|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-565 |
0e+00 |
|
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: 857.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 7 YRACHLCEAICGLVIETVveadsAPRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGDQWQPIAWQQAF 86
Cdd:cd02762 1 KRACILCEANCGLVVTVE-----DGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGSFEEIDWDEAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 87 DLVAERLYAIQQRHGQNAVAVYQGNPSVHNYGLMTHSNYFLGLLKTRNRFSATSVDQLPHHLSSFLMYGHGMLLPIPDID 166
Cdd:cd02762 76 DEIAERLRAIRARHGGDAVGVYGGNPQAHTHAGGAYSPALLKALGTSNYFSAATADQKPGHFWSGLMFGHPGLHPVPDID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 167 HTDFMLILGGNPLASNGSIMTVPDVEKRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLNTLFEEGL 246
Cdd:cd02762 156 RTDYLLILGANPLQSNGSLRTAPDRVLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAEGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 247 TRESHLP--VDGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAVCYGRMGVSTQTFGTLCHWLAQLINLVT 324
Cdd:cd02762 236 TDRRFLAehCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 325 GNLDRVGGALCTEPAVDLVSSTSGGHFNR--WQSRVSGLPEYGGELPVSALAEEMLVDGEGQVRALVTVAGNPVLSTPNG 402
Cdd:cd02762 316 GNLDRPGGAMFTTPALDLVGQTSGRTIGRgeWRSRVSGLPEIAGELPVNVLAEEILTDGPGRIRAMIVVAGNPVLSAPDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 403 RQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENDHYDtTFNTLAVRNVTRFNRAIFDKPEGALHDWEIFVGLAS 482
Cdd:cd02762 396 ARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHAT-FFNLEFPRNAFRYRRPLFPPPPGTLPEWEILARLVE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 483 AFaakaeralkptlppaqmiDRGLRAGLYGDASSHKLSLETLDSHPHGLDLGALKANLAQRLKTANGRIQAAPEVIMADL 562
Cdd:cd02762 475 AL------------------DAVLRAGFYGERAGGTLLLAALLERPSGVDLGPLTPRLWQRLRTPDGRIHLAPPELLDEL 536
|
...
gi 1336206682 563 ARF 565
Cdd:cd02762 537 RRL 539
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
1-699 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 557.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 1 MTRTEHYRACHLCEAICGLVIEtvVEADsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSG----DQ 76
Cdd:COG0243 19 AGTKTVKTTCPGCGVGCGLGVK--VEDG---RVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGprgsGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 77 WQPIAWQQAFDLVAERLYAIQQRHGQNAVAVYQGNPSVHNYGLMTHSNY--FLGLLKTRNRFSATSVDQLPHHLSSFLMY 154
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNEAAYLAqrFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 155 GHGMLL-PIPDIDHTDFMLILGGNPLASNGSIMTvpdvekRL-KAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAA 232
Cdd:COG0243 174 GSDKGTvSYEDLEHADLIVLWGSNPAENHPRLLR------RLrEAAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 233 LLFGLLNTLFEEGLTRESHLP--VDGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAVCYGRMGVSTQTFG 310
Cdd:COG0243 248 LLLALAHVLIEEGLYDRDFLArhTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 311 TLCHWLAQLINLVTGNLDRVGGALCTEPAvdlvsstsgghfnrwqsrvsglpeyggelpvsalaeEMLVDGEG-QVRALV 389
Cdd:COG0243 328 TQTVRAIANLALLTGNIGKPGGGPFSLTG------------------------------------EAILDGKPyPIKALW 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 390 TVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENDHYDTTFNtlavRNVTRFNRAIFDKPEG 469
Cdd:COG0243 372 VYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSE----DRRVHLSRPAVEPPGE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 470 ALHDWEIFVGLASAFAAKAERALKPTlpPAQMIDRGLRAGLYgdassHKLSLETLDSHpHGLDLGALKANL---AQRLKT 546
Cdd:COG0243 448 ARSDWEIFAELAKRLGFEEAFPWGRT--EEDYLRELLEATRG-----RGITFEELREK-GPVQLPVPPEPAfrnDGPFPT 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 547 ANGRIQAAPEVI-MADLARFAADPSPQASE-----LLLIGRRHVRSNNSWMHNYHRLVKGKPRHQLLMHPDDLACRGLSD 620
Cdd:COG0243 520 PSGKAEFYSETLaLPPLPRYAPPYEGAEPLdaeypLRLITGRSRDQWHSTTYNNPRLREIGPRPVVEINPEDAAALGIKD 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336206682 621 GQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHSRSGVKmaiaqslpGVSANDLTDERqLDVLSGNAALNGVPVQV 699
Cdd:COG0243 600 GDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPADDK--------GGNVNVLTPDA-TDPLSGTPAFKSVPVRV 669
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
10-699 |
1.54e-104 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 333.77 E-value: 1.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 10 CHLCEAICGLVIEtvVEADsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGDQWQPIAWQQAFDLV 89
Cdd:COG3383 11 CPYCGVGCGIDLE--VKDG---KIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDEALDLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 90 AERLYAIQQRHGQNAVAVYQGNpsvhnyGLMTHSNYFL-----GLLKTRN-----RF-SATSVDQLPHHLSSFLMYGhgm 158
Cdd:COG3383 86 AERLREIQAEHGPDAVAFYGSG------QLTNEENYLLqklarGVLGTNNidnnaRLcMASAVAGLKQSFGSDAPPN--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 159 llPIPDIDHTDFMLILGGNPLASNgsimtvPDVEKRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLL 238
Cdd:COG3383 157 --SYDDIEEADVILVIGSNPAEAH------PVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 239 NTLFEEGLTRESHLP--VDGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAV-CYGrMGVSTQTFGTlcHW 315
Cdd:COG3383 229 HVIIEEGLVDEDFIAerTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMiLWG-MGVNQHTQGT--DN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 316 LAQLINL--VTGNLDRVG------------------GALCTE-PA-VDLVSSTSGGHFNR-WQsrVSGLPEYGGeLPVSA 372
Cdd:COG3383 306 VNAIINLalATGNIGRPGtgpfpltgqnnvqggrdmGALPNVlPGyRDVTDPEHRAKVADaWG--VPPLPDKPG-LTAVE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 373 LAEEMlvdGEGQVRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENdhyDTTFnTLA 452
Cdd:COG3383 383 MFDAI---ADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEK---DGTF-TNT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 453 VRNVTRFNRAIfDKPEGALHDWEIFVGLASAFAAKAERAlkptlPPAQMID--RGLrAGLYGDASSHKLSLE-------T 523
Cdd:COG3383 456 ERRVQRVRKAV-EPPGEARPDWEIIAELARRLGYGFDYD-----SPEEVFDeiARL-TPDYSGISYERLEALggvqwpcP 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 524 LDSHPHGLDLgalkanLAQRLKTANGRiqaapevimadlARFAADPSPQASE-------LLLI-GRRhvrsnnswMHNYH 595
Cdd:COG3383 529 SEDHPGTPRL------FTGRFPTPDGK------------ARFVPVEYRPPAElpdeeypLVLTtGRL--------LDQWH 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 596 ---------RLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHSRsgvkmaia 666
Cdd:COG3383 583 tgtrtrrspRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMPFHWGEGA-------- 654
|
730 740 750
....*....|....*....|....*....|...
gi 1336206682 667 qslpgvsANDLTDERqLDVLSGNAALNGVPVQV 699
Cdd:COG3383 655 -------ANALTNDA-LDPVSKQPEYKACAVRV 679
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
9-484 |
1.90e-92 |
|
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: 292.31 E-value: 1.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 9 ACHLCEAICGLVIETVVEadsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSG--DQWQPIAWQQAF 86
Cdd:cd00368 3 VCPFCGVGCGILVYVKDG-----KVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 87 DLVAERLYAIQQRHGQNAVAVYQGNPSVHNYglMTHSNYFLGLLKTRNRFSATSVDQLPHHLSSFLMYGHGMLLPIPDID 166
Cdd:cd00368 78 DEIAEKLKEIREKYGPDAIAFYGGGGASNEE--AYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTLADIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 167 HTDFMLILGGNPLASNGSIMTvpdvekRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFgllntlfeegl 246
Cdd:cd00368 156 NADLILLWGSNPAETHPVLAA------RLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALAL----------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 247 treshlpvdgleqvrqaiagftAEAMSPRCGIAAEQIRQLARDFAAADKAVCYGRMGVSTQTFGTLCHWLAQLINLVTGN 326
Cdd:cd00368 219 ----------------------AEWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 327 LDRVGGALCTepavdlvsstsgghfnrwqsrvsglpeyggelpvsalaeemlvdgegqvralvtvAGNPVLSTPNGRQLE 406
Cdd:cd00368 277 IGRPGGGLGP-------------------------------------------------------GGNPLVSAPDANRVR 301
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336206682 407 QALEGLEFMLSIDLYINETTRHADLILPSTSALEndHYDTTFNTlaVRNVTRFNRAIfdKPEG-ALHDWEIFVGLASAF 484
Cdd:cd00368 302 AALKKLDFVVVIDIFMTETAAYADVVLPAATYLE--KEGTYTNT--EGRVQLFRQAV--EPPGeARSDWEILRELAKRL 374
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
9-487 |
3.28e-79 |
|
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: 263.32 E-value: 3.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 9 ACHLCEAICGLVIetVVEADsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRS-GDQWQPIAWQQAFD 87
