHV-QVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQ 620
Cdd:COG0243 545 GA---EPLDAEYPLRLITGRSRDQWHSTTynNPRLREIGPRpVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEG 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 806801541 621 AHAKTINIDEGMWAAF----GGSVNALTNDTNSDNGMGSTLFDCLVGLKKA 667
Cdd:COG0243 622 IRPGVVFAPHGWWYEPaddkGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
7-462 |
1.76e-116 |
|
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: 353.17 E-value: 1.76e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 7 SACPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQN--GEFVRISWEQALDEI 84
Cdd:cd00368 2 SVCPF-CGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 85 ADKLREIKETSETTAVL-HSHDYANNGLLKALDQRFFNGYGGVTEIVGSICWGSGIEAQSWDFGRSYGHGPLDIYNSKHV 163
Cdd:cd00368 81 AEKLKEIREKYGPDAIAfYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 164 VVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAvlkvliemgrtdetfisehsv 243
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA--------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 244 gfddvkellktvslEEFIVKTETSMEDLEYLAGLYAD-GPVSTFMGLGMQRYKNGGGTIRWIDALVAASGNVGIKGGGAN 322
Cdd:cd00368 220 --------------EWAAEITGVPAETIRALAREFAAaKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 323 FGnvqigesfaktkltlpelkttsrsfsmmtqaeevltaadpaiemiivtcGNPLTQVPNTNKVRQAFEKVPMTVAIDSI 402
Cdd:cd00368 286 PG-------------------------------------------------GNPLVSAPDANRVRAALKKLDFVVVIDIF 316
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 403 MTDTAELCDYVLPTATVFEEEDIYYSsmYHHYVQYGKKLVEPQGEAKSDSWIWSELAKRL 462
Cdd:cd00368 317 MTETAAYADVVLPAATYLEKEGTYTN--TEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
3-646 |
1.39e-107 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 340.71 E-value: 1.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 3 KVHQSACPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNGEFVRISWEQALD 82
Cdd:COG3383 5 KKVKTVCPY-CGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 83 EIADKLREIKET--SETTAVLHSHDYAN--NGLLkaldQRFFNGYGGVTEI--VGSICWGSGIEAQSWDFGRSYGHGPL- 155
Cdd:COG3383 84 LVAERLREIQAEhgPDAVAFYGSGQLTNeeNYLL----QKLARGVLGTNNIdnNARLCMASAVAGLKQSFGSDAPPNSYd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 156 DIYNSKHVVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDE 235
Cdd:COG3383 160 DIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 236 TFISEHSVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLAGLYADGPVSTFM-GLGMQRYKNGGGTIRWIDALVAASGNV 314
Cdd:COG3383 240 DFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILwGMGVNQHTQGTDNVNAIINLALATGNI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 315 GIKGGGANF----GNVQ----------------------IGESFAKTKLTLPELKTTSRSFSMMTQAeevltAADPAIEM 368
Cdd:COG3383 320 GRPGTGPFPltgqNNVQggrdmgalpnvlpgyrdvtdpeHRAKVADAWGVPPLPDKPGLTAVEMFDA-----IADGEIKA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 369 IIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIYYSSMYHhyVQYGKKLVEPQGEA 448
Cdd:COG3383 395 LWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERR--VQRVRKAVEPPGEA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 449 KSDSWIWSELAKRLGFGelFEYSTQE--FLEMGLSSLEAEDVTLERLKEKGHL--PLPVKQVPWDDY----QFLTPSGKF 520
Cdd:COG3383 473 RPDWEIIAELARRLGYG--FDYDSPEevFDEIARLTPDYSGISYERLEALGGVqwPCPSEDHPGTPRlftgRFPTPDGKA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 521 EFtsslaeqkgfsgslqlnVPEESVFHNEELAGKYPYTL----LSIHPQRSNHSQHVPFIEKLQ-HVQVDISPDIAAGQD 595
Cdd:COG3383 551 RF-----------------VPVEYRPPAELPDEEYPLVLttgrLLDQWHTGTRTRRSPRLNKHApEPFVEIHPEDAARLG 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 806801541 596 LQDGDEVVIFNDRGSMKGKVKVmkqahakTINIDEGM-WAAF---GGSVNALTND 646
Cdd:COG3383 614 IKDGDLVRVSSRRGEVVLRARV-------TDRVRPGTvFMPFhwgEGAANALTND 661
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
9-532 |
2.79e-94 |
|
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: 299.61 E-value: 2.79e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 9 CPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQN----GEFVRISWEQALDEI 84
Cdd:cd02759 4 CPG-CHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGergeNKWERISWDEALDEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 85 ADKLREIKETS--ETTAVLHSHDYANNGLLKALDQRFFNGYG-GVTEIVGSICWGSGIEAQSW--DFGRSYGHgpLDIYN 159
Cdd:cd02759 83 AEKLAEIKAEYgpESIATAVGTGRGTMWQDSLFWIRFVRLFGsPNLFLSGESCYWPRDMAHALttGFGLGYDE--PDWEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 160 SKHVVVWGRNVSRTNMHLY-HHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDETFI 238
Cdd:cd02759 161 PECIVLWGKNPLNSNLDLQgHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKDFV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 239 SEHSVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLAGLYADGPVSTF-MGLGMQRYKNGGGTIRWIDALVAASGNVGIK 317
Cdd:cd02759 241 ENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIqWGLAIDQQKNGTQTSRAIAILRAITGNLDVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 318 GGGanfgnvqigesfaktkLTLPelkttsrsfsmmtqaeevltaadPAIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTV 397
Cdd:cd02759 321 GGN----------------LLIP-----------------------YPVKMLIVFGTNPLASYADTAPVLEALKALDFIV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 398 AIDSIMTDTAELCDYVLPTATVFEEEDIYYSSMYHHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGELFEYstqefle 477
Cdd:cd02759 362 VVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAENFVQLRQKAVEPYGEAKSDYEIVLELGKRLGPEEAEYY------- 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 806801541 478 mglssleaedvtlerlKEKGHLPLPVKQVPwddyqFLTPSGKFEFTSSLAEQKGF 532
Cdd:cd02759 435 ----------------KYEKGLLRPDGQPG-----FNTPTGKVELYSTMLEELGY 468
|
|
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
3-644 |
1.52e-87 |
|
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: 290.52 E-value: 1.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 3 KVHQSACPLNCWDSCGFLVTVDDGKVTKVDGD-------PNHPItegKICGRGRMLETKTNSPDRLRYPM----KKQNGE 71
Cdd:TIGR02166 43 KVVWSACTVNCGSRCPLRVHVKDGEITRIETDntgddeyGNHQV---RACLRGRSMRRRVYNPDRLKYPMkrvgKRGEGK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 72 FVRISWEQALDEIADKLREIKETSETTAVLHSHDYANNG------LLKALDQRFFNGYGGVTEIVGSICWGSGIEAQSWD 145
Cdd:TIGR02166 120 FERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTGgtmsrsWPPTAVARLLNLCGGYLNQYGSYSTAQINEAMPYT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 146 FGRSY-GHGPLDIYNSKHVVVWGRNVSRTNM----HLYHHLQQVKKKGATITVIDPIFNPT-AKLADRYISVKPGMDGWL 219
Cdd:TIGR02166 200 YGISAdGSSLDDIENSKLVVMFGNNPAETRMsgggQTYYFLQALEKSNARVIVIDPRYTDTvAGREDEWIPIRPGTDAAL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 220 AAAVLKVLIEMGRTDETFISEHSVGFDdvKELL-----KTVSLEEFIV-----KTETSMEDLEYLAGLYAD--------- 280
Cdd:TIGR02166 280 VAAIAYVMISENLHDQAFLDRYCVGFD--EKTLpasapKNGSYKDYILgegadGTPKTPEWASKITGIPADtiiklarei 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 281 ---GPVSTFMGLGMQRYKNGGGTIRWIDALVAASGNVGIKGG--GANFGNVQIgeSFAKTkLTLPELKTTSRSFSMMTQA 355
Cdd:TIGR02166 358 gnaKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGnnGAREGNYSL--PFARM-PELPNPVKTSISCFLWTDA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 356 EE---VLTAA----------DPAIEMIIVTCGNPL-TQVPN---TNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTAT 418
Cdd:TIGR02166 435 IDrgtEMTAIkdgvrgkdklDSNIKFLWNYAGNCLiNQHSDinrTHKILQDESKCEMIVVIDNHMTSSAKYADILLPDTT 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 419 VFEEEDI----YYSSMyhHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGELF-EYSTQ-EFLEMGLSSLEAEDVTL-- 490
Cdd:TIGR02166 515 TLEQNDFiedsYASNM--SYLIFMQKAIEPLFECKPIYDMLSEVAKRLGVEAEFtEGRTQeEWLEHLYAQTRAADPALps 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 491 -ERLKEKGHLPLPVKQVP---WDDYQ-------FLTPSGKFEFTSSLAEQKGFSGSLQLN-----VPE-----ESVfhNE 549
Cdd:TIGR02166 593 fAELRKQGIYKAKSAPGPfvaFEDFRrdpeanpLKTPSGKIEIYSERLAQIAHTWELPEGdvitpLPEyvptfEGP--DD 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 550 ELAGKYPYTLLSIHPQRSNHSQH--VPFIEKLQHVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTIN 627
Cdd:TIGR02166 671 PLRKDFPLQLTGFHYKGRTHSTYgnVDWLREAAPQELWINPIDAQKRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVA 750
|
730 740
....*....|....*....|....
