|
Name |
Accession |
Description |
Interval |
E-value |
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
12-1234 |
0e+00 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 2278.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 12 GPLTDQLIKFGKFFSRWDETDDGRAVFREGGRKGDAFYRDRWSHDKEVRSTHGVNCTGSCSWKVYVKDGIITWEAQETDY 91
Cdd:COG5013 2 GPASSHLLDRLRFFRRGEVFSDGHGVTTEGGREWEDFYRDRWQHDKVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 92 PTVGPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPYVRGLLLEMYREAKALYGDPVEAFHSIVSDPVKRNRYISARGKGGL 171
Cdd:COG5013 82 PRTGPDLPNYEPRGCPRGASFSWYTYSPTRVKYPYVRGVLLELWREARARHGDPVEAWASIVEDPEKRRRYKSARGKGGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 172 VRSTWAEALELVAAAHVHTIKYYGPDRCTGFTPIPAMSMVSFSAGVRFIQLIGGVMTSFYDWYADLPVASPQVFGDQTDV 251
Cdd:COG5013 162 VRATWDEANEIIAAANVYTIKKYGPDRVAGFSPIPAMSMVSYAAGARFLSLIGGVMLSFYDWYADLPPASPQVWGEQTDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 252 PESGDWWDASYLIMWGSNIPVTRTPDAHWVAEVRYRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKEN 331
Cdd:COG5013 242 PESADWYNSGYLIMWGSNVPQTRTPDAHFMTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 332 YVDQRVEFFEDFALTYTDLPFLVTLEtREDGTKVPSKFLTAASLAGEKHQ-ENAAFKTAMMDRETGEVFIPNGTMGHRYS 410
Cdd:COG5013 322 HVDRQVPYFTDYARRYTDLPFLVTLE-ERDGGYVPGRFLRASDLGGALGEsNNPEWKTVVLDEATGEPVVPNGSIGFRWG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 411 ESdQGNWNLELDGR-----KPILSIRDlpqGEAAAVEIKLPTFDNPKGHGDIITRGVPVSYVE----GQEVTTVFDLMLA 481
Cdd:COG5013 401 ES-EGKWNLELKDAtgadvDPALSLLD---DHDEVVEVAFPYFGGETGGGGVLRRGVPVRRVTladgEVLVTTVFDLMLA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 482 TYGIGRpGLPGEWASGYDDwSIQNTPAWQEQITSVPPEAVIRVAREFAQNAIDSHGRSMIIFGAGICQWYHADTTYRAIL 561
Cdd:COG5013 477 NYGVDR-GLPGNWPTGYDD-DVPYTPAWQEKITGVPREQVIRVAREFAQNAEKTRGRSMIIMGAGTNHWYHSDMIYRAIL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 562 ALLNLTGCQGRNGGGWAHYVGQEKARPLTGLTNMANALDWSRPPRHMIGTGFWYMHTDQFRQDGYSTDYLQSPLGKGELK 641
Cdd:COG5013 555 NLLMLCGCQGVNGGGWAHYVGQEKLRPQTGWQPLAFALDWSRPPRQMNGTSFFYAHTDQWRYETLSADELLSPLADGKFW 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 642 NVHTADVVARSTRMGWMPFYPQFPENSLDLADKAEEAvargeAKDNADYLAQRLNSGDLEFSVEDVDNPVNWPRTLMLWR 721
Cdd:COG5013 635 GGHLADYNVRAARLGWLPSYPQFNRNPLDLADEAEAA-----GMEPADYVVDQLKSGELKFACEDPDNPENFPRNLFVWR 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 722 SNLFGSSAKGESYFLKHLVGSMDNVQGADHEESI-PREVKWYQDAPQGKLDLLVSSDFRMTTTTLLSDVVFPTATWYEKY 800
Cdd:COG5013 710 SNLLGSSGKGHEYFLKHLLGTDNGVQGEELGPGLrPREVVWRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKH 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 801 DISSTDMHPFLHAFSPAIDPPWEAKTDHETFKALAYEFTRQAKKHLGTRKDIVSVPLLHDTPGQIKQPGGHAPDWKnNPD 880
Cdd:COG5013 790 DLSTTDMHPFIHPFSPAVDPPWEARSDWDIFKGIAKKFSELAAGHLGVRKDVVATPLQHDTPGELAQPFGDVKDWK-KGE 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 881 MVGVPGMNMPNFMTVERDYGAMYDMYTSVGPLFDKVGATTKYVTYDLKDEVAQMAKEFGVMDS-GKGAGRPALDTDVKIA 959
Cdd:COG5013 869 CEPIPGKTMPKLVVVERDYPAIYEKFTSLGPLLEKLGNGGKGITWDTEEEVEELGKLNGVVREeGVAKGRPRLDTDIDAA 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 960 ESILRISGTSNGEVALKGFKELEKQTGLHLVDLAEGNEERKITFPMTQASPQPVMTSPEWSGSETGGRRYAPFTVNIEKK 1039
Cdd:COG5013 949 EAILALSPETNGHVAVKAWKALEKRTGRDLAHLAAGREEEKIRFRDIQAQPRKVITSPTWSGSESGGRRYSAFTTNVEEL 1028
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1040 KPFHTLTGRMHFFLDHDWMHEMGEATPIYRPPLDMTGLFKEPEIGATDGVSVAVRYLTPHNKWAIHSQYFDNQHMLTLFR 1119
Cdd:COG5013 1029 IPWRTLTGRQHFYLDHDWMREFGEGLPVYRPPLDMKTLFGEPGIGPNGNPEIVLRYLTPHQKWGIHSTYQDNLLMLTLSR 1108
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1120 GGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVHHAQERMM-TPKTETTGKRGGIHNSMTRILL 1198
Cdd:COG5013 1109 GGPTVWMSEEDAAKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHAQERIVnVPGSEITGKRGGIHNSVTRIVL 1188
|
1210 1220 1230
....*....|....*....|....*....|....*.