Cdd:cd02754 3 TCPYCGVGCGVEI--GVKDG---KVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRnGGELVPVSWDEALD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 88 LVAERLYAIQQRHGQNAVAVYQGnpsvhnyG-LMTHSNYFL-----GLLKTRN-----RF---SATSVdqlphHLSSFlm 153
Cdd:cd02754 78 LIAERFKAIQAEYGPDSVAFYGS-------GqLLTEEYYAAnklakGGLGTNNidtnsRLcmaSAVAG-----YKRSF-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 154 yghGMLLPIP---DIDHTDFMLILGGNPLASNGSIMtvPDVEKRLKAiqQRGGKLVVIDPRRSETAAIADQHLFVRPGGD 230
Cdd:cd02754 144 ---GADGPPGsydDIEHADCFFLIGSNMAECHPILF--RRLLDRKKA--NPGAKIIVVDPRRTRTADIADLHLPIRPGTD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 231 AALLFGLLNTLFEEGLTRE----SHlpVDGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAVCYGRMGVST 306
Cdd:cd02754 217 LALLNGLLHVLIEEGLIDRdfidAH--TEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 307 QTFGTlchWLAQLIN---LVTGNLDRVGGAL------CTEPAVDLVSSTS---GGH--FNRWQSR-----VSGLPEygGE 367
Cdd:cd02754 295 STQGT---AANNAIInlhLATGKIGRPGSGPfsltgqPNAMGGREVGGLAnllPGHrsVNNPEHRaevakFWGVPE--GT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 368 LP--VSALAEEMLVD-GEGQVRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYI-NETTRHADLILPSTSALEndh 443
Cdd:cd02754 370 IPpkPGLHAVEMFEAiEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAFAdTETAEYADLVLPAASWGE--- 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1336206682 444 yDTTFNTLAVRNVTRFNRAIfDKPEGALHDWEIFVGLASAFAAK 487
Cdd:cd02754 447 -KEGTMTNSERRVSLLRAAV-EPPGEARPDWWILADVARRLGFG 488
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
10-483 |
6.07e-79 |
|
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: 260.99 E-value: 6.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 10 CHLCEAICGLVIETVVEadsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGDQWQPIAWQQAFDLV 89
Cdd:cd02753 4 CPYCGVGCGLELWVKDN-----KIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEALSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 90 AERLYAIQQRHGQNAVAVYqGNPSVHNyglmtHSNYFLGLLkTRNRFSATSVD---QLPHH-----LSSFLMYGhGMLLP 161
Cdd:cd02753 79 ASRLKEIKDKYGPDAIAFF-GSAKCTN-----EENYLFQKL-ARAVGGTNNVDhcaRLCHSptvagLAETLGSG-AMTNS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 162 IPDIDHTDFMLILGGNPLASNGSIMTvpdvekRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLNTL 241
Cdd:cd02753 151 IADIEEADVILVIGSNTTEAHPVIAR------RIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 242 FEEGLTRESHLP--VDGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAVCYGRMGVSTQTFGT-----LCH 314
Cdd:cd02753 225 IEEGLYDEEFIEerTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTdnvmaLSN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 315 wLAqlinLVTGNLDRVGGalctepavdlvsstsGGHFNRWQSRVSG------LPEYggeLPvsalaeemlvdgeGQVRAL 388
Cdd:cd02753 305 -LA----LLTGNIGRPGT---------------GVNPLRGQNNVQGacdmgaLPNV---LP-------------GYVKAL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 389 VTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENdhyDTTFnTLAVRNVTRFNRAIfDKPE 468
Cdd:cd02753 349 YIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEK---DGTF-TNTERRVQRVRKAV-EPPG 423
|
490
....*....|....*
gi 1336206682 469 GALHDWEIFVGLASA 483
Cdd:cd02753 424 EARPDWEIIQELANR 438
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
10-481 |
6.49e-72 |
|
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: 241.44 E-value: 6.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 10 CHLCEAICGLVIEtvVEADsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGDQ----WQPIAWQQA 85
Cdd:cd02759 4 CPGCHSGCGVLVY--VKDG---KLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGERgenkWERISWDEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 86 FDLVAERLYAIQQRHGQNAVAVYQGNPSvhNYGLMTH--SNYFLGLLKTRNRFSATSVDQLPHHLSSFLMYGHGMLLPIP 163
Cdd:cd02759 79 LDEIAEKLAEIKAEYGPESIATAVGTGR--GTMWQDSlfWIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLGYDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 164 DIDHTDFMLILGGNPLASNGSIMTVpdvekRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLNTLFE 243
Cdd:cd02759 157 DWENPECIVLWGKNPLNSNLDLQGH-----WLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIIN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 244 EGL------TRESHlpvdGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAvcYGRMGV-------STQTFG 310
Cdd:cd02759 232 EGLydkdfvENWCY----GFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPA--CIQWGLaidqqknGTQTSR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 311 TLCHWLAqlinlVTGNLDRVGGALCTEPAvdlvsstsgghfnrwqsrvsglpeyggelpvsalaeemlvdgegqVRALVT 390
Cdd:cd02759 306 AIAILRA-----ITGNLDVPGGNLLIPYP---------------------------------------------VKMLIV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 391 VAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENDHYDTTF---NTLAVRnvtrfNRAIFDKP 467
Cdd:cd02759 336 FGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFeaeNFVQLR-----QKAVEPYG 410
|
490
....*....|....
gi 1336206682 468 EgALHDWEIFVGLA 481
Cdd:cd02759 411 E-AKSDYEIVLELG 423
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
6-483 |
2.51e-70 |
|
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: 236.42 E-value: 2.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 6 HYRACHLCEAICGlvIETVVEADsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGD----QWQPIA 81
Cdd:cd02755 1 VPSICEMCSSRCG--ILARVEDG---RVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGErgegKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 82 WQQAFDLVAERLYAIQQRHGQNAVAVyqgnpSVHNYGLMTHSNYFLGLLKTRNRFSATSVDQLPHHLSSFLMY--GHGML 159
Cdd:cd02755 76 WDEALQYIASKLKEIKEQHGPESVLF-----GGHGGCYSPFFKHFAAAFGSPNIFSHESTCLASKNLAWKLVIdsFGGEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 160 LPipDIDHTDFMLILGGNPLASngsiMTVPDVeKRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLN 239
Cdd:cd02755 151 NP--DFENARYIILFGRNLAEA----IIVVDA-RRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 240 TLFEEGLTRESHLP--VDGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAVCY--GRMGV-STQTFGTlch 314
Cdd:cd02755 224 VLISENLYDAAFVEkyTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVdpGWRGTfYSNSFQT--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 315 WLAQLI-NLVTGNLDRVGGalctepavdlvsstsgghfnrwqsrvsglpeyggeLPVSALAeemlvdGEGQVRALVTVAG 393
Cdd:cd02755 301 RRAIAIiNALLGNIDKRGG-----------------------------------LYYAGSA------KPYPIKALFIYRT 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 394 NPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENDHYDTTFNTLAVRNVTRFnRAIFDKPEgALHD 473
Cdd:cd02755 340 NPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAVATRQ-RAIEPLYD-TRPG 417
|
490
....*....|
gi 1336206682 474 WEIFVGLASA 483
Cdd:cd02755 418 WDILKELARR 427
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
9-559 |
5.87e-68 |
|
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: 231.37 E-value: 5.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 9 ACHL-CEAICGLVIETvveadSAPRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGD---QWQPIAWQQ 84
Cdd:cd02766 3 VCPLdCPDTCSLLVTV-----EDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRkggQWERISWDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 85 AFDLVAERLYAIQQRHGQNAVAVYqgnpsvHNYGLMTHSNYflgllKTRNRFS----ATSVDQLP----HHLSSFLMYGH 156
Cdd:cd02766 78 ALDTIAAKLKEIKAEYGPESILPY------SYAGTMGLLQR-----AARGRFFhalgASELRGTIcsgaGIEAQKYDFGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 157 GMLLPIPDIDHTDFMLILGGNPLASNGSIMtvpdveKRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFG 236
Cdd:cd02766 147 SLGNDPEDMVNADLIVIWGINPAATNIHLM------RIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 237 LLNTLFEEGLTRESHLP--VDGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAvcYGRMGVSTQTF---GT 311
Cdd:cd02766 221 VAKVLFREGLYDRDFLArhTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPP--SIRLGYGMQRYrngGQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 312 LCHWLAqLINLVTGNLDRVGGAlctepavdLVSSTSGghfnrwqsrvsglpeyggelpvsalaeemlvdgeGQVRALVTV 391
Cdd:cd02766 299 NVRAID-ALPALTGNIGVPGGG--------AFYSNSG----------------------------------PPVKALWVY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 392 AGNPVLSTPNGRQLEQAL-EGLEFMLSIDLYINETTRHADLILPSTSALEND--HYDTTFNTLAVrnvtrfNRAIFDKPE 468
Cdd:cd02766 336 NSNPVAQAPDSNKVRKGLaREDLFVVVHDQFMTDTARYADIVLPATTFLEHEdvYASYWHYYLQY------NEPAIPPPG 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 469 GALHDWEIFVGLASAFAAKAERALkptLPPAQMIDRGLRAGLygdassHKLSLETLDSHPHGLDLGALKANLAQR-LKTA 547
Cdd:cd02766 410 EARSNTEIFRELAKRLGFGEPPFE---ESDEEWLDQALDGTG------LPLEGIDLERLLGPRKAGFPLVAWEDRgFPTP 480
|
570
....*....|..
