|
Name |
Accession |
Description |
Interval |
E-value |
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
17-705 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 884.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 17 ETQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIPNL-ASEGRVCVKGMNAHQHAAHSQRLQYPLIRSNGELIPCSWDE 95
Cdd:COG3383 8 KTVCPYCGVGCGIDLEVKDGKI-------VKVEGDPDHpVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 96 AIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKTFGIDrGLTFRLS 175
Cdd:COG3383 81 ALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSD-APPNSYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 176 DIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDEGLLDE 255
Cdd:COG3383 160 DIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 256 GFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKI 335
Cdd:COG3383 240 DFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 336 GREGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEEDRAYVASVWGVKAssLPGK-GVSAYEMMELIHRGEIKSLFV 414
Cdd:COG3383 320 GRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPP--LPDKpGLTAVEMFDAIADGEIKALWI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 415 MGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPGEARHDWV 494
Cdd:COG3383 398 IGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 495 ILCAIADRLGRGeyFDFHEPEEIFSELRLASKggiaDYFGITYDRLRREEGVYWPCPSEEESGTGLLFRQSFAHPDGKAV 574
Cdd:COG3383 478 IIAELARRLGYG--FDYDSPEEVFDEIARLTP----DYSGISYERLEALGGVQWPCPSEDHPGTPRLFTGRFPTPDGKAR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 575 FS-VTPGNPWVGVSEEYPLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSV 653
Cdd:COG3383 552 FVpVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVL 631
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2254313745 654 RSRIKEHIRVDTLFVPMHWGGAqNVNHATRPELDPFCKMPGFKTAAVRIRSL 705
Cdd:COG3383 632 RARVTDRVRPGTVFMPFHWGEG-AANALTNDALDPVSKQPEYKACAVRVEKV 682
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
18-582 |
0e+00 |
|
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: 725.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIPNL-ASEGRVCVKGMNAHQHAAHSQRLQYPLIRSNG-ELIPCSWDE 95
Cdd:cd02754 2 TTCPYCGVGCGVEIGVKDGKV-------VAVRGDPEHpVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGgELVPVSWDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 96 AIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKTFGIDrGLTFRLS 175
Cdd:cd02754 75 ALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGAD-GPPGSYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 176 DIPLADCIVLAGTNIAECQPTLLPYFNQAKEN--GAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDEGLL 253
Cdd:cd02754 154 DIEHADCFFLIGSNMAECHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 254 DEGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATG 333
Cdd:cd02754 234 DRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 334 KIGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEEDRAYVASVWGVKASSLPGK-GVSAYEMMELIHRGEIKSL 412
Cdd:cd02754 314 KIGRPGSGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVPEGTIPPKpGLHAVEMFEAIEDGEIKAL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 413 FVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMF-MSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPGEARH 491
Cdd:cd02754 394 WVMCTNPAVSLPNANRVREALERLEFVVVQDAFaDTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 492 DWVILCAIADRLGRGEYFDFHEPEEIFSELRLASKGGIADYFGITYDRLRReEGVYWPCPSEEESGTGLLFR-QSFAHPD 570
Cdd:cd02754 474 DWWILADVARRLGFGELFPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEdGRFPTPD 552
|
570
....*....|..
gi 2254313745 571 GKAVFSVTPGNP 582
Cdd:cd02754 553 GRARFVAVPYRP 564
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
18-702 |
0e+00 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 612.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCKMTVAVEENGIpgqHKARYKVEGIPNlasEGRVCVKGMNAHQHAAHSQRLQYPLIRSNGELIPCSWDEAI 97
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKI---VRVEPYQGHKAN---RGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSWDEAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 98 AVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKTFGIDRGlTFRLSDI 177
Cdd:TIGR01591 75 SYIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAM-SNTISEI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 178 PLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDEGLLDEGF 257
Cdd:TIGR01591 154 ENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 258 IQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKIGR 337
Cdd:TIGR01591 234 IEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 338 EGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEEDRAYVASVWGVkaSSLPGK-GVSAYEMMELIHRGEIKSLFVMG 416
Cdd:TIGR01591 314 PGGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGV--VKLPAEpGLRIPEMIDAAADGDVKALYIMG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 417 SNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPGEARHDWVIL 496
Cdd:TIGR01591 392 EDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEII 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 497 CAIADRLGRGeyFDFHEPEEIFSELRLASKggiaDYFGITYDRLRREEGVYWPCPSEEESGTGLLFRQSFAHPDGKAVF- 575
Cdd:TIGR01591 472 QELANALGLD--WNYNHPQEIMDEIRELTP----LFAGLTYERLDELGSLQWPCNDSDASPTSYLYKDKFATPDGKAKFi 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 576 SVTPGNPWVGVSEEYPLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRS 655
Cdd:TIGR01591 546 PLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRA 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2254313745 656 RIKEHIRVDTLFVPMHWGGAQnVNHATRPELDPFCKMPGFKTAAVRI 702
Cdd:TIGR01591 626 KVSDRVNKGAIYITMHFWDGA-VNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
18-703 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 586.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIP-NLASEGRVCVKGMNAHQHAAHSQRLQYPLIR----SNGELIPCS 92
Cdd:COG0243 26 TTCPGCGVGCGLGVKVEDGRV-------VRVRGDPdHPVNRGRLCAKGAALDERLYSPDRLTYPMKRvgprGSGKFERIS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 93 WDEAIAVISDRFQAISERYGPDAHAVYGGGS----LTNETAYLLGKFARvALGTRYIDYNGRFCMSAAASAGSKTFGIDR 168
Cdd:COG0243 99 WDEALDLIAEKLKAIIDEYGPEAVAFYTSGGsagrLSNEAAYLAQRFAR-ALGTNNLDDNSRLCHESAVAGLPRTFGSDK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 169 GlTFRLSDIPLADCIVLAGTNIAECQPTLLPYFNQA-KENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMI 247
Cdd:COG0243 178 G-TVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 248 VDEGLLDEGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLN 327
Cdd:COG0243 257 IEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIAN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 328 LVLATGKIGREGCGYGAITGqgngqggrehgqkadqlpgyrsieneedrayvasvwgvkasslpgkgvsayEMMELIHRG 407
Cdd:COG0243 337 LALLTGNIGKPGGGPFSLTG---------------------------------------------------EAILDGKPY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 408 EIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLE-GRVLLRKAARQAP 486
Cdd:COG0243 366 PIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 487 GEARHDWVILCAIADRLGRGEYFDFHE-PEEIFSELRLASKGGiadyfGITYDRLRREEGVYWPCPSEEesgtglLFRQ- 564
Cdd:COG0243 446 GEARSDWEIFAELAKRLGFEEAFPWGRtEEDYLRELLEATRGR-----GITFEELREKGPVQLPVPPEP------AFRNd 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 565 -SFAHPDGKAVFS------------VTPGNPWVGVSEEYPLILTNGRVLSHYLTgvQTRRSPSLLARELENFVEIHPITA 631
Cdd:COG0243 515 gPFPTPSGKAEFYsetlalpplpryAPPYEGAEPLDAEYPLRLITGRSRDQWHS--TTYNNPRLREIGPRPVVEINPEDA 592
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254313745 632 QRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLFVPMHWG------GAQNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:COG0243 593 AALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWyepaddKGGNVNVLTPDATDPLSGTPAFKSVPVRVE 670
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
17-582 |
0e+00 |
|
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: 530.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 17 ETQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIPNL-ASEGRVCVKGMNAHQHAAHSQRLQYPLIRSNGELIPCSWDE 95
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKI-------VGVEPVKGHpVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 96 AIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKTFGIDRGlTFRLS 175
Cdd:cd02753 74 ALSLVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAM-TNSIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 176 DIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDEGLLDE 255
Cdd:cd02753 153 DIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 256 GFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKI 335
Cdd:cd02753 233 EFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 336 GREGCGYGAITGQGNGQGGREHGQKADQLPGYrsieneedrayvasvwgvkasslpgkgvsayemmelihrgeIKSLFVM 415
Cdd:cd02753 313 GRPGTGVNPLRGQNNVQGACDMGALPNVLPGY-----------------------------------------VKALYIM 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 416 GSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPGEARHDWVI 495
Cdd:cd02753 352 GENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 496 LCAIADRLGrGEYFDFHePEEIFSELRLASKggiaDYFGITYDRLRREEGVYWPCPSEEESGTGLLFRQSFAHPDGKAVF 575
Cdd:cd02753 432 IQELANRLG-YPGFYSH-PEEIFDEIARLTP----QYAGISYERLERPGGLQWPCPDEDHPGTPILHTERFATPDGKARF 505
|
....*..