gi 2519732638 1199 KPTHMIGGYAHQAFAFNYLGPTGNQRDIVSYIRRRK 1234
Cdd:COG5013 1189 KPTHMIGGYAQLSYGFNYYGPTGNQRDEVVVVRKRS 1224
|
|
| narG |
TIGR01580 |
respiratory nitrate reductase, alpha subunit; The Nitrate reductase enzyme complex allows ... |
13-1234 |
0e+00 |
|
respiratory nitrate reductase, alpha subunit; The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the alpha subunit for nitrate reductase I (narG) and nitrate reductase II (narZ) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model The seed members used to make the model include Nitrate reductases from Pseudomonas fluorescens (GP:11344601), E.coli (SP:P09152) and B.subtilis (SP:P42175). All seed members are experimentally characterized. Some unpublished nitrate reductases, that are shorter sequences, and probably fragments fall in between the noise and trusted cutoffs. Pfam models pfam00384 (Molybdopterin oxidoreductase) and pfam01568(Molydopterin dinucleotide binding domain) will also match the nitrate reductase, alpha subunit. [Energy metabolism, Anaerobic]
Pssm-ID: 162434 [Multi-domain] Cd Length: 1235 Bit Score: 1437.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 13 PLTDQLikfgKFFSRWDET-DDGRAVFREGGRKGDAFYRDRWSHDKEVRSTHGVNCTGSCSWKVYVKDGIITWEAQETDY 91
Cdd:TIGR01580 2 KLLDRL----RYFKQKGETfSDGHGQTLNENRDWENVYRQRWQYDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 92 PTVGPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPYVRGLLLEMYREAKALYGDPVEAFHSIVSDPVKRNRYISARGKGGL 171
Cdd:TIGR01580 78 PRTRPDLPNHEPRGCPRGASYSWYIYSANRLKYPMMRKRLMKLWREAKQTHSDPVEAWASIVENADKAKSYKQARGRGGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 172 VRSTWAEALELVAAAHVHTIKYYGPDRCTGFTPIPAMSMVSFSAGVRFIQLIGGVMTSFYDWYADLPVASPQVFGDQTDV 251
Cdd:TIGR01580 158 VRSSWQEVNELIAASNVYTVKNYGPDRVVGFSPIPAMSMVSYASGSRYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 252 PESGDWWDASYLIMWGSNIPVTRTPDAHWVAEVRYRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKEN 331
Cdd:TIGR01580 238 PESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAALALAMGHVILREF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 332 YVDQRVEFFEDFALTYTDLPFLVTLEtREDGTKVPSKFLTAASLAGEKHQE-NAAFKTAMMDrETGEVFIPNGTMGHRYS 410
Cdd:TIGR01580 318 HLDNPSQYFTEYAKRYTDMPMLVMLE-ERDGYYAAGRFLRAADLVDALGQEnNPEWKTVAFD-TNGEMVAPQGSIGFRWG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 411 EsdQGNWNLEL-DGR--KPILSIRDLPQGEAAAVEIKLPTFDN------PKGHGD-IITRGVPVSYV---EGQE--VTTV 475
Cdd:TIGR01580 396 E--KGKWNLEQrDGKtgEEIELQLSLLGSQDEIAEVGFPYFGGdgtehfNKVEGEnVLLRKLPVKRLqlaDGSTalVTTV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 476 FDLMLATYGIGRpGLPGEW-ASGYDDWSIQnTPAWQEQITSVPPEAVIRVAREFAQNAIDSHGRSMIIFGAGICQWYHAD 554
Cdd:TIGR01580 474 FDLTLANYGLER-GLGDVNcATSYDDVKAY-TPAWQEQITGVSREQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLD 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 555 TTYRAILALLNLTGCQGRNGGGWAHYVGQEKARPLTGLTNMANALDWSRPPRHMIGTGFWYMHTDQFRQDGYSTDYLQSP 634
Cdd:TIGR01580 552 MNYRGLINMLILCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPPRHMNGTSFFYNHSSQWRYETVTAEDLLSP 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 635 LGKGELKNVHTADVVARSTRMGWMPFYPQFPENSLDLADKAEEAVArgeakDNADYLAQRLNSGDLEFSVEDVDNPVNWP 714
Cdd:TIGR01580 632 MADKSRYTGHLIDYNVRAERMGWLPSAPQLNTNPLTIAGEAEKAGM-----NPVDYVVKSLQEGSLRFAAEQPDNGVNFP 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 715 RTLMLWRSNLFGSSAKGESYFLKHLVGSMDNVQGAD--HEESI-PREVKWYQDAPQGKLDLLVSSDFRMTTTTLLSDVVF 791
Cdd:TIGR01580 707 RNLFIWRSNLLGSSGKGHEYMLKYLLGTENGIMNKDlgQQGGVkPEEVDWQDNGLEGKLDLVVTLDFRMSSTCLYSDIVL 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 792 PTATWYEKYDISSTDMHPFLHAFSPAIDPPWEAKTDHETFKALAYEFTRQAKKHLGTRKDIVSVPLLHDTPGQIKQPGGh 871
Cdd:TIGR01580 787 PTATWYEKDDMNTSDMHPFIHPLSAAIDPAWESKSDWEIYKAIAKAFSEVCVGHLGKEKDIVTLPLQHDSAAELAQPFG- 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 872 APDWKNNpDMVGVPGMNMPNFMTVERDYGAMYDMYTSVGPLFDKVGATTKYVTYDLKDEVAQMAKEFG-VMDSGKGAGRP 950
Cdd:TIGR01580 866 VKDWKKG-ECDLIPGKTAPNIQVVERDYPAIYERFTSLGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYtKAEGSPAKGQP 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 951 ALDTDVKIAESILRISGTSNGEVALKGFKELEKQTGLHLVDLAEGNEERKITFPMTQASPQPVMTSPEWSGSETGGRRYA 1030
Cdd:TIGR01580 945 MINTAIDAAEMILTLAPETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYN 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1031 PFTVNIEKKKPFHTLTGRMHFFLDHDWMHEMGEATPIYRPPLDmTGLFKEPEIGATDGVS-VAVRYLTPHNKWAIHSQYF 1109
Cdd:TIGR01580 1025 AGYTNVHELIPWRTLTGRQQLYQDHQWMRDFGESLLVYRPPID-TRSFKEVIGQKSNGNQeIVLNFLTPHQKWGIHSTYS 1103
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1110 DNQHMLTLFRGGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVHHAQERMMT-PKTETTGKRGG 1188
Cdd:TIGR01580 1104 DNLLMLTLGRGGPVVWLSEADAKDLGIADNDWIECFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNvPGSEITQQRGG 1183
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*.
gi 2519732638 1189 IHNSMTRILLKPTHMIGGYAHQAFAFNYLGPTGNQRDIVSYIRRRK 1234
Cdd:TIGR01580 1184 IHNSVTRITPKPTHMIGGYAQLAYGFNYYGTVGSNRDEFVVVRKMK 1229
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
56-835 |
0e+00 |
|
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: 602.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 56 DKEVRSTHGVNCTGSCSWKVYVKDGIITWEAQETDYPTVGPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPYVRGlllemy 135
Cdd:cd02750 1 DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 136 reakalygdpveafhsivsdpvkrnryiSARGKGGLVRSTWAEALELVAAAHVHTIKYYGPDRCTGFTPIPAMSMVSFSA 215
Cdd:cd02750 75 ----------------------------GARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 216 GVRFIQLIGGVMTSFYDWYADLPVASPQVFGDQTDVPESGDWWDASYLIMWGSNIPVTRTPDAHWVAEVRYRGTKVVSVS 295
Cdd:cd02750 127 GSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 296 PDYADNTKFADEWLPAQAGTDAALAMAMGHVILKENYVDqrveffEDFALTYTDLPFLVtletredgtkvpskfltaasl 375
Cdd:cd02750 207 PDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYD------EDYLKEYTDLPFLV--------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 376 agekhqenaafktammdretgevfipngtmghrysesdqgnwnleldgrkpilsirdlpqgeaaaveiklptfdnpkghg 455
Cdd:cd02750 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 456 diitrgvpvsyvegqevttvfdlmlatygigrpglpgewasgyddwsiqNTPAWQEQITSVPPEAVIRVAREFAQNaids 535
Cdd:cd02750 260 -------------------------------------------------YTPAWQEAITGVPRETVIRLAREFATN---- 286
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 536 hGRSMIIFGAGICQWYHADTTYRAILALLNLTGCQGRNGGGWAHYVGqekarpltgltnmanaldwsrpprhmigtgfwy 615