gi 1336206682 548 NGRIQAAPEVIM 559
Cdd:cd02766 481 SGKFEFYSERAA 492
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
572-702 |
2.53e-63 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 206.47 E-value: 2.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 572 QASELLLIGRRHVRSNNSWMHNYHRLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLP 651
Cdd:cd02782 1 DYPFLLLIGRRHLRSNNSWLHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1336206682 652 HGWGHSRSGVKmaIAQSLPGVSANDLTDERQLDVLSGNAALNGVPVQVVAC 702
Cdd:cd02782 81 HGWGHDYPGVS--GAGSRPGVNVNDLTDDTQRDPLSGNAAHNGVPVRLARV 129
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
10-440 |
1.09e-47 |
|
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: 176.48 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 10 CHLCEAICGLVIETVVEadsapRIASIKGDPLDTFSRGHICPKA-VALQDIQnDPDRLRQPMLRSG--------DQWQPI 80
Cdd:cd02757 6 CQGCTAWCGLQAYVEDG-----RVTKVEGNPLHPGSRGRLCAKGhLGLQQVY-DPDRILYPMKRTNprkgrdvdPKFVPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 81 AWQQAFDLVAERLYAIQQRHGQNAVAVYQGNPSVHNYGLMthsNYFLGLLKTRNRFSATSVDQLPHHLSSFlMYGHGMLL 160
Cdd:cd02757 80 SWDEALDTIADKIRALRKENEPHKIMLHRGRYGHNNSILY---GRFTKMIGSPNNISHSSVCAESEKFGRY-YTEGGWDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 161 PIPDIDHTDFMLILGGNPLASN----GSIMTVPDVEKRlkaiqqrgGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFG 236
Cdd:cd02757 156 NSYDYANAKYILFFGADPLESNrqnpHAQRIWGGKMDQ--------AKVVVVDPRLSNTAAKADEWLPIKPGEDGALALA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 237 LLNTLFEEGL-----------------TRESHLPVDG--------LEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFA 291
Cdd:cd02757 228 IAHVILTEGLwdkdfvgdfvdgknyfkAGETVDEESFkeksteglVKWWNLELKDYTPEWAAKISGIPAETIERVAREFA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 292 -AADKAVCYGRMGVSTQTFGTL----CHWLaqliNLVTGNLDRVGGaLCTepavdlvsstsgghfNRWqsrvsglpeygg 366
Cdd:cd02757 308 tAAPAAAAFTWRGATMQNRGSYnsmaCHAL----NGLVGSIDSKGG-LCP---------------NMG------------ 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336206682 367 elpvsalaeemlvdgEGQVRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALE 440
Cdd:cd02757 356 ---------------VPKIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFE 414
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
9-489 |
1.18e-45 |
|
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: 172.41 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 9 ACHLCeaicglVIETVVEADsapRIASIKGDPLDTfsrGHICPKAVALQDIQNDPDRLRQPMLRSG-------------- 74
Cdd:cd02751 3 ACHWG------PFKAHVKDG---VIVRVEPDDTDQ---PRPCPRGRSVRDRVYSPDRIKYPMKRVGwlgngpgsrelrge 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 75 DQWQPIAWQQAFDLVAERLYAIQQRHGQNAVavYQGNPSVHNYGLMTHS--------NYFLGLLKTRNRFS-ATSVDQLP 145
Cdd:cd02751 71 GEFVRISWDEALDLVASELKRIREKYGNEAI--FGGSYGWASAGRLHHAqsllhrflNLIGGYLGSYGTYStGAAQVILP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 146 HHLSSFLMYGHGMLLPipDI-DHTDFMLILGGNPLASNGSIMTVPD--VEKRLKAIQQRGGKLVVIDPRRSETAA-IADQ 221
Cdd:cd02751 149 HVVGSDEVYEQGTSWD--DIaEHSDLVVLFGANPLKTRQGGGGGPDhgSYYYLKQAKDAGVRFICIDPRYTDTAAvLAAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 222 HLFVRPGGDAALLFGLLNTLFEEGLTRESHLP--VDGLEQVRQAIAGF------TAEAMSPRCGIAAEQIRQLARDFAAA 293
Cdd:cd02751 227 WIPIRPGTDVALMLAMAHTLITEDLHDQAFLAryTVGFDEFKDYLLGEsdgvpkTPEWAAEITGVPAETIRALAREIASK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 294 DKAVCYGrMGVSTQTFGTLCHWLAQLINLVTGNLDRVGGALCtepavdLVSSTSGGHFNRWQSRVSGLPEYGGE-----L 368
Cdd:cd02751 307 RTMIAQG-WGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFG------FGYGYSNGGGPPRGGAGGPGLPQGKNpvkdsI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 369 PVSALAeEML------VDGEGQ------VRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPST 436
Cdd:cd02751 380 PVARIA-DALlnpgkeFTANGKlktypdIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPAT 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1336206682 437 SALENDhyDTTFNTLAVRN-VTRFNRAIfdKPEG-ALHDWEIFVGLASAFAAKAE 489
Cdd:cd02751 459 TSLERN--DIGLTGNYSNRyLIAMKQAV--EPLGeARSDYEIFAELAKRLGVEEE 509
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
10-494 |
2.28e-44 |
|
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: 169.12 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 10 CHLCEAICGLVIETVVEadsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSG--DQWQPIAWQQAFD 87
Cdd:cd02752 4 CPYCSVGCGLIAYVQNG-----VWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPgsGKWEEISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 88 LVAERLYAIQQRH--GQNAVAVYQGNP-SVHNYGLMTHSN---Y-------FLGLLKTRNR---FSATSVDQLPhhlSSF 151
Cdd:cd02752 79 EIARKMKDIRDASfvEKNAAGVVVNRPdSIAFLGSAKLSNeecYlirkfarALGTNNLDHQariUHSPTVAGLA---NTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 152 lmyGHG-MLLPIPDIDHTDFMLILGGNPlASNGSImtvpDVEKRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGD 230
Cdd:cd02752 156 ---GRGaMTNSWNDIKNADVILVMGGNP-AEAHPV----SFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 231 AALLFGLLNTLFEegltreshlpvdgleqvrqaiagFTAEAMSPRCGIAAEQIRQLARDFAA---ADKA--VCYGrMGVS 305
Cdd:cd02752 228 IAFLGGMINYIIR-----------------------YTPEEVEDICGVPKEDFLKVAEMFAAtgrPDKPgtILYA-MGWT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 306 TQTFGTLCHWLAQLINLVTGNLDRVGG---ALctepavdlvsstsGGHFNrwqsrVSGLPEYGG---ELPvsalaeemlv 379
Cdd:cd02752 284 QHTVGSQNIRAMCILQLLLGNIGVAGGgvnAL-------------RGHSN-----VQGATDLGLlshNLP---------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 380 dgeGQVRALvtvagNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHAD-------------LILPSTSALENDHYDT 446
Cdd:cd02752 336 ---GYLGGQ-----NPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGSIT 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1336206682 447 TFNtlavRNVTRFNRAIfDKPEGALHDWEIFVGLASA--FAAKAERALKP 494
Cdd:cd02752 408 NSG----RWLQWRYKVV-EPPGEAKSDGDILVELAKRlgFLYEKEGGAFP 452
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
10-631 |
3.58e-44 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 169.85 E-value: 3.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 10 CHLCEAICglVIETVVEADsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGD----QWQPIAWQQA 85
Cdd:PRK15488 48 CEMCSTRC--PIEARVVNG---KNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGErgegKWQEISWDEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 86 FDLVAERLYAIQQRHGQNAVAVyqGNPSVHNYGLMTHSNYFLGllkTRNRFSATSVDQLPHHLSSFLMYGHGMLLpipDI 165
Cdd:PRK15488 123 YQEIAAKLNAIKQQHGPESVAF--SSKSGSLSSHLFHLATAFG---SPNTFTHASTCPAGYAIAAKVMFGGKLKR---DL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 166 DHTDFMLILGGNPLASngsiMTVPDVEKRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLNTLFEEG 245
Cdd:PRK15488 195 ANSKYIINFGHNLYEG----INMSDTRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEEN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 246 LTRESHLP--VDGLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFA-AADKAVC-YG-RMGVSTQTFGtlchwLAQLI 320
Cdd:PRK15488 271 LYDKAFVEryTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAaAAPHAIVdFGhRATFTPEEFD-----MRRAI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 321 ---NLVTGNLDRVGGalctepavdLVSSTSGGHFNRW--QSRVSGLPEYGGE-LPVSA-----LAEE---MLVDGEG--- 383
Cdd:PRK15488 346 faaNVLLGNIERKGG---------LYFGKNASVYNKLagEKVAPTLAKPGVKgMPKPTakridLVGEqfkYIAAGGGvvq 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 384 ------------QVRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENDHYDTTFNTL 451
Cdd:PRK15488 417 siidatltqkpyQIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISDKSGK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 452 ----AVRNvtrfnrAIFDKPEGALHDWEIFVGLASA-----------------FAAKAERALKPTLPPAQMIDRGLRAGL 510
Cdd:PRK15488 497 npayALRQ------RVVEPIGDTKPSWQIFKELGEKmglgqyypwqdmetlqlYQVNGDHALLKELKKKGYVSFGVPLLL 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 511 YGDASSHKLSLETLDSHPHGLDlGALKANLaqRLKTANGRIQAAPEVIMADLA-----RFAADPSPQASELLLI-GRRHV 584
Cdd:PRK15488 571 REPKMVAKFVARYPNAKAVDED-GTYGSQL--KFKTPSGKIELFSAKLEALAPgygvpRYRDVALKKEDELYFIqGKVAV 647
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1336206682 585 RSN-----NSWMHNyhrLVKGKPrhqLLMHPDDLACRGLSDGQQVRVSSRVG 631
Cdd:PRK15488 648 HTNgatqnVPLLAN---LMSDNA---VWIHPQTAGKLGIKNGDEIRLENSVG 693
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
46-485 |
1.44e-35 |
|
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: 140.53 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 46 RGhiCPKAVALQDIQNDPDRLRQPMLRSGDQ----WQPIAWQQAFDLVAERLYAIQQRHGQNAVAVYQGNPSVhnyGLMT 121
Cdd:cd02750 49 RG--CQRGASFSWYLYSPDRVKYPLKRVGARgegkWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAM---SMVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 122 HSNYFlgllktrnRFsATSVDQLPHHL---------SSFLMYG-HGMLLPIPDIDHTDFMLILGGNPlasngsIMT-VPD 190
Cdd:cd02750 124 YAAGS--------RF-ASLIGGVSLSFydwygdlppGSPQTWGeQTDVPESADWYNADYIIMWGSNV------PVTrTPD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 191 VEKRLKAiQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLNTLFEEGLTRESHLPvdglEQVRQAIAGFTAE 270
Cdd:cd02750 189 AHFLTEA-RYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLK----EYTDLPFLVYTPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 271 AMSPRCGIAAEQIRQLARDFAAADKAVCYgrMGVSTQTF--GTLCHWLAQLINLVTGNLDRVGGalctepavdlvsstsg 348
Cdd:cd02750 264 WQEAITGVPRETVIRLAREFATNGRSMII--VGAGINHWyhGDLCYRALILLLALTGNEGKNGG---------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 349 ghfnrwqsrvsGLPEYggelpvsalaeemlvdgEGQVRALVTVAGNPVLSTPNGRQL-EQALEG-LEFMLSIDLYINETT 426
Cdd:cd02750 326 -----------GWAHY-----------------VGQPRVLFVWRGNLFGSSGKGHEYfEDAPEGkLDLIVDLDFRMDSTA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 427 RHADLILPSTSALENDHYDTT-FNTLavrnVTRFNRAIfDKPEGALHDWEIFVGLASAFA 485
Cdd:cd02750 378 LYSDIVLPAATWYEKHDLSTTdMHPF----IHPFSPAV-DPLWEAKSDWEIFKALAKKVP 432
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
7-440 |
5.52e-35 |
|
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: 141.71 E-value: 5.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 7 YRACHLCEAICGLVIETVVEADsapRIASIKGDP---------LD------------------TFSRGHICPKAVALQDI 59
Cdd:cd02758 1 YSSCLGCWTQCGIRVRVDKETG---KVLRIAGNPyhplntapsLPyntplkeslylslvgengLKARATACARGNAGLQY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 60 QNDPDRLRQPMLRSG----DQWQPIAWQQAFDLVAE--RLYAIQQRHG---------------------QNAVAVYQGNP 112
Cdd:cd02758 78 LYDPYRVLQPLKRVGprgsGKWKPISWEQLIEEVVEggDLFGEGHVEGlkairdldtpidpdhpdlgpkANQLLYTFGRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 113 SVHNYGLMTHSNYFLGllkTRNRFSATSVDQLPHHLSSFLMYG--HGMLLPIPDIDHTDFMLILGGNP-LASNGsimtvP 189
Cdd:cd02758 158 EGRTPFIKRFANQAFG---TVNFGGHGSYCGLSYRAGNGALMNdlDGYPHVKPDFDNAEFALFIGTSPaQAGNP-----F 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 190 DVEKRL--KAIQQRGGKLVVIDPRRSETAAIADQH---LFVRPGGDAALLFGLLNTLFEEG------------------- 245
Cdd:cd02758 230 KRQARRlaEARTEGNFKYVVVDPVLPNTTSAAGENirwVPIKPGGDGALAMAMIRWIIENErynaeylsipskeaakaag 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 246 ---LTRESHLPVD-----GLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAVCYGRMGVSTQTFGTLCHWLA 317
Cdd:cd02758 310 epsWTNATHLVITvrvksALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHSNGFYNAYAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 318 QLINLVTGNLDRVGGALCT---------EPAVDLvsSTSGGHFNRWqsrvsGLP------------EY-----GGELP-- 369
Cdd:cd02758 390 RMLNALIGNLNWKGGLLMSgggfadnsaGPRYDF--KKFFGEVKPW-----GVPidrskkayektsEYkrkvaAGENPyp 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 370 --------VSALAEEMLVD-GEG---QVRALVTVAGNPVLSTPNGR-QLEQAL---EGLEFMLSIDLYINETTRHADLIL 433
Cdd:cd02758 463 akrpwyplTPELYTEVIASaAEGypyKLKALILWMANPVYGAPGLVkQVEEKLkdpKKLPLFIAIDAFINETSAYADYIV 542
|
....*..