gi 2254313745 576 SVTPGNP 582
Cdd:cd02753 506 MPVEYRP 512
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
17-503 |
2.75e-113 |
|
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: 346.24 E-value: 2.75e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 17 ETQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIPN-LASEGRVCVKGMNAHQHAAHSQRLQYPLIRSN--GELIPCSW 93
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKV-------VRIEGDPNhPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 94 DEAIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGKFARvALGTRYIDYNGRFCMSAAAsAGSKTFGIDrGLTFR 173
Cdd:cd00368 74 DEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLR-ALGSNNVDSHARLCHASAV-AALKAFGGG-APTNT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 174 LSDIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAmlkmivdegll 253
Cdd:cd00368 151 LADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA----------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 254 degfiqarttgyeelktyldsfdlSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATG 333
Cdd:cd00368 220 ------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 334 KIGREGCGYGAitgqgngqggrehgqkadqlpgyrsieneedrayvasvwgvkasslpgkgvsayemmelihrgeikslf 413
Cdd:cd00368 276 NIGRPGGGLGP--------------------------------------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 414 vmGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPGEARHDW 493
Cdd:cd00368 287 --GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDW 364
|
490
....*....|
gi 2254313745 494 VILCAIADRL 503
Cdd:cd00368 365 EILRELAKRL 374
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
20-572 |
2.89e-92 |
|
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: 296.08 E-value: 2.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 20 CPF-CSVQCKMTVAVEENGIpgqhkarYKVEGIP-NLASEGRVCVKGMNAHQHAAHSQRLQYPLIRSN---GELIPCSWD 94
Cdd:cd02766 4 CPLdCPDTCSLLVTVEDGRI-------VRVEGDPaHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGrkgGQWERISWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 95 EAIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNgrFCMSAAASAGSKTFGIDRGLTfrL 174
Cdd:cd02766 77 EALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHALGASELRGT--ICSGAGIEAQKYDFGASLGND--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 175 SDIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDEGLLD 254
Cdd:cd02766 153 EDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 255 EGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGK 334
Cdd:cd02766 233 RDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 335 IGREGCGYgaitgqgngqggrehgqkadqlpgyrsieneedrayvasvwgVKASSLPgkgvsayemmelihrgEIKSLFV 414
Cdd:cd02766 313 IGVPGGGA------------------------------------------FYSNSGP----------------PVKALWV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 415 MGSNPVVSNPNAGLVEEGL-NHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGR-VLLRKAARQAPGEARHD 492
Cdd:cd02766 335 YNSNPVAQAPDSNKVRKGLaREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYyLQYNEPAIPPPGEARSN 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 493 WVILCAIADRLGRGEYFdFHEPEEIFseLRLASKGGIADYFGITYDRLRReegvYWPCPSEEEsgtgLLFRQSFAHPDGK 572
Cdd:cd02766 415 TEIFRELAKRLGFGEPP-FEESDEEW--LDQALDGTGLPLEGIDLERLLG----PRKAGFPLV----AWEDRGFPTPSGK 483
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
76-502 |
2.07e-80 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 260.02 E-value: 2.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 76 RLQYPLIR-SNGELIPCSWDEAIAVISDRFQAISERYGPDAHAVYG--GGSLTNETAYLLGKFARVALG--TRYIDYNGR 150
Cdd:pfam00384 1 RLKYPMVRrGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGgsGGLTDVESLYALKKLLNRLGSknGNTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 151 FCMSAAASAGSkTFGIDRGLTFRLSDIPLADCIVLAGTNIAECQPTL-LPYFNQAKENGAKIIVIDPRRTATaaIADMHL 229
Cdd:pfam00384 81 LCTAAAAAFGS-DLRSNYLFNSSIADIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRLDLT--YADEHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 230 AIRPGTDAILADAMLKMIVDEGLLDEGFiqarttgyeelktyldsfdlsraadlcglnvelireaafsyamADTGMVLTA 309
Cdd:pfam00384 158 GIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------APKPIIIVG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 310 RGVEQQTDGHLAVRRYLNLVLATGKIGREGCGYGAITgqgNGQG-GREHGQKADQLPgyrsieneedrayvasvwgvkas 388
Cdd:pfam00384 195 AGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGaASPVGALDLGLV----------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 389 slpgKGVSAYEMMELIHRGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFM-SETARFADLVLPVTSYMENEG 467
Cdd:pfam00384 249 ----PGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNG 324
|
410 420 430
....*....|....*....|....*....|....*
gi 2254313745 468 TLTNLEGRVLLRKAARQAPGEARHDWVILCAIADR 502
Cdd:pfam00384 325 TYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
17-508 |
3.02e-78 |
|
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: 258.39 E-value: 3.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 17 ETQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIPN-LASEGRVCVKGMNAHQHAAHSQRLQYPLIRSN----GELIPC 91
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKL-------VKVEGDPNhPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGergeNKWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 92 SWDEAIAVISDRFQAISERYGPDAHAVY-GGGSLTNE-TAYLLGKFARVaLGTRYIDYNGRFCMSAAASAGSKTFGIdrG 169
Cdd:cd02759 74 SWDEALDEIAEKLAEIKAEYGPESIATAvGTGRGTMWqDSLFWIRFVRL-FGSPNLFLSGESCYWPRDMAHALTTGF--G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 170 LTFRLSDIPLADCIVLAGTNIAECQPTLLPY-FNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIV 248
Cdd:cd02759 151 LGYDEPDWENPECIVLWGKNPLNSNLDLQGHwLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 249 DEGLLDEGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNL 328
Cdd:cd02759 231 NEGLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 329 VlatgkigregcgygAITGQGNGQGGrehgqkaDQLPGYRsieneedrayvasvwgvkasslpgkgvsayemmelihrge 408
Cdd:cd02759 311 R--------------AITGNLDVPGG-------NLLIPYP---------------------------------------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 409 IKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGR--VLLRKAARQAP 486
Cdd:cd02759 330 VKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAEnfVQLRQKAVEPY 409
|
490 500
....*....|....*....|..
gi 2254313745 487 GEARHDWVILCAIADRLGRGEY 508
Cdd:cd02759 410 GEAKSDYEIVLELGKRLGPEEA 431
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
18-496 |
6.32e-78 |
|
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: 259.25 E-value: 6.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCKMTVAVEengipGQHKAryKVEGIP-NLASEGRVCVKG--MNAHQHaaHSQRLQYPLIRSNGELIPCSWD 94
Cdd:cd02762 2 RACILCEANCGLVVTVE-----DGRVA--SIRGDPdDPLSKGYICPKAaaLGDYQN--DPDRLRTPMRRRGGSFEEIDWD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 95 EAIAVISDRFQAISERYGPDAHAVYGGGSLTNEtaYLLGKFARV---ALGTRyidynGRFcmsAAASAGSKT-------- 163
Cdd:cd02762 73 EAFDEIAERLRAIRARHGGDAVGVYGGNPQAHT--HAGGAYSPAllkALGTS-----NYF---SAATADQKPghfwsglm 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 164 FGidRGLTFRLSDIPLADCIVLAGTNIAECQ--PTLLPYF----NQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDA 237
Cdd:cd02762 143 FG--HPGLHPVPDIDRTDYLLILGANPLQSNgsLRTAPDRvlrlKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 238 ILADAMLKMIVDEGLLDEGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTD 317
Cdd:cd02762 221 WLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 318 GHLAvrRYLN--LVLATGKIGREG---CGYGAITGQGN-GQGGREHGQKADQLPGYRSIENEedrayvasvwgvkassLP 391
Cdd:cd02762 301 GTLC--SWLVklLNLLTGNLDRPGgamFTTPALDLVGQtSGRTIGRGEWRSRVSGLPEIAGE----------------LP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 392 GKGVSayEMMELIHRGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMEN-EGTLT 470
Cdd:cd02762 363 VNVLA--EEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKpHATFF 440
|
490 500
....*....|....*....|....*....
gi 2254313745 471 NLE---GRVLLRKAARQAPGEARHDWVIL 496
Cdd:cd02762 441 NLEfprNAFRYRRPLFPPPPGTLPEWEIL 469
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
18-597 |
6.61e-75 |
|
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: 254.25 E-value: 6.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIP-NLASEGRVCVKGMNAHQHAAHSQRLQYPLIRSNG--ELIPCSWD 94
Cdd:cd02752 2 TICPYCSVGCGLIAYVQNGVW-------VHQEGDPdHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGsgKWEEISWD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 95 EAIAVISDRFQAISER------------YGPDAHAVYGGGSLTNETAYLLGKFARvALGTRYIDYNGRFCMSAAASAGSK 162