Cdd:cd02750 287 -GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG--------------------------------- 332
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 616 mhtdqfrqdgystdylqsplgkgelknvhtadvvarstrmgwmpfypqfpensldladkaeeavargeakdnadylaqrl 695
Cdd:cd02750 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 696 nsgdlefsvedvdnpvnWPRTLMLWRSNLFGSSAKGESYFlkhlvgsmdnvqgadheesiprevkwyQDAPQGKLDLLVS 775
Cdd:cd02750 333 -----------------QPRVLFVWRGNLFGSSGKGHEYF---------------------------EDAPEGKLDLIVD 368
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 776 SDFRMTTTTLLSDVVFPTATWYEKYDISSTDMHPFLHAFSPAIDPPWEAKTDHETFKALA 835
Cdd:cd02750 369 LDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALA 428
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
1093-1231 |
4.44e-71 |
|
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: 233.42 E-value: 4.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1093 VRYLTPHNKWAIHSQYFDNQHMLTLFRGGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVHHAQ 1172
Cdd:cd02776 2 LNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1173 ER-MMTPKTETTGKRGGIHNSMTRILLKPTHMIGGYAHQAFAFNYLGPTGNQRDIVSYIR 1231
Cdd:cd02776 82 ERhVNVPGSKLTGKRGGIHNSVTRVRIKPTHLVGGYGQLSYGFNYYGPTGVNRDTRVVVR 141
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
56-1170 |
3.35e-41 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 162.71 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 56 DKEVRSTHgVNCTGSCSWKVYVKDGIITweAQETDyptvgPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPYVRGlllemy 135
Cdd:COG0243 21 TKTVKTTC-PGCGVGCGLGVKVEDGRVV--RVRGD-----PDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRV------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 136 reakalygdpveafhsivsdpvkrnryiSARGKGGLVRSTWAEALELVAAAHVHTIKYYGPDRCTGFT---PIPAMSMVS 212
Cdd:COG0243 87 ----------------------------GPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTsggSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 213 FSAGVRFIQLIGGvmTSFYDW----YADLPVASPQVFGDQTDVPESGDWWDASYLIMWGSNIPVTRTPDAHWVAE-VRYR 287
Cdd:COG0243 139 AYLAQRFARALGT--NNLDDNsrlcHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 288 GTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKENYVDQrveffeDFaltytdlpflvtletredgtkvps 367
Cdd:COG0243 217 GAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYDR------DF------------------------ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 368 kfltaaslagekhqenaafktamMDRetgevfipngtmghrysesdqgnwnleldgrkpilsirdlpqgeaaaveiklpt 447
Cdd:COG0243 267 -----------------------LAR------------------------------------------------------ 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 448 fdnpkghgdiitrgvpvsYVEGqevttvFDlmlatygigrpglpgEWASGYDDWsiqnTPAWQEQITSVPPEAVIRVARE 527
Cdd:COG0243 270 ------------------HTVG------FD---------------ELAAYVAAY----TPEWAAEITGVPAEDIRELARE 306
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 528 FAQnaidsHGRSMIIFGAGICQWYHADTTYRAILALLNLTGCQGRNGGGwahyvgqekARPLTGltnmanaldwsrpprh 607
Cdd:COG0243 307 FAT-----AKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGG---------PFSLTG---------------- 356
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 608 migtgfwymhtdqfrqdgystdylqsplgkgelknvhtadvvarstrmgwmpfypqfpensldladkaeEAVARGEakdn 687
Cdd:COG0243 357 ---------------------------------------------------------------------EAILDGK---- 363
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 688 adylaqrlnsgdlefsvedvDNPVnwpRTLMLWRSNLFgssakgesyflkhlvgsmdnVQGADHEesipREVKWYQdapq 767
Cdd:COG0243 364 --------------------PYPI---KALWVYGGNPA--------------------VSAPDTN----RVREALR---- 392
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 768 gKLDLLVSSDFRMTTTTLLSDVVFPTATWYEKYDISSTDMHPFLHAFSPAIDPPWEAKTDHETFKALAyeftrqakKHLG 847
Cdd:COG0243 393 -KLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELA--------KRLG 463
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 848 TrkdivsvpllhdtpgqikqpgGHAPDWKNNPDmvgvpgmnmpnfmtverDYgamydmytsvgplfdkvgattkyvtydl 927
Cdd:COG0243 464 F---------------------EEAFPWGRTEE-----------------DY---------------------------- 477
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 928 kdevaqmakefgvmdsgkgagrpaldtdvkiaesilrisgtsngevalkgFKELEKQTGLHLVDLAEGNEERKITFPMTQ 1007
Cdd:COG0243 478 --------------------------------------------------LRELLEATRGRGITFEELREKGPVQLPVPP 507
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1008 aspqpvmtspewsgsetgGRRYApftvnieKKKPFHTLTGRMHFFLDHDWMHEMgeatPIYRPPldmtglfkePEIGATD 1087
Cdd:COG0243 508 ------------------EPAFR-------NDGPFPTPSGKAEFYSETLALPPL----PRYAPP---------YEGAEPL 549
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1088 GVSVAVRYLTPHNKWAIHSQyFDNQHMLTLFRGGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCY 1167
Cdd:COG0243 550 DAEYPLRLITGRSRDQWHST-TYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVF 628
|
...
gi 2519732638 1168 VHH 1170
Cdd:COG0243 629 APH 631
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
60-835 |
1.94e-40 |
|
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: 154.02 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 60 RSTHgVNCTGSCSWKVYVKDGIITWEaqETDyptvgPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPYVRGlllemyreak 139
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRI--EGD-----PNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRV---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 140 alygdpveafhsivsdpvkrnryisaRGKGGLVRSTWAEALELVAAAHVHTIKYYGPDRCTGFTPIPAMSMVSFSAGVRF 219
Cdd:cd00368 63 --------------------------GGRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 220 iQLIGGVMTSFYDWYADLP-VASPQVFGDQTDVPESGDWWDASYLIMWGSNIPVTRTPDAHWVAEVRYRGTKVVSVSPDY 298
Cdd:cd00368 117 -RALGSNNVDSHARLCHASaVAALKAFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 299 ADNTKFADEWLPAQAGTDAALAMAmghvilkenyvdqrveffedfaltytdlpflvtletredgtkvpskfltaaslage 378
Cdd:cd00368 196 TETAAKADEWLPIRPGTDAALALA-------------------------------------------------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 379 khqenaafktammdretgevfipngtmghrysesdqgnwnleldgrkpilsirdlpqgeaaaveiklptfdnpkghgdii 458
Cdd:cd00368 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 459 trgvpvsyvegqevttvfdlmlatygigrpglpgewasgyddwsiqntpAWQEQITSVPPEAVIRVAREFAQnaidsHGR 538
Cdd:cd00368 220 -------------------------------------------------EWAAEITGVPAETIRALAREFAA-----AKR 245
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 539 SMIIFGAGICQWYHADTTYRAILALLNLTGCQGRNGGGWAHyvgqekarpltgltnmanaldwsrpprhmigtgfwymht 618
Cdd:cd00368 246 AVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP--------------------------------------- 286