gi 1336206682 434 PSTSALE 440
Cdd:cd02758 543 PDTTYYE 549
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
65-483 |
2.07e-32 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 129.06 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 65 RLRQPMLRSGD-QWQPIAWQQAFDLVAERLYAIQQRHGQNAVAVYQGNPSvhnyGLMTHSNYFLG-LLKTRNRFSATSVD 142
Cdd:pfam00384 1 RLKYPMVRRGDgKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGG----LTDVESLYALKkLLNRLGSKNGNTED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 143 QLPHH-------LSSFLMYGHGMLLPIPDIDHTDFMLILGGNPLasngsiMTVPDVEKRL-KAIQQRGGKLVVIDPRRSE 214
Cdd:pfam00384 77 HNGDLctaaaaaFGSDLRSNYLFNSSIADIENADLILLIGTNPR------EEAPILNARIrKAALKGKAKVIVIGPRLDL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 215 TaaIADQHLFVRPGGDAALLFGLLNTLFEEGLtreshlpvdgleqvrqaiagftaeamsprcgiaaeqirqLARDFAAAd 294
Cdd:pfam00384 151 T--YADEHLGIKPGTDLALALAGAHVFIKELK---------------------------------------KDKDFAPK- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 295 KAVCYGrMGVSTQTFGTLCHWLAQLINLVTGNLDRVGGalctepavdlvSSTSGGHFNRWQSRVSGLPEygGELPVSALA 374
Cdd:pfam00384 189 PIIIVG-AGVLQRQDGEAIFRAIANLADLTGNIGRPGG-----------GWNGLNILQGAASPVGALDL--GLVPGIKSV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 375 EEMLVDGEGQVRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETT-RHADLILPSTSALENDhyDTTFNTLav 453
Cdd:pfam00384 255 EMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDKTaKYADVILPAAAYTEKN--GTYVNTE-- 330
|
410 420 430
....*....|....*....|....*....|
gi 1336206682 454 RNVTRFNRAIFDKPEgALHDWEIFVGLASA 483
Cdd:pfam00384 331 GRVQSTKQAVPPPGE-AREDWKILRALSEV 359
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
65-482 |
2.98e-32 |
|
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: 132.05 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 65 RLRQPM-LRSG-DQWQPIAWQQAFDLVAERLYAIQQRH--------GQNAVA-VYQ------GNPSVHNYGLMTHSnyfl 127
Cdd:cd02767 64 RLTYPMrYDAGsDHYRPISWDEAFAEIAARLRALDPDRaafytsgrASNEAAyLYQlfarayGTNNLPDCSNMCHE---- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 128 gllktrnrfsATSVdQLPHHLSSflmyGHGMLLpIPDIDHTDFMLILGGNPlASNGSIMTvpdveKRLKAIQQRGGKLVV 207
Cdd:cd02767 140 ----------PSSV-GLKKSIGV----GKGTVS-LEDFEHTDLIFFIGQNP-GTNHPRML-----HYLREAKKRGGKIIV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 208 IDPRRsETA------------------AIADQHLFVRPGGDAALLFGLLNTLFEEGLTRESHLPVD-------GLEQVRQ 262
Cdd:cd02767 198 INPLR-EPGlerfanpqnpesmltggtKIADEYFQVRIGGDIALLNGMAKHLIERDDEPGNVLDHDfiaehtsGFEEYVA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 263 AIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKAV-CYGrMGVSTQTFGTLChwLAQLIN--LVTGNLDRVGGALCtePA 339
Cdd:cd02767 277 ALRALSWDEIERASGLSREEIEAFAAMYAKSERVVfVWG-MGITQHAHGVDN--VRAIVNlaLLRGNIGRPGAGLM--PI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 340 vdlvsstsGGHFNRWQSRVSGLPE-------------YGGELP------VSALAEEMLvdgEGQVRALVTVAGNPVLSTP 400
Cdd:cd02767 352 --------RGHSNVQGDRTMGITEkpfpefldaleevFGFTPPrdpgldTVEAIEAAL---EGKVKAFISLGGNFAEAMP 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 401 NGRQLEQALEGLEFMLSIDLYINETTRH---ADLILPSTSALENDHYDTTFNTLAV----------RNVTRFNRAIFDKP 467
Cdd:cd02767 421 DPAATEEALRRLDLTVHVATKLNRSHLVhgeEALILPCLGRTEIDMQAGGAQAVTVedsmsmthtsRGRLKPASRVLLSE 500
|
490 500
....*....|....*....|....*..
gi 1336206682 468 EGALH------------DWEIFVGLAS 482
Cdd:cd02767 501 EAIVAgiagarlgeakpEWEILVEDYD 527
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
63-481 |
4.52e-31 |
|
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: 128.98 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 63 PDRLRQPMLRSG----DQWQPIAWQQAFDLVAERLYAIQQRHGQNAVAVYQGNPSvhnYGLMTHS--------NYFLGLL 130
Cdd:cd02770 57 PDRLKYPMKRVGkrgeGKFVRISWDEALDTIASELKRIIEKYGNEAIYVNYGTGT---YGGVPAGrgaiarllNLTGGYL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 131 KTRNRFSATSV-DQLPHhlsSFLMYGHGMLLpiPDIDHTDFMLILGGNPLASNGSIMTVPDVEKRLKaiqQRGGKLVVID 209
Cdd:cd02770 134 NYYGTYSWAQItTATPY---TYGAAASGSSL--DDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAK---KAGAKFIVID 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 210 PRRSETAA-IADQHLFVRPGGDAALLFGLLNTLFEEGLTR------------ESHLP--VDGLEQVRQAIAGF------- 267
Cdd:cd02770 206 PRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDqafldrycvgfdAEHLPegAPPNESYKDYVLGTgydgtpk 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 268 TAEAMSPRCGIAAEQIRQLARDFAAADK-AVCYGRmGVSTQTFGTLCHWLAQLINLVTGNLDRVG---GALCTEPAVDlV 343
Cdd:cd02770 286 TPEWASEITGVPAETIRRLAREIATTKPaAILQGW-GPQRHANGEQAARAIMMLAAMTGNVGIPGgntGARPGGSAYN-G 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 344 SSTSGGHfNRWQSRVSGLP-----EYGGELPvsalAEEMLVDGEGQVRA----LVTVAGNPVLSTPNG-----RQLEQAL 409
Cdd:cd02770 364 AGLPAGK-NPVKTSIPCFMwtdaiERGEEMT----ADDGGVKGADKLKSnikmIWNYAGNTLINQHSDdnnttRALLDDE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336206682 410 EGLEFMLSIDLYINETTRHADLILPSTSALENDHYDTTFNTLAVRNVTRFNRAIfdKPEG-ALHDWEIFVGLA 481
Cdd:cd02770 439 SKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNAGMMEYLIYSQKAI--EPLYeCKSDYEICAELA 509
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
58-489 |
1.31e-30 |
|
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: 127.38 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 58 DIQNDPDRLRQPMLRSG---------------DQWQPIAWQQAFDLVAERLYAIQQRHGqnAVAVYQGNPSVHNYGLMTH 122
Cdd:cd02769 39 DAVYSPTRIKYPMVRRGwlekgpgsdrslrgkEEFVRVSWDEALDLVAAELKRVRKTYG--NEAIFGGSYGWSSAGRFHH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 123 SNY----FLGLL----KTRNRFS--ATSVdQLPHHLSSFLMYGhGMLLPIPDI-DHTDFMLILGGNPLaSNGSIM--TVP 189
Cdd:cd02769 117 AQSllhrFLNLAggyvGSVGDYStgAAQV-ILPHVVGSMEVYT-EQQTSWPVIaEHTELVVAFGADPL-KNAQIAwgGIP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 190 D--VEKRLKAIQQRGGKLVVIDPRRSETAAIAD-QHLFVRPGGDAALLFGLLNTLFEEGLTRESHLP--VDGLEQVRQAI 264
Cdd:cd02769 194 DhqAYSYLKALKDRGIRFISISPLRDDTAAELGaEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLAryTVGFDKFLPYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 265 AGF------TAEAMSPRCGIAAEQIRQLARDFaAADKAVCYGRMGVSTQTFGTLCHWLAqlINLVT--GNLDRVGGAL-- 334
Cdd:cd02769 274 LGEsdgvpkTPEWAAAICGIPAETIRELARRF-ASKRTMIMAGWSLQRAHHGEQPHWMA--VTLAAmlGQIGLPGGGFgf 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 335 ---CTEPAVDLVSSTSGGHFNRWQSRVSGLpeyggeLPVSALAEEMLVDGE-----GQ------VRALVTVAGNPVLSTP 400
Cdd:cd02769 351 gyhYSNGGGPPRGAAPPPALPQGRNPVSSF------IPVARIADMLLNPGKpfdynGKkltypdIKLVYWAGGNPFHHHQ 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 401 NGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENDhyDTTFNT-----LAVRNVTrfnraifdKPEG-ALHDW 474
Cdd:cd02769 425 DLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERN--DIGGSGdnryiVAMKQVV--------EPVGeARDDY 494
|
490
....*....|....*
gi 1336206682 475 EIFVGLASAFAAKAE 489
Cdd:cd02769 495 DIFADLAERLGVEEQ 509
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-440 |
5.63e-30 |
|
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: 126.10 E-value: 5.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 7 YRACHLCEAICGlvIETVVEADsapRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGD----QWQPIAW 82
Cdd:cd02763 1 TTTCYMCACRCG--IRVHLRDG---KVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPrgsgQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 83 QQAFDLVAERLYAIQQRHGQNaVAVYQGNPSVHNYglmthSNYFLGLLKTRNrFSA----TSVDQLPHHL----SSFLMY 154
Cdd:cd02763 76 EEAFSIATKRLKAARATDPKK-FAFFTGRDQMQAL-----TGWFAGQFGTPN-YAAhggfCSVNMAAGGLysigGSFWEF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 155 GHgmllpiPDIDHTD-FMLILGGNPLASNgsimtvpDVEKRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAAL 233