gi 806801541 628 IDEGMWAA-------FGGSVNALT 644
Cdd:TIGR02166 751 LGQGAWYQpdkngidVGGCINTLT 774
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
6-527 |
2.62e-87 |
|
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: 285.37 E-value: 2.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 6 QSACPLNCWDSCGFLVTVDDGKVTKVDGDPNHPITEG----KICGRGRMLETKTNSPDRLRYPMKKQN----GEFVRISW 77
Cdd:cd02770 1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGfhqiRACLRGRSQRKRVYNPDRLKYPMKRVGkrgeGKFVRISW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 78 EQALDEIADKLREIKETSETTAVLH---SHDYANNGLLKALDQRFFNGYGGVTEIVGSICWGSGIEAQSWDFGRS-YGHG 153
Cdd:cd02770 81 DEALDTIASELKRIIEKYGNEAIYVnygTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAaSGSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 154 PLDIYNSKHVVVWGRNVSRTNM---HLYHHLQQVKKKGATITVIDPIFNPTAK-LADRYISVKPGMDGWLAAAVLKVLIE 229
Cdd:cd02770 161 LDDLKDSKLVVLFGHNPAETRMgggGSTYYYLQAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 230 MGRTDETFISEHSVGFDDvKELLKTVSLEEfivktetSMEDleYLAGLYADG---------------------------- 281
Cdd:cd02770 241 ENLHDQAFLDRYCVGFDA-EHLPEGAPPNE-------SYKD--YVLGTGYDGtpktpewaseitgvpaetirrlareiat 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 282 --PVSTFMGLGMQRYKNGGGTIRWIDALVAASGNVGIKGGgaNFGNVQIGESFAKTklTLPELKT---TSRSFSMMTQA- 355
Cdd:cd02770 311 tkPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGG--NTGARPGGSAYNGA--GLPAGKNpvkTSIPCFMWTDAi 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 356 --EEVLTAADPA----------IEMIIVTCGNPLT-QVPN----TNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTAT 418
Cdd:cd02770 387 erGEEMTADDGGvkgadklksnIKMIWNYAGNTLInQHSDdnntTRALLDDESKCEFIVVIDNFMTPSARYADILLPDTT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 419 VFEEEDIYYSSMY--HHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGELFEY--STQEFLEMGLSSL---EAEDVTLE 491
Cdd:cd02770 467 ELEREDIVLTSNAgmMEYLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEgkTEQEWLEELYGQTrakEPGLPTYE 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 806801541 492 RLKEKG----HLPLPVkqVPWDDYQ-------FLTPSGKFE-FTSSLA 527
Cdd:cd02770 547 EFREKGiyrvPRALPF--VAFEDFRedpennpLKTPSGKIEiYSKALA 592
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
9-654 |
8.13e-86 |
|
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: 282.82 E-value: 8.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 9 CPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNGEFVRISWEQALDEIADKL 88
Cdd:TIGR01591 3 CPY-CGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSWDEAISYIAEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 89 REIKET--SETTAVLHSHDYAN--NGLLkaldQRFFNGYGGVTEI--VGSICWGSGIEAQSWDFGRSYGHGPL-DIYNSK 161
Cdd:TIGR01591 82 KEIKEKygPDSIGFIGSSRGTNeeNYLL----QKLARAVIGTNNVdnCARVCHGPSVAGLKQTVGIGAMSNTIsEIENAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 162 HVVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDETFISEH 241
Cdd:TIGR01591 158 LIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFIEKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 242 SVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLAGLYADGP-VSTFMGLGMQRYKNGGGTIRWIDALVAASGNVGIKGGG 320
Cdd:TIGR01591 238 TEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGsAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 321 AN----FGNVQIGESFAKTKLTLPELKTTSRSFSMMTQA-----------------EEVLTAADPAIEMIIVTCGNPLTQ 379
Cdd:TIGR01591 318 VNplrgQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAkawgvvklpaepglripEMIDAAADGDVKALYIMGEDPLQS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 380 VPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIYYSSmyHHYVQYGKKLVEPQGEAKSDSWIWSELA 459
Cdd:TIGR01591 398 DPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNA--ERRIQRFFKAVEPKGESKPDWEIIQELA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 460 KRLGFGELFEYSTQEFLEMGLSSLEAEDVTLERLKEKGHLPLPVKQVPWDDY------QFLTPSGKFEFtsslaeqkgfs 533
Cdd:TIGR01591 476 NALGLDWNYNHPQEIMDEIRELTPLFAGLTYERLDELGSLQWPCNDSDASPTsylykdKFATPDGKAKF----------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 534 gslqlnVPEESVFHNEELAGKYPYTLLSI----HPQRSNHSQHVPFIEKL-QHVQVDISPDIAAGQDLQDGDEVVIFNDR 608
Cdd:TIGR01591 545 ------IPLEWVAPIEEPDDEYPLILTTGrvltHYNVGEMTRRVAGLRRLsPEPYVEINTEDAKKLGIKDGDLVKVKSRR 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 806801541 609 GSMKGKVKVMKQAHAKTINIdeGMWAAFgGSVNALTNDtNSDNGMG 654
Cdd:TIGR01591 619 GEITLRAKVSDRVNKGAIYI--TMHFWD-GAVNNLTTD-DLDPISG 660
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
17-527 |
2.71e-85 |
|
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: 279.88 E-value: 2.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 17 CGFLVTVDDGKVTKVDGDPNHPItegKICGRGRMLETKTNSPDRLRYPMKKQ--------------NGEFVRISWEQALD 82
Cdd:cd02751 7 GPFKAHVKDGVIVRVEPDDTDQP---RPCPRGRSVRDRVYSPDRIKYPMKRVgwlgngpgsrelrgEGEFVRISWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 83 EIADKLREIKETSETTAVL-HSHDYANNGLL---KALDQRFFNGYGGVTEIVGSICWGSGIEAQSWDFGRS--YGHGPL- 155
Cdd:cd02751 84 LVASELKRIREKYGNEAIFgGSYGWASAGRLhhaQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSDevYEQGTSw 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 156 -DIY-NSKHVVVWGRNVSRTNM-------H-LYHHLQQVKKKGATITVIDPIFNPTAK-LADRYISVKPGMDGWLAAAVL 224
Cdd:cd02751 164 dDIAeHSDLVVLFGANPLKTRQgggggpdHgSYYYLKQAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 225 KVLIEMGRTDETFISEHSVGFDDVKELL--------KTVSLEEFIvkTETSMEDLEYLAGLYADGPVSTFMGLGMQRYKN 296
Cdd:cd02751 244 HTLITEDLHDQAFLARYTVGFDEFKDYLlgesdgvpKTPEWAAEI--TGVPAETIRALAREIASKRTMIAQGWGLQRAHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 297 GGGTIRWIDALVAASGNVGIKGGGANFG----NVQIGESFAKTKLTLPELKTTSRSF---SMMTQA----EEVLTAA--- 362
Cdd:cd02751 322 GEQPAWMLVTLAAMLGQIGLPGGGFGFGygysNGGGPPRGGAGGPGLPQGKNPVKDSipvARIADAllnpGKEFTANgkl 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 363 --DPAIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIYYSSMY-HHYVQYGK 439
Cdd:cd02751 402 ktYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNYsNRYLIAMK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 440 KLVEPQGEAKSDSWIWSELAKRLGFGELFEY--STQEFLEMGLSSLEAEDV-------TLERLKEKGHLPLPVKQVPW-- 508
Cdd:cd02751 482 QAVEPLGEARSDYEIFAELAKRLGVEEEFTEgrDEMEWLEHLYEETRAKAAgpgpelpSFEEFWEKGIVRVPAAPKPFva 561
|
570 580
....*....|....*....|....*...
gi 806801541 509 -DDYQ-------FLTPSGKFE-FTSSLA 527
Cdd:cd02751 562 fADFRedpeanpLGTPSGKIEiYSETLA 589
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
6-519 |
3.12e-80 |
|
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: 265.24 E-value: 3.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 6 QSACPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPM-KKQNGEFVRISWEQALDEI 84
Cdd:cd02754 1 KTTCPY-CGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLlRRNGGELVPVSWDEALDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 85 ADKLREIKE--TSETTAVLHSHD------YANNGLLKAldqrFF--NGYGGVTEivgsICWGSGIEAqswdFGRSYGH-- 152
Cdd:cd02754 80 AERFKAIQAeyGPDSVAFYGSGQllteeyYAANKLAKG----GLgtNNIDTNSR----LCMASAVAG----YKRSFGAdg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 153 --GPL-DIYNSKHVVVWGRNVSrtNMH--LYHHLQQVKKK--GATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLK 225
Cdd:cd02754 148 ppGSYdDIEHADCFFLIGSNMA--ECHpiLFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 226 VLIEMGRTDETFISEHSVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLAGLYADGP--VSTF-MGLGmQRYkNGGGTIR 302
Cdd:cd02754 226 VLIEEGLIDRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARkvMSLWtMGVN-QST-QGTAANN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 303 WIDALVAASGNVGIKGGGAN----------------------FGNVQIGES---FAKTKLTLPELKTTSR----SFSMMT 353
Cdd:cd02754 304 AIINLHLATGKIGRPGSGPFsltgqpnamggrevgglanllpGHRSVNNPEhraEVAKFWGVPEGTIPPKpglhAVEMFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 354 QAEevltaaDPAIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDS-IMTDTAELCDYVLPTATVFEEEDIYYSSmyH 432
Cdd:cd02754 384 AIE------DGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEYADLVLPAASWGEKEGTMTNS--E 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 433 HYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGELFEYSTQE--FLEMGLSS----LEAEDVTLERLKEKG-HLPLPVKQ 505
Cdd:cd02754 456 RRVSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYTSPEevFEEYRRLSrgrgADLSGLSYERLRDGGvQWPCPDGP 535
|
570
....*....|....*....
