|
Name |
Accession |
Description |
Interval |
E-value |
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
2-1235 |
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: 2516.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 2 SKLLDKLRYFKqKGSTFSDGHGQEMDSNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 81
Cdd:COG5013 6 SHLLDRLRFFR-RGEVFSDGHGVTTEGGREWEDFYRDRWQHDKVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTDYPRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 82 RPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRKQLIRLWREALQQFSDPVEAWDSIVRDEKKATSYKQARGKGGFVRS 161
Cdd:COG5013 85 GPDLPNYEPRGCPRGASFSWYTYSPTRVKYPYVRGVLLELWREARARHGDPVEAWASIVEDPEKRRRYKSARGKGGFVRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 162 DWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMSMVSYAAGTRYLSLMGGTCLSFYDWYCDLPPASPMTWGEQTDVPES 241
Cdd:COG5013 165 TWDEANEIIAAANVYTIKKYGPDRVAGFSPIPAMSMVSYAAGARFLSLIGGVMLSFYDWYADLPPASPQVWGEQTDVPES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 242 ADWYNSAYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKEFHLD 321
Cdd:COG5013 245 ADWYNSGYLIMWGSNVPQTRTPDAHFMTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEFHVD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 322 NPSDYFINYCRRYTDMPMLVMLEETDkGYYSAGRLLRAADLVDNLGESNNPDWKTVAFDS-DGQLVVPNGSAGFRWG-QK 399
Cdd:COG5013 325 RQVPYFTDYARRYTDLPFLVTLEERD-GGYVPGRFLRASDLGGALGESNNPEWKTVVLDEaTGEPVVPNGSIGFRWGeSE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 400 GKWNLEAR-AAGQQTELRLSLAEGYDQLAEVAFPYFGGQPspyfrhvEQSPVLVHKLPVREISLADGRRaKAVSVYDLTL 478
Cdd:COG5013 404 GKWNLELKdATGADVDPALSLLDDHDEVVEVAFPYFGGET-------GGGGVLRRGVPVRRVTLADGEV-LVTTVFDLML 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 479 ANYGVGRGFDDsNTAGSYDEVKAYSPAWAEQICGVPRQQIIRIAREFADTAHKTHGRSMIIVGAGMNHWYHMDMNYRGLI 558
Cdd:COG5013 476 ANYGVDRGLPG-NWPTGYDDDVPYTPAWQEKITGVPREQVIRVAREFAQNAEKTRGRSMIIMGAGTNHWYHSDMIYRAIL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 559 NMLIFCGCVGQTGGGWAHYVGQEKLRPQTGWQPLAFALDWARPPRHMNSTSFFYNHSSQWRYEKLSVKELLSPLANPQDF 638
Cdd:COG5013 555 NLLMLCGCQGVNGGGWAHYVGQEKLRPQTGWQPLAFALDWSRPPRQMNGTSFFYAHTDQWRYETLSADELLSPLADGKFW 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 639 AGQLIDFNVRAERMGWLPSSPQLNTNPLTIAAKAKESGLSPADYTAKALQQGELRFASEQPDNGNNHPRNLFVWRSNLLG 718
Cdd:COG5013 635 GGHLADYNVRAARLGWLPSYPQFNRNPLDLADEAEAAGMEPADYVVDQLKSGELKFACEDPDNPENFPRNLFVWRSNLLG 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 719 SSAKGHEYMLRYLLGIESGIQGSETVadPEMSPQEVDWQTPAREGKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMN 798
Cdd:COG5013 715 SSGKGHEYFLKHLLGTDNGVQGEELG--PGLRPREVVWRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKHDLS 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 799 TSDMHPFIHPLSAAIDPVWESRSDWEIYKDIAKTFSALCPGHLGVENDVVLLPVQHDSPAEIAQPY-DVKQWHKGECELQ 877
Cdd:COG5013 793 TTDMHPFIHPFSPAVDPPWEARSDWDIFKGIAKKFSELAAGHLGVRKDVVATPLQHDTPGELAQPFgDVKDWKKGECEPI 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 878 PGKTAPHIMLVERDYPALSERFMSIGPLMEKLGNGGKGISWNTDKEIHLLRQLNHTHTR-GAGKGQPQLNSAIDAAEMIL 956
Cdd:COG5013 873 PGKTMPKLVVVERDYPAIYEKFTSLGPLLEKLGNGGKGITWDTEEEVEELGKLNGVVREeGVAKGRPRLDTDIDAAEAIL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 957 TLAPETNGQVAVKAWQALGEITGRDHTHLALPKQEEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNACYTNVHELIPWR 1036
Cdd:COG5013 953 ALSPETNGHVAVKAWKALEKRTGRDLAHLAAGREEEKIRFRDIQAQPRKVITSPTWSGSESGGRRYSAFTTNVEELIPWR 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1037 TLTGRQQLYQDHPWMRGFGESLVSYRPPVNTRSVEQMSHIPSNGYPEKILNFLTPHQKWGIHSTYSENLLMLTLSRGGPI 1116
Cdd:COG5013 1033 TLTGRQHFYLDHDWMREFGEGLPVYRPPLDMKTLFGEPGIGPNGNPEIVLRYLTPHQKWGIHSTYQDNLLMLTLSRGGPT 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1117 VWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMMYHAQERITNIPGSEVTGMRGGIHNSVTRISPKPTH 1196
Cdd:COG5013 1113 VWMSEEDAAKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHAQERIVNVPGSEITGKRGGIHNSVTRIVLKPTH 1192
|
1210 1220 1230
....*....|....*....|....*....|....*....