Cdd:cd02763 149 GG------PDLEHTKyFMMIGVAEDHHSN-------PFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 234 LFGLLNTLFEEGLtreshLPVDGLEQVRQA--IAGFTAEAMSPRCGIAAEQIRQLARDFA--AADKAV--------CYGR 301
Cdd:cd02763 216 ILALAHELLKAGL-----IDWEFLKRYTNAaeLVDYTPEWVEKITGIPADTIRRIAKELGvtARDQPIelpiawtdVWGR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 302 M---------------GVSTQTFG-TLCHWLAQLINLVtGNLDRVGGALCTEP---AVDLVSSTSGGHfnrwQSRVSGLP 362
Cdd:cd02763 291 KhekitgrpvsfhamrGIAAHSNGfQTIRALFVLMMLL-GTIDRPGGFRHKPPyprHIPPLPKPPKIP----SADKPFTP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 363 EYGGELPVSALAEEMLVDGEGQ-VRA-------------------------------------LVTVAGNPVLSTPNGRQ 404
Cdd:cd02763 366 LYGPPLGWPASPDDLLVDEDGNpLRIdkaysweyplaahgcmqnvitnawrgdpypidtlmiyMANMAWNSSMNTPEVRE 445
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1336206682 405 L-----EQALEGLEFMLSIDLYINETTRHADLILPSTSALE 440
Cdd:cd02763 446 MltdkdASGNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLE 486
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
40-484 |
2.32e-29 |
|
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: 123.36 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 40 PLDTFSRghICPKAVA-LQDIQNdPDRLRQPMLRSGD----QWQPIAWQQAFDLVAERLYAIQQRHGQNAVAVYQGNpsv 114
Cdd:cd02765 32 PDKTYKR--GCTRGLShLQRVYS-PDRLKYPMKRVGErgegKFERITWDEALDTIADKLTEAKREYGGKSILWMSSS--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 115 HNYGLMTHSNYFLGLLKTRNRFSaTSVDqlpHHLSS--FLMYGHGMLLPIPDID---HTDFMLILGGNPLASngsimTVP 189
Cdd:cd02765 106 GDGAILSYLRLALLGGGLQDALT-YGID---TGVGQgfNRVTGGGFMPPTNEITdwvNAKTIIIWGSNILET-----QFQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 190 DVEKRLKAiQQRGGKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLNTLFEEG---------------LTRE----- 249
Cdd:cd02765 177 DAEFFLDA-RENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNwydeaflksntsapfLVREdngtl 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 250 -----------------------SHLPVD---------------------GLEQVRQAIAGFTAEAMSPRCGIAAEQIRQ 285
Cdd:cd02765 256 lrqadvtatpaedgyvvwdtnsdSPEPVAatninpalegeytingvkvhtVLTALREQAASYPPKAAAEICGLEEAIIET 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 286 LARDFAAADKAVCYGRMGVSTQTFGTLCHWLAQLINLVTGNLDRVGGalctepavdlvsstsgghfnrwqsrvsglpeyg 365
Cdd:cd02765 336 LAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGG--------------------------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 366 gelpvsalaeemlvdGEGQVRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENDHYD 445
Cdd:cd02765 383 ---------------GVGQIKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLL 447
|
490 500 510
....*....|....*....|....*....|....*....
gi 1336206682 446 TTFNTlavRNVTRFNRAIFDKPEGALHDWEIFVGLASAF 484
Cdd:cd02765 448 VRYTT---HPHVLLQQKAIEPLFESKSDFEIEKGLAERL 483
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
576-696 |
3.29e-24 |
|
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: 97.73 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 576 LLLIGRRHVRSNNSWMHNYHRLVKGKPRH-QLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGW 654
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1336206682 655 GHsrsgvkmaiaqSLPGVSANDLTDERqLDVLSGNAALNGVP 696
Cdd:pfam01568 81 WY-----------EPRGGNANALTDDA-TDPLSGGPEFKTCA 110
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
7-699 |
7.52e-24 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 107.42 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 7 YRACHL-CEAICGLVIETV------VEADSApriasiKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGD---- 75
Cdd:PRK14990 60 WSACTVnCGSRCPLRMHVVdgeikyVETDNT------GDDNYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGArgeg 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 76 QWQPIAWQQAFDLVAERLYAIQQRHGQNAVAVYQGNPSVHnyGLMTHS------------NYFLGLLktrNRFSATSVDQ 143
Cdd:PRK14990 134 KFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTLG--GTMTRSwppgntlvarlmNCCGGYL---NHYGDYSSAQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 144 LPHHLSsfLMYGHGMLLPIP-DIDHTDFMLILGGNPLASNgsiMTVPDVEKRL-KAIQQRGGKLVVIDPRRSETAA-IAD 220
Cdd:PRK14990 209 IAEGLN--YTYGGWADGNSPsDIENSKLVVLFGNNPGETR---MSGGGVTYYLeQARQKSNARMIIIDPRYTDTGAgRED 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 221 QHLFVRPGGDAALLFGLLNTLFEEGLTRESHL----------------PVDG------LEQVRQAIAGfTAEAMSPRCGI 278
Cdd:PRK14990 284 EWIPIRPGTDAALVNGLAYVMITENLVDQPFLdkycvgydektlpasaPKNGhykayiLGEGPDGVAK-TPEWASQITGV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 279 AAEQIRQLARDFAAADKAVCYGRMGVSTQTFGTLCHWLAQLINLVTGNLDRVGG---------ALCTE--PAVDLVSSTS 347
Cdd:PRK14990 363 PADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGnsgaregsySLPFVrmPTLENPIQTS 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 348 GGHFnRWQSRVSGLPEyggelpVSALAEEmlVDGEGQ----VRALVTVAGNPVLSTPN----GRQLEQALEGLEFMLSID 419
Cdd:PRK14990 443 ISMF-MWTDAIERGPE------MTALRDG--VRGKDKldvpIKMIWNYAGNCLINQHSeinrTHEILQDDKKCELIVVID 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 420 LYINETTRHADLILPSTSALE-----------NDHYdTTFNTLAVRnvTRFN-RAIFDKP---------EGALHDWEIFV 478
Cdd:PRK14990 514 CHMTSSAKYADILLPDCTASEqmdfaldascgNMSY-VIFNDQVIK--PRFEcKTIYEMTselakrlgvEQQFTEGRTQE 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 479 GLASAFAAKAERALkPTLPPaqmIDRGLRAGLYG--DASSHKLSLETLDSHPHgldlgalkanlAQRLKTANGRIqaapE 556
Cdd:PRK14990 591 EWMRHLYAQSREAI-PELPT---FEEFRKQGIFKkrDPQGHHVAYKAFREDPQ-----------ANPLTTPSGKI----E 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 557 VIMADLARFAA------------------------DPSPQASELLLIGrRHVRSNNSWMHNYHRLVKGKPRHQLLMHPDD 612
Cdd:PRK14990 652 IYSQALADIAAtwelpegdvidplpiytpgfesyqDPLNKQYPLQLTG-FHYKSRVHSTYGNVDVLKAACRQEMWINPLD 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 613 LACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHSRSGVKMAIAQSLpgvsaNDLTDERQLDVLSGNAAL 692
Cdd:PRK14990 731 AQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAKRVDKGGCI-----NVLTTQRPSPLAKGNPSH 805
|
....*..
gi 1336206682 693 NGVpVQV 699
Cdd:PRK14990 806 TNL-VQV 811
|
|
| 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 ... |
61-483 |
4.01e-23 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 103.24 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 61 NDPDRLRQPMLRSGDQWQPIAWQQAFDLVAERLYAIQQrhgqnAVAVYqGNPSVHNyglmtHSNYFLG-LLKTRNRFSAT 139
Cdd:cd02771 50 NSRDRLTQPLIRRGGTLVPVSWNEALDVAAARLKEAKD-----KVGGI-GSPRASN-----ESNYALQkLVGAVLGTNNV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 140 SVDQLPHHLsSFLMYGHGMLLPIPDIDHTDFMLILGGNPLAsngsimTVPDVEKRLKAIQQRGGKLVVIDPRRSETAAIA 219
Cdd:cd02771 119 DHRARRLIA-EILRNGPIYIPSLRDIESADAVLVLGEDLTQ------TAPRIALALRQAARRKAVELAALSGIPKWQDAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 220 DQHLFVRPGGDAALLfGLLNTLFEEGLTRESHLPVDGLEQVRQAIAGFTAEAMSPRCGIAA-EQIRQLARDFAAADKAVC 298
Cdd:cd02771 192 VRNIAQGAKSPLFIV-NALATRLDDIAAESIRASPGGQARLGAALARAVDASAAGVSGLAPkEKAARIAARLTGAKKPLI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 299 ygrmgVStqtfGTLCHWLAQL-----INLVTGNLDRVGGALCTEPAVDLVsstsgghfnrwqsrvsGLPEYGGELPVSAL 373
Cdd:cd02771 271 -----VS----GTLSGSLELIkaaanLAKALKRRGENAGLTLAVEEGNSP----------------GLLLLGGHVTEPGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 374 -AEEMLVDGE-GQVRALVTVAGNPVLSTPNGRQlEQALEGLEFMLSIDLYINETTRHADLILPSTSALENdhyDTTFNTL 451
Cdd:cd02771 326 dLDGALAALEdGSADALIVLGNDLYRSAPERRV-EAALDAAEFVVVLDHFLTETAERADVVLPAASFAEK---SGTFVNY 401
|
410 420 430
....*....|....*....|....*....|..