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 619 dqfrqdgystdylqsplgkgelknvhtadvvarstrmgwmpfypqfpensldladkaeeavargeakdnadylaqrlnsg 698
Cdd:cd00368 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 699 dlefsvedvdnpvnwprtlmlwRSNLFGSSAKGESYFlkhlvgsmdnvqgadheesiprevkwyqdAPQGKLDLLVSSDF 778
Cdd:cd00368 287 ----------------------GGNPLVSAPDANRVR-----------------------------AALKKLDFVVVIDI 315
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 2519732638 779 RMTTTTLLSDVVFPTATWYEKYDIsSTDMHPFLHAFSPAIDPPWEAKTDHETFKALA 835
Cdd:cd00368 316 FMTETAAYADVVLPAATYLEKEGT-YTNTEGRVQLFRQAVEPPGEARSDWEILRELA 371
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
61-609 |
4.22e-36 |
|
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: 145.31 E-value: 4.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 61 STHGVNCTGSCSWKVYVKDG-IITWEAQEtdyptvgPDRPEYePRGCPRGAAFSWYTYSPTRVKYPyvrglllemyreak 139
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGkIVKVEPNE-------WPDKTY-KRGCTRGLSHLQRVYSPDRLKYP-------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 140 alygdpveafhsivsdpVKRnryISARGKGGLVRSTWAEALELVAAAHVHTIKYYGPDRCTGFTpipaMSMVSFSAGVRF 219
Cdd:cd02765 60 -----------------MKR---VGERGEGKFERITWDEALDTIADKLTEAKREYGGKSILWMS----SSGDGAILSYLR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 220 IQLIGGVMTSFYDWYADLPVASPQ--VFGDQTDVP--ESGDWWDASYLIMWGSNIPVTRTPDAHWVAEVRYRGTKVVSVS 295
Cdd:cd02765 116 LALLGGGLQDALTYGIDTGVGQGFnrVTGGGFMPPtnEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVID 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 296 PDYADNTKFADEWLPAQAGTDAALAMAMGHVILKENYVDqrveffEDFALTYTDLPFLVtletREDGtkvpSKFLTAASL 375
Cdd:cd02765 196 PVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYD------EAFLKSNTSAPFLV----REDN----GTLLRQADV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 376 AGEKHQENaafkTAMMDRETGEvfipngtmghrYSESDQGNWNLELDGrkpilsirdlpqgeaaaveiklptfdnpkghg 455
Cdd:cd02765 262 TATPAEDG----YVVWDTNSDS-----------PEPVAATNINPALEG-------------------------------- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 456 diitrgvpvSY-VEGQEVTTVFDLMLatygigrpglpgEWASGYddwsiqnTPAWQEQITSVPPEAVIRVAREFAQNaid 534
Cdd:cd02765 295 ---------EYtINGVKVHTVLTALR------------EQAASY-------PPKAAAEICGLEEAIIETLAEWYATG--- 343
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519732638 535 shGRSMIIFGAGICQWYHADTTYRAILALLNLTGCQGRNGGGwahyVGQEKArpltgLTNMANALDWSRPPRHMI 609
Cdd:cd02765 344 --KPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG----VGQIKF-----MYFMGSNFLGNQPDRDRW 407
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
65-850 |
4.67e-31 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 130.52 E-value: 4.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 65 VNCTGSCSWKVYVKDGIITWeaQETDypTVGPDRPEY-EPRGCPRGAAFSWYTYSPTRVKYPyvrgllleMYREAKalyg 143
Cdd:cd02770 6 VNCGGRCPLKAHVKDGVITR--IETD--DTGDDDPGFhQIRACLRGRSQRKRVYNPDRLKYP--------MKRVGK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 144 dpveafhsivsdpvkrnryisaRGKGGLVRSTWAEALELVAAAHVHTIKYYGPDR--CTGFTPIPAMSMVSFSAGVRFIQ 221
Cdd:cd02770 70 ----------------------RGEGKFVRISWDEALDTIASELKRIIEKYGNEAiyVNYGTGTYGGVPAGRGAIARLLN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 222 LIGGVMTSF--YDWyADLPVASPQVFGDQTDVPESGDWWDASYLIMWGSNIPVTR---TPDAHWVAEVRYRGTKVVSVSP 296
Cdd:cd02770 128 LTGGYLNYYgtYSW-AQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRmggGGSTYYYLQAKKAGAKFIVIDP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 297 DYADNTK-FADEWLPAQAGTDAALAMAMGHVILKENYVDQRveFFEDFALTYtdlpflvtletredgtkvpskfltaasl 375
Cdd:cd02770 207 RYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQA--FLDRYCVGF---------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 376 agekhqenaafktammDRETgevfipngtmghrysesdqgnwnleldgrkpilsirdLPQGEAAAveiklptfDNPKghg 455
Cdd:cd02770 257 ----------------DAEH-------------------------------------LPEGAPPN--------ESYK--- 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 456 diitrgvpvSYVEGQevttvfdlmlatygigrpglpgewasGYDdwSIQNTPAWQEQITSVPPEAVIRVAREFAqnaidS 535
Cdd:cd02770 273 ---------DYVLGT--------------------------GYD--GTPKTPEWASEITGVPAETIRRLAREIA-----T 310
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 536 HGRSMIIFGAGICQWYHADTTYRAILALLNLTGCQGRNGGGWAHYVGQeKARPLTGLTNMANALDWSrpprhmIGTGFWY 615
Cdd:cd02770 311 TKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGG-SAYNGAGLPAGKNPVKTS------IPCFMWT 383
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 616 mhtdqfrqdgystdylqsplgkgelknvhtadvvarstrmgwmpfypqfpenslDLADKAEEAVARGEAKDNADylaqrl 695
Cdd:cd02770 384 ------------------------------------------------------DAIERGEEMTADDGGVKGAD------ 403
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 696 nsgdlefsveDVDNPVNwprtlMLWrsNLFGssakgesyflkhlvGSMDNVQGADHeesipREVKWYQDAPQgKLDLLVS 775
Cdd:cd02770 404 ----------KLKSNIK-----MIW--NYAG--------------NTLINQHSDDN-----NTTRALLDDES-KCEFIVV 446
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519732638 776 SDFRMTTTTLLSDVVFPTATWYEKYDI---SSTDMHPFLHAFSPAIDPPWEAKTDHETFKALAyeftrqakKHLGTRK 850
Cdd:cd02770 447 IDNFMTPSARYADILLPDTTELEREDIvltSNAGMMEYLIYSQKAIEPLYECKSDYEICAELA--------KRLGVED 516
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
70-850 |
1.21e-29 |
|
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: 126.19 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 70 SCSW---KVYVKDGIITWeaqetdyptVGPDrPEYEPRGCPRGAAFSWYTYSPTRVKYPYVRglllEMYREakalygdpv 146
Cdd:cd02751 3 ACHWgpfKAHVKDGVIVR---------VEPD-DTDQPRPCPRGRSVRDRVYSPDRIKYPMKR----VGWLG--------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 147 eafhsivsdpvKRNRYISARGKGGLVRSTWAEALELVAAAHVHTIKYYGPD---------RCTGFTPiPAMSMVSfsagv 217
Cdd:cd02751 60 -----------NGPGSRELRGEGEFVRISWDEALDLVASELKRIREKYGNEaifggsygwASAGRLH-HAQSLLH----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 218 RFIQLIGGVMTSF--YDWyADLPVASPQVFGDqTDVPESGDWWD-----ASYLIMWGSNIPVTR--------TPDAHWVA 282
Cdd:cd02751 123 RFLNLIGGYLGSYgtYST-GAAQVILPHVVGS-DEVYEQGTSWDdiaehSDLVVLFGANPLKTRqgggggpdHGSYYYLK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 283 EVRYRGTKVVSVSPDYADNTK-FADEWLPAQAGTDAALAMAMGHVILKENYVDQrveffeDFALTYTdlpflvtletred 361
Cdd:cd02751 201 QAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITEDLHDQ------AFLARYT------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 362 gtkvpskfltaaslagekhqenaafktammdreTGevfipngtmghrysesdqgnwnleldgrkpilsirdlpqgeaaav 441