gi 2729246587 1197 MIGGYVHQSYGFNYYGTVGSNRDEFIIVRKMKNILWLDD 1235
Cdd:COG5013 1193 MIGGYAQLSYGFNYYGPTGNQRDEVVVVRKRSQVDWLED 1231
|
|
| narG |
TIGR01580 |
respiratory nitrate reductase, alpha subunit; The Nitrate reductase enzyme complex allows ... |
2-1234 |
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: 2250.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 2 SKLLDKLRYFKQKGSTFSDGHGQEMDSNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 81
Cdd:TIGR01580 1 SKLLDRLRYFKQKGETFSDGHGQTLNENRDWENVYRQRWQYDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 82 RPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRKQLIRLWREALQQFSDPVEAWDSIVRDEKKATSYKQARGKGGFVRS 161
Cdd:TIGR01580 81 RPDLPNHEPRGCPRGASYSWYIYSANRLKYPMMRKRLMKLWREAKQTHSDPVEAWASIVENADKAKSYKQARGRGGFVRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 162 DWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMSMVSYAAGTRYLSLMGGTCLSFYDWYCDLPPASPMTWGEQTDVPES 241
Cdd:TIGR01580 161 SWQEVNELIAASNVYTVKNYGPDRVVGFSPIPAMSMVSYASGSRYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 242 ADWYNSAYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKEFHLD 321
Cdd:TIGR01580 241 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAALALAMGHVILREFHLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 322 NPSDYFINYCRRYTDMPMLVMLEETDkGYYSAGRLLRAADLVDNLGESNNPDWKTVAFDSDGQLVVPNGSAGFRWGQKGK 401
Cdd:TIGR01580 321 NPSQYFTEYAKRYTDMPMLVMLEERD-GYYAAGRFLRAADLVDALGQENNPEWKTVAFDTNGEMVAPQGSIGFRWGEKGK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 402 WNLEAR--AAGQQTELRLSLAEGYDQLAEVAFPYFGGQPSPYFRHVEQSPVLVHKLPVREISLADGRRAKAVSVYDLTLA 479
Cdd:TIGR01580 400 WNLEQRdgKTGEEIELQLSLLGSQDEIAEVGFPYFGGDGTEHFNKVEGENVLLRKLPVKRLQLADGSTALVTTVFDLTLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 480 NYGVGRGFDDSNTAGSYDEVKAYSPAWAEQICGVPRQQIIRIAREFADTAHKTHGRSMIIVGAGMNHWYHMDMNYRGLIN 559
Cdd:TIGR01580 480 NYGLERGLGDVNCATSYDDVKAYTPAWQEQITGVSREQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLIN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 560 MLIFCGCVGQTGGGWAHYVGQEKLRPQTGWQPLAFALDWARPPRHMNSTSFFYNHSSQWRYEKLSVKELLSPLANPQDFA 639
Cdd:TIGR01580 560 MLILCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPPRHMNGTSFFYNHSSQWRYETVTAEDLLSPMADKSRYT 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 640 GQLIDFNVRAERMGWLPSSPQLNTNPLTIAAKAKESGLSPADYTAKALQQGELRFASEQPDNGNNHPRNLFVWRSNLLGS 719
Cdd:TIGR01580 640 GHLIDYNVRAERMGWLPSAPQLNTNPLTIAGEAEKAGMNPVDYVVKSLQEGSLRFAAEQPDNGVNFPRNLFIWRSNLLGS 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 720 SAKGHEYMLRYLLGIESGIQGSETVADPEMSPQEVDWQTPAREGKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNT 799
Cdd:TIGR01580 720 SGKGHEYMLKYLLGTENGIMNKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRMSSTCLYSDIVLPTATWYEKDDMNT 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 800 SDMHPFIHPLSAAIDPVWESRSDWEIYKDIAKTFSALCPGHLGVENDVVLLPVQHDSPAEIAQPYDVKQWHKGECELQPG 879
Cdd:TIGR01580 800 SDMHPFIHPLSAAIDPAWESKSDWEIYKAIAKAFSEVCVGHLGKEKDIVTLPLQHDSAAELAQPFGVKDWKKGECDLIPG 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 880 KTAPHIMLVERDYPALSERFMSIGPLMEKLGNGGKGISWNTDKEIHLLRQLNHTHTRGA-GKGQPQLNSAIDAAEMILTL 958
Cdd:TIGR01580 880 KTAPNIQVVERDYPAIYERFTSLGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKAEGSpAKGQPMINTAIDAAEMILTL 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 959 APETNGQVAVKAWQALGEITGRDHTHLALPKQEEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNACYTNVHELIPWRTL 1038
Cdd:TIGR01580 960 APETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTL 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1039 TGRQQLYQDHPWMRGFGESLVSYRPPVNTRSVEQMSHIPSNGYPEKILNFLTPHQKWGIHSTYSENLLMLTLSRGGPIVW 1118
Cdd:TIGR01580 1040 TGRQQLYQDHQWMRDFGESLLVYRPPIDTRSFKEVIGQKSNGNQEIVLNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVW 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1119 MSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMMYHAQERITNIPGSEVTGMRGGIHNSVTRISPKPTHMI 1198
Cdd:TIGR01580 1120 LSEADAKDLGIADNDWIECFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNVPGSEITQQRGGIHNSVTRITPKPTHMI 1199
|
1210 1220 1230
....*....|....*....|....*....|....*.
gi 2729246587 1199 GGYVHQSYGFNYYGTVGSNRDEFIIVRKMKNILWLD 1234
Cdd:TIGR01580 1200 GGYAQLAYGFNYYGTVGSNRDEFVVVRKMKNVDWLD 1235
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
43-833 |
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: 668.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 43 DKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRKQlirlw 122
Cdd:cd02750 1 DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 123 realqqfsdpveawdsivrdekkatsykqARGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMSMVSYAA 202
Cdd:cd02750 76 -----------------------------ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 203 GTRYLSLMGGTCLSFYDWYCDLPPASPMTWGEQTDVPESADWYNSAYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAIT 282
Cdd:cd02750 127 GSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 283 PDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKEFHLDNpsdyfiNYCRRYTDMPMLVmleetdkgyysagrllraadl 362
Cdd:cd02750 207 PDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDE------DYLKEYTDLPFLV--------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 363 vdnlgesnnpdwktvafdsdgqlvvpngsagfrwgqkgkwnlearaagqqtelrlslaegydqlaevafpyfggqpspyf 442
Cdd:cd02750 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 443 rhveqspvlvhklpvreisladgrrakavsvydltlanygvgrgfddsntagsydevkaYSPAWAEQICGVPRQQIIRIA 522
Cdd:cd02750 260 -----------------------------------------------------------YTPAWQEAITGVPRETVIRLA 280
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 523 REFADTahkthGRSMIIVGAGMNHWYHMDMNYRGLINMLIFCGCVGQTGGGWAHYVGQeklrpqtgwqplafaldwarpp 602
Cdd:cd02750 281 REFATN-----GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQ---------------------- 333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 603 rhmnstsffynhssqwryeklsvkellsplanpqdfagqlidfnvraermgwlpsspqlntnpltiaakakesglspady 682
Cdd:cd02750 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 683 takalqqgelrfaseqpdngnnhPRNLFVWRSNLLGSSAKGHEYMlryllgiesgiqgsetvadpemspqevdwqTPARE 762
Cdd:cd02750 334 -----------------------PRVLFVWRGNLFGSSGKGHEYF------------------------------EDAPE 360
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2729246587 763 GKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAIDPVWESRSDWEIYKDIAKTF 833
Cdd:cd02750 361 GKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
1086-1225 |
6.94e-78 |
|
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: 252.68 E-value: 6.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1086 LNFLTPHQKWGIHSTYSENLLMLTLSRGGPIVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMMYHAQ 1165
Cdd:cd02776 2 LNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1166 ERITNIPGSEVTGMRGGIHNSVTRISPKPTHMIGGYVHQSYGFNYYGTVGSNRDEFIIVR 1225
Cdd:cd02776 82 ERHVNVPGSKLTGKRGGIHNSVTRVRIKPTHLVGGYGQLSYGFNYYGPTGVNRDTRVVVR 141
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-1188 |
2.93e-56 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 208.16 E-value: 2.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 43 DKIVRSTHgVNCTGSCSWKIYVKNGLVTWetQQTDyprtrPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRKQlirlw 122
Cdd:COG0243 21 TKTVKTTC-PGCGVGCGLGVKVEDGRVVR--VRGD-----PDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVG----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 123 realqqfsdpveawdsivrdekkatsykqARGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMSMVSYAA 202
Cdd:COG0243 88 -----------------------------PRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 203 GTRYLSLMG--GTcLSFYDW--YCDLP--PASPMTWGEQTDVPESADWYNSAYIIAWGSNVPQTRTPDAHFFTE-VRYKG 275
Cdd:COG0243 139 AYLAQRFARalGT-NNLDDNsrLCHESavAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKRG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 276 TKTVAITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKEFHLDnpsdyfINYCRRYTDmpmlvmleetdkgyysagr 355
Cdd:COG0243 218 AKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYD------RDFLARHTV------------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 356 llraadlvdnlgesnnpdwktvafdsdgqlvvpngsagfrwgqkgkwnlearaagqqtelrlslaeGYDQLAEvafpyfg 435
Cdd:COG0243 273 ------------------------------------------------------------------GFDELAA------- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 436 gqpspyfrhveqspvlvhklpvreisladgrrakavsvydltlanygvgrgfddsntagsydEVKAYSPAWAEQICGVPR 515
Cdd:COG0243 280 --------------------------------------------------------------YVAAYTPEWAAEITGVPA 297
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 516 QQIIRIAREFAdtahkTHGRSMIIVGAGMNHWYHMDMNYRGLINMLIFCGCVGQTGGGWahyvgqeklrpqtgwqplafa 595
Cdd:COG0243 298 EDIRELAREFA-----TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGP--------------------- 351
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 596 ldwarpprhmnstsffynhssqwryeklsvkellsplanpqdfagqlidFNVRAERMgwlpsspqlntnpltiaakakES 675
Cdd:COG0243 352 -------------------------------------------------FSLTGEAI---------------------LD 361
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 676 GLspaDYTAKAlqqgelrfaseqpdngnnhprnLFVWRSNLLGS---SAKGHEyMLRyllgiesgiqgsetvadpemspq 752
Cdd:COG0243 362 GK---PYPIKA----------------------LWVYGGNPAVSapdTNRVRE-ALR----------------------- 392
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 753 evdwqtparegKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAIDPVWESRSDWEIYKDIAKt 832
Cdd:COG0243 393 -----------KLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAK- 460
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 833 fsalcpgHLGVEndvvllpvqhdspAEIAQPYDVKQWHKGECElqpgktaphimlverdypalserfmsigplmeklGNG 912
Cdd:COG0243 461 -------RLGFE-------------EAFPWGRTEEDYLRELLE----------------------------------ATR 486
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 913 GKGISWntdkeihllrqlnhthtrgagkgqpqlnsaidaaemiltlapetngqvavKAWQALGeitgrdhtHLALPKQEE 992
Cdd:COG0243 487 GRGITF--------------------------------------------------EELREKG--------PVQLPVPPE 508
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 993 KiRFRdiqaqprkiissptwsglEDEhvsynacytnvheliPWRTLTGRQQLYQDHPWMRGfgesLVSYRPPVNTRSVeq 1072
Cdd:COG0243 509 P-AFR------------------NDG---------------PFPTPSGKAEFYSETLALPP----LPRYAPPYEGAEP-- 548
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1073 mshiPSNGYPekiLNFLTPHQKWGIHSTYSeNLLMLTLSRGGPIVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQ 1152
Cdd:COG0243 549 ----LDAEYP---LRLITGRSRDQWHSTTY-NNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTE 620
|
1130 1140 1150
....*....|....*....|....*....|....*.