gi 806801541 506 VP-----WDDYQFLTPSGK 519
Cdd:cd02754 536 PEgtrrlFEDGRFPTPDGR 554
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
9-522 |
4.95e-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: 263.30 E-value: 4.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 9 CPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNGEFVRISWEQALDEIADKL 88
Cdd:cd02753 4 CPY-CGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEALSLVASRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 89 REIKET--SETTAVLHSHDYAN--NGLLkaldQRFfngyggVTEIVGS--------ICWGSGIEAQSWDFGRSYGHGPL- 155
Cdd:cd02753 83 KEIKDKygPDAIAFFGSAKCTNeeNYLF----QKL------ARAVGGTnnvdhcarLCHSPTVAGLAETLGSGAMTNSIa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 156 DIYNSKHVVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDE 235
Cdd:cd02753 153 DIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 236 TFISEHSVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLAGLYAD-GPVSTFMGLGMQRYKNGGGTIRWIDALVAASGNV 314
Cdd:cd02753 233 EFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATaKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 315 GIKGGGAN----FGNVQIGESFAKTKLTLPELkttsrsfsmmtqaeevltaadpaIEMIIVTCGNPLTQVPNTNKVRQAF 390
Cdd:cd02753 313 GRPGTGVNplrgQNNVQGACDMGALPNVLPGY-----------------------VKALYIMGENPALSDPNTNHVRKAL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 391 EKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIYYSSMyhHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGELFEY 470
Cdd:cd02753 370 ESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTE--RRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSH 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 806801541 471 STQEFLEMGLSSLEAEDVTLERLKEKGHLPLPVkqvpWDD----------YQFLTPSGKFEF 522
Cdd:cd02753 448 PEEIFDEIARLTPQYAGISYERLERPGGLQWPC----PDEdhpgtpilhtERFATPDGKARF 505
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
8-521 |
1.86e-76 |
|
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: 254.63 E-value: 1.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 8 ACPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNGEFVRISWEQALDEIADK 87
Cdd:cd02762 3 ACIL-CEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGSFEEIDWDEAFDEIAER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 88 LREIKETSETTAVL------HSHDYAN----NGLLKALDQRFFNGYGGVTEIVGsicwgsgiEAQSWDFGRSYGHGPL-D 156
Cdd:cd02762 82 LRAIRARHGGDAVGvyggnpQAHTHAGgaysPALLKALGTSNYFSAATADQKPG--------HFWSGLMFGHPGLHPVpD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 157 IYNSKHVVVWGRN--VS----RTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEM 230
Cdd:cd02762 154 IDRTDYLLILGANplQSngslRTAPDRVLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 231 GRTDETFISEHSVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLA-GLYADGPVSTFMGLGMQRYKNGGGTIRWIDALVA 309
Cdd:cd02762 234 GLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLArEFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 310 ASGNVGiKGGGANFgnvqigESFAKTKLTLPELKTTSRSF-----SMM----------TQAEEVLTAADPAIEMIIVTCG 374
Cdd:cd02762 314 LTGNLD-RPGGAMF------TTPALDLVGQTSGRTIGRGEwrsrvSGLpeiagelpvnVLAEEILTDGPGRIRAMIVVAG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 375 NPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEE--DIYYSSMYHHYVQYGKKLVEPQGEAKSDS 452
Cdd:cd02762 387 NPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPhaTFFNLEFPRNAFRYRRPLFPPPPGTLPEW 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806801541 453 WIWSELAK------RLGFgelfeystqefleMGLSSLeaEDVTLERLKEKGHlPLPVKQVPWDDYQFL-TPSGKFE 521
Cdd:cd02762 467 EILARLVEaldavlRAGF-------------YGERAG--GTLLLAALLERPS-GVDLGPLTPRLWQRLrTPDGRIH 526
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
3-666 |
1.71e-64 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 227.99 E-value: 1.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 3 KVHQSACPLNCWDSCGFLVTVDDGKVTKVD----GDPNHP-ITEGKICGRGRMLETKTNSPDRLRYPMKK----QNGEFV 73
Cdd:PRK14990 57 KVIWSACTVNCGSRCPLRMHVVDGEIKYVEtdntGDDNYDgLHQVRACLRGRSMRRRVYNPDRLKYPMKRvgarGEGKFE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 74 RISWEQALDEIADKL-REIKETSETTAVLHSHDYANNGLL-------KALDQRFFNGYGGVTEIVGSICWGSGIEAQSWD 145
Cdd:PRK14990 137 RISWEEAYDIIATNMqRLIKEYGNESIYLNYGTGTLGGTMtrswppgNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 146 FGR-SYGHGPLDIYNSKHVVVWGRNVSRTNMH---LYHHLQQVKKKG-ATITVIDPIFNPT-AKLADRYISVKPGMDGWL 219
Cdd:PRK14990 217 YGGwADGNSPSDIENSKLVVLFGNNPGETRMSgggVTYYLEQARQKSnARMIIIDPRYTDTgAGREDEWIPIRPGTDAAL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 220 AAAVLKVLIEMGRTDETFISEHSVGFDDvKEL---------LKTVSLEEFIVKTETSMEDLEYLAGLYAD---------- 280
Cdd:PRK14990 297 VNGLAYVMITENLVDQPFLDKYCVGYDE-KTLpasapknghYKAYILGEGPDGVAKTPEWASQITGVPADkiiklareig 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 281 --GPVSTFMGLGMQRYKNGGGTIRWIDALVAASGNVGIKGG--GANFGNVQIgeSFAKTKlTLPELKTTSRSFSMMTQAE 356
Cdd:PRK14990 376 stKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGnsGAREGSYSL--PFVRMP-TLENPIQTSISMFMWTDAI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 357 E---VLTA----------ADPAIEMIIVTCGNPL----TQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATV 419
Cdd:PRK14990 453 ErgpEMTAlrdgvrgkdkLDVPIKMIWNYAGNCLinqhSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTA 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 420 FEEEDIYY--SSMYHHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGELF-EYSTQEFLEMGLSSLEAEDV----TLER 492
Cdd:PRK14990 533 SEQMDFALdaSCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFtEGRTQEEWMRHLYAQSREAIpelpTFEE 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 493 LKEKGHLPLPVKQ---VPW----DDYQ---FLTPSGKFE-FTSSLAEqkgFSGSLQLnvPEESVF------------HNE 549
Cdd:PRK14990 613 FRKQGIFKKRDPQghhVAYkafrEDPQanpLTTPSGKIEiYSQALAD---IAATWEL--PEGDVIdplpiytpgfesYQD 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 550 ELAGKYPYTLLSIHPQRSNHSQH--VPFIEKLQHVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTIN 627
Cdd:PRK14990 688 PLNKQYPLQLTGFHYKSRVHSTYgnVDVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVA 767
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 806801541 628 IDEGMWAA-------FGGSVNALTNDTNSDNGMGSTLFDCLVGLKK 666
Cdd:PRK14990 768 LGEGAWYDpdakrvdKGGCINVLTTQRPSPLAKGNPSHTNLVQVEK 813
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
7-522 |
1.23e-63 |
|
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: 220.81 E-value: 1.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 7 SACPLNCWDSCGFLVTVDDGKVTKVDG----DPNHPitegKICGRGRMLETKTNSPDRLRYPMKKQ----NGEFVRISWE 78
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPnewpDKTYK----RGCTRGLSHLQRVYSPDRLKYPMKRVgergEGKFERITWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 79 QALDEIADKLREIKETSETTAVLHSHDYANNGLLKALDQRFFNGYGGVTEIVG-SICWGSGIEAQSWDFGRSYGHGPLDI 157
Cdd:cd02765 78 EALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRLALLGGGLQDALTYGiDTGVGQGFNRVTGGGFMPPTNEITDW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 158 YNSKHVVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDETF 237
Cdd:cd02765 158 VNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 238 ISEHS-----VGFDDVK-----ELLKTVSLEEFIV-----------------------------KTETSMEDL------- 271
Cdd:cd02765 238 LKSNTsapflVREDNGTllrqaDVTATPAEDGYVVwdtnsdspepvaatninpalegeytingvKVHTVLTALreqaasy 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 272 ----------------EYLAGLYADGPVSTFMGL-GMQRYKNGGGTIRWIDALVAASGNVGIKGGGAnfGNvqigesfak 334
Cdd:cd02765 318 ppkaaaeicgleeaiiETLAEWYATGKPSGIWGFgGVDRYYHSHVFGRTAAILAALTGNIGRVGGGV--GQ--------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 335 tkltlpelkttsrsfsmmtqaeevltaadpaIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVL 414
Cdd:cd02765 387 -------------------------------IKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVDIFHTPTVRYADIVL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 415 PTATVFEEEDIYYSSMYHHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGELFEYSTQEFLEMGLSSLEA--EDVTLER 492
Cdd:cd02765 436 PAAHWFEVEDLLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFPKTPEDYVRAFMNSDDPalDGITWEA 515
|
570 580 590
....*....|....*....|....*....|....*.
gi 806801541 493 LKEKGHLPL------PVkqVPWDDYQFLTPSGKFEF 522
Cdd:cd02765 516 LKEEGIIMRlatpedPY--VAYLDQKFGTPSGKLEF 549
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
7-480 |
1.99e-63 |
|
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: 217.16 E-value: 1.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 7 SACPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMK----KQNGEFVRISWEQALD 82
Cdd:cd02755 3 SICEM-CSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIrvgeRGEGKFREASWDEALQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 83 EIADKLREIKETSETTAVLHShdyANNGLLKALDQRFFNGYGGVTEIV-GSICWGSGIEAQSWDFGRSYGHGPLDIYNSK 161
Cdd:cd02755 82 YIASKLKEIKEQHGPESVLFG---GHGGCYSPFFKHFAAAFGSPNIFShESTCLASKNLAWKLVIDSFGGEVNPDFENAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 162 HVVVWGRNVSR-TNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDETFISE 240
Cdd:cd02755 159 YIILFGRNLAEaIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFVEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 241 HSVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLA-GLYADGPVSTFM-GLGMQRYKNGGGTIRWIDALVAASGNVGIKG 318
Cdd:cd02755 239 YTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIArEFAAAAPHAVVDpGWRGTFYSNSFQTRRAIAIINALLGNIDKRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 319 gganfgnvqiGESFAKTKLTLPelkttsrsfsmmtqaeevltaadpaIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVA 398
Cdd:cd02755 319 ----------GLYYAGSAKPYP-------------------------IKALFIYRTNPFHSMPDRARLIKALKNLDLVVA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 399 IDSIMTDTAELCDYVLPTATVFE-EEDIYYSSMYHHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGFGELF----EYSTQ 473
Cdd:cd02755 364 IDILPSDTALYADVILPEATYLErDEPFSDKGGPAPAVATRQRAIEPLYDTRPGWDILKELARRLGLFGTPsgkiELYSP 443
|
....*..