Cdd:cd02751 262 ---------------------------------VG--------------------------------------------- 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 442 eiklptFDnpkghgdiitrgVPVSYVEGQevttvfdlmlatygigrpglpgewasgyDDwSIQNTPAWQEQITSVPPEAV 521
Cdd:cd02751 264 ------FD------------EFKDYLLGE----------------------------SD-GVPKTPEWAAEITGVPAETI 296
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 522 IRVAREFAQNaidshgRSMIIFGAGICQWYHADTTYRAILALLNLTGCQGRNGGgwahyvgqekarpltgltnmanaldw 601
Cdd:cd02751 297 RALAREIASK------RTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGG-------------------------- 344
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 602 srpprhmiGTGFWYmhtdqfrqdGYSTDYLQSPLGKGelknvhtadvvarstrmgwMPFYPQfpensldLADKAEEA--V 679
Cdd:cd02751 345 --------GFGFGY---------GYSNGGGPPRGGAG-------------------GPGLPQ-------GKNPVKDSipV 381
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 680 ARgeakdnadyLAQRLNSGDLEFSVEdvDNPVNWPRTLMLWR--SNLFGssakgesyflkhlvgsmdnvqgadHEESIPR 757
Cdd:cd02751 382 AR---------IADALLNPGKEFTAN--GKLKTYPDIKMIYWagGNPLH------------------------HHQDLNR 426
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 758 EVKWYQdapqgKLDLLVSSDFRMTTTTLLSDVVFPTATWYEKYDI--SSTDMHPFLHAFSPAIDPPWEAKTDHETFKALA 835
Cdd:cd02751 427 LIKALR-----KDETIVVHDIFWTASARYADIVLPATTSLERNDIglTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELA 501
|
810
....*....|....*
gi 2519732638 836 yeftrqakKHLGTRK 850
Cdd:cd02751 502 --------KRLGVEE 508
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
166-335 |
1.41e-28 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 118.66 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 166 RGKGGLVRSTWAEALELVAAAHVHTIKYYGPDRC-TGFTPIPAMSMVSFSAGVRFIQLIGGVMTSFYDWYADLPVASPQV 244
Cdd:pfam00384 9 RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIaINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNGDLCTAAAAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 245 FG-DQTDVPESG----DWWDASYLIMWGSNIPVTRTPD-AHWVAEVRYRGTKVVSVSPDYadNTKFADEWLPAQAGTDAA 318
Cdd:pfam00384 89 FGsDLRSNYLFNssiaDIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRL--DLTYADEHLGIKPGTDLA 166
|
170
....*....|....*..
gi 2519732638 319 LAMAMGHVILKENYVDQ 335
Cdd:pfam00384 167 LALAGAHVFIKELKKDK 183
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
67-341 |
5.11e-24 |
|
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: 107.39 E-value: 5.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 67 CTGSCSWKVYVKDGIITWEAQETDYPTVGPdrpeyepRGCPRGAAFSWYTYSPTRVKYPyvrglllemyreakalygdpv 146
Cdd:cd02759 7 CHSGCGVLVYVKDGKLVKVEGDPNHPTNKG-------RLCMRGLAAPEIVYHPDRLLYP--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 147 eafhsivsdpVKRnryISARGKGGLVRSTWAEALELVAAAHVHTIKYYGPDR---CTGfTPIPAMSMVSFSAgVRFIQLI 223
Cdd:cd02759 59 ----------LKR---VGERGENKWERISWDEALDEIAEKLAEIKAEYGPESiatAVG-TGRGTMWQDSLFW-IRFVRLF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 224 G-----GVMTSFYdWYADLPVASPQVFGDQTDVPesgDWWDASYLIMWGSNiPVTRTPD--AHWVAEVRYRGTKVVSVSP 296
Cdd:cd02759 124 GspnlfLSGESCY-WPRDMAHALTTGFGLGYDEP---DWENPECIVLWGKN-PLNSNLDlqGHWLVAAMKRGAKLIVVDP 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2519732638 297 DYADNTKFADEWLPAQAGTDAALAMAMGHVILKENYVDQrvEFFE 341
Cdd:cd02759 199 RLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDK--DFVE 241
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
67-414 |
5.69e-18 |
|
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: 88.51 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 67 CTGSCSWKVYVKDGIItWEAQETdyptvgPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPYVRglllemyreakalygdpv 146
Cdd:cd02755 8 CSSRCGILARVEDGRV-VKIDGN------PLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIR------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 147 eafhsivsdpvkrnryISARGKGGLVRSTWAEALELVAAAHVHTIKYYGPDRCTGFTPIPAMSMVSFsagvRFIQLIGgv 226
Cdd:cd02755 63 ----------------VGERGEGKFREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFK----HFAAAFG-- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 227 mTSFYDWYADLPVASPQVFGDQTDVPESG----DWWDASYLIMWGSNI-PVTRTPDAHWVAEVRYRGTKVVSVSPDYADN 301
Cdd:cd02755 121 -SPNIFSHESTCLASKNLAWKLVIDSFGGevnpDFENARYIILFGRNLaEAIIVVDARRLMKALENGAKVVVVDPRFSEL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 302 TKFADEWLPAQAGTDAALAMAMGHVILKENYVDQrveffeDFALTYTDLPFLV-------TLETREDGTKVPskfltaAS 374
Cdd:cd02755 200 ASKADEWIPIKPGTDLAFVLALIHVLISENLYDA------AFVEKYTNGFELLkahvkpyTPEWAAQITDIP------AD 267
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2519732638 375 LAGEKHQENAAFKTAMMdretgevfIPNGTMGHRYSESDQ 414
Cdd:cd02755 268 TIRRIAREFAAAAPHAV--------VDPGWRGTFYSNSFQ 299
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
66-343 |
8.11e-17 |
|
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: 84.99 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 66 NCTGSCSWKVYVKDGIITweaqetdypTVGPDRPEYEPRG--CPRGAAFSWYTYSPTRVKYPYVRglllemyREAKALYG 143
Cdd:cd02766 7 DCPDTCSLLVTVEDGRIV---------RVEGDPAHPYTRGfiCAKGARYVERVYSPDRLLTPLKR-------VGRKGGQW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 144 DPV---EAFHSIVsdpvKRNRYISARgkgglvrstwaealelVAAAHVHTIKYYGPdrctgftpipaMSMVSFSAGVRFI 220
Cdd:cd02766 71 ERIswdEALDTIA----AKLKEIKAE----------------YGPESILPYSYAGT-----------MGLLQRAARGRFF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 221 QLIGgvMTSFYD---WYADLPvASPQVFGDQTDV-PEsgDWWDASYLIMWGSNIPVTRTPDAHWVAEVRYRGTKVVSVSP 296
Cdd:cd02766 120 HALG--ASELRGticSGAGIE-AQKYDFGASLGNdPE--DMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDP 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2519732638 297 DYADNTKFADEWLPAQAGTDAALAMAMGHVILKEN-----YVDQRVEFFEDF 343
Cdd:cd02766 195 YRTATAARADLHIQIRPGTDGALALGVAKVLFREGlydrdFLARHTEGFEEL 246
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
1094-1207 |
8.96e-17 |
|
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: 77.31 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1094 RYLTPHNKWAIHSQYfDNQHMLTLFRGGQ-TAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVHHAQ 1172
Cdd:pfam01568 2 YLITGRVLGQYHSQT-RTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2519732638 1173 ERMMtpktettgkRGGIHNSMTRILLKPTHMIGGY 1207
Cdd:pfam01568 81 WYEP---------RGGNANALTDDATDPLSGGPEF 106
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
1105-1207 |
1.22e-16 |
|
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: 76.59 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1105 HSQYFDNQHMLTLFRGGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVHHAQERMmtpktettG 1184
Cdd:cd02775 6 HSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHR--------G 77
|
90 100
....*....|....*....|...