gi 2729246587 1153 RVPAGMTMMYHAQeritnipGSEVTGMRGGIHNSVT 1188
Cdd:COG0243 621 GIRPGVVFAPHGW-------WYEPADDKGGNVNVLT 649
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-831 |
5.42e-51 |
|
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: 184.84 E-value: 5.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 47 RSTHgVNCTGSCSWKIYVKNGLVTWEtqqtdypRTRPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRKqlirlwreal 126
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRI-------EGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRV---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 127 qqfsdpveawdsivrdekkatsykqaRGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMSMVSYAAGTRY 206
Cdd:cd00368 63 --------------------------GGRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 207 LSLMGGTcLSFYDWYCDLPPASPMTW-GEQTDVPESADWYNSAYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDY 285
Cdd:cd00368 117 RALGSNN-VDSHARLCHASAVAALKAfGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 286 AEVAKLSDHWLAPKQGTdaalamamghvilkefhldnpsdyfinycrrytdmpmlvmleetdkgyysagrllraadlvdn 365
Cdd:cd00368 196 TETAAKADEWLPIRPGT--------------------------------------------------------------- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 366 lgesnnpdwktvafdsdgqlvvpngsagfrwgqkgkwnlearaagqqtelrlslaegydqlaevafpyfggqpspyfrhv 445
Cdd:cd00368 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 446 eqspvlvhklpvreisladgrrakavsvyDLTLANYgvgrgfddsntagsydevkayspAWAEQICGVPRQQIIRIAREF 525
Cdd:cd00368 213 -----------------------------DAALALA-----------------------EWAAEITGVPAETIRALAREF 240
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 526 AdtahkTHGRSMIIVGAGMNHWYHMDMNYRGLINMLIFCGCVGQTGGGWAHyvgqeklrpqtgwqplafaldwarpprhm 605
Cdd:cd00368 241 A-----AAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP----------------------------- 286
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 606 nstsffynhssqwryeklsvkellsplanpqdfagqlidfnvraermgwlpsspqlNTNPLTIAAkakesglsPADYTAK 685
Cdd:cd00368 287 --------------------------------------------------------GGNPLVSAP--------DANRVRA 302
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 686 ALQqgelrfaseqpdngnnhprnlfvwrsnllgssakgheymlryllgiesgiqgsetvadpemspqevdwqtparegKL 765
Cdd:cd00368 303 ALK---------------------------------------------------------------------------KL 307
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2729246587 766 DLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSdMHPFIHPLSAAIDPVWESRSDWEIYKDIAK 831
Cdd:cd00368 308 DFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTN-TEGRVQLFRQAVEPPGEARSDWEILRELAK 372
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
48-833 |
3.65e-43 |
|
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: 166.89 E-value: 3.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 48 STHGVNCTGSCSWKIYVKNGLVTWETQQtdyprtrpDLPNHE-PRGCPRGASYSWYIYSANRLKYPLVRKQlirlwreal 126
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPN--------EWPDKTyKRGCTRGLSHLQRVYSPDRLKYPMKRVG--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 127 qqfsdpveawdsivrdekkatsykqARGKGGFVRSDWNELNQLIAAANIWTVKNYGPdRVAGFSpipAMSMVSYAAGTRY 206
Cdd:cd02765 65 -------------------------ERGEGKFERITWDEALDTIADKLTEAKREYGG-KSILWM---SSSGDGAILSYLR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 207 LSLMGGTCLSFYDWYCDLPPASPMT----WGEQTDVPESADWYNSAYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAIT 282
Cdd:cd02765 116 LALLGGGLQDALTYGIDTGVGQGFNrvtgGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVID 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 283 PDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKEFHLDNPsdyfinYCRRYTDMPMLVmlEETDkgyysaGRLLRAADL 362
Cdd:cd02765 196 PVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEA------FLKSNTSAPFLV--REDN------GTLLRQADV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 363 VDNLGESNnpdwkTVAFDSDGQLVVPNGSAGFRWGQKGKWNLEAraagqqtelrlslaegydqlaevafpyfggqpspyf 442
Cdd:cd02765 262 TATPAEDG-----YVVWDTNSDSPEPVAATNINPALEGEYTING------------------------------------ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 443 rhveqspVLVHklpvreisladgrrakavSVYDLTLanygvgrgfddsntagsyDEVKAYSPAWAEQICGVPRQQIIRIA 522
Cdd:cd02765 301 -------VKVH------------------TVLTALR------------------EQAASYPPKAAAEICGLEEAIIETLA 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 523 REFAdtahkTHGRSMIIVGAGMNHWYHMDMNYRGLINMLIFCGCVGQTGGGwahyVGQEKlrpqtgwqplafaldwarpp 602
Cdd:cd02765 338 EWYA-----TGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG----VGQIK-------------------- 388
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 603 rhmnstsFFYNHSSqwryeklsvkellsplanpqDFAGQLIDFNVRAErmgWLPsspqlntnpltiaakakesglspady 682
Cdd:cd02765 389 -------FMYFMGS--------------------NFLGNQPDRDRWLK---VMK-------------------------- 412
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 683 takalqqgelrfaseqpdngnnhprnlfvwrsnllgssakgheymlryllgiesgiqgsetvadpemspqevdwqtpare 762
Cdd:cd02765 --------------------------------------------------------------------------------
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2729246587 763 gKLDLLVTLDFRMSSTCLFSDIVLPTATWYE-KDDMNTSDMHPFIHPLSAAIDPVWESRSDWEIYKDIAKTF 833
Cdd:cd02765 413 -NLDFIVVVDIFHTPTVRYADIVLPAAHWFEvEDLLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERL 483
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
57-844 |
1.89e-37 |
|
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: 150.07 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 57 SCSW---KIYVKNGLVTwetqqtdypRTRPDlPNHEPRGCPRGASYSWYIYSANRLKYPLVRKQlirlWREalqqfsdpv 133
Cdd:cd02751 3 ACHWgpfKAHVKDGVIV---------RVEPD-DTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVG----WLG--------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 134 eawdsivRDEKKatsyKQARGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRV-----AGFSP---IPAMSMVSyaagtR 205