Cdd:cd02752 75 EALDEIARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFAR-ALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 163 TFGidRG-LTFRLSDIPLADCIVLAGTNIAECQPTLLPYFNQAKE-NGAKIIVIDPRRTATAAIADMHLAIRPGTDAILA 240
Cdd:cd02752 154 TFG--RGaMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEkNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 241 DAMLKMIVdeglldegfiqarttgyeelktyldSFDLSRAADLCGLNVELIREAAFSYA---MAD-TGMVLTARGVEQQT 316
Cdd:cd02752 232 GGMINYII-------------------------RYTPEEVEDICGVPKEDFLKVAEMFAatgRPDkPGTILYAMGWTQHT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 317 DGHLAVRRYLNLVLATGKIGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSieneedrayvasvwgvkasslpgkgvs 396
Cdd:cd02752 287 VGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYLG--------------------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 397 ayemmelihrgeikslfvmGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFAD-------------LVLPVTSYM 463
Cdd:cd02752 340 -------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQY 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 464 ENEGTLTNlEGRVL-LRKAARQAPGEARHDWVILCAIADRLG-----------------RGEYFDFHEPEEI-------- 517
Cdd:cd02752 401 EKEGSITN-SGRWLqWRYKVVEPPGEAKSDGDILVELAKRLGflyekeggafpepitkwNYGYGDEPTPEEIareingga 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 518 ----------------------FSELRLasKGGIADYFGItYDRLRREEGVYWPCPSEEESGTGLLFRQSFAHP------ 569
Cdd:cd02752 480 ltdgytgqsperlkahgqnvhtFDTLRD--DGSTACGCWI-YSGSYTEEGRMARRDTSDPDGLGLYPGWPWPWPvnrril 556
|
650 660 670
....*....|....*....|....*....|
gi 2254313745 570 --DGKAVFSVTPGNPwvgvseEYPLILTNG 597
Cdd:cd02752 557 ynRASVDMEGKPGYP------ERPLVEWDG 580
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
76-575 |
6.38e-67 |
|
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: 230.66 E-value: 6.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 76 RLQYPLIRSNGE--LIPCSWDEAIAVISDRFQAISerygPDAHAVYGGGSLTNETAYLLGKFARvALGTRYIDYNGRFCM 153
Cdd:cd02767 64 RLTYPMRYDAGSdhYRPISWDEAFAEIAARLRALD----PDRAAFYTSGRASNEAAYLYQLFAR-AYGTNNLPDCSNMCH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 154 SAAASAGSKTFGIDRGlTFRLSDIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRR--------------- 218
Cdd:cd02767 139 EPSSVGLKKSIGVGKG-TVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLRepglerfanpqnpes 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 219 --TATAAIADMHLAIRPGTDAILADAMLKMIVDE-----GLLDEGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELI 291
Cdd:cd02767 218 mlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 292 REAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKIGREGCGYGAITGQGNGQGGREHGqkADQLPGyrsie 371
Cdd:cd02767 298 EAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMG--ITEKPF----- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 372 nEEDRAYVASVWGVKASSLPGKGVSayEMMELIHRGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMS---- 447
Cdd:cd02767 371 -PEFLDALEEVFGFTPPRDPGLDTV--EAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNrshl 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 448 ---ETArfadLVLPVTS--------------YMENEGTLTNL-------EGRVLL------RKAARQAPGEARHDWVILC 497
Cdd:cd02767 448 vhgEEA----LILPCLGrteidmqaggaqavTVEDSMSMTHTsrgrlkpASRVLLseeaivAGIAGARLGEAKPEWEILV 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254313745 498 AIADRLgRGEYfdfhepEEIFSElrlaskgGIADYfgitYDRLRREEGVYWPCPSEEesgtgllfRQsFAHPDGKAVF 575
Cdd:cd02767 524 EDYDRI-RDEI------AAVIYE-------GFADF----NQRGDQPGGFHLPNGARE--------RK-FNTPSGKAQF 574
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
20-702 |
1.01e-62 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 224.39 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 20 CPFCSVQCKMTVAVEENGIPGQHkarykveGIPnlASE---GRVCVKG------MNAHQhaahsqRLQYPLIR------- 83
Cdd:PRK13532 47 CRFCGTGCGVLVGTKDGRVVATQ-------GDP--DAPvnrGLNCIKGyflskiMYGKD------RLTQPLLRmkdgkyd 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 84 SNGELIPCSWDEAIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKT 163
Cdd:PRK13532 112 KEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMASAVVGFMRT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 164 FGIDR--GLtfrLSDIPLADCIVLAGTNIAECQPTLLPYFNQAK--ENGAKIIVIDPRRTATAAIADMHLAIRPGTDAIL 239
Cdd:PRK13532 192 FGIDEpmGC---YDDIEAADAFVLWGSNMAEMHPILWSRVTDRRlsNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 240 ADAMLKMIVDEGLLDEGFIQARTT--------GY--------------------------EELKTYLDSFDLSRAADLCG 285
Cdd:PRK13532 269 LNYIANYIIQNNAVNWDFVNKHTNfrkgatdiGYglrpthplekaaknpgtagksepisfEEFKKFVAPYTLEKTAKMSG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 286 LNVELIREAAFSYAMADTGMV-LTARGVEQQTDGHLAVRRYLNLVLATGKIGREGCGYGAITGQGNGQG-GREHGQKADQ 363
Cdd:PRK13532 349 VPKEQLEQLAKLYADPNRKVVsFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 364 LPGYRSIENEEDRAYVASVWGVKASSLPGK-GVSAYEMMELIHRGEIKSLFVMGSNPVVSNPNAGlvEEGL----NHLDF 438
Cdd:PRK13532 429 LPADMVVTNPKHREIAEKIWKLPEGTIPPKpGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNIN--EERLpgwrNPDNF 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 439 LVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPGEARHD-WVILcaiadrlgrgEYFDFHEPEEI 517
Cdd:PRK13532 507 IVVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV----------EFSKRFKTEEV 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 518 FSELRLASKG--------------GIADYFGIT---------------------------------------YDRLRREE 544
Cdd:PRK13532 577 WPEELLAKKPeyrgktlydvlfanGQVDKFPLSelaegylndeakhfgfyvqkglfeeyasfgrghghdlapFDTYHKVR 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 545 GVYWPCPSEEES--------------GTGLLFrqsFAHPDGKAVFSVTPGNPWVGV-SEEYPLILTNGRVLSHYLTGVQT 609
Cdd:PRK13532 657 GLRWPVVDGKETlwryregydpyvkaGEGFKF---YGKPDGKAVIFALPYEPPAESpDEEYDLWLSTGRVLEHWHTGSMT 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 610 RRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRfsVRSRIKEHIR----VDTLFVPmhWGGA-QNVNHATRP 684
Cdd:PRK13532 734 RRVPELYRAFPEAVCFMHPEDAKARGLRRGDEVKVVSRRGE--VKSRVETRGRnkppRGLVFVP--FFDAaQLINKLTLD 809
|
810
....*....|....*...
gi 2254313745 685 ELDPFCKMPGFKTAAVRI 702
Cdd:PRK13532 810 ATDPLSKQTDFKKCAVKI 827
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
59-547 |
1.87e-62 |
|
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: 219.50 E-value: 1.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 59 RVCVKGMNAHQHAAHSQRLQYPLIRSN----GELIPCSWDEAIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGK 134
Cdd:cd02770 42 RACLRGRSQRKRVYNPDRLKYPMKRVGkrgeGKFVRISWDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 135 FARV-ALGTRYIDYNGRFCMSAAASAGSKTFGIDrGLTFRLSDIPLADCIVLAGTNIAECQPTLLP---YFNQAKENGAK 210
Cdd:cd02770 122 IARLlNLTGGYLNYYGTYSWAQITTATPYTYGAA-ASGSSLDDLKDSKLVVLFGHNPAETRMGGGGstyYYLQAKKAGAK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 211 IIVIDPRRTATAA-IADMHLAIRPGTDAILADAMLKMIVDEGLLDEGFIQARTTGYEE------------LKTYLdsfdL 277
Cdd:cd02770 201 FIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFDAehlpegappnesYKDYV----L 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 278 SR-----------AADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKIGREGCGYGAit 346
Cdd:cd02770 277 GTgydgtpktpewASEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGA-- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 347 gqgngqggREHGQKAdQLPGYRSIENeedrayvasvwGVKASslpgkgVSAYEMMELIHRGE------------------ 408
Cdd:cd02770 355 --------RPGGSAY-NGAGLPAGKN-----------PVKTS------IPCFMWTDAIERGEemtaddggvkgadklksn 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 409 IKSLFVMGSNpVVSNPNAGLVEEGLNHLD------FLVVADMFMSETARFADLVLPVTSYMENEGTLTN----LEGRVLL 478
Cdd:cd02770 409 IKMIWNYAGN-TLINQHSDDNNTTRALLDdeskceFIVVIDNFMTPSARYADILLPDTTELEREDIVLTsnagMMEYLIY 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 479 RKAARQAPGEARHDWVILCAIADRLG-RGEYFDFHEPEEIFSElrLASKGGIADYFGITYDRLrREEGVY 547
Cdd:cd02770 488 SQKAIEPLYECKSDYEICAELAKRLGvEDQFTEGKTEQEWLEE--LYGQTRAKEPGLPTYEEF-REKGIY 554
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
20-528 |
1.21e-60 |
|
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: 210.62 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 20 CPFCSVQCKMTVAVEENgipgqhkARYKVEGIP-NLASEGRVCVKGMNAHQHAAHSQRLQYPLIRS----NGELIPCSWD 94
Cdd:cd02755 5 CEMCSSRCGILARVEDG-------RVVKIDGNPlSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVgergEGKFREASWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 95 EAIAVISDRFQAISERYGPDAhAVYGGGSLTNETayLLGKFARvALGTRYIDYNGRFCMSAAASAGSKTFGIDRGLTFRl 174
Cdd:cd02755 78 EALQYIASKLKEIKEQHGPES-VLFGGHGGCYSP--FFKHFAA-AFGSPNIFSHESTCLASKNLAWKLVIDSFGGEVNP- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 175 sDIPLADCIVLAGTNIAEC-QPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDEGLL 253