gi 1336206682 452 AVRnVTRFNRAIFDKPEGALHDWEIFVGLASA 483
Cdd:cd02771 402 EGR-AQRFFKAYDDPAGDARSDWRWLHALAAK 432
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
65-626 |
5.21e-23 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 104.36 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 65 RLRQPML--RSGDQWQPIAWQQAFDLVAERLyaiQQRHGQNAVAVYQGnpsvhnyGLMTHSNYFLGLLKTR----NRFSA 138
Cdd:PRK09939 108 RLTQPLKydAVSDCYKPLSWQQAFDEIGARL---QSYSDPNQVEFYTS-------GRTSNEAAFLYQLFAReygsNNFPD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 139 TSvdQLPHH-----LSSFLMYGHGMLLpIPDIDHTDFMLILGGNPLASNGSIMTvpdvekRLKAIQQRGGKLVVIDPRR- 212
Cdd:PRK09939 178 CS--NMCHEptsvgLAASIGVGKGTVL-LEDFEKCDLVICIGHNPGTNHPRMLT------SLRALVKRGAKMIAINPLQe 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 213 ------------------SETaAIADQHLFVRPGGDAALLFGLLNTLFE--EGLTRESHLPVDGLEQVRQAIAGFTA--- 269
Cdd:PRK09939 249 rglerftapqnpfemltnSET-QLASAYYNVRIGGDMALLKGMMRLLIErdDAASAAGRPSLLDDEFIQTHTVGFDElrr 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 270 EAMSPR-------CGIAAEQIRQLARDFAAADKA-VCYGrMGVSTQTFGTlcHWLAQLINLV--TGNLDRVGGALCT--- 336
Cdd:PRK09939 328 DVLNSEwkdieriSGLSQTQIAELADAYAAAERTiICYG-MGITQHEHGT--QNVQQLVNLLlmKGNIGKPGAGICPlrg 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 337 ------EPAVDLVSSTSGGHFNRWQSRVSGLPEYggeLPVSALAEEMLVDGEGQVRALVTVAGNPVLSTPNGRQLEQALE 410
Cdd:PRK09939 405 hsnvqgDRTVGITEKPSAEFLARLGERYGFTPPH---APGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLT 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 411 GLEFMLSIDLYINE----TTRHAdLILPSTSALENDHYDTTFNTLAVRN---VTRFNRAIFdKPEGA--LHDWEIFVGLA 481
Cdd:PRK09939 482 QLDLAVHVATKLNRshllTARHS-YILPVLGRSEIDMQKSGAQAVTVEDsmsMIHASRGVL-KPAGVmlKSECAVVAGIA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 482 SAFAAKAERALKPTLPPAQMIDRGLRAGLYGDASSHKLSletldSHPHGLDLgaLKANLAQRLKTANGRIQAAPEvimad 561
Cdd:PRK09939 560 QAALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRI-----RHPGGFHL--INAAAERRWMTPSGKANFITS----- 627
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336206682 562 lARFAADPSPQASELLLIG--RRHVRSNNSW--MHNYHRLVKGKpRHQLLMHPDDLACRGLSDGQQVRV 626
Cdd:PRK09939 628 -KGLLEDPSSAFNSKLVMAtvRSHDQYNTTIygMDDRYRGVFGQ-RDVVFMSAKQAKICRVKNGERVNL 694
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
10-440 |
4.82e-22 |
|
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: 101.59 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 10 CHLCEAICGLVIETVVEA---DSAPRIASIKGDPldtfSRGHICPKAVALQDIQNDPDRLRQPMLRSGDQ--------WQ 78
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGvatEIEPNFAAEDIHP----ARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKkgrnedpgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 79 PIAWQQAFDLVAERLYAIQQRHGQNAVAVYQGNPSVHNYGlmTHSNY------FLGLLKTRNrFSATSvDQLPHHLSSFL 152
Cdd:cd02760 80 PISWDEALDLVAAKLRRVREKGLLDEKGLPRLAATFGHGG--TPAMYmgtfpaFLAAWGPID-FSFGS-GQGVKCVHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 153 MYG---HGMLLPIPDIDHTDFMLILGGNPLASNGsimtvPDVEKRLKAIQQRGGKLVVIDPRRSETAAIADQHLFVRPGG 229
Cdd:cd02760 156 LYGefwHRAFTVAADTPLANYVISFGSNVEASGG-----PCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 230 DAALLFGLLNTLFEEG--------------------------------------------------------------LT 247
Cdd:cd02760 231 DPAFMFAMIHVMVHEQglgkldvpflrdrtsspylvgpdglylrdaatgkplvwdersgravpfdtrgavpavagdfaVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 248 RESHLPVDGLEQVRQAIAGFTAEAM--------SPR-----CGIAAEQIRQLARDFAAADK-----------------AV 297
Cdd:cd02760 311 GAVSVDADDETAIHQGVEGTTAFTMlvehmrkyTPEwaesiCDVPAATIRRIAREFLENASigstievdgvtlpyrpvAV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 298 CYGRmGVSTQTFGTLCHWLAQLINLVTGNLDRVGGALCTEPAVD-----------------LVSSTSGGHFNRWQSRVSG 360
Cdd:cd02760 391 TLGK-SVNNGWGAFECCWARTLLATLVGALEVPGGTLGTTVRLNrphddrlasvkpgedgfMAQGFNPTDKEHWVVKPTG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 361 ---------------LPEYGG--ELPVSALAEEMLVDG-EGQVRALVTVA--GNPVLSTPNGRQLEQALEGLEFMLSIDL 420
Cdd:cd02760 470 rnahrtlvpivgnsaWSQALGptQLAWMFLREVPLDWKfELPTLPDVWFNyrTNPAISFWDTATLVDNIAKFPFTVSFAY 549
|
570 580
....*....|....*....|
gi 1336206682 421 YINETTRHADLILPSTSALE 440
Cdd:cd02760 550 TEDETNWMADVLLPEATDLE 569
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
64-486 |
3.39e-20 |
|
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: 95.24 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 64 DRLRQPMLRSGDQWQPIAWQQAFDLVAERLYAIQQRHG-QNAVAVYQ------GNPSVHNYglMTHSNYFLGL----LKT 132
Cdd:cd02756 116 TRLTTPLVRRGGQLQPTTWDDAIDLVARVIKGILDKDGnDDAVFASRfdhgggGGGFENNW--GVGKFFFMALqtpfVRI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 133 RNR--FSAT---SVDQLPHHLSSFLMyghgmllpipDIDHTDFMLILGGNPLASNGSIMTV---PDVEKRLKAIQQRG-- 202
Cdd:cd02756 194 HNRpaYNSEvhaTREMGVGELNNSYE----------DARLADTIVLWGNNPYETQTVYFLNhwlPNLRGATVSEKQQWfp 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 203 -------GKLVVIDPRRSETAAIADQ--------HLFVRPGGDAALLFGLLNTLFE---EGLTRESH---LPVDGLEQVR 261
Cdd:cd02756 264 pgepvppGRIIVVDPRRTETVHAAEAaagkdrvlHLQVNPGTDTALANAIARYIYEsldEVLAEAEQitgVPRAQIEKAA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 262 QAIAGFTAEAMSPRCGIAAEqirqlardfaaadKAVCYGRMGVSTQtfgtlchwlAQLINLV--TGNLDRVGGALctepa 339
Cdd:cd02756 344 DWIAKPKEGGYRKRVMFEYE-------------KGIIWGNDNYRPI---------YSLVNLAiiTGNIGRPGTGC----- 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 340 vdlvsSTSGGHFNRWQSRVSGLPEYGGELPVSALAEEMLVDGEGQVraLVTVAGNPVLSTPNGRQLEQAL---------- 409
Cdd:cd02756 397 -----VRQGGHQEGYVRPPPPPPPWYPQYQYAPYIDQLLISGKGKV--LWVIGCDPYKTTPNAQRLRETInhrsklvtda 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 410 ------------------------EGLEFMLSIDLYINETTRHADLILPstSALENDHYDTTFNTLAVRnvTRFNRAIFD 465
Cdd:cd02756 470 veaalyagtydreamvcligdaiqPGGLFIVVQDIYPTKLAEDAHVILP--AAANGEMNETSMNGHERR--LRLYEKFMD 545
|
490 500
....*....|....*....|.
gi 1336206682 466 KPEGALHDWEIFVGLASAFAA 486
Cdd:cd02756 546 PPGEAMPDWWIAAMIANRIYE 566
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
582-693 |
1.20e-18 |
|
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: 81.60 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 582 RHVRSNNSWMHNYHRLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHsrsgv 661
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGH----- 75
|
90 100 110
....*....|....*....|....*....|..