Cdd:cd02751 60 -------NGPGS----RELRGEGEFVRISWDEALDLVASELKRIREKYGNEAIfggsyGWASAgrlHHAQSLLH-----R 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 206 YLSLMGGTCLSF--YDWYCdLPPASPMTWG------EQTDVPESADwyNSAYIIAWGSNVPQTR--------TPDAHFFT 269
Cdd:cd02751 124 FLNLIGGYLGSYgtYSTGA-AQVILPHVVGsdevyeQGTSWDDIAE--HSDLVVLFGANPLKTRqgggggpdHGSYYYLK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 270 EVRYKGTKTVAITPDYAEVAK-LSDHWLAPKQGTDAALAMAMGHVILKEfhldnpsdyfinycrrytdmpmlvmleetdk 348
Cdd:cd02751 201 QAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITE------------------------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 349 gyysagrllraadlvdNLgesnnpdwktvafdsdgqlvvpngsagfrwgqkgkwnlearaagqqtelrlslaegYDQlae 428
Cdd:cd02751 250 ----------------DL--------------------------------------------------------HDQ--- 254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 429 vAFpyfggqpspyfrhveqspvlvhklpvreisladgrrakavsvydltLANYGVgrGFDD--SNTAGSYDEVkAYSPAW 506
Cdd:cd02751 255 -AF----------------------------------------------LARYTV--GFDEfkDYLLGESDGV-PKTPEW 284
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 507 AEQICGVPRQQIIRIAREFADTahkthgRSMIIVGAGMNHWYHMDMNYRGLINMLIFCGCVGQTGGGWAHYVGQeklrpQ 586
Cdd:cd02751 285 AAEITGVPAETIRALAREIASK------RTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGY-----S 353
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 587 TGWQPLAFALDWARPPRHMNSTSFFynhssqwryekLSVKELLSPLANPqdfaGQLIDFNVRAE-----RMGWlpsspQL 661
Cdd:cd02751 354 NGGGPPRGGAGGPGLPQGKNPVKDS-----------IPVARIADALLNP----GKEFTANGKLKtypdiKMIY-----WA 413
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 662 NTNPltiaakakesglspadytakalqqgelrFASEQPDNgnnhpRNLFVWRsnllgssakgheymlryllgiesgiqgs 741
Cdd:cd02751 414 GGNP----------------------------LHHHQDLN-----RLIKALR---------------------------- 432
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 742 etvadpemspqevdwqtparegKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTS--DMHPFIHPLSAAIDPVWES 819
Cdd:cd02751 433 ----------------------KDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTgnYSNRYLIAMKQAVEPLGEA 490
|
810 820
....*....|....*....|....*
gi 2729246587 820 RSDWEIYKDIAKtfsalcpgHLGVE 844
Cdd:cd02751 491 RSDYEIFAELAK--------RLGVE 507
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
153-325 |
2.28e-35 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 138.69 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 153 RGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVA-GFSPIPAMSMVSYAAGTRYLSLMGGTCLSFYDWYCDLPPASPMT 231
Cdd:pfam00384 9 RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAiNGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNGDLCTAAAAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 232 WG-----EQTDVPESADWYNSAYIIAWGSNVPQTRTPD-AHFFTEVRYKGTKTVAITPDYAevAKLSDHWLAPKQGTDAA 305
Cdd:pfam00384 89 FGsdlrsNYLFNSSIADIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRLD--LTYADEHLGIKPGTDLA 166
|
170 180
....*....|....*....|
gi 2729246587 306 LAMAMGHVILKEFHLDNPSD 325
Cdd:pfam00384 167 LALAGAHVFIKELKKDKDFA 186
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
52-845 |
2.34e-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: 131.68 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 52 VNCTGSCSWKIYVKNGLVTW-ETQQTdyprTRPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRKQlirlwrealqqfs 130
Cdd:cd02770 6 VNCGGRCPLKAHVKDGVITRiETDDT----GDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVG------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 131 dpveawdsivrdekkatsykqARGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVagfspipamsMVSYAAGT------ 204
Cdd:cd02770 69 ---------------------KRGEGKFVRISWDEALDTIASELKRIIEKYGNEAI----------YVNYGTGTyggvpa 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 205 ------RYLSLMGGTcLSFYDWYC--DLPPASPMTWGEQTDVPESADWYNSAYIIAWGSNVPQTR---TPDAHFFTEVRY 273
Cdd:cd02770 118 grgaiaRLLNLTGGY-LNYYGTYSwaQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRmggGGSTYYYLQAKK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 274 KGTKTVAITPDYAEVAK-LSDHWLAPKQGTDAALAMAMGHVILKEfhldNPSDY-FINYCrrytdmpmlvmleetdkgyy 351
Cdd:cd02770 197 AGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITE----NLHDQaFLDRY-------------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 352 sagrllraadlvdnlgesnnpdwkTVAFDSDgqlvvpngsagfrwgqkgkwnlearaagqqtelrlSLAEGYDqlaevaf 431
Cdd:cd02770 253 ------------------------CVGFDAE-----------------------------------HLPEGAP------- 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 432 pyfggqPSPYFRhveqspvlvhklpvreisladgrrakavsvydltlaNYGVGRGfddsntagsYDEVkAYSPAWAEQIC 511
Cdd:cd02770 267 ------PNESYK------------------------------------DYVLGTG---------YDGT-PKTPEWASEIT 294
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 512 GVPRQQIIRIAREFADTAhkthgRSMIIVGAGMNHWYHMDMNYRGLINMLIFCGCVGQTGGGwahyvgqeklrpqTGwqp 591
Cdd:cd02770 295 GVPAETIRRLAREIATTK-----PAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-------------TG--- 353
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 592 lafaldwARPprhmnstsffYNHSSQwryeklsvkellsplanpqdfagqlidfnvraerMGWLPSSPqlntNPLtiaaK 671
Cdd:cd02770 354 -------ARP----------GGSAYN----------------------------------GAGLPAGK----NPV----K 374
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 672 AKESGLSPADytakALQQGELRFASEQPDNGNNHPRN----LFVWRSNllgssakgheymlrYLLGIESGI-QGSETVAD 746
Cdd:cd02770 375 TSIPCFMWTD----AIERGEEMTADDGGVKGADKLKSnikmIWNYAGN--------------TLINQHSDDnNTTRALLD 436
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 747 pemspqevdwqtpaREGKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDM----NTSDMHPFIHpLSAAIDPVWESRSD 822
Cdd:cd02770 437 --------------DESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIvltsNAGMMEYLIY-SQKAIEPLYECKSD 501
|
810 820
....*....|....*....|...