gi 2519732638 1185 KRGGIHNSMTRILLKPTHMIGGY 1207
Cdd:cd02775 78 GRGGNANVLTPDALDPPSGGPAY 100
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
54-351 |
2.00e-15 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 81.61 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 54 SHDKEVRSTHGVNCTGSCSWKVYVKDGIITWeaQETDypTVGPDRPE--YEPRGCPRGAAFSWYTYSPTRVKYPYVRgll 131
Cdd:PRK14990 54 SDEKVIWSACTVNCGSRCPLRMHVVDGEIKY--VETD--NTGDDNYDglHQVRACLRGRSMRRRVYNPDRLKYPMKR--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 132 lemyreakalygdpveafhsivsdpvkrnryISARGKGGLVRSTWAEALELVAAAHVHTIKYYGPDRCT---GFTPIPAM 208
Cdd:PRK14990 127 -------------------------------VGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnyGTGTLGGT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 209 SMVSFSAG----VRFIQLIGGVMTSFYDWY-ADLPVASPQVFGDQTDVPESGDWWDASYLIMWGSNIPVTRTPDA---HW 280
Cdd:PRK14990 176 MTRSWPPGntlvARLMNCCGGYLNHYGDYSsAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGgvtYY 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519732638 281 VAEVRYRGT-KVVSVSPDYADN-TKFADEWLPAQAGTDAALAMAMGHVILKENYVDQrvEFFEDFALTYTD--LP 351
Cdd:PRK14990 256 LEQARQKSNaRMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQ--PFLDKYCVGYDEktLP 328
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
493-835 |
3.25e-15 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 80.70 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 493 EWASGYDDW--SIQN-TPAWQEQITSVPPEAVIRVAREFAQNaidshGRSMIIFGAGICQWYHADTTYRAILALLNLTGC 569
Cdd:COG3383 244 ERTEGFEELkaSVAKyTPERVAEITGVPAEDIREAARLIAEA-----KRAMILWGMGVNQHTQGTDNVNAIINLALATGN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 570 QGRNGGGWAhyvgqekarPLTGLTNMANALDwsrpprhmigtgfwymhtdqfrqdgystdylqsplgkgelknvhtadvv 649
Cdd:COG3383 319 IGRPGTGPF---------PLTGQNNVQGGRD------------------------------------------------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 650 arstrMGWMPfyPQFPeNSLDLADkaEEAVARGEAKDNADYLaqrlnsgdlefsvedvdnpvnwPRTLMLWRSNLFGSSA 729
Cdd:COG3383 341 -----MGALP--NVLP-GYRDVTD--PEHRAKVADAWGVPPL----------------------PDKPGLTAVEMFDAIA 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 730 KGEsyfLKHLVgsmdnVQGADHEESIPrEVKWYQDAPQgKLDLLVSSDFRMTTTTLLSDVVFPTATWYEKyDISSTDMHP 809
Cdd:COG3383 389 DGE---IKALW-----IIGENPAVSDP-DANHVREALE-KLEFLVVQDIFLTETAEYADVVLPAASWAEK-DGTFTNTER 457
|
330 340
....*....|....*....|....*.
gi 2519732638 810 FLHAFSPAIDPPWEAKTDHETFKALA 835
Cdd:COG3383 458 RVQRVRKAVEPPGEARPDWEIIAELA 483
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
70-349 |
3.85e-15 |
|
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: 80.38 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 70 SCSWKVY---VKDGIIT-WEAQETD-YPTvgpdrpeyeprgcPRGAAFSWYTYSPTRVKYPYVRGLLLEmyreakalygd 144
Cdd:cd02769 3 ASHWGAFrarVKDGRIVgVRPFEEDpDPS-------------PLLDGVPDAVYSPTRIKYPMVRRGWLE----------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 145 pveafhsivsDPVKRNRyiSARGKGGLVRSTWAEALELVAAAHVHTIKYYGPdrctgfTPIPAMSMVSFSAGV------- 217
Cdd:cd02769 59 ----------KGPGSDR--SLRGKEEFVRVSWDEALDLVAAELKRVRKTYGN------EAIFGGSYGWSSAGRfhhaqsl 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 218 --RFIQLIGGVMTSFYDW-YADLPVASPQVFGDQTDVPESGDWWD-----ASYLIMWGSNIPVTR------TPDaH---- 279
Cdd:cd02769 121 lhRFLNLAGGYVGSVGDYsTGAAQVILPHVVGSMEVYTEQQTSWPviaehTELVVAFGADPLKNAqiawggIPD-Hqays 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519732638 280 WVAEVRYRGTKVVSVSPDYADNTKFAD-EWLPAQAGTDAALAMAMGHVILKENYVDqrveffEDFALTYTD 349
Cdd:cd02769 200 YLKALKDRGIRFISISPLRDDTAAELGaEWIAIRPGTDVALMLALAHTLVTEGLHD------KAFLARYTV 264
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
66-343 |
6.63e-12 |
|
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: 69.78 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 66 NCTGSCSWKVYVKDGIIT-WEAQetdyptvgPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPYVR-----GLLLE------ 133
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVTkVEGN--------PLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRtnprkGRDVDpkfvpi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 134 MYREAKALYGDPVEAFhsIVSDpvKRNRYISARGKGGlvrstwaealelvaaaHVHTIKY------YGPDRCTGFTPIPA 207
Cdd:cd02757 80 SWDEALDTIADKIRAL--RKEN--EPHKIMLHRGRYG----------------HNNSILYgrftkmIGSPNNISHSSVCA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 208 MSmvsfsagvrfiqligGVMTSFYdWYADLPVASPqvfgdqtdvpesgDWWDASYLIMWGSN-IPVTR-TPDAHWVAEVR 285
Cdd:cd02757 140 ES---------------EKFGRYY-TEGGWDYNSY-------------DYANAKYILFFGADpLESNRqNPHAQRIWGGK 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519732638 286 YRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKENYVDQRveFFEDF 343
Cdd:cd02757 191 MDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKD--FVGDF 246
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
62-532 |
7.00e-12 |
|
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: 70.00 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 62 THGVNCTGSCSW-KVYVKDGIITWEAQETDYPTVGPDRPeyepRGCPRGAAFSWYTYSPTRVKYPYVRGlllemyREAKA 140
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVATEIEPNFAAEDIHPARG----RVCVKAYGLVQKTYNPNRVLQPMKRT------NPKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 141 LYGDPV-------EAFhSIVSDPVKRNRYISARGKGGLVRSTWAEALELVAAAHVHTIkyygPDRCTGFTPiPAMSMVS- 212
Cdd:cd02760 72 RNEDPGfvpiswdEAL-DLVAAKLRRVREKGLLDEKGLPRLAATFGHGGTPAMYMGTF----PAFLAAWGP-IDFSFGSg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 213 -FSAGVRFIQLIGGVMTSFYDWYADLPVASpqvfgdqtdvpesgdwwdasYLIMWGSNIPVTRTPDA-HWVAEVRYRGTK 290
Cdd:cd02760 146 qGVKCVHSEHLYGEFWHRAFTVAADTPLAN--------------------YVISFGSNVEASGGPCAvTRHADARVRGYK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 291 VVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKENYVDQrveffedfaltyTDLPFLvtletrEDGTKVPskfl 370
Cdd:cd02760 206 RVQVEPHLSVTGACSAEWVPIRPKTDPAFMFAMIHVMVHEQGLGK------------LDVPFL------RDRTSSP---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 371 taaSLAGEKhqenaafKTAMMDRETGEVFIpngtmghrysesdqgnWNlELDGRKPILSIRdlPQGEAAAVEIKLPtfdn 450
Cdd:cd02760 264 ---YLVGPD-------GLYLRDAATGKPLV----------------WD-ERSGRAVPFDTR--GAVPAVAGDFAVD---- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 451 pkGHGDIITRGVPVSYvEGQEVTTVFDLMLatygigrpglpgEWASGYddwsiqnTPAWQEQITSVPPEAVIRVAREFAQ 530
Cdd:cd02760 311 --GAVSVDADDETAIH-QGVEGTTAFTMLV------------EHMRKY-------TPEWAESICDVPAATIRRIAREFLE 368
|
..