gi 1336206682 662 kmaiaQSLPGVSANDLTDERqLDVLSGNAALN 693
Cdd:cd02775 76 -----RGGRGGNANVLTPDA-LDPPSGGPAYK 101
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
17-440 |
1.26e-18 |
|
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: 89.86 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 17 CGLVIETVveaDSAPriASIKGDPLDTFSRGHICPKAVA-LQDIQnDPDRLRQPMLRSGD-QWQPIAWQQAFDLVAERLY 94
Cdd:cd02764 56 QGVLVKTV---DGRP--IKIEGNPDHPASLGGTSARAQAsVLSLY-DPDRAQGPLRRGIDgAYVASDWADFDAKVAEQLK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 95 AIqqRHGQNaVAVYQGNPsvhnygLMTHSNYFLGLLKtRNRFSATSVDQLPhhLSSFLM-------YGhGMLLPIPDIDH 167
Cdd:cd02764 130 AV--KDGGK-LAVLSGNV------NSPTTEALIGDFL-KKYPGAKHVVYDP--LSAEDVneawqasFG-KDVVPGYDFDK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 168 TDFMLILGGNPLASNGSimtvPDVEKRLKAIQQRGGK------LVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLNTL 241
Cdd:cd02764 197 AEVIVSIDADFLGSWIS----AIRHRHDFAAKRRLGAeepmsrLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 242 FEEGlTRESHLpvdglEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADKA-VCYGrmGVSTQTFGTLCHWLAQLI 320
Cdd:cd02764 273 IKKG-AGSSLP-----DFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAGKSlVVAG--SELSQTAGADTQVAVNAL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 321 NLVTGNLDRvggalctepAVDLVSSTSGGhfnrwqsrvsglpEYGGELPVSALAEEMlvdGEGQVRALVTVAGNPVLSTP 400
Cdd:cd02764 345 NSLLGNDGK---------TVDHARPIKGG-------------ELGNQQDLKALASRI---NAGKVSALLVYDVNPVYDLP 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1336206682 401 NGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALE 440
Cdd:cd02764 400 QGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGLE 439
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
61-434 |
6.07e-18 |
|
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: 86.64 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 61 NDPDRLRQPMLRSGDQWQPIAWQQAFDLVAERLYAIQQRHGQNAVAVYqGNPSVhnyglmTHSNYFLgLLKTRNRFSATS 140
Cdd:cd02772 50 NSEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGAL-ASPHS------TLEELYL-LQKLARGLGSDN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 141 VDQLPHH----LSSFLMYGHGMLLPIPDIDHTDFMLILGGN-----PLASngsimtvpdveKRLKAIQQRGGKLVVIDPR 211
Cdd:cd02772 122 IDHRLRQsdfrDDAKASGAPWLGMPIAEISELDRVLVIGSNlrkehPLLA-----------QRLRQAVKKGAKLSAINPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 212 RSETAAIADQHLFVRPGGDAALLFGLLNTLFEEgltrESHLPVDGLEQVRqaiagftaeamsprcgIAAEQIRQLARDFA 291
Cdd:cd02772 191 DDDFLFPLSGKAIVAPSALANALAQVAKALAEE----KGLAVPDEDAKVE----------------ASEEARKIAASLVS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 292 AADKAVCYGRMGVSTQTFGTLcHWLAQLINLVTGnldRVGGALcTEPAvdlvsSTSGGHFnrwqsrvsglpeyGGELPVS 371
Cdd:cd02772 251 AERAAVFLGNLAQNHPQAATL-RALAQEIAKLTG---ATLGVL-GEGA-----NSVGAYL-------------AGALPHG 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336206682 372 AL-AEEMLVDGegqVRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTR-HADLILP 434
Cdd:cd02772 308 GLnAAAMLEQP---RKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALLdYADVLLP 369
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
61-484 |
1.05e-15 |
|
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: 79.63 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 61 NDPDRLRQPMLRSGDQWQPIAWQQAFDLVAERLyaiqQRHGQNAVAVYqGNPSVHNyglmtHSNYFL---------GLLK 131
Cdd:cd02768 50 NSRQRLTQPLIKKGGKLVPVSWEEALKTVAEGL----KAVKGDKIGGI-AGPRADL-----ESLFLLkkllnklgsNNID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 132 TRNRFSAtsvdqLPHHLSSFLMYGHGMllPIPDIDHTDFMLILGGNPLAsngsimTVPDVEKRL-KAIQQRGGKLVVIDP 210
Cdd:cd02768 120 HRLRQSD-----LPADNRLRGNYLFNT--SIAEIEEADAVLLIGSNLRK------EAPLLNARLrKAVKKKGAKIAVIGP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 211 rrSETAAIADQHLFVRPGGDAallfglLNTLFEegltreshlpvdgleqvrqaiagftaeamsprcGIAAEQIRQLARDF 290
Cdd:cd02768 187 --KDTDLIADLTYPVSPLGAS------LATLLD---------------------------------IAEGKHLKPFAKSL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 291 AAADK-AVCYGRMGVSTQTFGTLCHWLAQLINLVTGNLDRVGGALCtepavdlvsstsgghfNRWQSRVSGlpeyggelp 369
Cdd:cd02768 226 KKAKKpLIILGSSALRKDGAAILKALANLAAKLGTGAGLWNGLNVL----------------NSVGARLGG--------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 370 vsALAEEMLVDGE-GQVRALVTVAGNPVLSTPNGRqleQALEGLEFMLSIDLYINETTRHADLILPSTSALENdhyDTTF 448
Cdd:cd02768 281 --AGLDAGLALLEpGKAKLLLLGEDELDRSNPPAA---VALAAADAFVVYQGHHGDTGAQADVILPAAAFTEK---SGTY 352
|
410 420 430
....*....|....*....|....*....|....*..
gi 1336206682 449 -NTLavRNVTRFNRAIFdKPEGALHDWEIFVGLASAF 484
Cdd:cd02768 353 vNTE--GRVQRFKKAVS-PPGDAREDWKILRALSNLL 386
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
55-489 |
2.29e-15 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 80.10 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 55 ALQDIQNDPDRLRQPMLR--------------SGD-QWQPIAWQQAFDLVAERLYAIQQRHGQNAV----AVYQGNPSVH 115
Cdd:PRK15102 80 GIKGHVYNPSRIRYPMVRldwlrkrhksdtsqRGDnRFVRVSWDEALDLFYEELERVQKTYGPSALhtgqTGWQSTGQFH 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 116 NYGLMT------HSNYflglLKTRNRFSaTSVDQ--LPHHLSSFLMYGHGMLLPIPdIDHTDFMLILGGNPLASNGSIMT 187
Cdd:PRK15102 160 SATGHMqraigmHGNS----VGTVGDYS-TGAGQviLPYVLGSTEVYEQGTSWPLI-LENSKTIVLWGSDPVKNLQVGWN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 188 VPDVE-----KRLKA-IQQRGGKLVVIDPRRSETAA-IADQHLFVRPGGDAALLFGLLNTLFEEGLTRESHLPVD--GLE 258
Cdd:PRK15102 234 CETHEsyaylAQLKEkVAKGEINVISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYclGFE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 259 QVRQAIAGF------TAEAMSPRCGIAAEQIRQLARDFAAADKAVCYGrMGVSTQTFGTLCHWLAQLINLVTGNLDRVGG 332
Cdd:PRK15102 314 QFLPYLLGEkdgvpkTPEWAEKICGIDAETIRELARQMAKGRTQIIAG-WCIQRQQHGEQPYWMGAVLAAMLGQIGLPGG 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 333 ALctepavdlvssTSGGHFNRWQSRVSGLPEYGG-----------------------ELPVSALAEEMLVDGE-----GQ 384
Cdd:PRK15102 393 GI-----------SYGHHYSGIGVPSSGGAIPGGfpgnldtgqkpkhdnsdykgyssTIPVARFIDAILEPGKtinwnGK 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 385 ------VRALVTVAGNPVLSTPNGRQLEQALEGLEFMLSIDLYINETTRHADLILPSTSALENDHYDtTFNTLAVRNVTR 458
Cdd:PRK15102 462 kvtlppLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDID-QYGSYSNRGIIA 540
|
490 500 510
....*....|....*....|....*....|....
gi 1336206682 459 FNRAI---FDkpegALHDWEIFVGLASAFAAKAE 489
Cdd:PRK15102 541 MKKVVeplFE----SRSDFDIFRELCRRFGREKE 570
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
50-699 |
1.35e-14 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 77.73 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 50 CPKAVALQDIQNDPDRLRQPMLRSGD----QWQPIAWQQAFDLVAER-----------LYAIQQRhgqnAVAVYQGNPSv 114
Cdd:PRK14991 142 CARGNAMLEQLDSPYRVLQPLKRVGKrgsgKWQRISFEQLVEEVVEGgdlfgeghvdgLRAIRDL----DTPIDAKNPE- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 115 hnYG------LMTHS-----NYFLgllktrNRFSATSVD--QLPHHLS----SF------LM-----YGHGMllpiPDID 166
Cdd:PRK14991 217 --YGpkanqlLVTNAsdegrDAFI------KRFAFNSFGtrNFGNHGSycglAYragsgaLMgdldkNPHVK----PDWD 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 167 HTDFMLILG------GNPLASNGsimtvpdveKRLKAIQQRGG-KLVVIDPR--RSETAAIADQH--LFVRPGGDAALLF 235
Cdd:PRK14991 285 NVEFALFIGtspaqsGNPFKRQA---------RQLANARTRGNfEYVVVAPAlpLSSSLAAGDNNrwLPIRPGTDSALAM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 236 GLLNTLFEE----------------------GLTRESHLPVD-------------------------------------- 255
Cdd:PRK14991 356 GMIRWIIDNqrynadylaqpgvaamqaageaSWTNATHLVIAdpghprygqflrasdlglpfegeargdgedtlvvdaad 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 256 --------------------------------GLEQVRQAIAGFTAEAMSPRCGIAAEQIRQLARDFAAADK---AVCYG 300
Cdd:PRK14991 436 gelvpatqaqparlfveqyvtladgqrvrvksSLQLLKEAARKLSLAEYSEQCGVPEAQIIALAEEFTSHGRkaaVISHG 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 301 RMgVSTQTFGTLchWLAQLINLVTGNLDRVGGAlctepavdlvsSTSGGHFN------RWQ-----SRV--SGLP----- 362
Cdd:PRK14991 516 GT-MSGNGFYNA--WAIMMLNALIGNLNLKGGV-----------VVGGGKFPgfgdgpRYNlasfaGKVkpKGVSlsrsk 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 363 -------EY-----GGELP----------VSALAEEML---VDGEG-QVRALVTVAGNPVLSTPNGRQ-LEQALEG---L 412
Cdd:PRK14991 582 fpyekssEYrrkveAGQSPypakapwypfVAGLLTEMLtaaLEGYPyPLKAWINHMSNPIYGVPGLRAvIEEKLKDpkkL 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 413 EFMLSIDLYINETTRHADLILPSTSALENDHYDTTFNTLAVRNVT-RF-------------------------------- 459
Cdd:PRK14991 662 PLFISIDAFINETTALADYIVPDTHTYESWGFTAPWGGVPTKASTaRWpvveprtaktadgqpvcmesfliavakrlqlp 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 460 ---NRAIFDKpEGALH------DWEIFVGLASAFAAKA---------------ER---ALKPTLPPAQMIDRGL---RAG 509
Cdd:PRK14991 742 gfgDNAIKDA-QGNTHplnraeDFYLRGAANIAYLGKTpvadasdedialtgvSRilpALQATLKPDEVRRVAFiyaRGG 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 510 LYGDASSHKLSLETLDSHPHGLDLgaLKANLAQRLKTANGRIQAAPEVIMAdlARFAaDPSP-------QASELLLIG-R 581
Cdd:PRK14991 821 RFAPAESAYDEERMGNRWKKPLQI--WNEDVAAARHSMTGERYSGCPTWYP--PRLA-DGTPlreqfpeSQWPLLLISfK 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 582 RHVRSNNSWMHNyhRLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGH----S 657
Cdd:PRK14991 896 SNLMSSMSIASP--RLRQVKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHGYGHrelgA 973
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1336206682 658 RS----GVKMAI-AQSLPGVSANDL-----TDERQ---LDVLSGNAALNGVPVQV 699
Cdd:PRK14991 974 RAhsidGKPMPAnPQIRAGVNLNDLgladpTREITnvwVDWVSGAAVRQGLPAKI 1028
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
581-700 |
9.92e-13 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 66.16 E-value: 9.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 581 RRHVRSNNSWMHnyhrlvKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHSRSG 660
Cdd:cd02780 13 NSHRSANAPWLK------EIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEHGYGHWAYG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1336206682 661 VKMA---------IAQSLPGVSANDL---TDERQ----LDVLSGNAALNGVPVQVV 700
Cdd:cd02780 87 AVAStidgkdlpgDAWRGAGVNINDIglvDPSRGgwslVDWVGGAAARYDTPVKIE 142
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
588-699 |
1.29e-10 |
|
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: 59.22 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 588 NSWMHNYHRLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHSRSGvkmaiaq 667
Cdd:cd02786 15 NSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGGWWREHSP------- 87
|
90 100 110
....*....|....*....|....*....|..
