|
Name |
Accession |
Description |
Interval |
E-value |
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
18-705 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 880.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEKSVpgrfrakYKVEGIPNL-ASEGRVCVKGMNAHQHAAHSQRLQHPLIRSNGELVPCSWDEA 96
Cdd:COG3383 9 TVCPYCGVGCGIDLEVKDGKI-------VKVEGDPDHpVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 97 MAVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKTFGIDrGLTFRLSD 176
Cdd:COG3383 82 LDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSD-APPNSYDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 177 IPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGLIDEG 256
Cdd:COG3383 161 IEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 257 FIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVG 336
Cdd:COG3383 241 FIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 337 REGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEEDRAYVASVWGVKAssLPGK-GVSAYEMMELIHEGEIKSLFVM 415
Cdd:COG3383 321 RPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPP--LPDKpGLTAVEMFDAIADGEIKALWII 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 416 GSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARPAPGEARHDWMI 495
Cdd:COG3383 399 GENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 496 LCSIADRLGKGeyFDFHEPEEIFNELRLASKggiaDYFGITYDRLRREEGVYWPCPSEEESGTGLLFRQSFAHPDGKAVF 575
Cdd:COG3383 479 IAELARRLGYG--FDYDSPEEVFDEIARLTP----DYSGISYERLEALGGVQWPCPSEDHPGTPRLFTGRFPTPDGKARF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 576 S-VTPGNPWVGVSEEYPLILTNGRLLSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVR 654
Cdd:COG3383 553 VpVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLR 632
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1915254118 655 SRIKEHIREDTLFVPMHWGGvQNVNHATRPELDPFCKMPGFKTAAVRIRSL 705
Cdd:COG3383 633 ARVTDRVRPGTVFMPFHWGE-GAANALTNDALDPVSKQPEYKACAVRVEKV 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: 726.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEKSVpgrfrakYKVEGIPNL-ASEGRVCVKGMNAHQHAAHSQRLQHPLIRSNG-ELVPCSWDE 95
Cdd:cd02754 2 TTCPYCGVGCGVEIGVKDGKV-------VAVRGDPEHpVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGgELVPVSWDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 96 AMAVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKTFGIDrGLTFRLS 175
Cdd:cd02754 75 ALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGAD-GPPGSYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 176 DIPLARCIVLAGTNIAECQPTLLPYFNQAKEN--GAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGLI 253
Cdd:cd02754 154 DIEHADCFFLIGSNMAECHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 254 DEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATG 333
Cdd:cd02754 234 DRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 334 KVGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEEDRAYVASVWGVKASSLPGK-GVSAYEMMELIHEGEIKSL 412
Cdd:cd02754 314 KIGRPGSGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVPEGTIPPKpGLHAVEMFEAIEDGEIKAL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 413 FVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMF-MSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARPAPGEARH 491
Cdd:cd02754 394 WVMCTNPAVSLPNANRVREALERLEFVVVQDAFaDTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 492 DWMILCSIADRLGKGEYFDFHEPEEIFNELRLASKGGIADYFGITYDRLRReEGVYWPCPSEEESGTGLLFR-QSFAHPD 570
Cdd:cd02754 474 DWWILADVARRLGFGELFPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEdGRFPTPD 552
|
570
....*....|..
gi 1915254118 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: 610.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEKSVpgrFRAKYKVEGIPNlasEGRVCVKGMNAHQHAAHSQRLQHPLIRSNGELVPCSWDEAM 97
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKI---VRVEPYQGHKAN---RGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSWDEAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 98 AVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKTFGIDRGlTFRLSDI 177
Cdd:TIGR01591 75 SYIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAM-SNTISEI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 178 PLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGLIDEGF 257
Cdd:TIGR01591 154 ENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 258 IQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGR 337
Cdd:TIGR01591 234 IEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 338 EGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEEDRAYVASVWGVkaSSLPGK-GVSAYEMMELIHEGEIKSLFVMG 416
Cdd:TIGR01591 314 PGGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGV--VKLPAEpGLRIPEMIDAAADGDVKALYIMG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 417 SNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARPAPGEARHDWMIL 496
Cdd:TIGR01591 392 EDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEII 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 497 CSIADRLGKGeyFDFHEPEEIFNELRLASKggiaDYFGITYDRLRREEGVYWPCPSEEESGTGLLFRQSFAHPDGKAVF- 575
Cdd:TIGR01591 472 QELANALGLD--WNYNHPQEIMDEIRELTP----LFAGLTYERLDELGSLQWPCNDSDASPTSYLYKDKFATPDGKAKFi 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 576 SVTPGNPWVGVSEEYPLILTNGRLLSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRS 655
Cdd:TIGR01591 546 PLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRA 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1915254118 656 RIKEHIREDTLFVPMHWGGVQnVNHATRPELDPFCKMPGFKTAAVRI 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: 582.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVE-EEEKSVpgrfrakyKVEGIP-NLASEGRVCVKGMNAHQHAAHSQRLQHPLIR----SNGELVPC 91
Cdd:COG0243 26 TTCPGCGVGCGLGVKvEDGRVV--------RVRGDPdHPVNRGRLCAKGAALDERLYSPDRLTYPMKRvgprGSGKFERI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 92 SWDEAMAVISDRFQAISERYGPDANAVYGGGS----LTNETAYLLGKFARvALGTRYIDYNGRFCMSAAASAGSKTFGID 167
Cdd:COG0243 98 SWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGsagrLSNEAAYLAQRFAR-ALGTNNLDDNSRLCHESAVAGLPRTFGSD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 168 RGlTFRLSDIPLARCIVLAGTNIAECQPTLLPYFNQA-KENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKM 246
Cdd:COG0243 177 KG-TVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 247 IVDEGLIDEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYL 326
Cdd:COG0243 256 LIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 327 NLVLATGKVGREGCGYGAITGqgngqggrehgqkadqlpgyrsieneedrayvasvwgvkasslpgkgvsayEMMELIHE 406
Cdd:COG0243 336 NLALLTGNIGKPGGGPFSLTG---------------------------------------------------EAILDGKP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 407 GEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLE-GRVLLRKAARPA 485
Cdd:COG0243 365 YPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 486 PGEARHDWMILCSIADRLGKGEYFDFHE-PEEIFNELRLASKGGiadyfGITYDRLRREEGVYWPCPSEEesgtglLFRQ 564
Cdd:COG0243 445 PGEARSDWEIFAELAKRLGFEEAFPWGRtEEDYLRELLEATRGR-----GITFEELREKGPVQLPVPPEP------AFRN 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 565 --SFAHPDGKAVFS------------VTPGNPWVGVSEEYPLILTNGRLLSHYLTgvQTRRSPSLLARELENFVEIHPII 630
Cdd:COG0243 514 dgPFPTPSGKAEFYsetlalpplpryAPPYEGAEPLDAEYPLRLITGRSRDQWHS--TTYNNPRLREIGPRPVVEINPED 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915254118 631 AQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFVPMHWG------GVQNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:COG0243 592 AAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWyepaddKGGNVNVLTPDATDPLSGTPAFKSVPVRVE 670
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
18-582 |
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 1915254118 18 TQCPFCSVQCKMTVEEEEKSVpgrFRAKYKVEGIPNlasEGRVCVKGMNAHQHAAHSQRLQHPLIRSNGELVPCSWDEAM 97
Cdd:cd02753 2 TVCPYCGVGCGLELWVKDNKI---VGVEPVKGHPVN---RGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 98 AVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKTFGIDRGlTFRLSDI 177
Cdd:cd02753 76 SLVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAM-TNSIADI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 178 PLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGLIDEGF 257
Cdd:cd02753 155 EEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 258 IQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGR 337
Cdd:cd02753 235 IEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 338 EGCGYGAITGQGNGQGGREHGQKADQLPGYrsieneedrayvasvwgvkasslpgkgvsayemmelihegeIKSLFVMGS 417
Cdd:cd02753 315 PGTGVNPLRGQNNVQGACDMGALPNVLPGY-----------------------------------------VKALYIMGE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 418 NPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRV-LLRKAARPaPGEARHDWMIL 496
Cdd:cd02753 354 NPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVqRVRKAVEP-PGEARPDWEII 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 497 CSIADRLGkGEYFDFHePEEIFNELRLASKggiaDYFGITYDRLRREEGVYWPCPSEEESGTGLLFRQSFAHPDGKAVFS 576
Cdd:cd02753 433 QELANRLG-YPGFYSH-PEEIFDEIARLTP----QYAGISYERLERPGGLQWPCPDEDHPGTPILHTERFATPDGKARFM 506
|
....*.
gi 1915254118 577 VTPGNP 582
Cdd:cd02753 507 PVEYRP 512
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
18-503 |
1.42e-112 |
|
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: 344.31 E-value: 1.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEksvpGRFRakyKVEGIPN-LASEGRVCVKGMNAHQHAAHSQRLQHPLIRSN--GELVPCSWD 94
Cdd:cd00368 2 SVCPFCGVGCGILVYVKD----GKVV---RIEGDPNhPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 95 EAMAVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGKFARvALGTRYIDYNGRFCMSAAAsAGSKTFGIDrGLTFRL 174
Cdd:cd00368 75 EALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLR-ALGSNNVDSHARLCHASAV-AALKAFGGG-APTNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 175 SDIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAmlkmivdeglid 254
Cdd:cd00368 152 ADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 255 egfiqarttgyeelktylgsfdlSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGK 334
Cdd:cd00368 220 -----------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 335 VGREGCGYGAitgqgngqggrehgqkadqlpgyrsieneedrayvasvwgvkasslpgkgvsayemmelihegeikslfv 414
Cdd:cd00368 277 IGRPGGGLGP---------------------------------------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 415 mGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARPAPGEARHDWM 494
Cdd:cd00368 287 -GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWE 365
|
....*....