gi 2729246587 823 WEIYKDIAKtfsalcpgHLGVEN 845
Cdd:cd02770 502 YEICAELAK--------RLGVED 516
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
54-335 |
5.38e-23 |
|
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: 104.31 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 54 CTGSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP---RGCPRGASYSWYIYSANRLKYPLVRKQlirlwrealqqfs 130
Cdd:cd02759 7 CHSGCGVLVYVKDGKLV---------KVEGD-PNHPTnkgRLCMRGLAAPEIVYHPDRLLYPLKRVG------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 131 dpveawdsivrdekkatsykqARGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMSMVSYAAGT-RYLSL 209
Cdd:cd02759 64 ---------------------ERGENKWERISWDEALDEIAEKLAEIKAEYGPESIATAVGTGRGTMWQDSLFWiRFVRL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 210 MGGTCLSFYDWYCDLPPASPMTWGEQT-DVPESADWYNSAYIIAWGSNvPQTRTPD--AHFFTEVRYKGTKTVAITPDYA 286
Cdd:cd02759 123 FGSPNLFLSGESCYWPRDMAHALTTGFgLGYDEPDWENPECIVLWGKN-PLNSNLDlqGHWLVAAMKRGAKLIVVDPRLT 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2729246587 287 EVAKLSDHWLAPKQGTDAALAMAMGHVILKEFHLD--------NPSDYFINYCRRYT 335
Cdd:cd02759 202 WLAARADLWLPIRPGTDAALALGMLNVIINEGLYDkdfvenwcYGFEELAERVQEYT 258
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
54-341 |
6.86e-23 |
|
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: 103.53 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 54 CTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLpnheprgCPRGASYSWYIYSANRLKYPLVRkqlirlwrealqqfsdpV 133
Cdd:cd02755 8 CSSRCGILARVEDGRVVKIDGNPLSPLSRGKL-------CARGNAGIQLLYDPDRLKKPLIR-----------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 134 EAwdsivrdekkatsykqaRGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMS--MVSYAAGT---RYLS 208
Cdd:cd02755 64 GE-----------------RGEGKFREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYSpfFKHFAAAFgspNIFS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 209 LMGgTCLSFYDWYCDLppaspMTWGEQTDVPesADWYNSAYIIAWGSNV-PQTRTPDAHFFTEVRYKGTKTVAITPDYAE 287
Cdd:cd02755 127 HES-TCLASKNLAWKL-----VIDSFGGEVN--PDFENARYIILFGRNLaEAIIVVDARRLMKALENGAKVVVVDPRFSE 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2729246587 288 VAKLSDHWLAPKQGTDAALAMAMGHVILKEFHLDnpsDYFInycRRYTDMPMLV 341
Cdd:cd02755 199 LASKADEWIPIKPGTDLAFVLALIHVLISENLYD---AAFV---EKYTNGFELL 246
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-860 |
2.31e-21 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 100.34 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 43 DKIVRST---HGVnctgSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP-RG--CPRGASYSWYIYSANRLKYPLVRK 116
Cdd:COG3383 4 MKKVKTVcpyCGV----GCGIDLEVKDGKIV---------KVEGD-PDHPVnRGrlCVKGRFGFEFVNSPDRLTTPLIRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 117 qlirlwrealqqfsdpveawdsivrdekkatsykqargKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVAGFSpipams 196
Cdd:COG3383 70 --------------------------------------GGEFREVSWDEALDLVAERLREIQAEHGPDAVAFYG------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 197 mvS--------YAA--------GTRYLSLMGGTCLSfydwycdlppasPMTWGEQTDVPESA------DWYNSAYIIAWG 254
Cdd:COG3383 106 --SgqltneenYLLqklargvlGTNNIDNNARLCMA------------SAVAGLKQSFGSDAppnsydDIEEADVILVIG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 255 SNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKEfhldnpsdyfinycrry 334
Cdd:COG3383 172 SNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEE----------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 335 tdmpmlvmleetdkgyysagrllraaDLVDNlgesnnpdwktvAFdsdgqlvvpngsagfrwgqkgkwnLEARAagqqte 414
Cdd:COG3383 235 --------------------------GLVDE------------DF------------------------IAERT------ 246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 415 lrlslaEGYDQLAEVafpyfggqpspyfrhveqspvlvhklpvreisladgrrakavsvydltlanygvgrgfddsntag 494
Cdd:COG3383 247 ------EGFEELKAS----------------------------------------------------------------- 255
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 495 sydeVKAYSPAWAEQICGVPRQQIIRIAREFAdtahkTHGRSMIIVGAGMNHWYHMDMNYRGLINMLIFCGCVGqtgggw 574
Cdd:COG3383 256 ----VAKYTPERVAEITGVPAEDIREAARLIA-----EAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIG------ 320
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 575 ahyvgqeklRPQTGWQPLAfaldwarpprhmnstsffynhssqwryeklsvkellsplanpqdfaGQlidFNVR-AERMG 653
Cdd:COG3383 321 ---------RPGTGPFPLT----------------------------------------------GQ---NNVQgGRDMG 342
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 654 WLPSS-P--QLNTNPLTIAAKAKESGLSPAD----YTA----KALQQGELRFaseqpdngnnhprnLFVWRSNLLGSsak 722
Cdd:COG3383 343 ALPNVlPgyRDVTDPEHRAKVADAWGVPPLPdkpgLTAvemfDAIADGEIKA--------------LWIIGENPAVS--- 405
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 723 gheymlryllgiesgiqgsetvaDPEmspqevdwQTPAREG--KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDD-MNT 799
Cdd:COG3383 406 -----------------------DPD--------ANHVREAleKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGtFTN 454
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2729246587 800 SDMHpfIHPLSAAIDPVWESRSDWEIYKDIAKtfsalcpgHLGvendvvlLPVQHDSPAEI 860
Cdd:COG3383 455 TERR--VQRVRKAVEPPGEARPDWEIIAELAR--------RLG-------YGFDYDSPEEV 498
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
53-839 |
2.19e-19 |
|
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: 93.08 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 53 NCTGSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP-RG--CPRGASYSWYIYSANRLKYPLVRkqlirlwrealqqf 129
Cdd:cd02766 7 DCPDTCSLLVTVEDGRIV---------RVEGD-PAHPYtRGfiCAKGARYVERVYSPDRLLTPLKR-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 130 sdpveawdsivrdekkatsykQARGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMSMVSYAAGTRYLSL 209
Cdd:cd02766 63 ---------------------VGRKGGQWERISWDEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 210 MGGTclSFYDWYCDLP--PASPMTWGEQTDV-PEsaDWYNSAYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYA 286
Cdd:cd02766 122 LGAS--ELRGTICSGAgiEAQKYDFGASLGNdPE--DMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 287 EVAKLSDHWLAPKQGTDAALAMAMGHVILKEfhldNPSDY-FINYCrrytdmpmlvmleetdkgyysagrllraadlvdn 365
Cdd:cd02766 198 ATAARADLHIQIRPGTDGALALGVAKVLFRE----GLYDRdFLARH---------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 366 lgesnnpdwktvafdsdgqlvvpngsagfrwgqkgkwnlearaagqqtelrlslAEGYDQLAevafpyfggqpspyfrhv 445
Cdd:cd02766 240 ------------------------------------------------------TEGFEELK------------------ 247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 446 eqspvlvhklpvreisladgrrakavsvydltlanygvgrgfddsntagsyDEVKAYSPAWAEQICGVPRQQIIRIAREF 525
Cdd:cd02766 248 ---------------------------------------------------AHLETYTPEWAAEITGVSAEEIEELARLY 276
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 526 ADTahkthGRSMIIVGAGMNHWYHMDMNYRG--LINMLIfcGCVGQTGGGwahyvgqeklrpqtgwqplafaldwarppr 603
Cdd:cd02766 277 GEA-----KPPSIRLGYGMQRYRNGGQNVRAidALPALT--GNIGVPGGG------------------------------ 319
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 604 hmnstsFFYNHSSqwryeklsvkellsplanPqdfagqlidfNVRAermgwlpsspqlntnpltiaakakesglspadyt 683
Cdd:cd02766 320 ------AFYSNSG------------------P----------PVKA---------------------------------- 331
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 684 akalqqgelrfaseqpdngnnhprnLFVWRSNLLgssakgheymlryllgiesgiqgsetVADPEmspqevdwQTPAREG 763
Cdd:cd02766 332 -------------------------LWVYNSNPV--------------------------AQAPD--------SNKVRKG 352
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2729246587 764 ---KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAIDPVWESRSDWEIYKDIAKTFSALCPG 839
Cdd:cd02766 353 larEDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPP 431
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
1086-1201 |
4.22e-19 |
|
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: 83.86 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1086 LNFLTPHQKWGIHSTYsENLLMLTLSRGGP-IVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMMYHA 1164
Cdd:pfam01568 1 LYLITGRVLGQYHSQT-RTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 2729246587 1165 QERitnipgsevtGMRGGIHNSVTRISPKPTHMIGGY 1201
Cdd:pfam01568 80 WWY----------EPRGGNANALTDDATDPLSGGPEF 106
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
53-317 |
6.59e-19 |
|
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: 91.73 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 53 NCTGSCSWKIYVKNGLVTwetqqtdYPRTRPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRK----------QLIRL- 121
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVT-------KVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgrdvdpKFVPIs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 122 WREALQQFSDPVEAwdsiVRDEKKATSYKQARGKGGFVRSDWNElnqliaaaniWTVKNYGPDRVAGFSpipamSMVSYA 201
Cdd:cd02757 81 WDEALDTIADKIRA----LRKENEPHKIMLHRGRYGHNNSILYG----------RFTKMIGSPNNISHS-----SVCAES 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 202 AGTRYLSLMGGtclsfydwycdlppaspmtWGEqtdvpESADWYNSAYIIAWGSNVPQTRTPDAHF--FTEVRYKGTKTV 279
Cdd:cd02757 142 EKFGRYYTEGG-------------------WDY-----NSYDYANAKYILFFGADPLESNRQNPHAqrIWGGKMDQAKVV 197
|
250 260 270
....*....|....*....|....*....|....*...