Cdd:cd02755 153 -DFENARYIILFGRNLAEAiIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 254 DEGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYA------MADTGMvltaRGVEQQTDghLAVRRYLN 327
Cdd:cd02755 232 DAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAaaaphaVVDPGW----RGTFYSNS--FQTRRAIA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 328 LVLA-TGKIGREGcGygaitgqgngqggrehgqkadqlpgyrsieneedrayvasvWGVKASSLPGKgvsayemmelihr 406
Cdd:cd02755 306 IINAlLGNIDKRG-G-----------------------------------------LYYAGSAKPYP------------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 407 geIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEG---RVLLRKAAR 483
Cdd:cd02755 331 --IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGpapAVATRQRAI 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2254313745 484 QAPGEARHDWVILCAIADRLGRgeyfdFHEPE---EIFSeLRLASKGG 528
Cdd:cd02755 409 EPLYDTRPGWDILKELARRLGL-----FGTPSgkiELYS-PILAKAGY 450
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
59-547 |
1.19e-58 |
|
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: 209.01 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 59 RVCVKGMNAHQHAAHSQRLQYPLIR--------------SNGELIPCSWDEAIAVISDRFQAISERYGPDA-HAVYGGGS 123
Cdd:cd02751 30 RPCPRGRSVRDRVYSPDRIKYPMKRvgwlgngpgsrelrGEGEFVRISWDEALDLVASELKRIREKYGNEAiFGGSYGWA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 124 LTNETAYLLGKFAR-VALGTRYIDYNGRFCMSAAASAGSKTFGIDRGL--TFRLSDIP-LADCIVLAGTNIAECQP---- 195
Cdd:cd02751 110 SAGRLHHAQSLLHRfLNLIGGYLGSYGTYSTGAAQVILPHVVGSDEVYeqGTSWDDIAeHSDLVVLFGANPLKTRQgggg 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 196 ----TLLPYFNQAKENGAKIIVIDPRRTATAA-IADMHLAIRPGTDAILADAMLKMIVDEGLLDEGFIQARTTGYEELKT 270
Cdd:cd02751 190 gpdhGSYYYLKQAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 271 YLdsfdLSR----------AADLCGLNVELIREAAFSYAmADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKIGREGC 340
Cdd:cd02751 270 YL----LGEsdgvpktpewAAEITGVPAETIRALAREIA-SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 341 GYGAITGQGNGQGGrehGQKADQLPGYRSIENeedrayvasvwGVKASslpgkgVSAYEMMELI-HRGE----------- 408
Cdd:cd02751 345 GFGFGYGYSNGGGP---PRGGAGGPGLPQGKN-----------PVKDS------IPVARIADALlNPGKeftangklkty 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 409 --IKSLFVMGSNPVVS-NPNAGLVEeGLNHLDFLVVADMFMSETARFADLVLPVTSYMENE--GTLTNLEGRVLLrkAAR 483
Cdd:cd02751 405 pdIKMIYWAGGNPLHHhQDLNRLIK-ALRKDETIVVHDIFWTASARYADIVLPATTSLERNdiGLTGNYSNRYLI--AMK 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254313745 484 QA--P-GEARHDWVILCAIADRLGRGEYFDFHEPE-----EIFSELRLASKGGIADYfgITYDRLrREEGVY 547
Cdd:cd02751 482 QAvePlGEARSDYEIFAELAKRLGVEEEFTEGRDEmewleHLYEETRAKAAGPGPEL--PSFEEF-WEKGIV 550
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
20-575 |
6.79e-57 |
|
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: 203.09 E-value: 6.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 20 CPF-CSVQCKMTVAVEENGIPGQHkarYKvegipnlasegRVCVKGMNAHQHAAHSQRLQYPLIR----SNGELIPCSWD 94
Cdd:cd02765 12 CPLkCHVRDGKIVKVEPNEWPDKT---YK-----------RGCTRGLSHLQRVYSPDRLKYPMKRvgerGEGKFERITWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 95 EAIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGkfaRVALGTRYIDYNGRFCMSAAASAGSKTFGIDRGLTFRL 174
Cdd:cd02765 78 EALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRL---ALLGGGLQDALTYGIDTGVGQGFNRVTGGGFMPPTNEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 175 SDIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDEGLLD 254
Cdd:cd02765 155 TDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 255 EGFIQART--------------------------------------------------------------TGYEELKTYL 272
Cdd:cd02765 235 EAFLKSNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhTVLTALREQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 273 DSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKIGREGCGygaitgqgngq 352
Cdd:cd02765 315 ASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG----------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 353 ggreHGQkadqlpgyrsieneedrayvasvwgvkasslpgkgvsayemmelihrgeIKSLFVMGSNPVVSNPNAGLVEEG 432
Cdd:cd02765 384 ----VGQ-------------------------------------------------IKFMYFMGSNFLGNQPDRDRWLKV 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 433 LNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGR--VLLRKAARQAPGEARHDWVILCAIADRLGRGEYFD 510
Cdd:cd02765 411 MKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHphVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFP 490
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254313745 511 fHEPEEIfseLRLASKGGIADYFGITYDRLrREEGVYWPCPSEEESGTGLLfRQSFAHPDGKAVF 575
Cdd:cd02765 491 -KTPEDY---VRAFMNSDDPALDGITWEAL-KEEGIIMRLATPEDPYVAYL-DQKFGTPSGKLEF 549
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
20-673 |
8.18e-55 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 200.66 E-value: 8.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 20 CPFCSVQCKMTVAVEENgipgqhKARYkVEGIPNLAS-EGRVCVKGMNAHQHAAHSQRLQYPLIRS----NGELIPCSWD 94
Cdd:PRK15488 48 CEMCSTRCPIEARVVNG------KNVF-IQGNPKAKSfGTKVCARGGSGHSLLYDPQRIVKPLKRVgergEGKWQEISWD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 95 EAIAVISDRFQAISERYGPDAHAVyggGSLTNETAYLLGKFARvALGTRYIDYNGRFCMSAAASAGSKTFGIDRGLtfrl 174
Cdd:PRK15488 121 EAYQEIAAKLNAIKQQHGPESVAF---SSKSGSLSSHLFHLAT-AFGSPNTFTHASTCPAGYAIAAKVMFGGKLKR---- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 175 sDIPLADCIV------LAGTNIAECQPtllpYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIV 248
Cdd:PRK15488 193 -DLANSKYIInfghnlYEGINMSDTRG----LMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 249 DEGLLDEGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIRE------AAFSYAMADTGMVLTArgveqqTDGHLAV 322
Cdd:PRK15488 268 EENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRiarelaAAAPHAIVDFGHRATF------TPEEFDM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 323 RRYL---NLVLatGKIGREG--------CGYGAITGQGNGQGGREHGQKADQLPGYRSIEN-EEDRAYVASVWGVkASSL 390
Cdd:PRK15488 342 RRAIfaaNVLL--GNIERKGglyfgknaSVYNKLAGEKVAPTLAKPGVKGMPKPTAKRIDLvGEQFKYIAAGGGV-VQSI 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 391 PGKGVSA--YemmelihrgEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGT 468
Cdd:PRK15488 419 IDATLTQkpY---------QIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 469 LTNLEGRV---LLRKAARQAPGEARHDWVILCAIADRLGRGEYFdfhePEEIFSELRLASKGGIADyfgiTYDRLRREEG 545
Cdd:PRK15488 490 ISDKSGKNpayALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYY----PWQDMETLQLYQVNGDHA----LLKELKKKGY 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 546 VYWPCPseeesgtgLLFRQ---------------------------SFAHPDGK------AVFSVTPG------NPwVGV 586
Cdd:PRK15488 562 VSFGVP--------LLLREpkmvakfvarypnakavdedgtygsqlKFKTPSGKielfsaKLEALAPGygvpryRD-VAL 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 587 SEEYPLILTNGRVLSHylTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTL 666
Cdd:PRK15488 633 KKEDELYFIQGKVAVH--TNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTL 710
|
....*..
gi 2254313745 667 FVPMHWG 673
Cdd:PRK15488 711 FAYMGFG 717
|
|
| 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 ... |
20-507 |
7.39e-51 |
|
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: 184.13 E-value: 7.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 20 CPFCSVQCkmtvaveeNGIPGQHKARYK-VEGIPNLA-SEGRVCVKGMNAHQHAAHSQRLQYPLIRSNGELIPCSWDEAI 97
Cdd:cd02771 4 CHHCSVGC--------NISLGERYGELRrVENRYNGAvNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 98 AVISDRFQAISERYGpdahaVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRfcMSAAASAgsKTFGIDRGltfRLSDI 177
Cdd:cd02771 76 DVAAARLKEAKDKVG-----GIGSPRASNESNYALQKLVGAVLGTNNVDHRAR--RLIAEIL--RNGPIYIP---SLRDI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 178 PLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDeglLDEGF 257
Cdd:cd02771 144 ESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDD---IAAES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 258 IQARTTGYEELKTYLDSFDLSRAADLCGLN-VELIREAAFSYAMAdtGMVLTARGVEQQTDGhlAVRRYLNLVLATGKIG 336
Cdd:cd02771 221 IRASPGGQARLGAALARAVDASAAGVSGLApKEKAARIAARLTGA--KKPLIVSGTLSGSLE--LIKAAANLAKALKRRG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 337 rEGCGYGAITGQGNgqggrehgqkadqLPGYRSIENEEDRAyvasvwgvkasslpgkGVSAYEMMELIHRGEIKSLFVMG 416
Cdd:cd02771 297 -ENAGLTLAVEEGN-------------SPGLLLLGGHVTEP----------------GLDLDGALAALEDGSADALIVLG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 417 SNPVVSNPNAGlVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRV-LLRKAARQAPGEARHDWVI 495
Cdd:cd02771 347 NDLYRSAPERR-VEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAqRFFKAYDDPAGDARSDWRW 425
|
490
....*....|..