gi 1915254118 495 ILCSIADRL 503
Cdd:cd00368 366 ILRELAKRL 374
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
20-572 |
7.37e-94 |
|
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: 300.32 E-value: 7.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 20 CPF-CSVQCKMTVEEEEksvpGRFRakyKVEGIP-NLASEGRVCVKGMNAHQHAAHSQRLQHPLIRSN---GELVPCSWD 94
Cdd:cd02766 4 CPLdCPDTCSLLVTVED----GRIV---RVEGDPaHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGrkgGQWERISWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 95 EAMAVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNgrFCMSAAASAGSKTFGIDRGLTfrL 174
Cdd:cd02766 77 EALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHALGASELRGT--ICSGAGIEAQKYDFGASLGND--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 175 SDIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGLID 254
Cdd:cd02766 153 EDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 255 EGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGK 334
Cdd:cd02766 233 RDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 335 VGREGCG--YGaitgqgngqggrehgqkadqlpgyrsieneedrayvasvwgvkasslpgkgvsayemmelIHEGEIKSL 412
Cdd:cd02766 313 IGVPGGGafYS------------------------------------------------------------NSGPPVKAL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 413 FVMGSNPVVSNPNAGLVEEGL-NHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGR-VLLRKAARPAPGEAR 490
Cdd:cd02766 333 WVYNSNPVAQAPDSNKVRKGLaREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYyLQYNEPAIPPPGEAR 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 491 HDWMILCSIADRLGKGEYFdFHEPEEIFneLRLASKGGIADYFGITYDRLRReegvYWPCPSEEEsgtgLLFRQSFAHPD 570
Cdd:cd02766 413 SNTEIFRELAKRLGFGEPP-FEESDEEW--LDQALDGTGLPLEGIDLERLLG----PRKAGFPLV----AWEDRGFPTPS 481
|
..
gi 1915254118 571 GK 572
Cdd:cd02766 482 GK 483
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
76-502 |
2.19e-80 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 260.02 E-value: 2.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 76 RLQHPLIR-SNGELVPCSWDEAMAVISDRFQAISERYGPDANAVYG--GGSLTNETAYLLGKFARVALG--TRYIDYNGR 150
Cdd:pfam00384 1 RLKYPMVRrGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGgsGGLTDVESLYALKKLLNRLGSknGNTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 151 FCMSAAASAGSkTFGIDRGLTFRLSDIPLARCIVLAGTNIAECQPTL-LPYFNQAKENGAKIIVIDPRRTATaaIADMHL 229
Cdd:pfam00384 81 LCTAAAAAFGS-DLRSNYLFNSSIADIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRLDLT--YADEHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 230 AIRPGTDAMLADAMLKMIVDEGLIDEGFiqarttgyeelktylgsfdlsraadlcgldvelireaavsyamADTGMVLTA 309
Cdd:pfam00384 158 GIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------APKPIIIVG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 310 RGVEQQTDGHLAVRRYLNLVLATGKVGREGCGYGAITgqgNGQG-GREHGQKADQLPgyrsieneedrayvasvwgvkas 388
Cdd:pfam00384 195 AGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGaASPVGALDLGLV----------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 389 slpgKGVSAYEMMELIHEGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFM-SETARFADLVLPVTSYMENEG 467
Cdd:pfam00384 249 ----PGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNG 324
|
410 420 430
....*....|....*....|....*....|....*
gi 1915254118 468 TLTNLEGRVLLRKAARPAPGEARHDWMILCSIADR 502
Cdd:pfam00384 325 TYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
18-496 |
8.81e-80 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 264.26 E-value: 8.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEKSVPgrfrakyKVEGIP-NLASEGRVCVKG--MNAHQHaaHSQRLQHPLIRSNGELVPCSWD 94
Cdd:cd02762 2 RACILCEANCGLVVTVEDGRVA-------SIRGDPdDPLSKGYICPKAaaLGDYQN--DPDRLRTPMRRRGGSFEEIDWD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 95 EAMAVISDRFQAISERYGPDANAVYGGGSLTNEtaYLLGKFARV---ALGTRyidynGRFcmsAAASAGSKT-------- 163
Cdd:cd02762 73 EAFDEIAERLRAIRARHGGDAVGVYGGNPQAHT--HAGGAYSPAllkALGTS-----NYF---SAATADQKPghfwsglm 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 164 FGidRGLTFRLSDIPLARCIVLAGTNIAECQ--PTLLPYF----NQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDA 237
Cdd:cd02762 143 FG--HPGLHPVPDIDRTDYLLILGANPLQSNgsLRTAPDRvlrlKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 238 MLADAMLKMIVDEGLIDEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTD 317
Cdd:cd02762 221 WLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 318 GHLAvrRYLN--LVLATGKVGREG---CGYGAITGQGN-GQGGREHGQKADQLPGYRSIENEedrayvasvwgvkassLP 391
Cdd:cd02762 301 GTLC--SWLVklLNLLTGNLDRPGgamFTTPALDLVGQtSGRTIGRGEWRSRVSGLPEIAGE----------------LP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 392 GKGVSayEMMELIHEGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMEN-EGTLT 470
Cdd:cd02762 363 VNVLA--EEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKpHATFF 440
|
490 500
....*....|....*....|....*....
gi 1915254118 471 NLE---GRVLLRKAARPAPGEARHDWMIL 496
Cdd:cd02762 441 NLEfprNAFRYRRPLFPPPPGTLPEWEIL 469
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
20-515 |
1.57e-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: 259.16 E-value: 1.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 20 CPFCSVQCKMTVE-EEEKSVpgrfrakyKVEGIPN-LASEGRVCVKGMNAHQHAAHSQRLQHPLIRSN----GELVPCSW 93
Cdd:cd02759 4 CPGCHSGCGVLVYvKDGKLV--------KVEGDPNhPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGergeNKWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 94 DEAMAVISDRFQAISERYGPDANAVY-GGGSLTNE-TAYLLGKFARVaLGTRYIDYNGRFCMSAAASAGSKTFGIdrGLT 171
Cdd:cd02759 76 DEALDEIAEKLAEIKAEYGPESIATAvGTGRGTMWqDSLFWIRFVRL-FGSPNLFLSGESCYWPRDMAHALTTGF--GLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 172 FRLSDIPLARCIVLAGTNIAECQPTLLPY-FNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDE 250
Cdd:cd02759 153 YDEPDWENPECIVLWGKNPLNSNLDLQGHwLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 251 GLIDEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVl 330
Cdd:cd02759 233 GLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILR- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 331 atgkvgregcgygAITGQGNGQGGrehgqkaDQLPGYRsieneedrayvasvwgvkasslpgkgvsayemmelihegeIK 410
Cdd:cd02759 312 -------------AITGNLDVPGG-------NLLIPYP----------------------------------------VK 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 411 SLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLR---KAARPApG 487
Cdd:cd02759 332 MLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAENFVQlrqKAVEPY-G 410
|
490 500 510
....*....|....*....|....*....|
gi 1915254118 488 EARHDWMILCSIADRLG--KGEYFDFHEPE 515
Cdd:cd02759 411 EAKSDYEIVLELGKRLGpeEAEYYKYEKGL 440
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
18-597 |
4.70e-71 |
|
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: 243.85 E-value: 4.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEksvpGRFrakYKVEGIP-NLASEGRVCVKGMNAHQHAAHSQRLQHPLIRSNG--ELVPCSWD 94
Cdd:cd02752 2 TICPYCSVGCGLIAYVQN----GVW---VHQEGDPdHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGsgKWEEISWD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 95 EAMAVISDRFQAISER------------YGPDANAVYGGGSLTNETAYLLGKFARvALGTRYIDYNGRFCMSAAASAGSK 162
Cdd:cd02752 75 EALDEIARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFAR-ALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 163 TFGidRG-LTFRLSDIPLARCIVLAGTNIAECQPTLLPYFNQAKE-NGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLA 240
Cdd:cd02752 154 TFG--RGaMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEkNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 241 DAMLKMIVdeglidegfiqarttgyeelktylgSFDLSRAADLCGLDVELIREAAVSYA---MAD-TGMVLTARGVEQQT 316
Cdd:cd02752 232 GGMINYII-------------------------RYTPEEVEDICGVPKEDFLKVAEMFAatgRPDkPGTILYAMGWTQHT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 317 DGHLAVRRYLNLVLATGKVGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSieneedrayvasvwgvkasslpgkgvs 396
Cdd:cd02752 287 VGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYLG--------------------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 397 ayemmelihegeikslfvmGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFAD-------------LVLPVTSYM 463
Cdd:cd02752 340 -------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQY 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 464 ENEGTLTNlEGRVL-LRKAARPAPGEARHDWMILCSIADRLG-----------------KGEYFDFHEPEEI-------- 517
Cdd:cd02752 401 EKEGSITN-SGRWLqWRYKVVEPPGEAKSDGDILVELAKRLGflyekeggafpepitkwNYGYGDEPTPEEIareingga 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 518 ----------------------FNELRLasKGGIADYFGItYDRLRREEGVYWPCPSEEESGTGLLFRQSFAHP------ 569
Cdd:cd02752 480 ltdgytgqsperlkahgqnvhtFDTLRD--DGSTACGCWI-YSGSYTEEGRMARRDTSDPDGLGLYPGWPWPWPvnrril 556
|
650 660 670
....*....|....*....|....*....|
gi 1915254118 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 |
3.18e-66 |
|
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: 228.73 E-value: 3.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 76 RLQHPLIRSNGE--LVPCSWDEAMAVISDRFQAISerygPDANAVYGGGSLTNETAYLLGKFARvALGTRYIDYNGRFCM 153
Cdd:cd02767 64 RLTYPMRYDAGSdhYRPISWDEAFAEIAARLRALD----PDRAAFYTSGRASNEAAYLYQLFAR-AYGTNNLPDCSNMCH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 154 SAAASAGSKTFGIDRGlTFRLSDIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRR--------------- 218