gi 2729246587 280 AITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKE 317
Cdd:cd02757 198 VVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTE 235
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
43-411 |
2.21e-18 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 91.24 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 43 DKIVRSTHGVNCTGSCSWKIYVKNGLVTW-ETQQT---DYPRTrpdlpnHEPRGCPRGASYSWYIYSANRLKYPLVRKQl 118
Cdd:PRK14990 56 EKVIWSACTVNCGSRCPLRMHVVDGEIKYvETDNTgddNYDGL------HQVRACLRGRSMRRRVYNPDRLKYPMKRVG- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 119 irlwrealqqfsdpveawdsivrdekkatsykqARGKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVA---GFSPIPAM 195
Cdd:PRK14990 129 ---------------------------------ARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnyGTGTLGGT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 196 SMVSYAAGTRYLSLMGGTCLSFYDWYCDLPPAS-----PMTWGEQTDVPESADWYNSAYIIAWGSNVPQTRTPDA---HF 267
Cdd:PRK14990 176 MTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQiaeglNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGgvtYY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 268 FTEVRYKGT-KTVAITPDYAEV-AKLSDHWLAPKQGTDAALAMAMGHVILKEFHLDNPsdYFINYCRRYTDMPMLVmlEE 345
Cdd:PRK14990 256 LEQARQKSNaRMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQP--FLDKYCVGYDEKTLPA--SA 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 346 TDKGYYSAGRLLRAADlvdnlGESNNPDWKT----VAFDSDGQLVVPNGSAGFRWGQKGkWNLEARAAGQ 411
Cdd:PRK14990 332 PKNGHYKAYILGEGPD-----GVAKTPEWASqitgVPADKIIKLAREIGSTKPAFISQG-WGPQRHANGE 395
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
54-831 |
4.80e-18 |
|
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: 89.19 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 54 CTGSCSWKIYVKNGLVTwetqqtdYPRTRPDLPNHEPRGCPRGAsYSW-YIYSANRLKYPLVRKqlirlwrealqqfsdp 132
Cdd:cd02753 7 CGVGCGLELWVKDNKIV-------GVEPVKGHPVNRGKLCVKGR-FGFdFVNSKDRLTKPLIRK---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 133 veawdsivrdekkatsykqargKGGFVRSDWNE-LNqlIAAANIWTVK-NYGPDRVAGFSPipamsmvsyAAGTR---YL 207
Cdd:cd02753 63 ----------------------NGKFVEASWDEaLS--LVASRLKEIKdKYGPDAIAFFGS---------AKCTNeenYL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 208 -----SLMGGT-----CLSfydwYCDlppaSPMTWGEQTDVPESADW------YNSAYIIAWGSNvpqtrTPDAH--FFT 269
Cdd:cd02753 110 fqklaRAVGGTnnvdhCAR----LCH----SPTVAGLAETLGSGAMTnsiadiEEADVILVIGSN-----TTEAHpvIAR 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 270 EVR---YKGTKTVAITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKEfhldnpsdyfinycrrytdmpmlvmleet 346
Cdd:cd02753 177 RIKrakRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEE----------------------------- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 347 dkgyysagrllraaDLVDNlgesnnpdwktvAFdsdgqlvvpngsagfrwgqkgkwnLEARAagqqtelrlslaEGYDQL 426
Cdd:cd02753 228 --------------GLYDE------------EF------------------------IEERT------------EGFEEL 245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 427 AEVafpyfggqpspyfrhveqspvlvhklpvreisladgrrakavsvydltlanygvgrgfddsntagsydeVKAYSPAW 506
Cdd:cd02753 246 KEI---------------------------------------------------------------------VEKYTPEY 256
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 507 AEQICGVPRQQIIRIAREFAdtahkTHGRSMIIVGAGMNHWYHMDMNYRGLINMLIFCGCVGQTGGGwahyvgqeklrpq 586
Cdd:cd02753 257 AERITGVPAEDIREAARMYA-----TAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTG------------- 318
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 587 tgwqplafaldwarpprhmnstsffynhssqwryeklsvkelLSPLanpqdfAGQlidFNVR-AERMGWLPsspqlNTNP 665
Cdd:cd02753 319 ------------------------------------------VNPL------RGQ---NNVQgACDMGALP-----NVLP 342
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 666 ltiaakakesglspaDYTaKALqqgelrfaseqpdngnnhprnlfvwrsnllgssakgheymlrYLLGiesgiqgsetvA 745
Cdd:cd02753 343 ---------------GYV-KAL------------------------------------------YIMG-----------E 353
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 746 DPEMSPQEVdwqTPAREG--KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPfIHPLSAAIDPVWESRSDW 823
Cdd:cd02753 354 NPALSDPNT---NHVRKAleSLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERR-VQRVRKAVEPPGEARPDW 429
|
....*...
gi 2729246587 824 EIYKDIAK 831
Cdd:cd02753 430 EIIQELAN 437
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
1094-1201 |
5.00e-17 |
|
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: 77.75 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1094 KWGIHSTYSENLLMLTLSRGGPIVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMMYHAQERitnipg 1173
Cdd:cd02775 2 RDHFHSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGH------ 75
|
90 100
....*....|....*....|....*...
gi 2729246587 1174 sevTGMRGGIHNSVTRISPKPTHMIGGY 1201
Cdd:cd02775 76 ---RGGRGGNANVLTPDALDPPSGGPAY 100
|
|
| Nitr_red_alph_N |
pfam14710 |
Respiratory nitrate reductase alpha N-terminal; This is the N-terminal tail of the respiratory ... |
4-40 |
1.59e-15 |
|
Respiratory nitrate reductase alpha N-terminal; This is the N-terminal tail of the respiratory nitrate reductase alpha chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. The N-terminal tail of the alpha chain interacts with the beta chain and contributes to the stability of the heterotrimer.