gi 2519732638 531 NA 532
Cdd:cd02760 369 NA 370
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
259-390 |
7.68e-12 |
|
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: 69.16 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 259 DASYLIMWGSNipvtrTPDAHWVAEVRY-----RGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKEN-- 331
Cdd:cd02753 156 EADVILVIGSN-----TTEAHPVIARRIkrakrNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGly 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2519732638 332 ---YVDQRVEFFEDFALTYTDlpflVTLETREDGTKVPSKFL-TAASLAGEKhqENAAFKTAM 390
Cdd:cd02753 231 deeFIEERTEGFEELKEIVEK----YTPEYAERITGVPAEDIrEAARMYATA--KSAAILWGM 287
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
505-600 |
4.12e-11 |
|
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: 66.85 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 505 NTPAWQEQITSVPPEAVIRVAREFAQNaidshGRSMIIFGAGICQWYHADTTYRAILALLNLTGCQGRNGGGwahyvgqe 584
Cdd:cd02753 252 YTPEYAERITGVPAEDIREAARMYATA-----KSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTG-------- 318
|
90
....*....|....*.
gi 2519732638 585 kARPLTGLTNMANALD 600
Cdd:cd02753 319 -VNPLRGQNNVQGACD 333
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
67-378 |
1.54e-10 |
|
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: 65.62 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 67 CTGSCSWKVYVKDGiitweaqETDYPTVGPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPYVR------GLLLEM-YREAK 139
Cdd:cd02763 7 CACRCGIRVHLRDG-------KVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRkgprgsGQFEEIeWEEAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 140 ALYGDPVEAFHSivSDPvKRNRYISARGKGGLVRSTWAEalelvaaaHVHTIKY--YGpdrctGFTPipamsmVSFSAGV 217
Cdd:cd02763 80 SIATKRLKAARA--TDP-KKFAFFTGRDQMQALTGWFAG--------QFGTPNYaaHG-----GFCS------VNMAAGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 218 rfIQLIGGvmtSFYDwyadlpvaspqvFGDQtdvpesgDWWDASYLIMWGSNIPVTRTPDAHWVAEVRYRGTKVVSVSPD 297
Cdd:cd02763 138 --LYSIGG---SFWE------------FGGP-------DLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 298 YADNTKFADEWLPAQAGTDAALAMAMGHVILKENYVDQrveffeDFALTYTDLPFLV--TLETREDGTKVPSKflTAASL 375
Cdd:cd02763 194 RTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDW------EFLKRYTNAAELVdyTPEWVEKITGIPAD--TIRRI 265
|
...
gi 2519732638 376 AGE 378
Cdd:cd02763 266 AKE 268
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
221-337 |
5.10e-10 |
|
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: 63.57 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 221 QLIGGVMTS--FYDWYAD-LP--VASPQVFGDQTDVPeSGDWWDASYLIM-----WGSNIPVTRTPDA-HWVAEVRYRGT 289
Cdd:cd02762 114 ALLKALGTSnyFSAATADqKPghFWSGLMFGHPGLHP-VPDIDRTDYLLIlganpLQSNGSLRTAPDRvLRLKAAKDRGG 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2519732638 290 KVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKENYVDQRV 337
Cdd:cd02762 193 SLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAEGLTDRRF 240
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
769-886 |
7.48e-10 |
|
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: 63.04 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 769 KLDLLVSSDFRMTTTTLLSDVVFPTATWYEKYDISSTDMHPFLHAFSPAIDPPWEAKTDHETFKALAYEFTRQAKKHLGT 848
Cdd:cd02766 356 EDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFEES 435
|
90 100 110
....*....|....*....|....*....|....*...
gi 2519732638 849 RKDIVSVPLLHDTPgqikQPGGHAPDWKNNPDMVGVPG 886
Cdd:cd02766 436 DEEWLDQALDGTGL----PLEGIDLERLLGPRKAGFPL 469
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
1095-1212 |
3.92e-09 |
|
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: 55.84 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 1095 YLTPHNKWAIHSQYFDNQHMLTLfrggQT---AWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVcyVHHA 1171
Cdd:cd02785 6 CIQRHSRFRVHSQFSNVPWLLEL----QPeprVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGV--VTAE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2519732638 1172 Q---ERMMtpktettgkRGGIHNSMTRILLKPTHMIGGYAHQAF 1212
Cdd:cd02785 80 QgwwSRYF---------QEGSLQDLTSPFVNPVHEYIYGPNSAF 114
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
259-379 |
5.09e-09 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. 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: 60.32 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 259 DASYLIMWGSNipvtrTPDAH-----WVAEVR--YRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKEN 331
Cdd:cd02754 157 HADCFFLIGSN-----MAECHpilfrRLLDRKkaNPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEG 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2519732638 332 YVDQ-----RVEFFEDFALTYTDLpflvTLETREDGTKVP-SKFLTAASLAGEK 379
Cdd:cd02754 232 LIDRdfidaHTEGFEELKAFVADY----TPEKVAEITGVPeADIREAARLFGEA 281
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1096-1170 |
1.15e-08 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 54.51 E-value: 1.15e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519732638 1096 LTPHNKWAIHSQYfDNQHMLTL---FRGGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVHH 1170
Cdd:cd02777 6 ISPHPKRRLHSQL-DNVPWLREaykVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALPE 82
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
256-452 |
3.08e-08 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 58.14 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 256 DWWDASYLIMWGSN----IPVtrtPDAHWVAEVRY-RGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILKE 330
Cdd:PRK15488 193 DLANSKYIINFGHNlyegINM---SDTRGLMTAQMeKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 331 N-----YVDQRVEFFEDFALTYTDLpflvTLETREDGTKVPSK--------FLTAASLAGEKHQENAAFKTAMMDRETGe 397
Cdd:PRK15488 270 NlydkaFVERYTSGFEELAASVKEY----TPEWAEAISDVPADdirriareLAAAAPHAIVDFGHRATFTPEEFDMRRA- 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519732638 398 VFIPNGTMGhrysesdqgnwNLELDGrkpilsirDLPQGEAAAV------EIKLPTFDNPK 452
Cdd:PRK15488 345 IFAANVLLG-----------NIERKG--------GLYFGKNASVynklagEKVAPTLAKPG 386
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
56-118 |
5.87e-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: 47.63 E-value: 5.87e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519732638 56 DKEVRSTHGVnCTGSCSWKVYVKDGIITWeaqetdypTVG-PDRPEYEPRGCPRGAAFSWYTYS 118
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVR--------VRGdPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
1126-1174 |
1.53e-06 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 48.27 E-value: 1.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2519732638 1126 MSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYV--HHAQER 1174
Cdd:cd00508 39 IHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMpfHWGGEV 89
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
1094-1168 |
1.84e-06 |
|
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: 48.05 E-value: 1.84e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519732638 1094 RYLTPHNKWAIHSQYFDNQHMLTLfRGGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYV 1168
Cdd:cd02786 4 RLITPPAHNFLNSTFANLPELRAK-EGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVA 77
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
506-835 |
3.27e-06 |
|
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: 51.46 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 506 TPAWQEQITSVPPEAVIRVAREFAQNaidshGRSMIIFGAGICQWYHADTTYRAILALLNLTGCQGRNGGGwahyvgqek 585
Cdd:cd02754 256 TPEKVAEITGVPEADIREAARLFGEA-----RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSG--------- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 586 arPLTgLTNMANAldwsrpprhmiGTGfwymhtdqfRQDGYSTDYLqsPLGKGELKNVHTADVvARStrmgW-MPFYPQF 664
Cdd:cd02754 322 --PFS-LTGQPNA-----------MGG---------REVGGLANLL--PGHRSVNNPEHRAEV-AKF----WgVPEGTIP 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 665 PENSLDlADKAEEAVARGEAKdnadylaqrlnsgdlefsvedvdnpvnwprtlMLWrsnlfgssakgesyflkhLVGSmD 744
Cdd:cd02754 372 PKPGLH-AVEMFEAIEDGEIK--------------------------------ALW------------------VMCT-N 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 745 NVQGADHEESIPREVKwyqdapqgKLDLLVSSD-FRMTTTTLLSDVVFPTATWYEKyDISSTDMHPFLHAFSPAIDPPWE 823
Cdd:cd02754 400 PAVSLPNANRVREALE--------RLEFVVVQDaFADTETAEYADLVLPAASWGEK-EGTMTNSERRVSLLRAAVEPPGE 470
|
330
....*....|..