Cdd:cd02767 139 EPSSVGLKKSIGVGKG-TVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLRepglerfanpqnpes 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 219 --TATAAIADMHLAIRPGTDAMLADAMLKMIVDE-----GLIDEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELI 291
Cdd:cd02767 218 mlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 292 REAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGREGCGYGAITGQGNGQGGREHGqkADQLPGyrsie 371
Cdd:cd02767 298 EAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMG--ITEKPF----- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 372 nEEDRAYVASVWGVKASSLPGKGVSayEMMELIHEGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMS---- 447
Cdd:cd02767 371 -PEFLDALEEVFGFTPPRDPGLDTV--EAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNrshl 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 448 ---ETArfadLVLPVTS--------------YMENEGTLTNL-------EGRVLL------RKAARPAPGEARHDWMILC 497
Cdd:cd02767 448 vhgEEA----LILPCLGrteidmqaggaqavTVEDSMSMTHTsrgrlkpASRVLLseeaivAGIAGARLGEAKPEWEILV 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915254118 498 SIADRLGKgeyfdfhEPEEIFNElrlaskgGIADYfgitYDRLRREEGVYWPCPSEEesgtgllfRQsFAHPDGKAVF 575
Cdd:cd02767 524 EDYDRIRD-------EIAAVIYE-------GFADF----NQRGDQPGGFHLPNGARE--------RK-FNTPSGKAQF 574
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
59-547 |
1.69e-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: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 59 RVCVKGMNAHQHAAHSQRLQHPLIRSN----GELVPCSWDEAMAVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGK 134
Cdd:cd02770 42 RACLRGRSQRKRVYNPDRLKYPMKRVGkrgeGKFVRISWDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 135 FARV-ALGTRYIDYNGRFCMSAAASAGSKTFGIDrGLTFRLSDIPLARCIVLAGTNIAECQPTLLP---YFNQAKENGAK 210
Cdd:cd02770 122 IARLlNLTGGYLNYYGTYSWAQITTATPYTYGAA-ASGSSLDDLKDSKLVVLFGHNPAETRMGGGGstyYYLQAKKAGAK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 211 IIVIDPRRTATAA-IADMHLAIRPGTDAMLADAMLKMIVDEGLIDEGFIQARTTGYEE------------LKTY-LGSFD 276
Cdd:cd02770 201 FIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFDAehlpegappnesYKDYvLGTGY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 277 LSR------AADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGREGCGYGAitgqgn 350
Cdd:cd02770 281 DGTpktpewASEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGA------ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 351 gqggREHGQKAdQLPGYRSIENeedrayvasvwGVKASslpgkgVSAYEMMELIHEGE------------------IKSL 412
Cdd:cd02770 355 ----RPGGSAY-NGAGLPAGKN-----------PVKTS------IPCFMWTDAIERGEemtaddggvkgadklksnIKMI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 413 FVMGSNpVVSNPNAGLVEEGLNHLD------FLVVADMFMSETARFADLVLPVTSYMENEGTLT--NLEGRVLL---RKA 481
Cdd:cd02770 413 WNYAGN-TLINQHSDDNNTTRALLDdeskceFIVVIDNFMTPSARYADILLPDTTELEREDIVLtsNAGMMEYLiysQKA 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915254118 482 ARPApGEARHDWMILCSIADRLGKG-EYFDFHEPEEIFNElrLASKGGIADYFGITYDRLrREEGVY 547
Cdd:cd02770 492 IEPL-YECKSDYEICAELAKRLGVEdQFTEGKTEQEWLEE--LYGQTRAKEPGLPTYEEF-REKGIY 554
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
59-547 |
6.63e-60 |
|
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: 212.47 E-value: 6.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 59 RVCVKGMNAHQHAAHSQRLQHPLIR--------------SNGELVPCSWDEAMAVISDRFQAISERYGPDA--NAVYGG- 121
Cdd:cd02751 30 RPCPRGRSVRDRVYSPDRIKYPMKRvgwlgngpgsrelrGEGEFVRISWDEALDLVASELKRIREKYGNEAifGGSYGWa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 122 --GSLTNETAyLLGKFARVALGtrYIDYNGRFCMSAAASAGSKTFGIDRGL--TFRLSDIP-LARCIVLAGTNIAECQP- 195
Cdd:cd02751 110 saGRLHHAQS-LLHRFLNLIGG--YLGSYGTYSTGAAQVILPHVVGSDEVYeqGTSWDDIAeHSDLVVLFGANPLKTRQg 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 196 -------TLLPYFNQAKENGAKIIVIDPRRTATAA-IADMHLAIRPGTDAMLADAMLKMIVDEGLIDEGFIQARTTGYEE 267
Cdd:cd02751 187 ggggpdhGSYYYLKQAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 268 LKTYL-GSFD-----LSRAADLCGLDVELIREAAVSYAmADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGREGCG 341
Cdd:cd02751 267 FKDYLlGESDgvpktPEWAAEITGVPAETIRALAREIA-SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 342 YGAITGQGNGQGGREHGQKADQLP-GYRSIEneeDRAYVASVWgvKASSLPGKGVSAyeMMELIHEGEIKSLFVMGSNPV 420
Cdd:cd02751 346 FGFGYGYSNGGGPPRGGAGGPGLPqGKNPVK---DSIPVARIA--DALLNPGKEFTA--NGKLKTYPDIKMIYWAGGNPL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 421 VS-NPNAGLVEeGLNHLDFLVVADMFMSETARFADLVLPVTSYMENE--GTLTNLEGRVLL--RKAARPApGEARHDWMI 495
Cdd:cd02751 419 HHhQDLNRLIK-ALRKDETIVVHDIFWTASARYADIVLPATTSLERNdiGLTGNYSNRYLIamKQAVEPL-GEARSDYEI 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915254118 496 LCSIADRLGKGEYFDFHEPE-----EIFNELRLASKGGIADYfgITYDRLrREEGVY 547
Cdd:cd02751 497 FAELAKRLGVEEEFTEGRDEmewleHLYEETRAKAAGPGPEL--PSFEEF-WEKGIV 550
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
20-528 |
6.68e-59 |
|
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: 205.61 E-value: 6.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 20 CPFCSVQCKMTVEEEEKSVpgrfrakYKVEGIP-NLASEGRVCVKGMNAHQHAAHSQRLQHPLIRS----NGELVPCSWD 94
Cdd:cd02755 5 CEMCSSRCGILARVEDGRV-------VKIDGNPlSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVgergEGKFREASWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 95 EAMAVISDRFQAISERYGPDAnAVYGGGSLTNETayLLGKFARvALGTRYIDYNGRFCMSAAASAGSKTFGIDRGLTFRl 174
Cdd:cd02755 78 EALQYIASKLKEIKEQHGPES-VLFGGHGGCYSP--FFKHFAA-AFGSPNIFSHESTCLASKNLAWKLVIDSFGGEVNP- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 175 sDIPLARCIVLAGTNIAEC-QPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGLI 253
Cdd:cd02755 153 -DFENARYIILFGRNLAEAiIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 254 DEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIRE------AAVSYAMADTGMvltaRGVEQQTDghLAVRRYLN 327
Cdd:cd02755 232 DAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRiarefaAAAPHAVVDPGW----RGTFYSNS--FQTRRAIA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 328 LVLA-TGKVGREGcGygaitgqgngqggrehgqkadqlpgyrsieneedrayvasvWGVKASSLPGKgvsayemmelihe 406
Cdd:cd02755 306 IINAlLGNIDKRG-G-----------------------------------------LYYAGSAKPYP------------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 407 geIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEG---RVLLRKAAR 483
Cdd:cd02755 331 --IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGpapAVATRQRAI 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1915254118 484 PAPGEARHDWMILCSIADRLGKgeyfdFHEPE---EIFNeLRLASKGG 528
Cdd:cd02755 409 EPLYDTRPGWDILKELARRLGL-----FGTPSgkiELYS-PILAKAGY 450
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
20-702 |
1.05e-58 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 212.84 E-value: 1.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 20 CPFCSVQCKMTVEEEEksvpGRFRAkykVEGIPnlASE---GRVCVKG------MNAHQhaahsqRLQHPLIR------- 83
Cdd:PRK13532 47 CRFCGTGCGVLVGTKD----GRVVA---TQGDP--DAPvnrGLNCIKGyflskiMYGKD------RLTQPLLRmkdgkyd 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 84 SNGELVPCSWDEAMAVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCMSAAASAGSKT 163
Cdd:PRK13532 112 KEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMASAVVGFMRT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 164 FGIDR--GLtfrLSDIPLARCIVLAGTNIAECQPTLLPYFNQAK--ENGAKIIVIDPRRTATAAIADMHLAIRPGTDAML 239
Cdd:PRK13532 192 FGIDEpmGC---YDDIEAADAFVLWGSNMAEMHPILWSRVTDRRlsNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 240 ADAMLKMIVDEGLIDEGFIQARTT--------GY--------------------------EELKTYLGSFDLSRAADLCG 285
Cdd:PRK13532 269 LNYIANYIIQNNAVNWDFVNKHTNfrkgatdiGYglrpthplekaaknpgtagksepisfEEFKKFVAPYTLEKTAKMSG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 286 LDVELIREAAVSYAMADTGMV-LTARGVEQQTDGHLAVRRYLNLVLATGKVGREGCGYGAITGQGNGQG-GREHGQKADQ 363
Cdd:PRK13532 349 VPKEQLEQLAKLYADPNRKVVsFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 364 LPGYRSIENEEDRAYVASVWGVKASSLPGK-GVSAYEMMELIHEGEIKSLFVMGSNPVVSNPNAGlvEEGL----NHLDF 438
Cdd:PRK13532 429 LPADMVVTNPKHREIAEKIWKLPEGTIPPKpGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNIN--EERLpgwrNPDNF 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 439 LVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARPAPGEARHD-WMILcSIADRL------------GK 505
Cdd:PRK13532 507 IVVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV-EFSKRFkteevwpeellaKK 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 506 GEY-----FD----------FHEPEEIFNELRLAS--------KGGIADY--FG-------ITYDRLRREEGVYWPCPSE 553
Cdd:PRK13532 586 PEYrgktlYDvlfangqvdkFPLSELAEGYLNDEAkhfgfyvqKGLFEEYasFGrghghdlAPFDTYHKVRGLRWPVVDG 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 554 EES--------------GTGLLFrqsFAHPDGKAVFSVTPGNPWVGV-SEEYPLILTNGRLLSHYLTGVQTRRSPSLLAR 618
Cdd:PRK13532 666 KETlwryregydpyvkaGEGFKF---YGKPDGKAVIFALPYEPPAESpDEEYDLWLSTGRVLEHWHTGSMTRRVPELYRA 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 619 ELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRfsVRSRIKEHIR----EDTLFVPmhW-GGVQNVNHATRPELDPFCKMP 693
Cdd:PRK13532 743 FPEAVCFMHPEDAKARGLRRGDEVKVVSRRGE--VKSRVETRGRnkppRGLVFVP--FfDAAQLINKLTLDATDPLSKQT 818
|
....*....