gi 806801541 474 EFLEMGL 480
Cdd:cd02755 444 ILAKAGY 450
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
7-617 |
2.71e-61 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 218.38 E-value: 2.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 7 SACPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQ----NGEFVRISWEQALD 82
Cdd:PRK15488 46 SICEM-CSTRCPIEARVVNGKNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVgergEGKWQEISWDEAYQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 83 EIADKLREIKETSETTAVLHShdyANNGLLKALDQRFFNGYGGV-TEIVGSICWGSGIEAQSWDFGRSYGhgpLDIYNSK 161
Cdd:PRK15488 125 EIAAKLNAIKQQHGPESVAFS---SKSGSLSSHLFHLATAFGSPnTFTHASTCPAGYAIAAKVMFGGKLK---RDLANSK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 162 HVVVWGRNVSR-TNMHLYHHLQQVK-KKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDETFIS 239
Cdd:PRK15488 199 YIINFGHNLYEgINMSDTRGLMTAQmEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 240 EHSVGFDDVKELLKTVSLEEFIVKTETSMEDLEYLAGLYAD---------GPVSTFMG--LGMQRykngggTIRWIDALV 308
Cdd:PRK15488 279 RYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAaaphaivdfGHRATFTPeeFDMRR------AIFAANVLL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 309 aasGNVGIKGG-----GANFGNVQIGESFAKT----------KLTLPELKTTSRSFSMMTQAEEVLTAADPA-------- 365
Cdd:PRK15488 353 ---GNIERKGGlyfgkNASVYNKLAGEKVAPTlakpgvkgmpKPTAKRIDLVGEQFKYIAAGGGVVQSIIDAtltqkpyq 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 366 IEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFE-EEDIYYSSMYH--HYVQygKKLV 442
Cdd:PRK15488 430 IKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLErDEEISDKSGKNpaYALR--QRVV 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 443 EPQGEAKsDSW-IWSELAKRLGFGELFEYSTQEFLEMglSSLEAEDVTLERLKEKGHL----PL---------------P 502
Cdd:PRK15488 508 EPIGDTK-PSWqIFKELGEKMGLGQYYPWQDMETLQL--YQVNGDHALLKELKKKGYVsfgvPLllrepkmvakfvaryP 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 503 VKQVPWDD------YQFLTPSGKFEFTSSLAEqKGFSGSLQLNVPEESVFHNEEL---AGKYPytllsIHpqrSN-HSQH 572
Cdd:PRK15488 585 NAKAVDEDgtygsqLKFKTPSGKIELFSAKLE-ALAPGYGVPRYRDVALKKEDELyfiQGKVA-----VH---TNgATQN 655
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 806801541 573 VPFIEKLQ-HVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKV 617
Cdd:PRK15488 656 VPLLANLMsDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALV 701
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
12-545 |
3.65e-60 |
|
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: 210.37 E-value: 3.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 12 NCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQN--------GEFVRISWEQALDE 83
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNprkgrdvdPKFVPISWDEALDT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 84 IADKLREIKETSETTAV-LHSHDYANNGLLkaLDQRFFNGYGGVTEIV-GSICwgsgieAQSWDFGRSY-----GHGPLD 156
Cdd:cd02757 88 IADKIRALRKENEPHKImLHRGRYGHNNSI--LYGRFTKMIGSPNNIShSSVC------AESEKFGRYYteggwDYNSYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 157 IYNSKHVVVWGRNVSRTNMHLYHHLQ--QVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTD 234
Cdd:cd02757 160 YANAKYILFFGADPLESNRQNPHAQRiwGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 235 ETFISEhsvgFDDVKELLKTVSLEEFIVKTETSMEDL-EYLAGLYAD----------------------------GPVST 285
Cdd:cd02757 240 KDFVGD----FVDGKNYFKAGETVDEESFKEKSTEGLvKWWNLELKDytpewaakisgipaetiervarefataaPAAAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 286 FMGLGMQRYKNGGGTIRWIDALVAASGNVGIKGG-GANFGNvqigesfaktkltlpelkttsrsfsmmtqaeevltaadP 364
Cdd:cd02757 316 FTWRGATMQNRGSYNSMACHALNGLVGSIDSKGGlCPNMGV--------------------------------------P 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 365 AIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIyySSMYHH---YVQYGKKL 441
Cdd:cd02757 358 KIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDV--MSQENNlhpWLSIRQPV 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 442 VEPQGEAKSDSWIWSELAKRL---GFGELFEYSTQEFLEmglssleaedvtlerlkekghlPLPVKQVPWD-DYQFLTPS 517
Cdd:cd02757 436 VKSLGEVREETEILIELAKKLdpkGSDGMKRYAPGQFKD----------------------PETGKNNRWEfENVFPTET 493
|
570 580
....*....|....*....|....*...
gi 806801541 518 GKFEFTSSLAEQKGFSGSLQLNVPEESV 545
Cdd:cd02757 494 GKFEFYSETLKKYLQNHADKKKVSWDEV 521
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
3-479 |
5.97e-54 |
|
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: 191.76 E-value: 5.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 3 KVHQSACPLNCWDSCGFLVTVDDGKVTKV-------DGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQ----NGE 71
Cdd:cd02750 2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREeqatdypETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVgargEGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 72 FVRISWEQALDEIADKLREIKETSETTAV-LHSHDYANNGLLKALDQRFFNGYGGVTeIVGSICWGSGIEAQSWDFG-RS 149
Cdd:cd02750 82 WKRISWDEALELIADAIIDTIKKYGPDRViGFSPIPAMSMVSYAAGSRFASLIGGVS-LSFYDWYGDLPPGSPQTWGeQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 150 YGHGPLDIYNSKHVVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIE 229
Cdd:cd02750 161 DVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 230 MGRTDETFISEHSvgfdDVKELLKTVSLEEFIvkTETSMEDLEYLAGLYAD-GPVSTFMGLGMQRYKNGGGTIRWIDALV 308
Cdd:cd02750 241 EKLYDEDYLKEYT----DLPFLVYTPAWQEAI--TGVPRETVIRLAREFATnGRSMIIVGAGINHWYHGDLCYRALILLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 309 AASGNVGIKGGGAN--FGNVQigesfaktkltlpelkttsrsfsmmtqaeevltaadpaieMIIVTCGNPLTQVPNTNKV 386
Cdd:cd02750 315 ALTGNEGKNGGGWAhyVGQPR----------------------------------------VLFVWRGNLFGSSGKGHEY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 387 RQA--FEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIYYSSMyHHYVQYGKKLVEPQGEAKSDSWIWSELAKRLGF 464
Cdd:cd02750 355 FEDapEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDM-HPFIHPFSPAVDPLWEAKSDWEIFKALAKKVPW 433
|
490 500
....*....|....*....|
gi 806801541 465 GEL-----FEYSTQEFLEMG 479
Cdd:cd02750 434 RTLtgrqqFYLDHDWFLELG 453
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
7-517 |
2.93e-51 |
|
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: 188.38 E-value: 2.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 7 SACPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNG--EFVRISWEQALDEI 84
Cdd:cd02752 2 TICPY-CSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGsgKWEEISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 85 ADKLREIKETS--------------ETTAVLHSHDYANNGllKALDQRFFNGYGGV-TEIVGSICWGSGIEAqswdFGRS 149
Cdd:cd02752 81 ARKMKDIRDASfveknaagvvvnrpDSIAFLGSAKLSNEE--CYLIRKFARALGTNnLDHQARIUHSPTVAG----LANT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 150 YGHGPL-----DIYNSKHVVVWGRNVSRTNMHLYHHLQQVKKK-GATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAV 223
Cdd:cd02752 155 FGRGAMtnswnDIKNADVILVMGGNPAEAHPVSFKWILEAKEKnGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 224 LKVLIEmgrtdetfisehsvgFD-DVKELLKTVSLEEFIVKTETsmedleYLAGLYADGPvSTFM-GLGMQRYKNGGGTI 301
Cdd:cd02752 235 INYIIR---------------YTpEEVEDICGVPKEDFLKVAEM------FAATGRPDKP-GTILyAMGWTQHTVGSQNI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 302 RWIDALVAASGNVGIKGGGANF----GNVQigesfAKTKLTLpelkttsrsfsMMTQAEEVLTAAdpaiemiivtcgNPL 377
Cdd:cd02752 293 RAMCILQLLLGNIGVAGGGVNAlrghSNVQ-----GATDLGL-----------LSHNLPGYLGGQ------------NPN 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 378 TQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCD-------------YVLPTATVFEEEDIYYSSmyHHYVQYGKKLVEP 444
Cdd:cd02752 345 SSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGSITNS--GRWLQWRYKVVEP 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806801541 445 QGEAKSDSWIWSELAKRLGFgeLFEystqeflemglssleaedvtlerlKEKGHLPLPVKQVPWDDYQFLTPS 517
Cdd:cd02752 423 PGEAKSDGDILVELAKRLGF--LYE------------------------KEGGAFPEPITKWNYGYGDEPTPE 469
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
19-525 |
5.07e-51 |
|
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: 187.08 E-value: 5.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 19 FLVTVDDGKVTKV-----DGDPNHPITEGkicgRGRMletktNSPDRLRYPMKKQ---------------NGEFVRISWE 78
Cdd:cd02769 9 FRARVKDGRIVGVrpfeeDPDPSPLLDGV----PDAV-----YSPTRIKYPMVRRgwlekgpgsdrslrgKEEFVRVSWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 79 QALDEIADKLREIKETSETTAVLH-SHDYANNGLL---KALDQRFFNGYGGVTEIVGSICWGSG--------------IE 140