gi 2254313745 496 LCAIADRLGRGE 507
Cdd:cd02771 426 LHALAAKLGGKL 437
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
588-703 |
2.23e-44 |
|
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: 154.97 E-value: 2.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 588 EEYPLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLF 667
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVF 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2254313745 668 VPMHWGG---AQNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd00508 81 MPFHWGGevsGGAANALTNDALDPVSGQPEFKACAVRIE 119
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
18-520 |
4.42e-42 |
|
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: 159.02 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCKMTVAVEeNGIP----GQHKARYKVEGIPNLasEGRVCVKGMNAHQHAAHSQRLQYPLIRS----NGELI 89
Cdd:cd02750 7 THGVNCTGSCSWNVYVK-NGIVtreeQATDYPETPPDLPDY--NPRGCQRGASFSWYLYSPDRVKYPLKRVgargEGKWK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 90 PCSWDEAIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYllgkfarvALGTRYIDYNGRFCMSAAA------SAGSKT 163
Cdd:cd02750 84 RISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSY--------AAGSRFASLIGGVSLSFYDwygdlpPGSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 164 FGiDRGLTFRLSDIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAM 243
Cdd:cd02750 156 WG-EQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 244 LKMIVDEGLLDEGFiqarttgyeeLKTYLD----SFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGH 319
Cdd:cd02750 235 AHVIIKEKLYDEDY----------LKEYTDlpflVYTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 320 LAVRRYLNLVLATGKIGRegcgygaitgqgngqggrehgqkadqlpgyrsieneedrayvasvwgvkasslPGKGVSAYE 399
Cdd:cd02750 305 LCYRALILLLALTGNEGK-----------------------------------------------------NGGGWAHYV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 400 mmelihrGEIKSLFVMGSNPVVSNPNAG-LVEEGLN-HLDFLVVADMFMSETARFADLVLP-VTSYMENEGTLTNLEGRV 476
Cdd:cd02750 332 -------GQPRVLFVWRGNLFGSSGKGHeYFEDAPEgKLDLIVDLDFRMDSTALYSDIVLPaATWYEKHDLSTTDMHPFI 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2254313745 477 LLRKAARQAPGEARHDWVILCAIADRL------GRGEYFDFHEPEEIFSE 520
Cdd:cd02750 405 HPFSPAVDPLWEAKSDWEIFKALAKKVpwrtltGRQQFYLDHDWFLELGE 454
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
75-586 |
4.86e-41 |
|
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: 159.57 E-value: 4.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 75 QRLQYPLIRSNGELIPCSWDEAIAVISDRFQAISERYGPDaHAV------YGGGSLTNETAYLLGKFARVALGTRYIDYN 148
Cdd:cd02756 116 TRLTTPLVRRGGQLQPTTWDDAIDLVARVIKGILDKDGND-DAVfasrfdHGGGGGGFENNWGVGKFFFMALQTPFVRIH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 149 GRFCMSAAASAGSktfgiDRG---LTFRLSDIPLADCIVLAGTNIAECQPT-----LLPYF--------NQAKENG---- 208
Cdd:cd02756 195 NRPAYNSEVHATR-----EMGvgeLNNSYEDARLADTIVLWGNNPYETQTVyflnhWLPNLrgatvsekQQWFPPGepvp 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 209 -AKIIVIDPRRTATAAIAD--------MHLAIRPGTDAILADAMLKMIVDeglldegfiqarttgyeelkTYLDSfdLSR 279
Cdd:cd02756 270 pGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALANAIARYIYE--------------------SLDEV--LAE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 280 AADLCGLNVELIREAAFSYAMADTG------MVLTARGVEQQTDGHLAVRRYLNLVLATGKIGREGCGYGAitgqgngQG 353
Cdd:cd02756 328 AEQITGVPRAQIEKAADWIAKPKEGgyrkrvMFEYEKGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCVR-------QG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 354 GREHGQKADQLPGYRSIENEEDRAYVAsvwgvkasslpgkgvsayemmELIHRGEIKSLFVMGSNPVVSNPNAGLVEEGL 433
Cdd:cd02756 401 GHQEGYVRPPPPPPPWYPQYQYAPYID---------------------QLLISGKGKVLWVIGCDPYKTTPNAQRLRETI 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 434 NHLD----------------------------------FLVVADMFMSETARFADLVLPVTSYME-NEGTLTNLEGRVLL 478
Cdd:cd02756 460 NHRSklvtdaveaalyagtydreamvcligdaiqpgglFIVVQDIYPTKLAEDAHVILPAAANGEmNETSMNGHERRLRL 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 479 RKAARQAPGEARHDWVILCAIADRL-------GRGEY-------FDFHEPEEIFSE-LRLASKGGIADYF---------- 533
Cdd:cd02756 540 YEKFMDPPGEAMPDWWIAAMIANRIyelyqeeGKGGSaqyqffgFIWKTEEDNFMDgSQEFADGGEFSEDyyvlgqerye 619
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2254313745 534 GITYDRLRR--EEGVYWPCPSEEESGTGLL-FRQS---FAHPDGKAVFsvTPGNPWVGV 586
Cdd:cd02756 620 GVTYNRLKAvgVNGIQLPVTTDTVTKILVTnVLRTegvFDTEDGKAYV--IDLAPWPGL 676
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
56-509 |
4.89e-40 |
|
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: 155.88 E-value: 4.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 56 SEGRV---CV-KGMNAHQHAAHSQRlqypliRSNGELIPCSWDEAIAVISDRFQAISERYGPDAhaVYGG-------GSL 124
Cdd:cd02769 43 SPTRIkypMVrRGWLEKGPGSDRSL------RGKEEFVRVSWDEALDLVAAELKRVRKTYGNEA--IFGGsygwssaGRF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 125 TNETAyLLGKFARVALGtrYIDYNGRFCMSAAASAGSKTFGIDRGLTFRLSDIPL----ADCIVLAGTNIAECQPT---- 196
Cdd:cd02769 115 HHAQS-LLHRFLNLAGG--YVGSVGDYSTGAAQVILPHVVGSMEVYTEQQTSWPViaehTELVVAFGADPLKNAQIawgg 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 197 -----LLPYFNQAKENGAKIIVIDPRRTATAAIADM-HLAIRPGTDAILADAMLKMIVDEGLLDEGFIQARTTGYEELKT 270
Cdd:cd02769 192 ipdhqAYSYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 271 YLDSF------DLSRAADLCGLNVELIREAAFSYAMADTgMVLTARGVEQQTDGHLAVrrYLNLVLAT--GKIGREGCGY 342
Cdd:cd02769 272 YLLGEsdgvpkTPEWAAAICGIPAETIRELARRFASKRT-MIMAGWSLQRAHHGEQPH--WMAVTLAAmlGQIGLPGGGF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 343 GAITGQGNGQGGREHGQKADQLPgyrsieneEDRAYVASVWGVK--ASSL--PGKgvsAYEMM-ELIHRGEIKSLFVMGS 417
Cdd:cd02769 349 GFGYHYSNGGGPPRGAAPPPALP--------QGRNPVSSFIPVAriADMLlnPGK---PFDYNgKKLTYPDIKLVYWAGG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 418 NPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYME-NEGTLTNLEGRVLLRKAARQAPGEARHDWVIL 496
Cdd:cd02769 418 NPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLErNDIGGSGDNRYIVAMKQVVEPVGEARDDYDIF 497
|
490
....*....|...
gi 2254313745 497 CAIADRLGRGEYF 509
Cdd:cd02769 498 ADLAERLGVEEQF 510
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
18-516 |
4.66e-38 |
|
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: 148.74 E-value: 4.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIPN-LASEGRVCVKGMNAHQHAAHSQRLQYPLIRSN--------GEL 88
Cdd:cd02757 4 STCQGCTAWCGLQAYVEDGRV-------TKVEGNPLhPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNprkgrdvdPKF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 89 IPCSWDEAIAVISDRFQAISERYGPDAHAV-YGGGSLTNETAYllGKFARvALGTRYIDYNGRFCMSAAASAGSKTfgiD 167
Cdd:cd02757 77 VPISWDEALDTIADKIRALRKENEPHKIMLhRGRYGHNNSILY--GRFTK-MIGSPNNISHSSVCAESEKFGRYYT---E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 168 RGLTFRLSDIPLADCIVLAGTNIAECQpTLLPYFNQ---AKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAML 244
Cdd:cd02757 151 GGWDYNSYDYANAKYILFFGADPLESN-RQNPHAQRiwgGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 245 KMIVDEGLLDEGFI----------QARTTGYE-----------------ELKTYLDSFdlsrAADLCGLNVELIREAAFS 297
Cdd:cd02757 230 HVILTEGLWDKDFVgdfvdgknyfKAGETVDEesfkeksteglvkwwnlELKDYTPEW----AAKISGIPAETIERVARE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 298 YAMADT-GMVLTARGVEQQTDGHLAVRRYLNLVLATGKIGREGcgyGAITGQGNgqggrehgqkadqlpgyrsieneedr 376
Cdd:cd02757 306 FATAAPaAAAFTWRGATMQNRGSYNSMACHALNGLVGSIDSKG---GLCPNMGV-------------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 377 ayvasvwgvkasslpgkgvsayemmelihrGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLV 456
Cdd:cd02757 357 ------------------------------PKIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIV 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254313745 457 LPVTSYMENEGTL---TNLEGRVLLRKAARQAPGEARHDWVILCAIADRLG--------RGEYFDFHEPEE 516
Cdd:cd02757 407 LPDGHHFERWDVMsqeNNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDpkgsdgmkRYAPGQFKDPET 477
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
17-503 |
4.73e-35 |
|
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: 137.41 E-value: 4.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 17 ETQCPFCSVQCKMTVAVEENGI----PGQHkarykvEGIpNlasEGRVCVKGMNAHQHAAHSQRLQYPLIRSNGELIPCS 92
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVmrilPREN------EAI-N---EEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 93 WDEAIAVISDRFQAISerygPDAHAVYGGGSLTNETAYLLGKFARvALGTRYIDYNGRFcMSAAASAGSKTFGIdrgLTF 172
Cdd:cd02768 71 WEEALKTVAEGLKAVK----GDKIGGIAGPRADLESLFLLKKLLN-KLGSNNIDHRLRQ-SDLPADNRLRGNYL---FNT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 173 RLSDIPLADCIVLAGTNIAECQPTLlpyfNQ-----AKENGAKIIVIDPrrTATAAIADMHLAIRPGTDAIlaDAMLKmi 247
Cdd:cd02768 142 SIAEIEEADAVLLIGSNLRKEAPLL----NArlrkaVKKKGAKIAVIGP--KDTDLIADLTYPVSPLGASL--ATLLD-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 248 VDEGLLDEGFIQArttgyeelktyldSFDLSRAADLCGLNVELIREAAFSYAMAdtgmvltargveqqtdghlavrrylN 327
Cdd:cd02768 212 IAEGKHLKPFAKS-------------LKKAKKPLIILGSSALRKDGAAILKALA-------------------------N 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 328 LVLATGKIGREGCGYGAITGQGngqggrehgqkadqlpgyrsieneedrAYVAsvwgvkasslpgkGVSAYEMMELIHRG 407
Cdd:cd02768 254 LAAKLGTGAGLWNGLNVLNSVG---------------------------ARLG-------------GAGLDAGLALLEPG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 408 EIKSLFVMGSNPVVSNPNAGLVeegLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPG 487
Cdd:cd02768 294 KAKLLLLGEDELDRSNPPAAVA---LAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPG 370
|
490
....*....|....*.