gi 1915254118 694 GFKTAAVRI 702
Cdd:PRK13532 819 DFKKCAVKI 827
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
59-575 |
1.37e-54 |
|
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: 196.93 E-value: 1.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 59 RVCVKGMNAHQHAAHSQRLQHPLIR----SNGELVPCSWDEAMAVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGk 134
Cdd:cd02765 38 RGCTRGLSHLQRVYSPDRLKYPMKRvgerGEGKFERITWDEALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRL- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 135 faRVALGTRYIDYNGRFCMSAAASAGSKTFGIDRGLTFRLSDIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVI 214
Cdd:cd02765 117 --ALLGGGLQDALTYGIDTGVGQGFNRVTGGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 215 DPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGLIDEGFIQART-------------------------------- 262
Cdd:cd02765 195 DPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEAFLKSNTsapflvredngtllrqadvtatpaedgyvvwd 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 263 ------------------------------TGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGV 312
Cdd:cd02765 275 tnsdspepvaatninpalegeytingvkvhTVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 313 EQQTDGHLAVRRYLNLVLATGKVGREGCGygaitgqgngqggreHGQkadqlpgyrsieneedrayvasvwgvkasslpg 392
Cdd:cd02765 355 DRYYHSHVFGRTAAILAALTGNIGRVGGG---------------VGQ--------------------------------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 393 kgvsayemmelihegeIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNL 472
Cdd:cd02765 387 ----------------IKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRY 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 473 EGR--VLLRKAARPAPGEARHDWMILCSIADRLGKGEYFDfHEPEEIfneLRLASKGGIADYFGITYDRLrREEGVYWPC 550
Cdd:cd02765 451 TTHphVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFP-KTPEDY---VRAFMNSDDPALDGITWEAL-KEEGIIMRL 525
|
570 580
....*....|....*....|....*
gi 1915254118 551 PSEEESGTGLLfRQSFAHPDGKAVF 575
Cdd:cd02765 526 ATPEDPYVAYL-DQKFGTPSGKLEF 549
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
20-675 |
1.12e-52 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 194.89 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 20 CPFCSVQCKMTVE-EEEKSVpgrFrakykVEGIPNLAS-EGRVCVKGMNAHQHAAHSQRLQHPLIRS----NGELVPCSW 93
Cdd:PRK15488 48 CEMCSTRCPIEARvVNGKNV---F-----IQGNPKAKSfGTKVCARGGSGHSLLYDPQRIVKPLKRVgergEGKWQEISW 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 94 DEAMAVISDRFQAISERYGPDANAVyggGSLTNETAYLLGKFARvALGTRYIDYNGRFCMSAAASAGSKTFGIDRGLtfr 173
Cdd:PRK15488 120 DEAYQEIAAKLNAIKQQHGPESVAF---SSKSGSLSSHLFHLAT-AFGSPNTFTHASTCPAGYAIAAKVMFGGKLKR--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 174 lsDIPLARCIV------LAGTNIAECQPtllpYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMI 247
Cdd:PRK15488 193 --DLANSKYIInfghnlYEGINMSDTRG----LMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 248 VDEGLIDEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIRE------AAVSYAMADTGMVLTArgveqqTDGHLA 321
Cdd:PRK15488 267 IEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRiarelaAAAPHAIVDFGHRATF------TPEEFD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 322 VRRYL---NLVLatGKVGREG--------CGYGAITGQGNGQGGREHGQKADQLPGYRSIEN-EEDRAYVASVWGVkASS 389
Cdd:PRK15488 341 MRRAIfaaNVLL--GNIERKGglyfgknaSVYNKLAGEKVAPTLAKPGVKGMPKPTAKRIDLvGEQFKYIAAGGGV-VQS 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 390 LPGKGVSA--YemmelihegEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEG 467
Cdd:PRK15488 418 IIDATLTQkpY---------QIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDE 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 468 TLTNLEGRV---LLRKAARPAPGEARHDWMILCSIADRLGKGEYFdfhePEEIFNELRLASKGGIADyfgiTYDRLRREE 544
Cdd:PRK15488 489 EISDKSGKNpayALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYY----PWQDMETLQLYQVNGDHA----LLKELKKKG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 545 GVYWPCPseeesgtgLLFRQ---------------------------SFAHPDGK------AVFSVTPG------NPwVG 585
Cdd:PRK15488 561 YVSFGVP--------LLLREpkmvakfvarypnakavdedgtygsqlKFKTPSGKielfsaKLEALAPGygvpryRD-VA 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 586 VSEEYPLILTNGRLLSHylTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDT 665
Cdd:PRK15488 632 LKKEDELYFIQGKVAVH--TNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDT 709
|
730
....*....|
gi 1915254118 666 LFVPMHWGGV 675
Cdd:PRK15488 710 LFAYMGFGSK 719
|
|
| 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 ... |
20-528 |
1.83e-50 |
|
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: 182.97 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 20 CPFCSVQCKMTVEEEEksvpGRFRakyKVEGIPNLA-SEGRVCVKGMNAHQHAAHSQRLQHPLIRSNGELVPCSWDEAMA 98
Cdd:cd02771 4 CHHCSVGCNISLGERY----GELR---RVENRYNGAvNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEALD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 99 VISDRFQAISERYGpdanaVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRfcMSAAASAgsKTFGIDRGltfRLSDIP 178
Cdd:cd02771 77 VAAARLKEAKDKVG-----GIGSPRASNESNYALQKLVGAVLGTNNVDHRAR--RLIAEIL--RNGPIYIP---SLRDIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 179 LARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDeglIDEGFI 258
Cdd:cd02771 145 SADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDD---IAAESI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 259 QARTTGYEELKTYLGSFDLSRAADLCGLD-VELIREAAVSYAMAdtGMVLTARGVEQQTDGhlAVRRYLNLVLATGKVGr 337
Cdd:cd02771 222 RASPGGQARLGAALARAVDASAAGVSGLApKEKAARIAARLTGA--KKPLIVSGTLSGSLE--LIKAAANLAKALKRRG- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 338 EGCGYGAITGQGNgqggrehgqkadqLPGYRSIENEEDRAyvasvwgvkasslpgkGVSAYEMMELIHEGEIKSLFVMGS 417
Cdd:cd02771 297 ENAGLTLAVEEGN-------------SPGLLLLGGHVTEP----------------GLDLDGALAALEDGSADALIVLGN 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 418 NPVVSNPNAGlVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRV-LLRKAARPAPGEARHDWMIL 496
Cdd:cd02771 348 DLYRSAPERR-VEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAqRFFKAYDDPAGDARSDWRWL 426
|
490 500 510
....*....|....*....|....*....|...
gi 1915254118 497 CSIADRLGKGE-YFDFHEPEEIFNELRLASKGG 528
Cdd:cd02771 427 HALAAKLGGKLvPSDAAILDEIIALVPGKAPVG 459
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
588-703 |
1.91e-43 |
|
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: 152.28 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 588 EEYPLILTNGRLLSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLF 667
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVF 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1915254118 668 VPMHWGGV---QNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd00508 81 MPFHWGGEvsgGAANALTNDALDPVSGQPEFKACAVRIE 119
|
|
| 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 1915254118 75 QRLQHPLIRSNGELVPCSWDEAMAVISDRFQAISERYGPDANAV-----YGGGSLTNETAYLLGKFARVALGTRYIDYNG 149
Cdd:cd02756 116 TRLTTPLVRRGGQLQPTTWDDAIDLVARVIKGILDKDGNDDAVFasrfdHGGGGGGFENNWGVGKFFFMALQTPFVRIHN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 150 RFCMSAAASAGSktfgiDRG---LTFRLSDIPLARCIVLAGTNIAECQPT-----LLPYF--------NQAKENG----- 208
Cdd:cd02756 196 RPAYNSEVHATR-----EMGvgeLNNSYEDARLADTIVLWGNNPYETQTVyflnhWLPNLrgatvsekQQWFPPGepvpp 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 209 AKIIVIDPRRTATAAIAD--------MHLAIRPGTDAMLADAMLKMIVDeglidegfiqarttGYEELktylgsfdLSRA 280
Cdd:cd02756 271 GRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALANAIARYIYE--------------SLDEV--------LAEA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 281 ADLCGLDVELIREAAVSYAMADTG------MVLTARGVEQQTDGHLAVRRYLNLVLATGKVGREGCGYGAitgqgngQGG 354
Cdd:cd02756 329 EQITGVPRAQIEKAADWIAKPKEGgyrkrvMFEYEKGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCVR-------QGG 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 355 REHGQKADQLPGYRSIENEEDRAYVAsvwgvkasslpgkgvsayemmELIHEGEIKSLFVMGSNPVVSNPNAGLVEEGLN 434
Cdd:cd02756 402 HQEGYVRPPPPPPPWYPQYQYAPYID---------------------QLLISGKGKVLWVIGCDPYKTTPNAQRLRETIN 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 435 HLD----------------------------------FLVVADMFMSETARFADLVLPVTSYME-NEGTLTNLEGRVLLR 479
Cdd:cd02756 461 HRSklvtdaveaalyagtydreamvcligdaiqpgglFIVVQDIYPTKLAEDAHVILPAAANGEmNETSMNGHERRLRLY 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 480 KAARPAPGEARHDWMILCSIADRL-------GKGEY-------FDFHEPEEIFNE-LRLASKGGIADYF----------G 534
Cdd:cd02756 541 EKFMDPPGEAMPDWWIAAMIANRIyelyqeeGKGGSaqyqffgFIWKTEEDNFMDgSQEFADGGEFSEDyyvlgqeryeG 620
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915254118 535 ITYDRLRR--EEGVYWPCPSEEESGTGLL-FRQS---FAHPDGKAVFsvTPGNPWVGV 586
Cdd:cd02756 621 VTYNRLKAvgVNGIQLPVTTDTVTKILVTnVLRTegvFDTEDGKAYV--IDLAPWPGL 676
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
56-509 |
1.63e-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: 157.42 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 56 SEGRV---CV-KGMNAHQHAAHSQRlqhpliRSNGELVPCSWDEAMAVISDRFQAISERYGPDAnaVYGG-------GSL 124
Cdd:cd02769 43 SPTRIkypMVrRGWLEKGPGSDRSL------RGKEEFVRVSWDEALDLVAAELKRVRKTYGNEA--IFGGsygwssaGRF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 125 TNETAyLLGKFARVALGtrYIDYNGRFCMSAAASAGSKTFGIDRGLTFRLSDIPL----ARCIVLAGTNIAECQPT---- 196
Cdd:cd02769 115 HHAQS-LLHRFLNLAGG--YVGSVGDYSTGAAQVILPHVVGSMEVYTEQQTSWPViaehTELVVAFGADPLKNAQIawgg 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 197 -----LLPYFNQAKENGAKIIVIDPRRTATAAIADM-HLAIRPGTDAMLADAMLKMIVDEGLIDEGFIQARTTGYEELKT 270
Cdd:cd02769 192 ipdhqAYSYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 271 YL-GSFD-----LSRAADLCGLDVELIREAAVSYAMADTgMVLTARGVEQQTDGHLAVrrYLNLVLAT--GKVGREGCGY 342
Cdd:cd02769 272 YLlGESDgvpktPEWAAAICGIPAETIRELARRFASKRT-MIMAGWSLQRAHHGEQPH--WMAVTLAAmlGQIGLPGGGF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 343 GAITGQGNGQGGREHGQKADQLPgyrsieneEDRAYVASVWGVK--ASSL--PGKgvsayemmELIHEGE------IKSL 412
Cdd:cd02769 349 GFGYHYSNGGGPPRGAAPPPALP--------QGRNPVSSFIPVAriADMLlnPGK--------PFDYNGKkltypdIKLV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 413 FVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYME-NEGTLTNLEGRVL-LRKAARPApGEAR 490
Cdd:cd02769 413 YWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLErNDIGGSGDNRYIVaMKQVVEPV-GEAR 491
|
490
....*....|....*....