gi 1336206682 668 slPGVSANDLTDERQLDvLSGNAALNGVPVQV 699
Cdd:cd02786 88 --DGRGVNALTSARLTD-LGGGSTFHDTRVEV 116
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
576-654 |
1.45e-09 |
|
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: 56.44 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 576 LLLIGRRHVRSNNSWMHN---YHRLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPH 652
Cdd:cd02777 3 LQLISPHPKRRLHSQLDNvpwLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALPE 82
|
...
gi 1336206682 653 G-W 654
Cdd:cd02777 83 GaW 85
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
58-273 |
3.24e-09 |
|
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: 59.85 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 58 DIQNDPDRLRQPMLRSGDQWQPIAWQQAFDLVAERLYAiqqrhgqnavavyqgnpsvhnyglmthsnyflgLLKTRNRFS 137
Cdd:COG1034 265 DGLNSPDRLTRPLVRKDGELVEASWEEALAAAAEGLKA---------------------------------LKKAENSVG 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 138 ATSVDQLPHhlssflmyGHGMLLPIPDiDHTDFMLILGGNPLASNGSimtvpDVEKRLKAiqqrGGKLVVIDPRRSETAA 217
Cdd:COG1034 312 AALLGALPD--------AAAILEAAEA-GKLKALVLLGADPYDLDPA-----AALAALAK----ADFVVVLDHFGSATAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 218 IAD----------------------QHLF--VRPGGDAALLFGLLNTLfeeGLTRESHLPVDGLEQVRQAIAGFTAEAMS 273
Cdd:COG1034 374 RADvvlpaaafaeksgtfvnlegrvQRFNaaVPPPGEARPDWRVLRAL---ANALGAGLPYDSLEEVRAELAAEAPATVS 450
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
577-700 |
4.05e-09 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 55.39 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 577 LLIGRRHVRSNNSWMHNYHRLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIeVQVLGSLDMMR-GVVSLPHGWG 655
Cdd:cd02781 6 LTTGARSYYYFHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRA-RQKARLTPGIRpGVVRAEHGWW 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1336206682 656 HSRSGVKMAIAQSLPGVSANDLTDERQLDVLSGNAALNGVPVQVV 700
Cdd:cd02781 85 YPEREAGEPALGGVWESNANALTSDDWNDPVSGSSPLRSMLCKIY 129
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
9-325 |
8.88e-09 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 58.76 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 9 ACHLCEAICGLVIETvveadSAPRIASIKGDPLDTFSRGHICPKAVALQDIQNDPDRLRQPMLRSGD-------QWQPIA 81
Cdd:PRK13532 46 PCRFCGTGCGVLVGT-----KDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPLLRMKDgkydkegEFTPVS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 82 WQQAFDLVAERLYAIQQRHGQNAVA--------VYQGNPSVHnygLMthsnyflgllktRNRFSATSVDqlP---HHLSS 150
Cdd:PRK13532 121 WDQAFDVMAEKFKKALKEKGPTAVGmfgsgqwtIWEGYAASK---LM------------KAGFRSNNID--PnarHCMAS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 151 ----FlMYGHGMLLPI---PDIDHTDFMLILGGNpLASNGSIMTVPDVEKRLKAiqqRGGKLVVIDPRRSETAAIADQHL 223
Cdd:PRK13532 184 avvgF-MRTFGIDEPMgcyDDIEAADAFVLWGSN-MAEMHPILWSRVTDRRLSN---PDVKVAVLSTFEHRSFELADNGI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 224 FVRPGGDAALL----------------FGLLNTLFEEGLT------RESHL---------------PVDgLEQVRQAIAG 266
Cdd:PRK13532 259 IFTPQTDLAILnyianyiiqnnavnwdFVNKHTNFRKGATdigyglRPTHPlekaaknpgtagksePIS-FEEFKKFVAP 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 267 FTAEAMSPRCGIAAEQIRQLARDFAAAD-KAVCYGRMGVSTQTFGTLCHWLAQLINLVTG 325
Cdd:PRK13532 338 YTLEKTAKMSGVPKEQLEQLAKLYADPNrKVVSFWTMGFNQHTRGVWANNLVYNIHLLTG 397
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
596-700 |
1.20e-08 |
|
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: 53.67 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 596 RLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHSRsgvkmaiaqslPGVSAN 675
Cdd:cd00508 27 RLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMPFHWGGEV-----------SGGAAN 95
|
90 100
....*....|....*....|....*
gi 1336206682 676 DLTDERqLDVLSGNAALNGVPVQVV 700
Cdd:cd00508 96 ALTNDA-LDPVSGQPEFKACAVRIE 119
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
169-440 |
2.95e-08 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 56.57 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 169 DFMLILGGNPLASNGSIMT----VPDVEKRLKAIQQRggKLVVIDPRRSETAAIADQHLFVRPGGDAALLFGLLNTLFEE 244
Cdd:cd02761 133 DVIVYWGTNPMHAHPRHMSrysvFPRGFFREGGREDR--TLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRALLRGA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 245 GLTREshlpvdgleqvrqaiagftaeamsPRCGIAAEQIRQLARDFAAADKAVCYGRMGVsTQTFGTlcHWLAQLINLVT 324
Cdd:cd02761 211 GLVPD------------------------EVAGIPAETILELAERLKNAKFGVIFWGLGL-LPSRGA--HRNIEAAIRLV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 325 GNLDRVGGALCTePAvdlvsstsGGHFN--------RWQS----RVSGLPEYGGELPVSALAEEMLVDGEgqVRALVTVA 392
Cdd:cd02761 264 KALNEYTKFALL-PL--------RGHYNvrgfnqvlTWLTgypfRVDFSRGYPRYNPGEFTAVDLLAEGE--ADALLIIA 332
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1336206682 393 GNPVLSTPnGRQLEQALEGLefMLSIDLYINETTRHADLILPS-TSALE 440
Cdd:cd02761 333 SDPPAHFP-QSAVKHLAEIP--VIVIDPPPTPTTRVADVVIPVaIPGIE 378
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
4-62 |
4.89e-08 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 49.94 E-value: 4.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336206682 4 TEHYRACHLCEAICGLVIEtvVEADsapRIASIKGDPLDTFSRGHICPKAVALQDIQND 62
Cdd:smart00926 2 KWVPTVCPLCGVGCGLLVE--VKDG---RVVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
606-651 |
6.12e-08 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 51.47 E-value: 6.12e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1336206682 606 LLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLP 651
Cdd:cd02790 37 VEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFMP 82
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
576-654 |
6.32e-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: 51.52 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 576 LLLIGRRHVRSNNSWMHNYHRLVKGKPrHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHG-W 654
Cdd:cd02794 3 LQLIGWHYKRRTHSTFDNVPWLREAFP-QEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGaW 81
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
596-699 |
1.27e-07 |
|
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: 50.65 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 596 RLVKGKPRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGhsrsgvkmaiAQSLPGVSAN 675
Cdd:cd02791 27 RLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFVPMHWG----------DQFGRSGRVN 96
|
90 100
....*....|....*....|....
gi 1336206682 676 DLTDeRQLDVLSGNAALNGVPVQV 699
Cdd:cd02791 97 ALTL-DATDPVSGQPEFKHCAVRI 119
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
577-699 |
4.62e-07 |
|
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: 49.29 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 577 LLIGRRHVR-------SNNSWMhnyhRLVKGKPRHQLlmHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVS 649
Cdd:cd02785 4 LACIQRHSRfrvhsqfSNVPWL----LELQPEPRVKI--NPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1336206682 650 LPHGWGhsrsgvkmaiAQSLPGVSANDLT----DERQLDVLSGNAALNGVPVQV 699
Cdd:cd02785 78 AEQGWW----------SRYFQEGSLQDLTspfvNPVHEYIYGPNSAFYDTLVEV 121
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
598-654 |
5.64e-07 |
|
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: 49.17 E-value: 5.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336206682 598 VKGkpRHQLLMHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHG-W 654
Cdd:cd02793 29 VQG--REPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLPTGaW 84
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
608-699 |
2.12e-06 |
|
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: 47.27 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 608 MHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHsRSGVKMAIAQslPGVSANDLTDERqLDVLS 687
Cdd:cd02778 34 INPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGFGH-WAPALSRAYG--GGVNDNNLLPGS-TEPVS 109
|
90
....*....|..
gi 1336206682 688 GNAALNGVPVQV 699
Cdd:cd02778 110 GGAGLQEFTVTV 121
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
608-678 |
6.79e-04 |
|
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: 39.90 E-value: 6.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336206682 608 MHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHGWGHSRSGvkmaiaqslPGVSANDLT 678
Cdd:cd02792 39 ISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIPYHWGGMGLV---------IGDSANTLT 100
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| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
608-654 |
7.23e-04 |
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Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 40.22 E-value: 7.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1336206682 608 MHPDDLACRGLSDGQQVRVSSRVGMIEVQVLGSLDMMRGVVSLPHG-W 654
Cdd:COG1153 35 LNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGpW 82
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| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
603-697 |
5.81e-03 |
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The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 37.26 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336206682 603 RHQLLMHPDDLACRGLSDGQQVRVSSRVG-MIEVQVLGsldmMRGVV-SLPHGwghsrsgvkmAIAQSLPgvSANDLTDE 680
Cdd:cd02787 30 RDVVFMNPDDIARLGLKAGDRVDLESAFGdGQGRIVRG----FRVVEyDIPRG----------CLAAYYP--EGNVLVPL 93
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90
....*....|....*..
gi 1336206682 681 RQLDVLSGNAALNGVPV 697
Cdd:cd02787 94 DHRDPQSKTPAYKSVPV 110
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| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
65-97 |
5.87e-03 |
|
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: 39.56 E-value: 5.87e-03
10 20 30
....*....|....*....|....*....|...
gi 1336206682 65 RLRQPMLRSGDQWQPIAWQQAFDLVAERLYAIQ 97
Cdd:cd02773 53 RLDKPYIRKNGKLKPATWEEALAAIAKALKGVK 85
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