gi 2254313745 488 EARHDWVILCAIADRL 503
Cdd:cd02768 371 DAREDWKILRALSNLL 386
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
588-703 |
8.39e-35 |
|
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: 128.12 E-value: 8.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 588 EEYPLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLF 667
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVF 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 2254313745 668 VPMHWGGAqNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd02790 81 MPFHFAEA-AANLLTNAALDPVAKIPEFKVCAVRVE 115
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
588-703 |
9.47e-34 |
|
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: 125.38 E-value: 9.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 588 EEYPLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLF 667
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2254313745 668 VPMHWGG----AQNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd02791 81 VPMHWGDqfgrSGRVNALTLDATDPVSGQPEFKHCAVRIE 120
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
588-703 |
3.14e-31 |
|
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: 118.09 E-value: 3.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 588 EEYPLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLF 667
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2254313745 668 VPMHWGGA-----QNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd02792 81 IPYHWGGMglvigDSANTLTPYVGDPNTQTPEYKAFLVNIE 121
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
90-702 |
1.27e-30 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 128.62 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 90 PCSWDEAIAVISDRFQAISErygPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGrFCMSAAASAGSKTFGIDRG 169
Cdd:PRK09939 124 PLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSN-MCHEPTSVGLAASIGVGKG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 170 lTFRLSDIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDP-------RRTA-----------TAAIADMHLAI 231
Cdd:PRK09939 200 -TVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApqnpfemltnsETQLASAYYNV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 232 RPGTDAILADAMLKMIVDE----------GLLDEGFIQARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMA 301
Cdd:PRK09939 279 RIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 302 DTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKIGREGCGYGAITGQGNGQGgrehgqkaDQLPGYRSIENEEDRAYVAS 381
Cdd:PRK09939 359 ERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQG--------DRTVGITEKPSAEFLARLGE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 382 VWGVKASSLPGKgvSAYEMMELIHRGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSE----TARFAdLVL 457
Cdd:PRK09939 431 RYGFTPPHAPGH--AAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRshllTARHS-YIL 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 458 PVTSY----MENEGT-LTNLEGRVLLRKAARQAPGEARHDWVILCAIADRLGRGEYfdfhePEEIfselrLASKGGIADy 532
Cdd:PRK09939 508 PVLGRseidMQKSGAqAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAAL-----PQSV-----VAWEYLVED- 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 533 fgitYDRLRREEGVYWPCPSE------EESGTGLL---FRQSFAHPDGKAVFSVTPG---NPWVGVSEEypLILTNGRVL 600
Cdd:PRK09939 577 ----YDRIRNDIEAVLPEFADynqrirHPGGFHLInaaAERRWMTPSGKANFITSKGlleDPSSAFNSK--LVMATVRSH 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 601 SHY---LTGVQTRRSPSLLARELenfVEIHPITAQRYRIRDGEWVEIV--SEHGRFSVRsrikehiRVDTLFVPMHWGGA 675
Cdd:PRK09939 651 DQYnttIYGMDDRYRGVFGQRDV---VFMSAKQAKICRVKNGERVNLIalTPDGKRSSR-------RMDRLKVVIYPMAD 720
|
650 660 670
....*....|....*....|....*....|....*
gi 2254313745 676 QNV-------NHA-TRPELDPFCKMPGFKTAAVRI 702
Cdd:PRK09939 721 RSLvtyfpesNHMlTLDNHDPLSGIPGYKSIPVEL 755
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
592-699 |
2.02e-30 |
|
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: 115.45 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 592 LILTNGRVLSHYLTGVQTRRSPSLLARElENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLFVPMH 671
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPE-PEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|.
gi 2254313745 672 WGG---AQNVNHATRPELDPFCKMPGFKTAA 699
Cdd:pfam01568 80 WWYeprGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
396-521 |
1.26e-28 |
|
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: 119.56 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 396 SAYEMMELIHRGEIKSLFVMGSNPVVSNPNAglVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGR 475
Cdd:COG1034 320 DAAAILEAAEAGKLKALVLLGADPYDLDPAA--ALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGR 397
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2254313745 476 VLLRKAARQAPGEARHDWVILCAIADRLGRGeyFDFHEPEEIFSEL 521
Cdd:COG1034 398 VQRFNAAVPPPGEARPDWRVLRALANALGAG--LPYDSLEEVRAEL 441
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
67-496 |
2.44e-28 |
|
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: 118.23 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 67 AHQHAAHSQRLQYPLIRSNGELIPCSWDEAIAVISDRFQAISERYGPDAHAVYGGGSLTNETAYLLGKFARvALGTRYID 146
Cdd:cd02772 45 SYEGLNSEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLAR-GLGSDNID 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 147 YNGRfcmSAAASAGSKtFGIDRGLTFRLSDIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPrrtataAIAD 226
Cdd:cd02772 124 HRLR---QSDFRDDAK-ASGAPWLGMPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINP------ADDD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 227 MHLAIrPGTDAILADAM-------LKMIVDEGLLDEGFIQARTTGYEELKTYLDSF-DLSRAADLCGLNVELIREAAFSY 298
Cdd:cd02772 194 FLFPL-SGKAIVAPSALanalaqvAKALAEEKGLAVPDEDAKVEASEEARKIAASLvSAERAAVFLGNLAQNHPQAATLR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 299 AMADTgmvltargVEQQTDGHLAvrrylnlVLATGkigregcgygaitgqGNGQGGREHGqkadqlpgyrsieneedray 378
Cdd:cd02772 273 ALAQE--------IAKLTGATLG-------VLGEG---------------ANSVGAYLAG-------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 379 vasvwgvkasSLPGKGVSAYEMMELihrgEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETAR-FADLVL 457
Cdd:cd02772 303 ----------ALPHGGLNAAAMLEQ----PRKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALLdYADVLL 368
|
410 420 430
....*....|....*....|....*....|....*....
gi 2254313745 458 PVTSYMENEGTLTNLEGRVLLRKAARQAPGEARHDWVIL 496
Cdd:cd02772 369 PIAPFTETSGTFVNLEGRVQSFKGVVKPLGEARPAWKVL 407
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
61-522 |
3.45e-28 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 120.82 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 61 CVKGMNAHQHAAHSQRLQYPLIR-SNGELIPCSWDEAIAVISDRFQAISERYGpdahaVYGGGSLTNETAYLLGKFARVA 139
Cdd:PRK07860 263 CDKGRWAFTYATQPDRITTPLVRdEDGELEPASWSEALAVAARGLAAARGRVG-----VLVGGRLTVEDAYAYAKFARVA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 140 LGTRYIDYNGRfcmsaAASAGSKTF------GIDRGLTFrlSDIPLADCIVLAGTNIAECQPTL-LPYFNQAKENGAKII 212
Cdd:PRK07860 338 LGTNDIDFRAR-----PHSAEEADFlaarvaGRGLGVTY--ADLEKAPAVLLVGFEPEEESPIVfLRLRKAARKHGLKVY 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 213 VIDPrrTATAAIADMH---LAIRPGTDAILADAMLK--MIVDEGLLDEGFIQarTTGyeelktyldsfdlSRAADLCGLn 287
Cdd:PRK07860 411 SIAP--FATRGLEKMGgtlLRTAPGGEAAALDALATgaPDVAELLRTPGAVI--LVG-------------ERLATVPGA- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 288 velireaafsyamadtgmvLTArgveqqtdghlAVRrylnLVLATGK----IGREGCGYGAItgqgngqggrEHGQKADQ 363
Cdd:PRK07860 473 -------------------LSA-----------AAR----LADATGArlawVPRRAGERGAL----------EAGALPTL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 364 LPGYRSIENEEDRAYVASVWGVkaSSLPGK-GVSAYEMMELIHRGEIKSLFVMGSNPV-VSNPNAglVEEGLNHLDFLVV 441
Cdd:PRK07860 509 LPGGRPVADPAARAEVAAAWGV--DELPAApGRDTAGILAAAAAGELGALLVGGVEPAdLPDPAA--ALAALDAAGFVVS 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 442 ADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPGeARHDWVILCAIADRLGRgeYFDFHEPEEIFSEL 521
Cdd:PRK07860 585 LELRHSAVTERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGV--DLGLPTVAAARAEL 661
|
.
gi 2254313745 522 R 522
Cdd:PRK07860 662 A 662
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
59-657 |
1.00e-27 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 119.75 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 59 RVCVKGMNAHQHAAHSQRLQYPL----IRSNGELIPCSWDEAIAVISDRFQAISERYGPDA-HAVYG----GGSLTNE-- 127
Cdd:PRK14990 102 RACLRGRSMRRRVYNPDRLKYPMkrvgARGEGKFERISWEEAYDIIATNMQRLIKEYGNESiYLNYGtgtlGGTMTRSwp 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 128 -TAYLLGKFARVALGtrYIDYNGRFCMSAAASAGSKTFG--IDRGLTfrlSDIPLADCIVLAGTNIAECQPT---LLPYF 201
Cdd:PRK14990 182 pGNTLVARLMNCCGG--YLNHYGDYSSAQIAEGLNYTYGgwADGNSP---SDIENSKLVVLFGNNPGETRMSgggVTYYL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 202 NQAKE-NGAKIIVIDPRRTATAA-IADMHLAIRPGTDAILADAMLKMIVDEGLLDEGFIQARTTGYEElKT--------- 270
Cdd:PRK14990 257 EQARQkSNARMIIIDPRYTDTGAgREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDE-KTlpasapkng 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 271 YLDSFDLSRAAD-----------LCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKIGREG 339
Cdd:PRK14990 336 HYKAYILGEGPDgvaktpewasqITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGING 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 340 cgygaitgqGNgQGGREHGQKadqLPGYR--SIENEEDRAYVASVW------GVKASSLPgKGVSAYEMMELihrgEIKS 411
Cdd:PRK14990 416 ---------GN-SGAREGSYS---LPFVRmpTLENPIQTSISMFMWtdaierGPEMTALR-DGVRGKDKLDV----PIKM 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 412 LFVMGSNPVVS-----NPNAGLVEEGlNHLDFLVVADMFMSETARFADLVLPVTSYMEN-----EGTLTNLEgRVLLRKA 481
Cdd:PRK14990 478 IWNYAGNCLINqhseiNRTHEILQDD-KKCELIVVIDCHMTSSAKYADILLPDCTASEQmdfalDASCGNMS-YVIFNDQ 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 482 ARQAPGEARHDWVILCAIADRLGRGEYF-DFHEPEEIFSELRLASKGGIADYfgITYDRLRReEGVY------------- 547
Cdd:PRK14990 556 VIKPRFECKTIYEMTSELAKRLGVEQQFtEGRTQEEWMRHLYAQSREAIPEL--PTFEEFRK-QGIFkkrdpqghhvayk 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 548 ------WPCPSEEESGTGLLFRQSFAH-------PDGKAVFSV---TPG-----NPwvgVSEEYPLILTNgrvlSHYLTG 606
Cdd:PRK14990 633 afredpQANPLTTPSGKIEIYSQALADiaatwelPEGDVIDPLpiyTPGfesyqDP---LNKQYPLQLTG----FHYKSR 705
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2254313745 607 VQ-TRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRI 657
Cdd:PRK14990 706 VHsTYGNVDVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKV 757
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
599-696 |
1.99e-24 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 98.16 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 599 VLSHYLTGVQTRrSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLFVPMHWG----G 674
Cdd:cd02775 1 LRDHFHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGhrggR 79
|
90 100
....*....|....*....|..