gi 1915254118 491 HDWMILCSIADRLGKGEYF 509
Cdd:cd02769 492 DDYDIFADLAERLGVEEQF 510
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
49-520 |
3.59e-39 |
|
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: 150.93 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 49 EGIPNLasEGRVCVKGMNAHQHAAHSQRLQHPLIRS----NGELVPCSWDEAMAVISDRFQAISERYGPDANAVYGGGSL 124
Cdd:cd02750 41 PDLPDY--NPRGCQRGASFSWYLYSPDRVKYPLKRVgargEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 125 TNETAYllgkfarvALGTRYIDYNGRFCMSAAA------SAGSKTFGiDRGLTFRLSDIPLARCIVLAGTNIAECQPTLL 198
Cdd:cd02750 119 MSMVSY--------AAGSRFASLIGGVSLSFYDwygdlpPGSPQTWG-EQTDVPESADWYNADYIIMWGSNVPVTRTPDA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 199 PYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGLIDEGFiqarttgyeeLKTY----LGS 274
Cdd:cd02750 190 HFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDY----------LKEYtdlpFLV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 275 FDLSRAADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGRegcgygaitgqgngqgg 354
Cdd:cd02750 260 YTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGK----------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 355 rehgqkadqlpgyrsieneedrayvasvwgvkasslPGKGVSAYemmelihEGEIKSLFVMGSNPVVSNPNAG-LVEEGL 433
Cdd:cd02750 323 ------------------------------------NGGGWAHY-------VGQPRVLFVWRGNLFGSSGKGHeYFEDAP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 434 N-HLDFLVVADMFMSETARFADLVLP-VTSYMENEGTLTNLEGRVLLRKAARPAPGEARHDWMILCSIADRL------GK 505
Cdd:cd02750 360 EgKLDLIVDLDFRMDSTALYSDIVLPaATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKVpwrtltGR 439
|
490
....*....|....*
gi 1915254118 506 GEYFDFHEPEEIFNE 520
Cdd:cd02750 440 QQFYLDHDWFLELGE 454
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
18-516 |
3.66e-37 |
|
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: 146.05 E-value: 3.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEksvpGRFRakyKVEGIPN-LASEGRVCVKGMNAHQHAAHSQRLQHPLIRSN--------GEL 88
Cdd:cd02757 4 STCQGCTAWCGLQAYVED----GRVT---KVEGNPLhPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNprkgrdvdPKF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 89 VPCSWDEAMAVISDRFQAISERYGPDANAV-YGGGSLTNETAYllGKFARvALGTRYIDYNGRFCMSAAASAGSKTfgiD 167
Cdd:cd02757 77 VPISWDEALDTIADKIRALRKENEPHKIMLhRGRYGHNNSILY--GRFTK-MIGSPNNISHSSVCAESEKFGRYYT---E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 168 RGLTFRLSDIPLARCIVLAGTNIAECQpTLLPYFNQ---AKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAML 244
Cdd:cd02757 151 GGWDYNSYDYANAKYILFFGADPLESN-RQNPHAQRiwgGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 245 KMIVDEGLIDEGFI----------QARTTGYE-----------------ELKTYLGSFdlsrAADLCGLDVELIREAAVS 297
Cdd:cd02757 230 HVILTEGLWDKDFVgdfvdgknyfKAGETVDEesfkeksteglvkwwnlELKDYTPEW----AAKISGIPAETIERVARE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 298 YAMADT-GMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGREGcgyGAITGQGNgqggrehgqkadqlpgyrsieneedr 376
Cdd:cd02757 306 FATAAPaAAAFTWRGATMQNRGSYNSMACHALNGLVGSIDSKG---GLCPNMGV-------------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 377 ayvasvwgvkasslpgkgvsayemmeliheGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLV 456
Cdd:cd02757 357 ------------------------------PKIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIV 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915254118 457 LPVTSYMENEGTL---TNLEGRVLLRKAARPAPGEARHDWMILCSIADRL-GKG-------EYFDFHEPEE 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 ... |
20-503 |
4.64e-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: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 20 CPFCSVQCKMTVEEEEKSVpgrFRAKYKVEGIPNlasEGRVCVKGMNAHQHAAHSQRLQHPLIRSNGELVPCSWDEAMAV 99
Cdd:cd02768 4 DVHDALGSNIRVDVRGGEV---MRILPRENEAIN---EEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEALKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 100 ISDRFQAISerygPDANAVYGGGSLTNETAYLLGKFARvALGTRYIDYNGRFcMSAAASAGSKTFGIdrgLTFRLSDIPL 179
Cdd:cd02768 78 VAEGLKAVK----GDKIGGIAGPRADLESLFLLKKLLN-KLGSNNIDHRLRQ-SDLPADNRLRGNYL---FNTSIAEIEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 180 ARCIVLAGTNIAECQPTLlpyfNQ-----AKENGAKIIVIDPrrTATAAIADmhlairpgtdamladamLKMIVDeglid 254
Cdd:cd02768 149 ADAVLLIGSNLRKEAPLL----NArlrkaVKKKGAKIAVIGP--KDTDLIAD-----------------LTYPVS----- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 255 egfiqarttgyeelktYLGsFDLSRAADLCGLDVelIREAAVSYAMADTGMVLTARGVeQQTDGHLAVRRYLNLVLATGK 334
Cdd:cd02768 201 ----------------PLG-ASLATLLDIAEGKH--LKPFAKSLKKAKKPLIILGSSA-LRKDGAAILKALANLAAKLGT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 335 VGREGCGYGAITGQGngqggrehgqkadqlpgyrsieneedrAYVAsvwgvkasslpgkGVSAYEMMELIHEGEIKSLFV 414
Cdd:cd02768 261 GAGLWNGLNVLNSVG---------------------------ARLG-------------GAGLDAGLALLEPGKAKLLLL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 415 MGSNPVVSNPNAGLVeegLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARPAPGEARHDWM 494
Cdd:cd02768 301 GEDELDRSNPPAAVA---LAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWK 377
|
....*....