Cdd:cd02769 80 EALDLVAAELKRVRKTYGNEAIFGgSYGWSSAGRFhhaQSLLHRFLNLAGGYVGSVGDYSTGAAqvilphvvgsmevyTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 141 AQ-SWdfgrsyghgPLDIYNSKHVVVWGRNVSRTNM--------H-LYHHLQQVKKKGATITVIDPIFNPTAKLAD-RYI 209
Cdd:cd02769 160 QQtSW---------PVIAEHTELVVAFGADPLKNAQiawggipdHqAYSYLKALKDRGIRFISISPLRDDTAAELGaEWI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 210 SVKPGMDGWLAAAVLKVLIEMGRTDETFISEHSVGFDDVKELL--------KTVSLEEFIvkTETSMEDLEYLAGLYADG 281
Cdd:cd02769 231 AIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLlgesdgvpKTPEWAAAI--CGIPAETIRELARRFASK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 282 PVSTFMGLGMQRYKNGGGTIRWIDALVAASGNVGIKGGGANFG---NVQIGESFAKTKL-TLPELKTTSRSFSMMTQAEE 357
Cdd:cd02769 309 RTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGyhySNGGGPPRGAAPPpALPQGRNPVSSFIPVARIAD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 358 VL------------TAADPAIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDI 425
Cdd:cd02769 389 MLlnpgkpfdyngkKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 426 -YYSSMYHHYVQygKKLVEPQGEAKSDSWIWSELAKRLGFGELFEYSTQE------FLEMGLSSLEAEDVTL---ERLKE 495
Cdd:cd02769 469 gGSGDNRYIVAM--KQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEmewlrhLYEESRAQAAARGVEMpsfDEFWA 546
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 806801541 496 KGHLPLPVKQVPWDDYQ-FL---------TPSGKFEFTSS 525
Cdd:cd02769 547 QGYVELPIPEADFVRLAdFRedpeanplgTPSGRIEIFSE 586
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
60-461 |
4.47e-47 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 169.89 E-value: 4.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 60 RLRYPMKKQN-GEFVRISWEQALDEIADKLREIKETSETTAVLH---SHDYANNGLLKALdQRFFNGYGGvtEIVGSICW 135
Cdd:pfam00384 1 RLKYPMVRRGdGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAInggSGGLTDVESLYAL-KKLLNRLGS--KNGNTEDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 136 GSGIEAQS-------WDFGRSYGHGPLDIYNSKHVVVWGRNVSRTNMHLYHHL-QQVKKKGATITVIDPIFNptAKLADR 207
Cdd:pfam00384 78 NGDLCTAAaaafgsdLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIrKAALKGKAKVIVIGPRLD--LTYADE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 208 YISVKPGMDGWLAAAVLKVLIEMGRTDETFisehsvgfddvkellKTVSLeeFIVktetsmedleylaglyadgpvstfm 287
Cdd:pfam00384 156 HLGIKPGTDLALALAGAHVFIKELKKDKDF---------------APKPI--IIV------------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 288 GLGMQRYKNGGGTIRWIDALVAASGNVGIKGGGANFGNV--QIGESFAKTKLTLpelkTTSRSFSMMTQAeevltAADPA 365
Cdd:pfam00384 194 GAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNIlqGAASPVGALDLGL----VPGIKSVEMINA-----IKKGG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 366 IEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIM-TDTAELCDYVLPTATVFEEEDIYYSSMyhHYVQYGKKLVEP 444
Cdd:pfam00384 265 IKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTE--GRVQSTKQAVPP 342
|
410
....*....|....*..
gi 806801541 445 QGEAKSDSWIWSELAKR 461
Cdd:pfam00384 343 PGEAREDWKILRALSEV 359
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
57-643 |
2.01e-39 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 155.60 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 57 SPDRLRYPM------KK-------QNGE--FVRISWEQALDEIADKLREIKE--------TSET----TAVLHShdyANN 109
Cdd:PRK15102 87 NPSRIRYPMvrldwlRKrhksdtsQRGDnrFVRVSWDEALDLFYEELERVQKtygpsalhTGQTgwqsTGQFHS---ATG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 110 GLLKALDQrffngYGGVTEIVGSICWGSG------------IEAQ--SWdfgrsyghgPLDIYNSKHVVVWGrNVSRTNM 175
Cdd:PRK15102 164 HMQRAIGM-----HGNSVGTVGDYSTGAGqvilpyvlgsteVYEQgtSW---------PLILENSKTIVLWG-SDPVKNL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 176 HL---------YHHLQQVKKKGAT--ITVI--DPIFNPTAK-LADRYISVKPGMDGWLAAAVLKVLIEMGRTDETFISEH 241
Cdd:PRK15102 229 QVgwncethesYAYLAQLKEKVAKgeINVIsiDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNY 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 242 SVGFDD-VKELL-------KTVSLEEFIvkTETSMEDLEYLAGLYADGPVSTFMGLGMQRYKNGGGTIrWIDALVAAS-G 312
Cdd:PRK15102 309 CLGFEQfLPYLLgekdgvpKTPEWAEKI--CGIDAETIRELARQMAKGRTQIIAGWCIQRQQHGEQPY-WMGAVLAAMlG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 313 NVGIKGGGANFGN--VQIG---------ESFAKTKLTLPELKTTSRSF--------------SMMTQAEEV------LTA 361
Cdd:PRK15102 386 QIGLPGGGISYGHhySGIGvpssggaipGGFPGNLDTGQKPKHDNSDYkgysstipvarfidAILEPGKTInwngkkVTL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 362 ADpaIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIyysSMYHHYVQYG--- 438
Cdd:PRK15102 466 PP--LKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDI---DQYGSYSNRGiia 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 439 -KKLVEPQGEAKSDSWIWSELAKRlgFGELFEYsTQEFLEMG-LSSLEAEDVTLERLK----------EKGHLPLPVKQv 506
Cdd:PRK15102 541 mKKVVEPLFESRSDFDIFRELCRR--FGREKEY-TRGMDEMGwLKRLYQECKQQNKGKfhmpefdefwKKGYVEFGEGQ- 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 507 PW-------DD---YQFLTPSGKFEFTSSLAEQKGFSG----SLQLNVPEESvfHNEELAGKYPYTLLSIHPQRSNHSQH 572
Cdd:PRK15102 617 PWvrhadfrEDpelNPLGTPSGLIEIYSRKIADMGYDDcqghPMWFEKIERS--HGGPGSDKYPLWLQSVHPDKRLHSQL 694
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806801541 573 VPFIEKLQH--VQ----VDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINIDEGMW--AAFGGSVNAL 643
Cdd:PRK15102 695 CESEELRETytVQgrepVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWygPDKGGEIGAL 773
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
60-522 |
2.15e-30 |
|
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: 126.27 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 60 RLRYPMKKQNGE--FVRISWEQALDEIADKLREIketSETTAVLHSHDYANN--GLLKALDQRFFngygGVTEI--VGSI 133
Cdd:cd02767 64 RLTYPMRYDAGSdhYRPISWDEAFAEIAARLRAL---DPDRAAFYTSGRASNeaAYLYQLFARAY----GTNNLpdCSNM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 134 CWgsgiEAQSWDFGRSYGHGPL-----DIYNSKHVVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPI--------FNP 200
Cdd:cd02767 137 CH----EPSSVGLKKSIGVGKGtvsleDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLrepglerfANP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 201 TA---------KLADRYISVKPGMDGWLAAAVLKVLIEMGRT-----DETFISEHSVGFDDVKELLKTVSLEEFIVKTET 266
Cdd:cd02767 213 QNpesmltggtKIADEYFQVRIGGDIALLNGMAKHLIERDDEpgnvlDHDFIAEHTSGFEEYVAALRALSWDEIERASGL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 267 SMEDLEYLAGLYADGPVSTFM-GLGMQRYKNGGGTIRWIDALVAASGNVGIKGGGA----NFGNVQ-IGESFAKTKLTLP 340
Cdd:cd02767 293 SREEIEAFAAMYAKSERVVFVwGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLmpirGHSNVQgDRTMGITEKPFPE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 341 ELKTTSRSFSM-------MTQAEEVLTAADPAIEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSIMTDTAEL---C 410
Cdd:cd02767 373 FLDALEEVFGFtpprdpgLDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVhgeE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 411 DYVLPTATVFEEED--------IYYSSMYHHYVQYGKK-------LVEPQ----------GEAKSDSWIWSELAKRlgfg 465
Cdd:cd02767 453 ALILPCLGRTEIDMqaggaqavTVEDSMSMTHTSRGRLkpasrvlLSEEAivagiagarlGEAKPEWEILVEDYDR---- 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806801541 466 eLFEYSTQEFLEMglssleaedvtLERLKEKG------HLPlpvkqVPWDDYQFLTPSGKFEF 522
Cdd:cd02767 529 -IRDEIAAVIYEG-----------FADFNQRGdqpggfHLP-----NGARERKFNTPSGKAQF 574
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
13-463 |
2.05e-25 |
|
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: 111.46 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 13 CWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQ----NGEFVRISWEQALDEIADKL 88
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKgprgSGQFEEIEWEEAFSIATKRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 89 REIKETS-ETTAVLHSHD--YANNGLLKA----LDQRFFNGYGGVTEIVGSIcwgSGIEAQSWDFGrsyghGPlDIYNSK 161
Cdd:cd02763 87 KAARATDpKKFAFFTGRDqmQALTGWFAGqfgtPNYAAHGGFCSVNMAAGGL---YSIGGSFWEFG-----GP-DLEHTK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 162 HVVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGRTDETFISEH 241
Cdd:cd02763 158 YFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 242 S------------------VGFDDVKELLKTVSLEEF-------IVKTETSMEDLEYLAGlyadGPVSTFMGLGMQRYKN 296
Cdd:cd02763 238 TnaaelvdytpewvekitgIPADTIRRIAKELGVTARdqpielpIAWTDVWGRKHEKITG----RPVSFHAMRGIAAHSN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 297 GGGTIRWIDALVAASGNVGIKGG-------------GANFGN----VQIGESFAKTKLTLP------------ELKTTSR 347
Cdd:cd02763 314 GFQTIRALFVLMMLLGTIDRPGGfrhkppyprhippLPKPPKipsaDKPFTPLYGPPLGWPaspddllvdedgNPLRIDK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 348 SFS---------MMtqaEEVLTAA---DP-AIEMIIVTCGN-PLTQVPNTNKVRQAFE--------KVPMTVAIDSIMTD 405