gi 2254313745 675 AQNVNHATRPELDPFCKMPGFK 696
Cdd:cd02775 80 GGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
20-503 |
2.92e-21 |
|
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: 97.02 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 20 CPFCSVQCK-MTVAVEENGIPGQHKArykvegipnlasegrvCVKGMNAHQHAAHsqRLQYPLIrsNGEliPCSWDEAIA 98
Cdd:cd02761 4 CPFCGLLCDdIEVEVEDNKITKVRNA----------------CRIGAAKFARYER--RITTPRI--DGK--PVSLEEAIE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 99 VISDRFQAiSERygPdahAVYGGGSLTNE---TAYLLGKfarvALGTrYIDYNGRFCMSAAASAGsktfgIDRGLTF-RL 174
Cdd:cd02761 62 KAAEILKE-AKR--P---LFYGLGTTVCEaqrAGIELAE----KLGA-IIDHAASVCHGPNLLAL-----QDSGWPTtTL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 175 SDIP-LADCIVLAGTNIAECQPTLL--------PYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLK 245
Cdd:cd02761 126 GEVKnRADVIVYWGTNPMHAHPRHMsrysvfprGFFREGGREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 246 MIVDEGLLDEGfiqarttgyeelktyldsfdlsraadLCGLNVELIREAAFSYAMADTGMVLTARGVEQQTDGHLAVRRY 325
Cdd:cd02761 206 LLRGAGLVPDE--------------------------VAGIPAETILELAERLKNAKFGVIFWGLGLLPSRGAHRNIEAA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 326 LNLVLATGKIGREGCgyGAITGQGNGQGgreHGQKADQLPGYrsieneedrayvasVWGVKASSLPGKGvSAYEMM--EL 403
Cdd:cd02761 260 IRLVKALNEYTKFAL--LPLRGHYNVRG---FNQVLTWLTGY--------------PFRVDFSRGYPRY-NPGEFTavDL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 404 IHRGEIKSLFVMGSNPVVSNPnaglvEEGLNHLDF--LVVADMFMSETARFADLVLPV-TSYMENEGTLTNLEGRVLLRK 480
Cdd:cd02761 320 LAEGEADALLIIASDPPAHFP-----QSAVKHLAEipVIVIDPPPTPTTRVADVVIPVaIPGIEAGGTAYRMDGVVVLPL 394
|
490 500
....*....|....*....|...
gi 2254313745 481 AARqaPGEARHDWVILCAIADRL 503
Cdd:cd02761 395 KAV--ETERLPDEEILKQLLEKV 415
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
18-473 |
4.72e-20 |
|
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: 94.90 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCKMTVAVEENgipgqhKARYkVEGIPNLA-SEGRVCVKGMNAHQHAAHSQRLQYPLIRS----NGELIPCS 92
Cdd:cd02763 2 TTCYMCACRCGIRVHLRDG------KVRY-IKGNPDHPlNKGVICAKGSSGIMKQYSPARLTKPLLRKgprgSGQFEEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 93 WDEAIAVISDRFQAISeRYGPDAHAVYGGgslTNETAYLLGKFARvALGTRYIDYNGRFCMSAAASAGSKTFGiDRGLTF 172
Cdd:cd02763 75 WEEAFSIATKRLKAAR-ATDPKKFAFFTG---RDQMQALTGWFAG-QFGTPNYAAHGGFCSVNMAAGGLYSIG-GSFWEF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 173 RLSDIPLADCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAILADAMLKMIVDEGL 252
Cdd:cd02763 149 GGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 253 LDEGFIQARTTGYEelktyLDSFDLSRAADLCGLNVELIREAAFSYAMA--DTGMVL----------------------- 307
Cdd:cd02763 229 IDWEFLKRYTNAAE-----LVDYTPEWVEKITGIPADTIRRIAKELGVTarDQPIELpiawtdvwgrkhekitgrpvsfh 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 308 TARGVEQQTDGHLAVRRYLNLVLATGKIGREG--------------CGYGAITGQGNGQGGREHG------QKADQLpgy 367
Cdd:cd02763 304 AMRGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhkppyprhippLPKPPKIPSADKPFTPLYGpplgwpASPDDL--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 368 rSIENEE-----DRAYV----ASVWGVKASSLPgkgvSAYemmelihRGE---IKSLFVMGSNPVV-SNPNAGLVEEGLN 434
Cdd:cd02763 381 -LVDEDGnplriDKAYSweypLAAHGCMQNVIT----NAW-------RGDpypIDTLMIYMANMAWnSSMNTPEVREMLT 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2254313745 435 HLD--------FLVVADMFMSETARFADLVLPVTSYMENEGTLTNLE 473
Cdd:cd02763 449 DKDasgnykipFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSLLD 495
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
54-531 |
5.38e-18 |
|
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: 88.55 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 54 LASEGRVCVKGMNAHQHAAHSQRLQYPLIR----SNGELIPCSWDEAIAVIS---DRFQA---------------ISER- 110
Cdd:cd02758 61 LKARATACARGNAGLQYLYDPYRVLQPLKRvgprGSGKWKPISWEQLIEEVVeggDLFGEghveglkairdldtpIDPDh 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 111 --YGPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFC---MSAAASAGSKTFGidrGLTFRLSDIPLADCIVL 185
Cdd:cd02758 141 pdLGPKANQLLYTFGRDEGRTPFIKRFANQAFGTVNFGGHGSYCglsYRAGNGALMNDLD---GYPHVKPDFDNAEFALF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 186 AGTNIAECQPtllPYFNQAK-------ENGAKIIVIDPRRTATAAIADMH---LAIRPGTDAILADAMLKMIVDEGLLDE 255
Cdd:cd02758 218 IGTSPAQAGN---PFKRQARrlaeartEGNFKYVVVDPVLPNTTSAAGENirwVPIKPGGDGALAMAMIRWIIENERYNA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 256 GF------------------------IQART-TGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTGMVLTAR 310
Cdd:cd02758 295 EYlsipskeaakaagepswtnathlvITVRVkSALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHH 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 311 GVEQQTDGHLAVRRYLNLVLATGKIGREGcgyGAITGQG----NGQGGR------------------EHGQKADQLPGYR 368
Cdd:cd02758 375 GGTMHSNGFYNAYAIRMLNALIGNLNWKG---GLLMSGGgfadNSAGPRydfkkffgevkpwgvpidRSKKAYEKTSEYK 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 369 S-IENEEDrAYVAsvwgvKASSLPGKGVSAYEMMELIHRG---EIKSLFVMGSNPVVSNPnaGL---VEEGLN---HLDF 438
Cdd:cd02758 452 RkVAAGEN-PYPA-----KRPWYPLTPELYTEVIASAAEGypyKLKALILWMANPVYGAP--GLvkqVEEKLKdpkKLPL 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 439 LVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQ----------APGEARHDWVILCAIADRLG---- 504
Cdd:cd02758 524 FIAIDAFINETSAYADYIVPDTTYYESWGFSTPWGGVPTKASTARWpviapltektANGHPVSMESFLIDLAKALGlpgf 603
|
570 580 590
....*....|....*....|....*....|....*....
gi 2254313745 505 --------RGEYFDFHEPEE----IFSELRLASKGGIAD 531
Cdd:cd02758 604 gpnaikdgQGNKFPLNRAEDyylrVAANIAYDGKAPVPD 642
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
18-554 |
2.30e-15 |
|
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: 80.01 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 18 TQCPFCSVQCK-MTVAVEEN---GIPGQHkarykvEGIPNLASEGRVCVKGMNAHQHAAHSQRLQYPLIRSNGE------ 87
Cdd:cd02760 2 TYCYNCVAGPDfMAVKVVDGvatEIEPNF------AAEDIHPARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKkgrned 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 88 --LIPCSWDEAIAVISDRFQAISERYGPD-------AHAVYGGGSLTNETAYLLGKFArvALGTryIDYN----GRFCMS 154
Cdd:cd02760 76 pgFVPISWDEALDLVAAKLRRVREKGLLDekglprlAATFGHGGTPAMYMGTFPAFLA--AWGP--IDFSfgsgQGVKCV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 155 AAASAGSKTFgiDRGLTFrLSDIPLADCIVLAGTNI-AECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRP 233
Cdd:cd02760 152 HSEHLYGEFW--HRAFTV-AADTPLANYVISFGSNVeASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 234 GTDAILADAMLKMIVDE---GLLDEGFIQARTTGyeelkTYL---DSFDLSRAADLCGLNVELIREAAFSYAMADTGMVL 307
Cdd:cd02760 229 KTDPAFMFAMIHVMVHEqglGKLDVPFLRDRTSS-----PYLvgpDGLYLRDAATGKPLVWDERSGRAVPFDTRGAVPAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 308 TAR------------GVEQQTDG------------HLA-----------------VRRYLNLVLATGKIGR--EGCGY-- 342
Cdd:cd02760 304 AGDfavdgavsvdadDETAIHQGvegttaftmlveHMRkytpewaesicdvpaatIRRIAREFLENASIGStiEVDGVtl 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 343 -----GAITGQG--NGQGGRE---------HGQKADQLPG------YRSIENEEDR------------------------ 376
Cdd:cd02760 384 pyrpvAVTLGKSvnNGWGAFEccwartllaTLVGALEVPGgtlgttVRLNRPHDDRlasvkpgedgfmaqgfnptdkehw 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 377 --------AYVASVWGVKASSLPGKG------------VSAYEMMELIHRGEIksLFVMGSNPVVSNPNAGLVEEGLNHL 436
Cdd:cd02760 464 vvkptgrnAHRTLVPIVGNSAWSQALgptqlawmflreVPLDWKFELPTLPDV--WFNYRTNPAISFWDTATLVDNIAKF 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 437 DFLVVADMFMSETARFADLVLPVTSYMENEGTLTN-----LEGR-----VLLRKAARQAPGEARHDWVILCAIADRLG-- 504
Cdd:cd02760 542 PFTVSFAYTEDETNWMADVLLPEATDLESLQMIKVggtkfVEQFwehrgVVLRQPAVEPQGEARDFTWISTELAKRTGll 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254313745 505 ----------------RGEYFDF-------HEPEEIFSELRLASKGGIADYFGITYDRLRREEGVY-WPCPSEE 554
Cdd:cd02760 622 adynaalnrgaggaplKGEGYDQsldesqeHDVEYIWDAICRASSASLSKGGEVHGLEWFKEHGFYtVPMSKEE 695
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
54-503 |
3.10e-14 |
|
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: 74.99 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 54 LASEGRVCVKGMNahqhaahSQRLQYPLIRSNGELIPCSWDEAIAVISDRFQAIseryGPDAHAVYGGGSLTNETAYLLG 133
Cdd:cd02773 38 ISDKTRFAYDGLK-------RQRLDKPYIRKNGKLKPATWEEALAAIAKALKGV----KPDEIAAIAGDLADVESMVALK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 134 KFARvALGTRYIDYNGRFCMSAAASAGSKTFGIdrgltfRLSDIPLADCIVLAGTNIA-ECqptllPYFN-----QAKEN 207
Cdd:cd02773 107 DLLN-KLGSENLACEQDGPDLPADLRSNYLFNT------TIAGIEEADAVLLVGTNPRfEA-----PVLNarirkAWLHG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 208 GAKIIVIDPRRTATAAIAdmHLairpGTD-AILADAmlkmivdeglldegfiqarttgyeelktyldsfdlsraadlcgl 286
Cdd:cd02773 175 GLKVGVIGPPVDLTYDYD--HL----GTDaKTLQDI-------------------------------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 287 nveLIREAAFSYAM--ADTGMVLTARGVEQQTDGhlavrrylNLVLATgkIGREGCGYGAITGQGNGqggrehgqkadql 364
Cdd:cd02773 205 ---ASGKHPFSKALkdAKKPMIIVGSGALARKDG--------AAILAA--VAKLAKKNGVVREGWNG------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 365 pgYRSIENeedraYVASVWGVKASSLPGKGvsayemmELIHRGEIKSLFVMGS---NPVVSNPNAGLVEEGLnHLDFlvv 441
Cdd:cd02773 259 --FNVLHR-----AASRVGALDLGFVPGAG-------AIRKSGPPKVLYLLGAdeiDITPIPKDAFVVYQGH-HGDR--- 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254313745 442 admfmseTARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARQAPGEARHDWVILCAIADRL 503
Cdd:cd02773 321 -------GAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
591-703 |
1.19e-13 |
|
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: 68.07 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 591 PLILTNGRVLSHylTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLFVPM 670
Cdd:cd02778 1 EFRLIYGKSPVH--THGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2254313745 671 ---HW--------GGAQNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd02778 79 gfgHWapalsrayGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVR 122
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
589-676 |
1.63e-13 |
|
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: 67.72 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 589 EYPLILTNG-RVLSHylTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLF 667
Cdd:cd02781 1 EYPLILTTGaRSYYY--FHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVR 78
|
....*....