gi 1915254118 495 ILCSIADRL 503
Cdd:cd02768 378 ILRALSNLL 386
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
588-703 |
1.73e-34 |
|
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: 126.97 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 588 EEYPLILTNGRLLSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLF 667
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVF 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1915254118 668 VPMHWgGVQNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd02790 81 MPFHF-AEAAANLLTNAALDPVAKIPEFKVCAVRVE 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 |
4.63e-33 |
|
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: 123.45 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 588 EEYPLILTNGRLLSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLF 667
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1915254118 668 VPMHWGGVQN----VNHATRPELDPFCKMPGFKTAAVRIR 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 |
1.29e-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: 119.25 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 588 EEYPLILTNGRLLSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLF 667
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1915254118 668 VPMHWGGV-----QNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd02792 81 IPYHWGGMglvigDSANTLTPYVGDPNTQTPEYKAFLVNIE 121
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
61-504 |
1.65e-29 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 125.06 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 61 CVKGMNAHQHAAHSQRLQHPLIR-SNGELVPCSWDEAMAVISDRFQAISERYGpdanaVYGGGSLTNETAYLLGKFARVA 139
Cdd:PRK07860 263 CDKGRWAFTYATQPDRITTPLVRdEDGELEPASWSEALAVAARGLAAARGRVG-----VLVGGRLTVEDAYAYAKFARVA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 140 LGTRYIDYNGRfcmsaAASAGSKTF------GIDRGLTFrlSDIPLARCIVLAGTNIAECQPTL-LPYFNQAKENGAKII 212
Cdd:PRK07860 338 LGTNDIDFRAR-----PHSAEEADFlaarvaGRGLGVTY--ADLEKAPAVLLVGFEPEEESPIVfLRLRKAARKHGLKVY 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 213 VIDPrrTATAAIADMH---LAIRPGTDAMLADAMLK--MIVDEGLIDEGfiqarttgyeelktylgsfdlsrAADLCGld 287
Cdd:PRK07860 411 SIAP--FATRGLEKMGgtlLRTAPGGEAAALDALATgaPDVAELLRTPG-----------------------AVILVG-- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 288 vEliREAAVSYAmadtgmvLTArgveqqtdghlAVRrylnLVLATGK----VGREGCGYGAItgqgngqggrEHGQKADQ 363
Cdd:PRK07860 464 -E--RLATVPGA-------LSA-----------AAR----LADATGArlawVPRRAGERGAL----------EAGALPTL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 364 LPGYRSIENEEDRAYVASVWGVkaSSLPGK-GVSAYEMMELIHEGEIKSLFVMGSNPV-VSNPNAglVEEGLNHLDFLVV 441
Cdd:PRK07860 509 LPGGRPVADPAARAEVAAAWGV--DELPAApGRDTAGILAAAAAGELGALLVGGVEPAdLPDPAA--ALAALDAAGFVVS 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915254118 442 ADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARPAPGeARHDWMILCSIADRLG 504
Cdd:PRK07860 585 LELRHSAVTERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMG 646
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
59-657 |
1.92e-29 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 125.14 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 59 RVCVKGMNAHQHAAHSQRLQHPL----IRSNGELVPCSWDEAMAVISDRFQAISERYGPDANAV-YG----GGSLTNE-- 127
Cdd:PRK14990 102 RACLRGRSMRRRVYNPDRLKYPMkrvgARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLnYGtgtlGGTMTRSwp 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 128 -TAYLLGKFARVALGtrYIDYNGRFCMSAAASAGSKTFG--IDRGLTfrlSDIPLARCIVLAGTNIAECQPT---LLPYF 201
Cdd:PRK14990 182 pGNTLVARLMNCCGG--YLNHYGDYSSAQIAEGLNYTYGgwADGNSP---SDIENSKLVVLFGNNPGETRMSgggVTYYL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 202 NQAKE-NGAKIIVIDPRRTATAA-IADMHLAIRPGTDAMLADAMLKMIVDEGLIDEGFIQARTTGYEE------------ 267
Cdd:PRK14990 257 EQARQkSNARMIIIDPRYTDTGAgREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEktlpasapkngh 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 268 LKTYL---GSFDLSR----AADLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGREGc 340
Cdd:PRK14990 337 YKAYIlgeGPDGVAKtpewASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGING- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 341 gygaitgqGNgQGGREHGQKadqLPGYR--SIENEEDRAYVASVW------GVKASSLPgKGVSAYEMMELihegEIKSL 412
Cdd:PRK14990 416 --------GN-SGAREGSYS---LPFVRmpTLENPIQTSISMFMWtdaierGPEMTALR-DGVRGKDKLDV----PIKMI 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 413 FVMGSNPVVS-----NPNAGLVEEGlNHLDFLVVADMFMSETARFADLVLPVTSYMEN-----EGTLTNLEGRVLLRKAA 482
Cdd:PRK14990 479 WNYAGNCLINqhseiNRTHEILQDD-KKCELIVVIDCHMTSSAKYADILLPDCTASEQmdfalDASCGNMSYVIFNDQVI 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 483 RPApGEARHDWMILCSIADRLGKGEYF-DFHEPEEIFNELRLASKGGIADYfgITYDRLRReEGVY-------------- 547
Cdd:PRK14990 558 KPR-FECKTIYEMTSELAKRLGVEQQFtEGRTQEEWMRHLYAQSREAIPEL--PTFEEFRK-QGIFkkrdpqghhvayka 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 548 -----WPCPSEEESGTGLLFRQSFAH-------PDGKAVFSV---TPG-----NPwvgVSEEYPLILTNgrllSHYLTGV 607
Cdd:PRK14990 634 fredpQANPLTTPSGKIEIYSQALADiaatwelPEGDVIDPLpiyTPGfesyqDP---LNKQYPLQLTG----FHYKSRV 706
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1915254118 608 Q-TRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRI 657
Cdd:PRK14990 707 HsTYGNVDVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKV 757
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
592-699 |
2.19e-29 |
|
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: 112.37 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 592 LILTNGRLLSHYLTGVQTRRSPSLLARElENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFVPMH 671
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPE-PEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|.
gi 1915254118 672 WGGV---QNVNHATRPELDPFCKMPGFKTAA 699
Cdd:pfam01568 80 WWYEprgGNANALTDDATDPLSGGPEFKTCA 110
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
396-521 |
3.46e-29 |
|
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: 121.49 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 396 SAYEMMELIHEGEIKSLFVMGSNPVVSNPNAglVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGR 475
Cdd:COG1034 320 DAAAILEAAEAGKLKALVLLGADPYDLDPAA--ALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGR 397
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1915254118 476 VLLRKAARPAPGEARHDWMILCSIADRLGKGeyFDFHEPEEIFNEL 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 |
2.78e-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: 117.84 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 67 AHQHAAHSQRLQHPLIRSNGELVPCSWDEAMAVISDRFQAISERYGPDANAVYGGGSLTNETAYLLGKFARvALGTRYID 146
Cdd:cd02772 45 SYEGLNSEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLAR-GLGSDNID 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 147 YNGRfcmSAAASAGSKtFGIDRGLTFRLSDIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDP---------R 217
Cdd:cd02772 124 HRLR---QSDFRDDAK-ASGAPWLGMPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPadddflfplS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 218 RTATAAIADMHlairpgtdAMLADAMLKMIVDEGLIDEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVS 297
Cdd:cd02772 200 GKAIVAPSALA--------NALAQVAKALAEEKGLAVPDEDAKVEASEEARKIAASLVSAERAAVFLGNLAQNHPQAATL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 298 YAMADTgmvltargVEQQTDGHLAvrrylnlVLATGkvgregcgygaitgqGNGQGGREHGqkadqlpgyrsieneedra 377
Cdd:cd02772 272 RALAQE--------IAKLTGATLG-------VLGEG---------------ANSVGAYLAG------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 378 yvasvwgvkasSLPGKGVSAYEMMELihegEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETAR-FADLV 456
Cdd:cd02772 303 -----------ALPHGGLNAAAMLEQ----PRKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALLdYADVL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1915254118 457 LPVTSYMENEGTLTNLEGRVLLRKAARPAPGEARHDWMIL 496
Cdd:cd02772 368 LPIAPFTETSGTFVNLEGRVQSFKGVVKPLGEARPAWKVL 407
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
90-702 |
2.93e-28 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 120.92 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 90 PCSWDEAMAVISDRFQAISErygPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGrFCMSAAASAGSKTFGIDRG 169
Cdd:PRK09939 124 PLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSN-MCHEPTSVGLAASIGVGKG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 170 lTFRLSDIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDP-------RRTA-----------TAAIADMHLAI 231
Cdd:PRK09939 200 -TVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApqnpfemltnsETQLASAYYNV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 232 RPGTDAMLADAMLKMIVDE----------GLIDEGFIQARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMA 301
Cdd:PRK09939 279 RIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 302 DTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGREGCGYGAITGQGNGQGgrehgqkaDQLPGYRSIENEEDRAYVAS 381
Cdd:PRK09939 359 ERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQG--------DRTVGITEKPSAEFLARLGE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 382 VWGVKASSLPGKgvSAYEMMELIHEGEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSE----TARFAdLVL 457
Cdd:PRK09939 431 RYGFTPPHAPGH--AAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRshllTARHS-YIL 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 458 PVTSY----MENEGT-LTNLEGRVLLRKAAR----PAPGEARHDWMILCSIADRLGKGEYFDFHEPEEIFNELRLASKGG 528
Cdd:PRK09939 508 PVLGRseidMQKSGAqAVTVEDSMSMIHASRgvlkPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAV 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 529 IADYFGITyDRLRREEGVYWPCPSEEesgtgllfrQSFAHPDGKAVFSVTPG---NPWVGVSEEypLILTNGRLLSHY-- 603
Cdd:PRK09939 588 LPEFADYN-QRIRHPGGFHLINAAAE---------RRWMTPSGKANFITSKGlleDPSSAFNSK--LVMATVRSHDQYnt 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 604 -LTGVQTRRSPSLLARELenfVEIHPIIAQRYRIRDGEWVEIV--SEHGRFSVRsrikehiREDTLFVPMHWGGVQNV-- 678
Cdd:PRK09939 656 tIYGMDDRYRGVFGQRDV---VFMSAKQAKICRVKNGERVNLIalTPDGKRSSR-------RMDRLKVVIYPMADRSLvt 725
|
650 660 670
....*....|....*....|....*....|
gi 1915254118 679 -----NHA-TRPELDPFCKMPGFKTAAVRI 702
Cdd:PRK09939 726 yfpesNHMlTLDNHDPLSGIPGYKSIPVEL 755
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
599-696 |
1.10e-23 |
|
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: 95.85 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 599 LLSHYLTGVQTRrSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFVPMHWGGV--- 675
Cdd:cd02775 1 LRDHFHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRggr 79
|
90 100
....*....|....*....|..