Cdd:cd02763 394 AYSweyplaahgCM---QNVITNAwrgDPyPIDTLMIYMANmAWNSSMNTPEVREMLTdkdasgnyKIPFIIVCDAFYSE 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806801541 406 TAELCDYVLPTATVFEEEDIYysSMYHHYVQYG--------KKLVEPQGEAKSDSWIWSELAKRLG 463
Cdd:cd02763 471 MVAFADLVLPDTTYLERHDAM--SLLDRPISEAdgpvdairVPIVEPKGDVKPFQEVLIELGTRLG 534
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
7-466 |
4.64e-23 |
|
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: 104.35 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 7 SACpLNCWDSCGFLVTVDD--GKVTKVDGDPNHPITE---------------------------GKICGRGRMLETKTNS 57
Cdd:cd02758 2 SSC-LGCWTQCGIRVRVDKetGKVLRIAGNPYHPLNTapslpyntplkeslylslvgenglkarATACARGNAGLQYLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 58 PDRLRYPMKKQ----NGEFVRISWEQALDEIA-----------DKLREIKEtsETTAVLHSH-DYA--NNGLL------- 112
Cdd:cd02758 81 PYRVLQPLKRVgprgSGKWKPISWEQLIEEVVeggdlfgeghvEGLKAIRD--LDTPIDPDHpDLGpkANQLLytfgrde 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 113 --KALDQRFF-NGYGGVTEIV-GSICWGS---GIEAQSWDFGrSYGHGPLDIYNSKHVVVWGRNVSRTNMHLYHHLQQVK 185
Cdd:cd02758 159 grTPFIKRFAnQAFGTVNFGGhGSYCGLSyraGNGALMNDLD-GYPHVKPDFDNAEFALFIGTSPAQAGNPFKRQARRLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 186 KKGAT----ITVIDPIFNPTAKLAD---RYISVKPGMDGWLAAAVLKVLIEMGRTDETFISEHS---------VGFDDVK 249
Cdd:cd02758 238 EARTEgnfkYVVVDPVLPNTTSAAGeniRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSIPSkeaakaagePSWTNAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 250 ELLKTVSLEE--FIVKTET---SMEDLEYLAGLYADGPVST---FMGLGMQRY--KNGGG----------TIRWIDALVa 309
Cdd:cd02758 318 HLVITVRVKSalQLLKEEAfsySLEEYAEICGVPEAKIIELakeFTSHGRAAAvvHHGGTmhsngfynayAIRMLNALI- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 310 asGNVGIKGG-----GANFGNVQIGESFAKTKLTLPELKTT--SRS---------FSMMTQAE----------------- 356
Cdd:cd02758 397 --GNLNWKGGllmsgGGFADNSAGPRYDFKKFFGEVKPWGVpiDRSkkayektseYKRKVAAGenpypakrpwypltpel 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 357 --EVLTAADPA----IEMIIVTCGNPLTQVPNTNKVRQAF----EKVPMTVAIDSIMTDTAELCDYVLPTATVFEEEDIy 426
Cdd:cd02758 475 ytEVIASAAEGypykLKALILWMANPVYGAPGLVKQVEEKlkdpKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGF- 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 806801541 427 ysSMYHHYVQYG---------KKLVE--PQGEAKSdswIWS---ELAKRL---GFGE 466
Cdd:cd02758 554 --STPWGGVPTKastarwpviAPLTEktANGHPVS---MESfliDLAKALglpGFGP 605
|
|
| 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 ... |
7-455 |
1.10e-20 |
|
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: 95.53 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 7 SACPlNCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNGEFVRISWEQALDEIAD 86
Cdd:cd02771 2 SICH-HCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEALDVAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 87 KLREIKetsETTAVLHSHDYANNGLLkALdQRFFNGYGGVTEIVGSICWGSgieAQSWDFGRSYGHGPLDIYNSKHVVVW 166
Cdd:cd02771 81 RLKEAK---DKVGGIGSPRASNESNY-AL-QKLVGAVLGTNNVDHRARRLI---AEILRNGPIYIPSLRDIESADAVLVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 167 GRNVSRTNMHLYHHLQQ-VKKKGATITVIDPIfNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMGrtDETFiseHSVGF 245
Cdd:cd02771 153 GEDLTQTAPRIALALRQaARRKAVELAALSGI-PKWQDAAVRNIAQGAKSPLFIVNALATRLDDIA--AESI---RASPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 246 DDVKEllkTVSLEEFIVKTETSMEDLEYLAGLYADGpvstfmglgmQRYKNGG------GTIRWIDALVAASGNVG--IK 317
Cdd:cd02771 227 GQARL---GAALARAVDASAAGVSGLAPKEKAARIA----------ARLTGAKkplivsGTLSGSLELIKAAANLAkaLK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 318 GGGANFGnvqigesfaktkLTLPELKTTSRSFSMMT--------QAEEVL-TAADPAIEMIIVTCGNPLTQVPNTnKVRQ 388
Cdd:cd02771 294 RRGENAG------------LTLAVEEGNSPGLLLLGghvtepglDLDGALaALEDGSADALIVLGNDLYRSAPER-RVEA 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806801541 389 AFEKVPMTVAIDSIMTDTAELCDYVLPTAtVFEEEDIYYSSMYHHYVQYGKKLVEPQGEAKSDsWIW 455
Cdd:cd02771 361 ALDAAEFVVVLDHFLTETAERADVVLPAA-SFAEKSGTFVNYEGRAQRFFKAYDDPAGDARSD-WRW 425
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
554-667 |
3.44e-19 |
|
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: 83.96 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 554 KYPYTLLSIHPQRSNHSQH--VPFIEKLQ-HVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINIDE 630
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFsnVPWLLELQpEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 806801541 631 GMWAAF--GGSVNALTNDT-----NSDNGMGSTLFDCLVGLKKA 667
Cdd:cd02785 81 GWWSRYfqEGSLQDLTSPFvnpvhEYIYGPNSAFYDTLVEVRKA 124
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
12-497 |
4.65e-19 |
|
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: 91.57 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 12 NCWDSCGFL-VTVDDGKVTKVDGDPN----HPiTEGKICGRGRMLETKTNSPDRLRYPMKKQNGE--------FVRISWE 78
Cdd:cd02760 6 NCVAGPDFMaVKVVDGVATEIEPNFAaediHP-ARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKkgrnedpgFVPISWD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 79 QALDEIADKLREIKETSE---------TTAVLHSHDYANN-GLLKALDQRF------FNGYGGVTEIVGSICWGsgieaQ 142
Cdd:cd02760 85 EALDLVAAKLRRVREKGLldekglprlAATFGHGGTPAMYmGTFPAFLAAWgpidfsFGSGQGVKCVHSEHLYG-----E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 143 SWDfgRSYGHGPlDIYNSKHVVVWGRNV----SRTNMHLYhhlQQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGW 218
Cdd:cd02760 160 FWH--RAFTVAA-DTPLANYVISFGSNVeasgGPCAVTRH---ADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 219 LAAAVLKVLI---EMGRTDETFI------------------------------------------------------SEH 241
Cdd:cd02760 234 FMFAMIHVMVheqGLGKLDVPFLrdrtsspylvgpdglylrdaatgkplvwdersgravpfdtrgavpavagdfavdGAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 242 SVGFDDVKELLKTVS-----------LEEFIVKTETSMEDL----------EYL------AGLYADG------PVSTFMG 288
Cdd:cd02760 314 SVDADDETAIHQGVEgttaftmlvehMRKYTPEWAESICDVpaatirriarEFLenasigSTIEVDGvtlpyrPVAVTLG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 289 LGMQrykNGGGTIR--W----IDALVAASGNVG-------------------IKGGGANF----------GNVQIGESFA 333
Cdd:cd02760 394 KSVN---NGWGAFEccWartlLATLVGALEVPGgtlgttvrlnrphddrlasVKPGEDGFmaqgfnptdkEHWVVKPTGR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 334 KTKLTLPELKTTSR--------SFSMMTQAEEVLTAADPA---IEMIIVTCGNPLTQVPNTNKVRQAFEKVPMTVAIDSI 402
Cdd:cd02760 471 NAHRTLVPIVGNSAwsqalgptQLAWMFLREVPLDWKFELptlPDVWFNYRTNPAISFWDTATLVDNIAKFPFTVSFAYT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 403 MTDTAELCDYVLPTATVFEEED-------IYYSSMYHHY-VQYGKKLVEPQGEAKSDSWIWSELAKRLGFgeLFEYSTQE 474
Cdd:cd02760 551 EDETNWMADVLLPEATDLESLQmikvggtKFVEQFWEHRgVVLRQPAVEPQGEARDFTWISTELAKRTGL--LADYNAAL 628
|
650 660
....*....|....*....|....*
gi 806801541 475 FLEMGLSSLEAE--DVTLERLKEKG 497
Cdd:cd02760 629 NRGAGGAPLKGEgyDQSLDESQEHD 653
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
21-455 |
2.51e-18 |
|
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: 87.34 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 21 VTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNGEFVRISWEQALDEIADKLREIKEtsETTAV 100
Cdd:cd02768 15 VDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEALKTVAEGLKAVKG--DKIGG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 101 LhSHDYANNGLLKALdQRFFNGYGgvTEIVGSICWGSGIEAQSwDFGRSYGHGPL--DIYNSKHVVVWGRNVSRTNMHLY 178
Cdd:cd02768 93 I-AGPRADLESLFLL-KKLLNKLG--SNNIDHRLRQSDLPADN-RLRGNYLFNTSiaEIEEADAVLLIGSNLRKEAPLLN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 179 HHLQQ-VKKKGATITVIDPifNPTAKLADRYISVKPGmdGWLAAAVLKVLIemGRTDETFISEhsvgfddvkellktvsl 257
Cdd:cd02768 168 ARLRKaVKKKGAKIAVIGP--KDTDLIADLTYPVSPL--GASLATLLDIAE--GKHLKPFAKS----------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 258 eefIVKTETSMedleylaglyadgpvsTFMGLGMQRyKNGGGTIRWIDALVAASGNVGIKGGGANFGN---VQIGESFAK 334
Cdd:cd02768 225 ---LKKAKKPL----------------IILGSSALR-KDGAAILKALANLAAKLGTGAGLWNGLNVLNsvgARLGGAGLD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 335 TKLTLPELKTtsrsfsmmtqAEEVLTAADpaiemiivtcgNPLTQVPNTnkvRQAFEKVPMTVAIDSIMTDTAELCDYVL 414
Cdd:cd02768 285 AGLALLEPGK----------AKLLLLGED-----------ELDRSNPPA---AVALAAADAFVVYQGHHGDTGAQADVIL 340
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 806801541 415 PTATVFEEEDIYYSsmYHHYVQYGKKLVEPQGEAKSDsWIW 455
Cdd:cd02768 341 PAAAFTEKSGTYVN--TEGRVQRFKKAVSPPGDARED-WKI 378
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
3-57 |
6.80e-18 |
|