Pssm-ID: 434147 [Multi-domain] Cd Length: 37 Bit Score: 71.11 E-value: 1.59e-15
10 20 30
....*....|....*....|....*....|....*..
gi 2729246587 4 LLDKLRYFKQKGSTFSDGHGQEMDSNRDWEDGYRQRW 40
Cdd:pfam14710 1 FLDRLRFFKRKRETFADGHGETTNEDRDWEDAYRQRW 37
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
475-860 |
5.04e-13 |
|
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: 73.41 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 475 DLTLANY---------GVGRGFDDSNTAGsYDEVKA----YSPAWAEQICGVPRQQIIRIAREFADTahkthGRSMIIVG 541
Cdd:cd02754 216 DLALLNGllhvlieegLIDRDFIDAHTEG-FEELKAfvadYTPEKVAEITGVPEADIREAARLFGEA-----RKVMSLWT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 542 AGMNHWYHMDMNYRGLINMLIFCGCVGQTGGGWAHYVGQeklrP--QTGWQPLAFAldwARPPRHMNstsffynhssqwr 619
Cdd:cd02754 290 MGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQ----PnaMGGREVGGLA---NLLPGHRS------------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 620 yeklsvkellspLANPQDFAgqlidfnvRAERMgWlpsspqlNTNPLTIAAKAkesglsPADYTA--KALQQGELRFase 697
Cdd:cd02754 350 ------------VNNPEHRA--------EVAKF-W-------GVPEGTIPPKP------GLHAVEmfEAIEDGEIKA--- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 698 qpdngnnhprnLFVWRSNLLGSSAkgHEYMLRYLLGiesgiqgsetvadpemspqevdwqtparegKLDLLVTLD-FRMS 776
Cdd:cd02754 393 -----------LWVMCTNPAVSLP--NANRVREALE------------------------------RLEFVVVQDaFADT 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 777 STCLFSDIVLPTATWYEKDDMNTsDMHPFIHPLSAAIDPVWESRSDWEIYKDIAKtfsALCPGHLgvendvvllpVQHDS 856
Cdd:cd02754 430 ETAEYADLVLPAASWGEKEGTMT-NSERRVSLLRAAVEPPGEARPDWWILADVAR---RLGFGEL----------FPYTS 495
|
....
gi 2729246587 857 PAEI 860
Cdd:cd02754 496 PEEV 499
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
1081-1196 |
6.27e-12 |
|
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: 63.92 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1081 YPekiLNFLTPHQKWGIHSTYSENLLMLTLSrGGPIVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTM 1160
Cdd:cd02785 2 YP---LACIQRHSRFRVHSQFSNVPWLLELQ-PEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVT 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 2729246587 1161 MYHaqeritnipGSEVTGMRGGIHNSVTRISPKPTH 1196
Cdd:cd02785 78 AEQ---------GWWSRYFQEGSLQDLTSPFVNPVH 104
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
49-529 |
4.80e-11 |
|
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: 67.30 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 49 THGVNCTGSCSW-KIYVKNGLVTWETQQTDYPRTRPDlpnhEPRGCPRGASYSWYIYSANRLKYPLVRkqlirlwrealq 127
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVATEIEPNFAAEDIHPA----RGRVCVKAYGLVQKTYNPNRVLQPMKR------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 128 qfsdpveawdsivrdekkaTSYKQARGKG-GFVRSDWNELNQLIAAaNIWTVKNYG-------PDRVAGFSP--IPAMSM 197
Cdd:cd02760 66 -------------------TNPKKGRNEDpGFVPISWDEALDLVAA-KLRRVREKGlldekglPRLAATFGHggTPAMYM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 198 VSYAAgtrYLSLMGGTCLSFYDWYCDLPPASPMTWGE--QTDVPESADWYNSAYIIAWGSNVPQTRTPDA-HFFTEVRYK 274
Cdd:cd02760 126 GTFPA---FLAAWGPIDFSFGSGQGVKCVHSEHLYGEfwHRAFTVAADTPLANYVISFGSNVEASGGPCAvTRHADARVR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 275 GTKTVAITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKEFHLDNpsdYFINYCRRYTDMPMLVMLEetdkgyysaG 354
Cdd:cd02760 203 GYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMFAMIHVMVHEQGLGK---LDVPFLRDRTSSPYLVGPD---------G 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 355 RLLRAAdlvdnlgesnnPDWKTVAFDSDGQLVVPNGSAGFrwgqkgkwnLEARAAgqqtelRLSLAEGYDQLAEVAFPYF 434
Cdd:cd02760 271 LYLRDA-----------ATGKPLVWDERSGRAVPFDTRGA---------VPAVAG------DFAVDGAVSVDADDETAIH 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 435 GGqpspyfrhveqspvlvhklpvreisladgrrAKAVSVYDLTLanygvgrgfddsntagsyDEVKAYSPAWAEQICGVP 514
Cdd:cd02760 325 QG-------------------------------VEGTTAFTMLV------------------EHMRKYTPEWAESICDVP 355
|
490
....*....|....*
gi 2729246587 515 RQQIIRIAREFADTA 529
Cdd:cd02760 356 AATIRRIAREFLENA 370
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
103-833 |
1.42e-10 |
|
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: 65.36 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 103 IYSANRLKYPLVRKQLIrlwrealqqfsdpveawdsivrdEKKATSYKQARGKGGFVRSDWNELNQLIAAANIWTVKNYG 182
Cdd:cd02769 41 VYSPTRIKYPMVRRGWL-----------------------EKGPGSDRSLRGKEEFVRVSWDEALDLVAAELKRVRKTYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 183 PDRVAG-----FSP---IPAMSMV-----------------SYAAGTRYLSLMGGTclsfYDWYCdlppaspmtwGEQTD 237
Cdd:cd02769 98 NEAIFGgsygwSSAgrfHHAQSLLhrflnlaggyvgsvgdySTGAAQVILPHVVGS----MEVYT----------EQQTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 238 VPESADwyNSAYIIAWGSNVPQTR------TPDaH----FFTEVRYKGTKTVAITPDYAEVAKLSD-HWLAPKQGTDAAL 306
Cdd:cd02769 164 WPVIAE--HTELVVAFGADPLKNAqiawggIPD-HqaysYLKALKDRGIRFISISPLRDDTAAELGaEWIAIRPGTDVAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 307 AMAMGHVILKEfhldNPSDYfiNYCRRYTDmpmlvmleetdkgyysagrllraadlvdnlgesnnpdwktvafdsdgqlv 386
Cdd:cd02769 241 MLALAHTLVTE----GLHDK--AFLARYTV-------------------------------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 387 vpngsagfrwgqkgkwnlearaagqqtelrlslaeGYDQLAevafPYFGGQpspyfrhveqspvlvhklpvreislADGR 466
Cdd:cd02769 265 -----------------------------------GFDKFL----PYLLGE-------------------------SDGV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 467 rAKavsvydltlanygvgrgfddsntagsydevkaySPAWAEQICGVPRQQIIRIAREFADtahkthGRSMIIVGAGMNH 546
Cdd:cd02769 281 -PK---------------------------------TPEWAAAICGIPAETIRELARRFAS------KRTMIMAGWSLQR 320
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 547 WYHMDMNYRGLINMLIFCGCVGQTGGGWA---HYVGqeklrpqtGWQPLAFALDWARPPRHMNSTSFFynhssqwryekL 623
Cdd:cd02769 321 AHHGEQPHWMAVTLAAMLGQIGLPGGGFGfgyHYSN--------GGGPPRGAAPPPALPQGRNPVSSF-----------I 381
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 624 SVKELLSPLANPqdfaGQLIDFNVRaermgwlpsspqlntnpltiaakakesglspadytakalqqgELRFaseqPD--- 700
Cdd:cd02769 382 PVARIADMLLNP----GKPFDYNGK------------------------------------------KLTY----PDikl 411
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 701 ---NGNN---HPRNLfvwrsNLLgssakgheymlryllgiesgIQGsetvadpemspqevdWQtparegKLDLLVTLDFR 774
Cdd:cd02769 412 vywAGGNpfhHHQDL-----NRL--------------------IRA---------------WQ------KPETVIVHEPF 445
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 2729246587 775 MSSTCLFSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAIDPVWESRSDWEIYKDIAKTF 833
Cdd:cd02769 446 WTATARHADIVLPATTSLERNDIGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERL 504
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
54-341 |
1.71e-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: 65.24 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 54 CTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLpnheprgCPRGASYSWYIYSANRLKYPLVRKQlirlwrealqqfsdpv 133
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIKGNPDHPLNKGVI-------CAKGSSGIMKQYSPARLTKPLLRKG---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 134 eawdsivrdekkatsykqARGKGGFVRSDWNELNQlIAAANIWTVKNYGPDRVAGFSPIPAMSMVS--YAA--GTRYLSL 209
Cdd:cd02763 64 ------------------PRGSGQFEEIEWEEAFS-IATKRLKAARATDPKKFAFFTGRDQMQALTgwFAGqfGTPNYAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 210 MGGTClsfydwYCDLPPASPMTWGEQTDVPESADWYNSAYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEVA 289
Cdd:cd02763 125 HGGFC------SVNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYA 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2729246587 290 KLSDHWLAPKQGTDAALAMAMGHVILKEFHLDnpsdyfINYCRRYTDMPMLV 341
Cdd:cd02763 199 AIADEWVPIKPGTDGAFILALAHELLKAGLID------WEFLKRYTNAAELV 244
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
764-833 |
9.16e-10 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 63.15 E-value: 9.16e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2729246587 764 KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPF--IHPLSAAIDPVWESRSDWEIYKDIAKTF 833
Cdd:PRK15102 494 KLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNrgIIAMKKVVEPLFESRSDFDIFRELCRRF 565
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1081-1163 |
1.29e-09 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 57.21 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1081 YPekiLNFLTPHQKWGIHSTYSENLlmlTLSRGGPI-----VWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVP 1155
Cdd:cd02777 1 YP---LQLISPHPKRRLHSQLDNVP---WLREAYKVkgrepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIM 74
|
....*...