gi 1915254118 676 -QNVNHATRPELDPFCKMPGFK 696
Cdd:cd02775 80 gGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
18-473 |
2.74e-19 |
|
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: 92.59 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEKSVpgrfraKYkVEGIPNLA-SEGRVCVKGMNAHQHAAHSQRLQHPLIRS----NGELVPCS 92
Cdd:cd02763 2 TTCYMCACRCGIRVHLRDGKV------RY-IKGNPDHPlNKGVICAKGSSGIMKQYSPARLTKPLLRKgprgSGQFEEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 93 WDEAMAVISDRFQAISeRYGPDANAVYGGgslTNETAYLLGKFARvALGTRYIDYNGRFCMSAAASAGSKTFGiDRGLTF 172
Cdd:cd02763 75 WEEAFSIATKRLKAAR-ATDPKKFAFFTG---RDQMQALTGWFAG-QFGTPNYAAHGGFCSVNMAAGGLYSIG-GSFWEF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 173 RLSDIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLKMIVDEGL 252
Cdd:cd02763 149 GGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 253 IDEGFIQARTTGYEelktyLGSFDLSRAADLCGLDVELIREAAVSYAMA--DTGMVL----------------------- 307
Cdd:cd02763 229 IDWEFLKRYTNAAE-----LVDYTPEWVEKITGIPADTIRRIAKELGVTarDQPIELpiawtdvwgrkhekitgrpvsfh 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 308 TARGVEQQTDGHLAVRRYLNLVLATGKVGREG--------------CGYGAITGQGNGQGGREHG------QKADQLpgy 367
Cdd:cd02763 304 AMRGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhkppyprhippLPKPPKIPSADKPFTPLYGpplgwpASPDDL--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 368 rSIENEE-----DRAYV----ASVWGVKASSLPgkgvSAYemmelihEGE---IKSLFVMGSNPVV-SNPNAGLVEEGLN 434
Cdd:cd02763 381 -LVDEDGnplriDKAYSweypLAAHGCMQNVIT----NAW-------RGDpypIDTLMIYMANMAWnSSMNTPEVREMLT 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1915254118 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 ... |
54-524 |
3.15e-19 |
|
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: 92.41 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 54 LASEGRVCVKGMNAHQHAAHSQRLQHPLIR----SNGELVPCSWDeamavisdrfQAISE-------------------- 109
Cdd:cd02758 61 LKARATACARGNAGLQYLYDPYRVLQPLKRvgprGSGKWKPISWE----------QLIEEvveggdlfgeghveglkair 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 110 -----------RYGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFC---MSAAASAGSKTFGidrGLTFRLS 175
Cdd:cd02758 131 dldtpidpdhpDLGPKANQLLYTFGRDEGRTPFIKRFANQAFGTVNFGGHGSYCglsYRAGNGALMNDLD---GYPHVKP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 176 DIPLARCIVLAGTNIAECQPtllPYFNQAK-------ENGAKIIVIDPRRTATAAIADMH---LAIRPGTDAMLADAMLK 245
Cdd:cd02758 208 DFDNAEFALFIGTSPAQAGN---PFKRQARrlaeartEGNFKYVVVDPVLPNTTSAAGENirwVPIKPGGDGALAMAMIR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 246 MIVDEGLIDEGF------------------------IQART-TGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAM 300
Cdd:cd02758 285 WIIENERYNAEYlsipskeaakaagepswtnathlvITVRVkSALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 301 ADTGMVLTARGVEQQTDGHLAVRRYLNLVLATGKVGREGcgyGAITGQG----NGQGGR------------------EHG 358
Cdd:cd02758 365 HGRAAAVVHHGGTMHSNGFYNAYAIRMLNALIGNLNWKG---GLLMSGGgfadNSAGPRydfkkffgevkpwgvpidRSK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 359 QKADQLPGYRS-IENEEDrAYVAsvwgvKASSLPGKGVSAYEMMELIHEG---EIKSLFVMGSNPVVSNPnaGL---VEE 431
Cdd:cd02758 442 KAYEKTSEYKRkVAAGEN-PYPA-----KRPWYPLTPELYTEVIASAAEGypyKLKALILWMANPVYGAP--GLvkqVEE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 432 GLN---HLDFLVVADMFMSETARFADLVLPVTSYMENEGTLTNLEGRVLLRKAAR------PAP----GEARHDWMILCS 498
Cdd:cd02758 514 KLKdpkKLPLFIAIDAFINETSAYADYIVPDTTYYESWGFSTPWGGVPTKASTARwpviapLTEktanGHPVSMESFLID 593
|
570 580 590
....*....|....*....|....*....|....*...
gi 1915254118 499 IADRLG------------KGEYFDFHEPEEIFneLRLA 524
Cdd:cd02758 594 LAKALGlpgfgpnaikdgQGNKFPLNRAEDYY--LRVA 629
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
20-485 |
1.88e-18 |
|
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: 88.16 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 20 CPFCSVQCK-MTVEEEEKSVPGRFRAkykvegipnlasegrvCVKGMNAHQHAAHsqRLQHPLIRSngelVPCSWDEAMA 98
Cdd:cd02761 4 CPFCGLLCDdIEVEVEDNKITKVRNA----------------CRIGAAKFARYER--RITTPRIDG----KPVSLEEAIE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 99 VISDRFQAiSERygPdanAVYGGGSLTNE---TAYLLGKfarvALGTrYIDYNGRFCMSAAASAGsktfgIDRGLTF-RL 174
Cdd:cd02761 62 KAAEILKE-AKR--P---LFYGLGTTVCEaqrAGIELAE----KLGA-IIDHAASVCHGPNLLAL-----QDSGWPTtTL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 175 SDIP-LARCIVLAGTNIAECQPTLL--------PYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDAMLADAMLK 245
Cdd:cd02761 126 GEVKnRADVIVYWGTNPMHAHPRHMsrysvfprGFFREGGREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 246 MIVDEGLIDEGfiqarttgyeelktylgsfdlsraadLCGLDVELIREAAVSYAMADTGMVLTARGVEQQTDGHLAVRRY 325
Cdd:cd02761 206 LLRGAGLVPDE--------------------------VAGIPAETILELAERLKNAKFGVIFWGLGLLPSRGAHRNIEAA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 326 LNLVLATGKVGREGCgyGAITGQGNGQGgreHGQKADQLPGYrsieneedrayvasVWGVKASSLPGKGvSAYEMM--EL 403
Cdd:cd02761 260 IRLVKALNEYTKFAL--LPLRGHYNVRG---FNQVLTWLTGY--------------PFRVDFSRGYPRY-NPGEFTavDL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 404 IHEGEIKSLFVMGSNPVVSNPnaglvEEGLNHLDF--LVVADMFMSETARFADLVLPV-TSYMENEGTLTNLEG-RVLLR 479
Cdd:cd02761 320 LAEGEADALLIIASDPPAHFP-----QSAVKHLAEipVIVIDPPPTPTTRVADVVIPVaIPGIEAGGTAYRMDGvVVLPL 394
|
....*.
gi 1915254118 480 KAARPA 485
Cdd:cd02761 395 KAVETE 400
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
18-554 |
2.00e-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: 80.40 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 18 TQCPFCSVQCKMTVEEEEKSVPGRFRAKYKVEGIPnlASEGRVCVKGMNAHQHAAHSQRLQHPLIRSNGE--------LV 89
Cdd:cd02760 2 TYCYNCVAGPDFMAVKVVDGVATEIEPNFAAEDIH--PARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKkgrnedpgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 90 PCSWDEAMAVISDRFQAISERYGPD-------ANAVYGGGSLTNETAYLLGKFArvALGTryIDYN----GRFCMSAAAS 158
Cdd:cd02760 80 PISWDEALDLVAAKLRRVREKGLLDekglprlAATFGHGGTPAMYMGTFPAFLA--AWGP--IDFSfgsgQGVKCVHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 159 AGSKTFgiDRGLTFrLSDIPLARCIVLAGTNI-AECQPTLLPYFNQAKENGAKIIVIDPRRTATAAIADMHLAIRPGTDA 237
Cdd:cd02760 156 LYGEFW--HRAFTV-AADTPLANYVISFGSNVeASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 238 MLADAMLKMIVDE---GLIDEGFIQARTTGYEEL---KTYL-------------------------------GSFDLSRA 280
Cdd:cd02760 233 AFMFAMIHVMVHEqglGKLDVPFLRDRTSSPYLVgpdGLYLrdaatgkplvwdersgravpfdtrgavpavaGDFAVDGA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 281 ADLCGLDVELIREAA---VSYAMADTGM---------------VLTARGVEQQ------------TDGHLAVRRYLNLVL 330
Cdd:cd02760 313 VSVDADDETAIHQGVegtTAFTMLVEHMrkytpewaesicdvpAATIRRIAREflenasigstieVDGVTLPYRPVAVTL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 331 ATGKVGREGCGY------------GAITGQGN--GQGGREHGQKADQL----------------PGYRS--IENEEDR-A 377
Cdd:cd02760 393 GKSVNNGWGAFEccwartllatlvGALEVPGGtlGTTVRLNRPHDDRLasvkpgedgfmaqgfnPTDKEhwVVKPTGRnA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 378 YVASVWGVKASSLPGKG------------VSAYEMMELIHEGEIksLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMF 445
Cdd:cd02760 473 HRTLVPIVGNSAWSQALgptqlawmflreVPLDWKFELPTLPDV--WFNYRTNPAISFWDTATLVDNIAKFPFTVSFAYT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 446 MSETARFADLVLPVTSYMENEGTLTN-----LEGR-----VLLRKAARPAPGEARHDWMILCSIADRLG----------- 504
Cdd:cd02760 551 EDETNWMADVLLPEATDLESLQMIKVggtkfVEQFwehrgVVLRQPAVEPQGEARDFTWISTELAKRTGlladynaalnr 630
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915254118 505 -------KGEYFDF-------HEPEEIFNELRLASKGGIADYFGITYDRLRREEGVY-WPCPSEE 554
Cdd:cd02760 631 gaggaplKGEGYDQsldesqeHDVEYIWDAICRASSASLSKGGEVHGLEWFKEHGFYtVPMSKEE 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 |
2.63e-15 |
|
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: 78.08 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 54 LASEGRVCVKGMNahqhaahSQRLQHPLIRSNGELVPCSWDEAMAVISDRFQAIseryGPDANAVYGGGSLTNETAYLLG 133
Cdd:cd02773 38 ISDKTRFAYDGLK-------RQRLDKPYIRKNGKLKPATWEEALAAIAKALKGV----KPDEIAAIAGDLADVESMVALK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 134 KFARvALGTRYIDYNGRFCMSAAASAGSKTFGIdrgltfRLSDIPLARCIVLAGTNIA-ECqptllPYFN-----QAKEN 207
Cdd:cd02773 107 DLLN-KLGSENLACEQDGPDLPADLRSNYLFNT------TIAGIEEADAVLLVGTNPRfEA-----PVLNarirkAWLHG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 208 GAKIIVIDPRRTATAAIAdmHLairpGTDAmladAMLKMIVdEGLIDegFIQArttgyeeLKTylgsfdlsraadlcgld 287
Cdd:cd02773 175 GLKVGVIGPPVDLTYDYD--HL----GTDA----KTLQDIA-SGKHP--FSKA-------LKD----------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 288 velireaavsyamADTGMVLTARGVEQQTDGhlavrrylNLVLATgkVGREGCGYGAITGQGNGqggrehgqkadqlpgY 367
Cdd:cd02773 218 -------------AKKPMIIVGSGALARKDG--------AAILAA--VAKLAKKNGVVREGWNG---------------F 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 368 RSIENeedraYVASVWGVKASSLPGKGvsayemmELIHEGEIKSLFVMGS---NPVVSNPNAGLVEEGLnHLDFlvvadm 444