gi 2254313745 668 VPMHWGGAQ 676
Cdd:cd02781 79 AEHGWWYPE 87
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
76-527 |
9.81e-13 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 71.63 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 76 RLQYPLIR---------SNGE------LIPCSWDEAIAVISDRFQAISERYGPDA-HAVYGG----GSLTNETAYLlgkf 135
Cdd:PRK15102 90 RIRYPMVRldwlrkrhkSDTSqrgdnrFVRVSWDEALDLFYEELERVQKTYGPSAlHTGQTGwqstGQFHSATGHM---- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 136 AR-VALGTRYIDYNGRFCMSAAAS-----AGSkTFGIDRGLTFRLSdIPLADCIVLAGTN-IAECQ-----PTLLP--YF 201
Cdd:PRK15102 166 QRaIGMHGNSVGTVGDYSTGAGQVilpyvLGS-TEVYEQGTSWPLI-LENSKTIVLWGSDpVKNLQvgwncETHESyaYL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 202 NQAKENGAK----IIVIDPRRTATAA-IADMHLAIRPGTDAILADAMLKMIVDEGLLDEGFIQARTTGYEELKTYL---- 272
Cdd:PRK15102 244 AQLKEKVAKgeinVISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPYLlgek 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 273 DSF--DLSRAADLCGLNVELIREAAFSYAMADTGMVLtarGVEQQTDGHLAVRRYLNLVLAT--GKIGREGCGY------ 342
Cdd:PRK15102 324 DGVpkTPEWAEKICGIDAETIRELARQMAKGRTQIIA---GWCIQRQQHGEQPYWMGAVLAAmlGQIGLPGGGIsyghhy 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 343 ---GAITGQGNGQGGREHGQKADQLPGYrsiENEEDRAYVASV----WgVKASSLPGKgvsayemmELIHRG------EI 409
Cdd:PRK15102 401 sgiGVPSSGGAIPGGFPGNLDTGQKPKH---DNSDYKGYSSTIpvarF-IDAILEPGK--------TINWNGkkvtlpPL 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 410 KSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYME-NE----GTLTNlEGRVLLRKAARq 484
Cdd:PRK15102 469 KMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFErNDidqyGSYSN-RGIIAMKKVVE- 546
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2254313745 485 aP-GEARHDWVILCAIADRLGRGEYF----DFHE-PEEIFSELRLASKG 527
Cdd:PRK15102 547 -PlFESRSDFDIFRELCRRFGREKEYtrgmDEMGwLKRLYQECKQQNKG 594
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
76-467 |
1.02e-12 |
|
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: 70.98 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 76 RLQYPLIRS-NGELIPCSWDEAIAVISDRFQAISeryGPDAHAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGrfcMS 154
Cdd:cd02764 99 RAQGPLRRGiDGAYVASDWADFDAKVAEQLKAVK---DGGKLAVLSGNVNSPTTEALIGDFLKKYPGAKHVVYDP---LS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 155 A--AASAGSKTFGIDRGLTFrlsDIPLADCIVLAGTNIAECQPTLLPYFNQ--------AKENGAKIIVIDPRRTATAAI 224
Cdd:cd02764 173 AedVNEAWQASFGKDVVPGY---DFDKAEVIVSIDADFLGSWISAIRHRHDfaakrrlgAEEPMSRLVAAESVYTLTGAN 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 225 ADMHLAIRPGTDAILADAMLKMIVDEGlldegfiqARTTGYEELKTYLDSFDLSRAADLCGLNVELIREAAFSYAMADTG 304
Cdd:cd02764 250 ADVRLAIRPSQEKAFALGLAHKLIKKG--------AGSSLPDFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAGKS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 305 MVLTargveqqtdghlavrrylnlvlatgkigregcgyGAITGQGNGQGGREHGQKADQLPGyrsieneedrAYVASVwG 384
Cdd:cd02764 322 LVVA----------------------------------GSELSQTAGADTQVAVNALNSLLG----------NDGKTV-D 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 385 VKASSLPGKGVSAYEMMELIHR---GEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTS 461
Cdd:cd02764 357 HARPIKGGELGNQQDLKALASRinaGKVSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSH 436
|
....*.
gi 2254313745 462 YMENEG 467
Cdd:cd02764 437 GLESWG 442
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
18-73 |
1.24e-10 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 57.30 E-value: 1.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254313745 18 TQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIPN-LASEGRVCVKGMNAHQHAAH 73
Cdd:pfam04879 6 TICPYCGVGCGLEVHVKDGKI-------VKVEGDPDhPVNEGRLCVKGRFGYERVYN 55
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
18-73 |
7.35e-09 |
|
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: 52.25 E-value: 7.35e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254313745 18 TQCPFCSVQCKMTVAVEENGIpgqhkarYKVEGIPNL-ASEGRVCVKGMNAHQHAAH 73
Cdd:smart00926 6 TVCPLCGVGCGLLVEVKDGRV-------VRVRGDPDHpVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
590-686 |
3.28e-08 |
|
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: 52.28 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 590 YPLILTNGRvlSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIR-----VD 664
Cdd:cd02786 1 YPLRLITPP--AHNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPpgvvvAE 78
|
90 100
....*....|....*....|..
gi 2254313745 665 TLFVPMHWGGAQNVNHATRPEL 686
Cdd:cd02786 79 GGWWREHSPDGRGVNALTSARL 100
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
590-673 |
8.88e-08 |
|
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: 51.91 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 590 YPLILTN--GRVLSHYLTGvqtrrSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLF 667
Cdd:cd02780 1 YPFILVTfkSNLNSHRSAN-----APWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVA 75
|
....*.
gi 2254313745 668 VPMHWG 673
Cdd:cd02780 76 IEHGYG 81
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
589-662 |
7.47e-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: 48.52 E-value: 7.47e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254313745 589 EYPLILTNGRVLshYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIR 662
Cdd:cd02785 1 KYPLACIQRHSR--FRVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQ 72
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
590-705 |
2.12e-06 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 47.07 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 590 YPLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLFVP 669
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFML 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2254313745 670 M-HWGGAqnVNHATRPELDPFCKMPGFKTAAVRIRSL 705
Cdd:cd02779 81 MaHPRPG--ANGLVTPYVDPETIIPYYKGTWANIRKI 115
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
589-703 |
1.40e-03 |
|
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: 39.30 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254313745 589 EYPLILTNGRvlsHYLTGVQT--RRSPSLLARELENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTL 666
Cdd:cd02782 1 DYPFLLLIGR---RHLRSNNSwlHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2254313745 667 FVPMHWG-GAQNVNHATRPE------------LDPFCKMPGFKTAAVRIR 703
Cdd:cd02782 78 SLPHGWGhDYPGVSGAGSRPgvnvndltddtqRDPLSGNAAHNGVPVRLA 127
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
621-668 |
1.64e-03 |
|
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239184 [Multi-domain] Cd Length: 156 Bit Score: 39.75 E-value: 1.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2254313745 621 ENFVEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLFV 668
Cdd:cd02783 31 RNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTETVEPGTVWT 78
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
624-672 |
1.92e-03 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 39.28 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2254313745 624 VEIHPITAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIRVDTLFVpMHW 672
Cdd:cd02776 33 VWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFM-YHA 80
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