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: 77.72 E-value: 6.80e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 806801541 3 KVHQSACPlNCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNS 57
Cdd:pfam04879 2 KVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
3-49 |
6.86e-17 |
|
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: 74.98 E-value: 6.86e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 806801541 3 KVHQSACPLnCWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGR 49
Cdd:smart00926 2 KWVPTVCPL-CGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGR 47
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
13-461 |
3.53e-16 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 82.64 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 13 CWDSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYP---MKK----QNGEFVRISWEQALDEIA 85
Cdd:PRK13532 50 CGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPllrMKDgkydKEGEFTPVSWDQAFDVMA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 86 DKLREIKETSETTAV--LHS------HDYANNGLLKA------LD--QRFfngyggvteivgsiCWGSGIEAqswdFGRS 149
Cdd:PRK13532 130 EKFKKALKEKGPTAVgmFGSgqwtiwEGYAASKLMKAgfrsnnIDpnARH--------------CMASAVVG----FMRT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 150 YG-HGPL----DIYNSKHVVVWGRNVSRtnMH--LYHHL--QQVKKKGATITVIDPIFNPTAKLADRYISVKPGMDGWLA 220
Cdd:PRK13532 192 FGiDEPMgcydDIEAADAFVLWGSNMAE--MHpiLWSRVtdRRLSNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAIL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 221 AAVLKVLIEMGRTDETFISEHSV----------------------------------GFDDVKELLKTVSLEEFIVKTET 266
Cdd:PRK13532 270 NYIANYIIQNNAVNWDFVNKHTNfrkgatdigyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 267 SMEDLEYLAGLYADgP---VSTFMGLGMQRYKNGggtiRWIDALVAasgNVGIKGGganfgnvqigesfaktKLTLPelk 343
Cdd:PRK13532 350 PKEQLEQLAKLYAD-PnrkVVSFWTMGFNQHTRG----VWANNLVY---NIHLLTG----------------KISTP--- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 344 tTSRSFSMMTQ------AEEVLTAAD--PAiEMII--------------------------------------------V 371
Cdd:PRK13532 403 -GNGPFSLTGQpsacgtAREVGTFSHrlPA-DMVVtnpkhreiaekiwklpegtippkpgyhavaqdrmlkdgklnaywV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 372 TCGNPLTQVPNTNKvrqafEKVP-------MTVAIDSIMTDTAELCDYVLPTATVFEEEDIYYSSmyHHYVQYGKKLVEP 444
Cdd:PRK13532 481 MCNNNMQAGPNINE-----ERLPgwrnpdnFIVVSDPYPTVSALAADLILPTAMWVEKEGAYGNA--ERRTQFWRQQVKA 553
|
570
....*....|....*..
gi 806801541 445 QGEAKSDSWIWSELAKR 461
Cdd:PRK13532 554 PGEAKSDLWQLVEFSKR 570
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
15-421 |
4.11e-15 |
|
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: 78.68 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 15 DSCGFLVTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQ-NGEFVRISWEQALDEIADKLREIKE 93
Cdd:cd02764 54 EGQGVLVKTVDGRPIKIEGNPDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGiDGAYVASDWADFDAKVAEQLKAVKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 94 tSETTAVLHSHDyaNNGLLKALDQRFFNGYGGVTEIVGSICWGSGI-EAQSWDFGRSYGHGpLDIYNSKHVVVWGRNVSR 172
Cdd:cd02764 134 -GGKLAVLSGNV--NSPTTEALIGDFLKKYPGAKHVVYDPLSAEDVnEAWQASFGKDVVPG-YDFDKAEVIVSIDADFLG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 173 TNMHLYHHLQQVKKK---GATITV-----IDPIFNPTAKLADRYISVKPGMDGWLAAAVLKVLIEMG--RTDETFISEHS 242
Cdd:cd02764 210 SWISAIRHRHDFAAKrrlGAEEPMsrlvaAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKGagSSLPDFFRALN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 243 VGF--DDVKELlkTVSLEEFIVKtetsmedleyLAGLYADGPVSTFMGLGMQRYKNGGGTIRWIDALVAASGNVGikggg 320
Cdd:cd02764 290 LAFkpAKVAEL--TVDLDKALAA----------LAKALAAAGKSLVVAGSELSQTAGADTQVAVNALNSLLGNDG----- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 321 anfGNVQIGESFAKTKLTLPElkttsrsfSMMTQAEEVLTAADPAIEMIIVtcgNPLTQVPNTNKVRQAFEKVPMTVAID 400
Cdd:cd02764 353 ---KTVDHARPIKGGELGNQQ--------DLKALASRINAGKVSALLVYDV---NPVYDLPQGLGFAKALEKVPLSVSFG 418
|
410 420
....*....|....*....|.
gi 806801541 401 SIMTDTAELCDYVLPTATVFE 421
Cdd:cd02764 419 DRLDETAMLCDWVAPMSHGLE 439
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
5-93 |
2.57e-14 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 75.65 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 5 HQSACPLncwDSCGFLVTVD--DGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNGEFVRISWEQALD 82
Cdd:COG1034 218 TPSICPH---CSVGCNIRVDvrGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASWEEALA 294
|
90
....*....|.
gi 806801541 83 EIADKLREIKE 93
Cdd:COG1034 295 AAAEGLKALKK 305
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
567-658 |
5.06e-14 |
|
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: 68.12 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 567 SNHSQHVPFIEKLQHVQ-VDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINIDEGMWAAF--GGSVNAL 643
Cdd:cd02775 7 SGTRTRNPWLRELAPEPvVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGgrGGNANVL 86
|
90
....*....|....*
gi 806801541 644 TNDTNSDNGMGSTLF 658
Cdd:cd02775 87 TPDALDPPSGGPAYK 101
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
21-449 |
1.27e-13 |
|
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: 73.16 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 21 VTVDDGKVTKVDGDPNHPITEGKICGRGRMLETKTNSPDRLRYPMKKQNGEFVRISWEQALDEIADKLREIKET---SET 97
Cdd:cd02772 15 VHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKKhgaDQI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 98 TAVLHSHDYANNGLLKaldQRFFNGYGgvteiVGSIcwgsGIEAQSWDFgRSYGHGPL---------DIYNSKHVVVWGR 168
Cdd:cd02772 95 GALASPHSTLEELYLL---QKLARGLG-----SDNI----DHRLRQSDF-RDDAKASGapwlgmpiaEISELDRVLVIGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 169 NVSRTNMHLYHHLQQVKKKGATITVIDPI-FNPTAKLADRYISVKPGMDGWLaAAVLKVLIEMgrtdetfisehsvgfdd 247
Cdd:cd02772 162 NLRKEHPLLAQRLRQAVKKGAKLSAINPAdDDFLFPLSGKAIVAPSALANAL-AQVAKALAEE----------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 248 vkellKTVSLEEFIVKTETSMEDLEYLAGLYADGPVSTFMGLGMQRYKnGGGTIR-WIDALVAASG-NVGIKGGGAN--- 322
Cdd:cd02772 224 -----KGLAVPDEDAKVEASEEARKIAASLVSAERAAVFLGNLAQNHP-QAATLRaLAQEIAKLTGaTLGVLGEGANsvg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 323 ---FGNVQIGESFAKTKLTLPELKTtsrsfsMMTQAEEVLTAADPAiemiivtcgnpltqvpntnKVRQAFEKVPMTVAI 399
Cdd:cd02772 298 aylAGALPHGGLNAAAMLEQPRKAY------LLLNVEPELDCANPA-------------------QALAALNQAEFVVAL 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 806801541 400 DSIMTDTAE-LCDYVLPTATvFEEEDIYYSSMYHHyVQYGKKLVEPQGEAK 449
Cdd:cd02772 353 SAFASAALLdYADVLLPIAP-FTETSGTFVNLEGR-VQSFKGVVKPLGEAR 401
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
555-662 |
1.85e-12 |
|
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: 64.22 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 555 YPYTLLSiHPQR----SNHSQHVPFIEKLQHVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVmKQAHAKTINIDE 630
Cdd:cd02786 1 YPLRLIT-PPAHnflnSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKV-TDDVPPGVVVAE 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 806801541 631 GMW----AAFGGSVNALTNDTNSDNGMGSTLFDCLV 662
Cdd:cd02786 79 GGWwrehSPDGRGVNALTSARLTDLGGGSTFHDTRV 114
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
34-522 |
6.93e-12 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 68.66 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 34 DPNHPITEGKICGRGRMLETKTNSPD------RLRYPMKKQNGEFVRISWEQALDEIADKLREI--KETSETTAVLHSHD 105
Cdd:cd02756 85 DKECPVNSGNYSTRGGTNAERIWSPDnrvgetRLTTPLVRRGGQLQPTTWDDAIDLVARVIKGIldKDGNDDAVFASRFD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 106 -------YANN---GLLkaldqrFFNGYGgvTEIV--------GSICWGSGiEAQSWDFGRSYghgpLDIYNSKHVVVWG 167
Cdd:cd02756 165 hggggggFENNwgvGKF------FFMALQ--TPFVrihnrpayNSEVHATR-EMGVGELNNSY----EDARLADTIVLWG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 168 RN--VSRTNMHLYHHLQQVkkKGAT------------------ITVIDPIFNPTAKLA------DR--YISVKPGMDGWL 219
Cdd:cd02756 232 NNpyETQTVYFLNHWLPNL--RGATvsekqqwfppgepvppgrIIVVDPRRTETVHAAeaaagkDRvlHLQVNPGTDTAL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 220 AAAVLKVLIEmgrTDETFISE-HSVGFDDVKELLKTVsleEFIVKTEtsmedleylAGLYAdgPVSTFM---GL--GMQR 293
Cdd:cd02756 310 ANAIARYIYE---SLDEVLAEaEQITGVPRAQIEKAA---DWIAKPK---------EGGYR--KRVMFEyekGIiwGNDN 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 294 YKNGGGtirwIDALVAASGNVGIKGGG-ANFGNVQIGESFAKTkltlPELKTTSRSFSMMTqAEEVLTAADPAIeMIIVT 372
Cdd:cd02756 373 YRPIYS----LVNLAIITGNIGRPGTGcVRQGGHQEGYVRPPP----PPPPWYPQYQYAPY-IDQLLISGKGKV-LWVIG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 373 CgNPLTQVPN-----------TNKVRQAFEKVP-----------------------MTVAIDSIMTDTAELCDYVLPTAT 418