Cdd:cd02773 260 NVLHR-----AASRVGALDLGFVPGAG-------AIRKSGPPKVLYLLGAdeiDITPIPKDAFVVYQGH-HGDR------ 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915254118 445 fmseTARFADLVLPVTSYMENEGTLTNLEGRVLLRKAARPAPGEARHDWMILCSIADRL 503
Cdd:cd02773 321 ----GAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
200-527 |
4.75e-14 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 75.86 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 200 YFNQAKENGAK----IIVIDPRRTATAA-IADMHLAIRPGTDAMLADAMLKMIVDEGLIDEGFIQARTTGYEELKTYL-G 273
Cdd:PRK15102 242 YLAQLKEKVAKgeinVISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPYLlG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 274 SFD-----LSRAADLCGLDVELIREAAVSYAMADTGMVLtarGVEQQTDGHLAVRRYLNLVLAT--GKVGREGCGY---- 342
Cdd:PRK15102 322 EKDgvpktPEWAEKICGIDAETIRELARQMAKGRTQIIA---GWCIQRQQHGEQPYWMGAVLAAmlGQIGLPGGGIsygh 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 343 -----GAITGQGNGQGGREHGQKADQLPGYrsiENEEDRAYVASV----WgVKASSLPGKgvsayemmELIHEG------ 407
Cdd:PRK15102 399 hysgiGVPSSGGAIPGGFPGNLDTGQKPKH---DNSDYKGYSSTIpvarF-IDAILEPGK--------TINWNGkkvtlp 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 408 EIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTSYME-NE----GTLTNlEGRVLLRKAA 482
Cdd:PRK15102 467 PLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFErNDidqyGSYSN-RGIIAMKKVV 545
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1915254118 483 RPApGEARHDWMILCSIADRLGKGEYF----DFHE-PEEIFNELRLASKG 527
Cdd:PRK15102 546 EPL-FESRSDFDIFRELCRRFGREKEYtrgmDEMGwLKRLYQECKQQNKG 594
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
76-467 |
1.60e-13 |
|
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: 73.68 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 76 RLQHPLIRS-NGELVPCSWDEAMAVISDRFQAISeryGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGrfcMS 154
Cdd:cd02764 99 RAQGPLRRGiDGAYVASDWADFDAKVAEQLKAVK---DGGKLAVLSGNVNSPTTEALIGDFLKKYPGAKHVVYDP---LS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 155 A--AASAGSKTFGIDRGLTFrlsDIPLARCIVLAGTNIAECQPTLLPYFNQ--------AKENGAKIIVIDPRRTATAAI 224
Cdd:cd02764 173 AedVNEAWQASFGKDVVPGY---DFDKAEVIVSIDADFLGSWISAIRHRHDfaakrrlgAEEPMSRLVAAESVYTLTGAN 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 225 ADMHLAIRPGTDAMLADAMLKMIVDEGlidegfiqARTTGYEELKTYLGSFDLSRAADLCGLDVELIREAAVSYAMADTG 304
Cdd:cd02764 250 ADVRLAIRPSQEKAFALGLAHKLIKKG--------AGSSLPDFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAGKS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 305 MVLTargveqqtdghlavrrylnlvlatgkvgregcgyGAITGQGNGQGGREHGQKADQLPGyrsieneedrAYVASVwG 384
Cdd:cd02764 322 LVVA----------------------------------GSELSQTAGADTQVAVNALNSLLG----------NDGKTV-D 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 385 VKASSLPGKGVSAYEMMELIHE---GEIKSLFVMGSNPVVSNPNAGLVEEGLNHLDFLVVADMFMSETARFADLVLPVTS 461
Cdd:cd02764 357 HARPIKGGELGNQQDLKALASRinaGKVSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSH 436
|
....*.
gi 1915254118 462 YMENEG 467
Cdd:cd02764 437 GLESWG 442
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
589-676 |
3.06e-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: 66.95 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 589 EYPLILTNGRLlSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFV 668
Cdd:cd02781 1 EYPLILTTGAR-SYYYFHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRA 79
|
....*....
gi 1915254118 669 PM-HWGGVQ 676
Cdd:cd02781 80 EHgWWYPER 88
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
591-703 |
3.08e-12 |
|
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: 63.83 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 591 PLILTNGRLLSHylTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFVPM 670
Cdd:cd02778 1 EFRLIYGKSPVH--THGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1915254118 671 ---HW--------GGVQNVNHATRPELDPFCKMPGFKTAAVRIR 703
Cdd:cd02778 79 gfgHWapalsrayGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVR 122
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
18-73 |
2.06e-09 |
|
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: 53.84 E-value: 2.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915254118 18 TQCPFCSVQCKMTVEEEEksvpGRFRakyKVEGIPN-LASEGRVCVKGMNAHQHAAH 73
Cdd:pfam04879 6 TICPYCGVGCGLEVHVKD----GKIV---KVEGDPDhPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
590-673 |
1.66e-07 |
|
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: 51.14 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 590 YPLILTN--GRLLSHYLTGvqtrrSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLF 667
Cdd:cd02780 1 YPFILVTfkSNLNSHRSAN-----APWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVA 75
|
....*.
gi 1915254118 668 VPMHWG 673
Cdd:cd02780 76 IEHGYG 81
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
18-73 |
1.79e-07 |
|
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: 48.40 E-value: 1.79e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915254118 18 TQCPFCSVQCKMTVEEEEKSVpgrfrakYKVEGIPNL-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 |
1.93e-07 |
|
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: 49.97 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 590 YPLILTNGRllSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFVP 669
Cdd:cd02786 1 YPLRLITPP--AHNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAE 78
|
90 100
....*....|....*....|..
gi 1915254118 670 MHW-----GGVQNVNHATRPEL 686
Cdd:cd02786 79 GGWwrehsPDGRGVNALTSARL 100
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
589-688 |
2.78e-06 |
|
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: 46.98 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 589 EYPL--ILTNGRLLSHyltgVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTL 666
Cdd:cd02785 1 KYPLacIQRHSRFRVH----SQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVV 76
|
90 100
....*....|....*....|....*...
gi 1915254118 667 FVPMHW------GGvqNVNHATRPELDP 688
Cdd:cd02785 77 TAEQGWwsryfqEG--SLQDLTSPFVNP 102
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
590-705 |
3.31e-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: 46.68 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 590 YPLILTNGRLLSHYLTGVQTRRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFVP 669
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFML 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1915254118 670 M-HWGGvqNVNHATRPELDPFCKMPGFKTAAVRIRSL 705
Cdd:cd02779 81 MaHPRP--GANGLVTPYVDPETIIPYYKGTWANIRKI 115
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
621-668 |
3.81e-04 |
|
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: 41.68 E-value: 3.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1915254118 621 ENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFV 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 |
5.36e-04 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 40.82 E-value: 5.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1915254118 624 VEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTLFVpMHW 672
Cdd:cd02776 33 VWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFM-YHA 80
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
111-329 |
1.27e-03 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 42.29 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 111 YGPDANAVYGGGSLTNETAYLLGKFARVALGTRYIDYNGRFCmsaaasagsktfgidrGLTFR------LSDIPL----- 179
Cdd:PRK14991 217 YGPKANQLLVTNASDEGRDAFIKRFAFNSFGTRNFGNHGSYC----------------GLAYRagsgalMGDLDKnphvk 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 180 -----ARCIVLAGTNIAEC------QPTLLPyfNQAKENGAKIIVIDPRRTATA--AIADMH--LAIRPGTDAMLADAML 244
Cdd:PRK14991 281 pdwdnVEFALFIGTSPAQSgnpfkrQARQLA--NARTRGNFEYVVVAPALPLSSslAAGDNNrwLPIRPGTDSALAMGMI 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 245 KMIVDEGLIDEGFIQ------ARTTGY------------EELKTYLGSFdlSRAADLcgldvELIREAAVSYAMADTGMV 306
Cdd:PRK14991 359 RWIIDNQRYNADYLAqpgvaaMQAAGEaswtnathlviaDPGHPRYGQF--LRASDL-----GLPFEGEARGDGEDTLVV 431
|
250 260
....*....|....*....|....*..
gi 1915254118 307 LTARG----VEQQTDGHLAVRRYLNLV 329
Cdd:PRK14991 432 DAADGelvpATQAQPARLFVEQYVTLA 458
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
589-703 |
1.73e-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: 38.91 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915254118 589 EYPLILTNGRllsHYLTGVQT--RRSPSLLARELENFVEIHPIIAQRYRIRDGEWVEIVSEHGRFSVRSRIKEHIREDTL 666
Cdd:cd02782 1 DYPFLLLIGR---RHLRSNNSwlHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1915254118 667 FVPMHWG-------------GVqNVNHATRPE-LDPFCKMPGFKTAAVRIR 703
Cdd:cd02782 78 SLPHGWGhdypgvsgagsrpGV-NVNDLTDDTqRDPLSGNAAHNGVPVRLA 127
|
|
| |