gi 2519732638 824 AKTDHETFKALA 835
Cdd:cd02754 471 ARPDWWILADVA 482
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
256-336 |
1.75e-05 |
|
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: 49.26 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 256 DWWDASYLIMWG-----SNIPVTRTpdAHWVAEVRYRGT-KVVSVSPDYADNTKFADE---WLPAQAGTDAALAMAMGHV 326
Cdd:cd02758 208 DFDNAEFALFIGtspaqAGNPFKRQ--ARRLAEARTEGNfKYVVVDPVLPNTTSAAGEnirWVPIKPGGDGALAMAMIRW 285
|
90
....*....|
gi 2519732638 327 ILKENYVDQR 336
Cdd:cd02758 286 IIENERYNAE 295
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
1126-1168 |
5.73e-05 |
|
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: 43.72 E-value: 5.73e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2519732638 1126 MSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYV 1168
Cdd:cd02791 39 IHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFV 81
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1096-1165 |
1.04e-04 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 43.39 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519732638 1096 LTPHNKWAIHSQYFDNQHMLTL-FRGGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGV 1165
Cdd:cd02793 6 LSNQPATRLHSQLDHGSLSRAYkVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGV 76
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
67-329 |
1.11e-04 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. 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: 46.62 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 67 CTGSCSWKVYVKDGIITweAQETDyptvgPDRPEYEPRGCPRGAAFSWYTYSPTRVKYPyvrgllleMYREAKALYGDPV 146
Cdd:cd02752 7 CSVGCGLIAYVQNGVWV--HQEGD-----PDHPVNRGSLCPKGAALRDFVHSPKRLKYP--------MYRAPGSGKWEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 147 ---EAFHSIvSDPVK--RNRYISARGKGGLVRSTWAEALELVAAAHVHTIKYYgpdrCTGFTPIPAMSMVSFSAGVRFIQ 221
Cdd:cd02752 72 swdEALDEI-ARKMKdiRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYL----IRKFARALGTNNLDHQARIUHSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519732638 222 LIGGVMTSFYdwyadlpvaspqvFGDQTDvpesgDWWD---ASYLIMWGSNipvtrTPDAH-----WVAEVR-YRGTKVV 292
Cdd:cd02752 147 TVAGLANTFG-------------RGAMTN-----SWNDiknADVILVMGGN-----PAEAHpvsfkWILEAKeKNGAKLI 203
|
250 260 270
....*....|....*....|....*....|....*..
gi 2519732638 293 SVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVILK 329
Cdd:cd02752 204 VVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYIIR 240
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
1097-1170 |
1.43e-04 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 42.66 E-value: 1.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519732638 1097 TPHNKWAIHSQYFDNQHMLTLFRggQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVHH 1170
Cdd:cd02794 7 GWHYKRRTHSTFDNVPWLREAFP--QEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQ 78
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
1126-1169 |
1.43e-04 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 42.65 E-value: 1.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2519732638 1126 MSPQDAEKIGVKDGEWIECVNTNGVFVGRAV-----VSHRMPEGVCYVH 1169
Cdd:cd02787 35 MNPDDIARLGLKAGDRVDLESAFGDGQGRIVrgfrvVEYDIPRGCLAAY 83
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
769-841 |
2.57e-04 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 45.43 E-value: 2.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519732638 769 KLDLLVSSDFRMTTTTLLSDVVFPTATWYEKYDISSTDMHPF--LHAFSPAIDPPWEAKTDHETFKALAYEFTRQ 841
Cdd:PRK15102 494 KLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNrgIIAMKKVVEPLFESRSDFDIFRELCRRFGRE 568
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
1124-1165 |
4.18e-04 |
|
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: 41.90 E-value: 4.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2519732638 1124 AWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGV 1165
Cdd:cd02780 32 VWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGV 73
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
1123-1170 |
4.73e-04 |
|
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: 41.53 E-value: 4.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2519732638 1123 TAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVHH 1170
Cdd:cd02781 34 VAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEH 81
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
1125-1169 |
5.80e-04 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 44.28 E-value: 5.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2519732638 1125 WMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYVH 1169
Cdd:PRK15102 713 YINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIH 757
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
506-575 |
5.84e-04 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 44.27 E-value: 5.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2519732638 506 TPAWQEQITSVPPEAVIRVAREFAQNAidshGRSMIIFGagicqwyHADTTY-------RAILALLNLTGCQGRNGG 575
Cdd:PRK15488 295 TPEWAEAISDVPADDIRRIARELAAAA----PHAIVDFG-------HRATFTpeefdmrRAIFAANVLLGNIERKGG 360
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
1126-1168 |
1.49e-03 |
|
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: 39.53 E-value: 1.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2519732638 1126 MSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYV 1168
Cdd:cd02790 39 INPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFM 81
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
1126-1168 |
3.31e-03 |
|
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: 38.74 E-value: 3.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2519732638 1126 MSPQDAEKIGVKDGEWIECVNTNGVFVGRAVVSHRMPEGVCYV 1168
Cdd:cd02792 39 ISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGI 81
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
1094-1157 |
4.35e-03 |
|
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: 38.41 E-value: 4.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519732638 1094 RYLTPHNKWAIHSQYFDNQHMLTLfRGGQTAWMSPQDAEKIGVKDGEWIECVNTNGVFVGRAVV 1157
Cdd:cd02778 3 RLIYGKSPVHTHGHTANNPLLHEL-TPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARL 65
|
|
| |