Cdd:cd02756 443 C-DPYKTTPNaqrlretinhrSKLVTDAVEAALyagtydreamvcligdaiqpgglFIVVQDIYPTKLAEDAHVILPAAA 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 419 VFEEEDIyysSMYHH--YVQYGKKLVEPQGEAKSDSWIWSELAKRL-------GFGEL-------FEYSTQE--FLEMG- 479
Cdd:cd02756 522 NGEMNET---SMNGHerRLRLYEKFMDPPGEAMPDWWIAAMIANRIyelyqeeGKGGSaqyqffgFIWKTEEdnFMDGSq 598
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806801541 480 --------------LSSLEAEDVTLERLKEKG----HLPLP--------VKQVPWDDYQFLTPSGKFEF 522
Cdd:cd02756 599 efadggefsedyyvLGQERYEGVTYNRLKAVGvngiQLPVTtdtvtkilVTNVLRTEGVFDTEDGKAYV 667
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
557-646 |
7.56e-12 |
|
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: 62.29 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 557 YTLLSIHPQRSNHSQH----VPFIEKLQHVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINIDEGM 632
Cdd:pfam01568 1 LYLITGRVLGQYHSQTrtrrVLRLAKPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90
....*....|....*
gi 806801541 633 WAAF-GGSVNALTND 646
Cdd:pfam01568 81 WYEPrGGNANALTDD 95
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
555-666 |
2.23e-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: 61.45 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 555 YPYTLLSIHPQRSNHSQ--HVPFIEKLQHVQ----VDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINI 628
Cdd:cd02777 1 YPLQLISPHPKRRLHSQldNVPWLREAYKVKgrepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 806801541 629 DEGMWAAF--------GGSVNALTND-TNSDNGMGSTLFDCLVGLKK 666
Cdd:cd02777 81 PEGAWYDPddnggldkGGNPNVLTSDiPTSKLAQGNPANTCLVEIEK 127
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
4-239 |
3.01e-10 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 63.48 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 4 VHQSACpLNCWDSCGFLVTVD--DGKVTKVDGDPNHPIT------------------------EGK--ICGRGR-MLEtK 54
Cdd:PRK14991 74 VANTQC-LGCWTQCGVRVRVDnaTNKILRIAGNPYHPLStdhhidmstpvkeafeslsgesglEGRstACARGNaMLE-Q 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 55 TNSPDRLRYPMK---KQN-GEFVRISWEQALDEI-----------ADKLREIKETseTTAVlhshDYAN-------NGLL 112
Cdd:PRK14991 152 LDSPYRVLQPLKrvgKRGsGKWQRISFEQLVEEVveggdlfgeghVDGLRAIRDL--DTPI----DAKNpeygpkaNQLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 113 ---------KALDQRF-FNGYGGVTEIV-GSICWGS---GIEAQSWDFgRSYGHGPLDIYNSKHVVVWG----------- 167
Cdd:PRK14991 226 vtnasdegrDAFIKRFaFNSFGTRNFGNhGSYCGLAyraGSGALMGDL-DKNPHVKPDWDNVEFALFIGtspaqsgnpfk 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 168 -------RNVSRTNMHlYhhlqqvkkkgatiTVIDPIFNPTAKLA----DRYISVKPGMDGWLAAAVLKVLIEMGRTDET 236
Cdd:PRK14991 305 rqarqlaNARTRGNFE-Y-------------VVVAPALPLSSSLAagdnNRWLPIRPGTDSALAMGMIRWIIDNQRYNAD 370
|
...
gi 806801541 237 FIS 239
Cdd:PRK14991 371 YLA 373
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
555-666 |
1.99e-08 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.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: 53.02 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 555 YPYTLLSIHPQRSNHSQ--HVPF--IEKLQ-HVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINID 629
Cdd:cd02793 1 YPLHLLSNQPATRLHSQldHGSLsrAYKVQgREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 806801541 630 EGMWAAFG-----------GSVNALTNDT-NSDNGMGSTLFDCLVGLKK 666
Cdd:cd02793 81 TGAWYDPDdpgepgplckhGNPNVLTLDIgTSSLAQGCSAQTCLVQIEK 129
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
60-320 |
2.11e-08 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 57.36 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 60 RLRYPMKKQ--NGEFVRISWEQALDEIADKLREIKETSET---TAVLHSHDYAnngllkALDQRFFNGYGGVTeivGSIC 134
Cdd:PRK09939 108 RLTQPLKYDavSDCYKPLSWQQAFDEIGARLQSYSDPNQVefyTSGRTSNEAA------FLYQLFAREYGSNN---FPDC 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 135 WGSGIEAQSWDFGRSYGHGP-----LDIYNSKHVVVWGRNVSRTNMHLYHHLQQVKKKGATITVIDPI------------ 197
Cdd:PRK09939 179 SNMCHEPTSVGLAASIGVGKgtvllEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLqerglerftapq 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 198 ------FNPTAKLADRYISVKPGMDGWLAAAVLKVLIE-------MGRT---DETFISEHSVGFDDVKELLKTVSLEEFI 261
Cdd:PRK09939 259 npfemlTNSETQLASAYYNVRIGGDMALLKGMMRLLIErddaasaAGRPsllDDEFIQTHTVGFDELRRDVLNSEWKDIE 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 262 VKTETSMEDLEYLAGLYADGPVSTF-MGLGMQRYKNGGGTIRWIDALVAASGNVGIKGGG 320
Cdd:PRK09939 339 RISGLSQTQIAELADAYAAAERTIIcYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAG 398
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| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
555-662 |
2.18e-08 |
|
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: 53.08 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 555 YPYTLLSIHPQRSN-HSQH--VPFIEKLQHV-QVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINIDE 630
Cdd:cd02781 2 YPLILTTGARSYYYfHSEHrqLPSLRELHPDpVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEH 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 806801541 631 GMW---------AAFGG---SVNALTNDTNSDNGMGSTLFDCLV 662
Cdd:cd02781 82 GWWypereagepALGGVwesNANALTSDDWNDPVSGSSPLRSML 125
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|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
555-666 |
3.97e-08 |
|
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: 51.91 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 555 YPYTLLSIHPQRSNHSQH--VPFIEKLQHVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINIDEGM 632
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFdnVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 806801541 633 WAAF-------GGSVNALTNDTNSDNGMGSTLFDCLVGLKK 666
Cdd:cd02794 81 WYEPdangidkGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
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|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
554-646 |
4.14e-08 |
|
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: 52.23 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 554 KYPYTLLSI----HPQRSNHSQHVPFI-EKLQHVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINI 628
Cdd:cd02792 2 EFPLVLTTGrlteHFHGGNMTRNSPYLaELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGI 81
|
90 100
....*....|....*....|.
gi 806801541 629 D---EGMWAAFGGSVNALTND 646
Cdd:cd02792 82 PyhwGGMGLVIGDSANTLTPY 102
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
584-646 |
2.63e-06 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 46.73 E-value: 2.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806801541 584 VDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVmkqahakTINIDEGM--------WAAFGGSVNALTND 646
Cdd:cd00508 37 VEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARV-------TDRVRPGTvfmpfhwgGEVSGGAANALTND 100
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
565-644 |
1.19e-04 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 42.06 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 565 QRSNHSQHVPFI-EKLQHVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINIDEGMWAafgGSVNAL 643
Cdd:cd02779 15 QTAYHDQNNSEIaERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHPR---PGANGL 91
|
.
gi 806801541 644 T 644
Cdd:cd02779 92 V 92
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
60-92 |
1.66e-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: 44.56 E-value: 1.66e-04
10 20 30
....*....|....*....|....*....|...
gi 806801541 60 RLRYPMKKQNGEFVRISWEQALDEIADKLREIK 92
Cdd:cd02773 53 RLDKPYIRKNGKLKPATWEEALAAIAKALKGVK 85
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
563-666 |
1.82e-04 |
|
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: 41.49 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806801541 563 HPQRSN-HSQHVPFIEKL-QHVQVDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKVMKQAHAKTINIDEG-------MW 633
Cdd:cd02778 9 SPVHTHgHTANNPLLHELtPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGfghwapaLS 88
|
90 100 110
....*....|....*....|....*....|....*
gi 806801541 634 AAF--GGSVNALTNDTNSDNGMGSTLFDCLVGLKK 666
Cdd:cd02778 89 RAYggGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
584-646 |
3.29e-04 |
|
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: 41.02 E-value: 3.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806801541 584 VDISPDIAAGQDLQDGDEVVIFNDRGSMKGKVKV---MKQAHAkTINIDEGMWAAFGGSVNALTND 646
Cdd:cd02791 37 VEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVtdrVRPGEV-FVPMHWGDQFGRSGRVNALTLD 101
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