gi 2729246587 1156 AGMTMMYH 1163
Cdd:cd02777 75 PGVVALPE 82
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
764-831 |
4.72e-09 |
|
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: 60.40 E-value: 4.72e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2729246587 764 KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDD-MNTSDMHPFIHPLSAAIDPVWESRSDWEIYKDIAK 831
Cdd:cd02759 356 ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGlRGGFEAENFVQLRQKAVEPYGEAKSDYEIVLELGK 424
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
1081-1159 |
1.11e-08 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 54.21 E-value: 1.11e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2729246587 1081 YPekiLNFLTPHQKWGIHSTYSeNLLMLTLSRGGPIVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMT 1159
Cdd:cd02786 1 YP---LRLITPPAHNFLNSTFA-NLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV 75
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
43-105 |
2.59e-08 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 51.48 E-value: 2.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2729246587 43 DKIVRSTHGVnCTGSCSWKIYVKNGLVTWETQqtdyprtRPDLPNHEPRGCPRGASYSWYIYS 105
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVRG-------DPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
54-317 |
1.82e-07 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 55.44 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 54 CTGSCSWKIYVKNGlvtwetqQTDYPRTRPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRKQlirlwrealqqfsdpv 133
Cdd:PRK15488 51 CSTRCPIEARVVNG-------KNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVG---------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 134 eawdsivrdekkatsykqARGKGGFVRSDWNELNQLIAAaNIWTVK-NYGPDRVAgFSpipamsmvsyaagtrylSLMGg 212
Cdd:PRK15488 108 ------------------ERGEGKWQEISWDEAYQEIAA-KLNAIKqQHGPESVA-FS-----------------SKSG- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 213 tclSFYDWYCDLPPA--SPMTWGEQTDVP---ESA-----------DWYNSAYIIAWGSN------VPQTRTPdAHFFTE 270
Cdd:PRK15488 150 ---SLSSHLFHLATAfgSPNTFTHASTCPagyAIAakvmfggklkrDLANSKYIINFGHNlyeginMSDTRGL-MTAQME 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2729246587 271 vryKGTKTVAITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILKE 317
Cdd:PRK15488 226 ---KGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEE 269
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
497-529 |
1.03e-06 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 53.13 E-value: 1.03e-06
10 20 30
....*....|....*....|....*....|...
gi 2729246587 497 DEVKAYSPAWAEQICGVPRQQIIRIAREFADTA 529
Cdd:PRK15488 289 ASVKEYTPEWAEAISDVPADDIRRIARELAAAA 321
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1086-1157 |
3.00e-06 |
|
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: 47.63 E-value: 3.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2729246587 1086 LNFLTPHQKWGIHSTYSENLLMLTLSRGG--PIvWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAG 1157
Cdd:cd02793 3 LHLLSNQPATRLHSQLDHGSLSRAYKVQGrePI-RINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPG 75
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
67-317 |
9.34e-06 |
|
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: 49.70 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 67 GLVTwETQQTDYPRTRPDlPNHE-PRG--CPRGASYSWYIYSANRLKYPLVRKqlirlwrealqqfsdpveawdsivrde 143
Cdd:cd02762 12 GLVV-TVEDGRVASIRGD-PDDPlSKGyiCPKAAALGDYQNDPDRLRTPMRRR--------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 144 kkatsykqargKGGFVRSDWNELNQLIAAANIWTVKNYGPDRVAGFSPIPAMSMVSYAAGTRYLSLMGGTCLSFYDWYCD 223
Cdd:cd02762 63 -----------GGSFEEIDWDEAFDEIAERLRAIRARHGGDAVGVYGGNPQAHTHAGGAYSPALLKALGTSNYFSAATAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 224 LPP---ASPMTWGEQTDVPeSADWYNSAYII-----AWGSNVPQTRTPDA-HFFTEVRYKGTKTVAITPDYAEVAKLSDH 294
Cdd:cd02762 132 QKPghfWSGLMFGHPGLHP-VPDIDRTDYLLilganPLQSNGSLRTAPDRvLRLKAAKDRGGSLVVIDPRRTETAKLADE 210
|
250 260
....*....|....*....|...
gi 2729246587 295 WLAPKQGTDAALAMAMGHVILKE 317
Cdd:cd02762 211 HLFVRPGTDAWLLAAMLAVLLAE 233
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
1081-1163 |
5.78e-05 |
|
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: 43.82 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 1081 YPekiLNFLTPHQKWGIHSTYSeNLLMLTLSRGGPiVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTM 1160
Cdd:cd02794 1 YP---LQLIGWHYKRRTHSTFD-NVPWLREAFPQE-VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVA 75
|
...
gi 2729246587 1161 MYH 1163
Cdd:cd02794 76 LPQ 78
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
54-316 |
1.47e-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: 46.24 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 54 CTGSCSWKIYVKNGlvTWETQQTDyprtrPDLPNHEPRGCPRGASYSWYIYSANRLKYPLVRK----QLIRL-WREALQQ 128
Cdd:cd02752 7 CSVGCGLIAYVQNG--VWVHQEGD-----PDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRApgsgKWEEIsWDEALDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 129 FSDPVeawdsivrdekkatsyKQARGKGgfvrsdwnelnqlIAAANIWTVKNYGPDRV-----AGFSPIPAMSMVSYAA- 202
Cdd:cd02752 80 IARKM----------------KDIRDAS-------------FVEKNAAGVVVNRPDSIaflgsAKLSNEECYLIRKFARa 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2729246587 203 -GTRYLS----LMGGTCLSfydwycdlppASPMTWGEQTDVPESADWYNSAYIIAWGSNvpqtrTPDAH-----FFTEVR 272
Cdd:cd02752 131 lGTNNLDhqarIUHSPTVA----------GLANTFGRGAMTNSWNDIKNADVILVMGGN-----PAEAHpvsfkWILEAK 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2729246587 273 YK-GTKTVAITPDYAEVAKLSDHWLAPKQGTDAALAMAMGHVILK 316
Cdd:cd02752 196 EKnGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYIIR 240
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
1088-1163 |
2.89e-04 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 41.88 E-value: 2.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2729246587 1088 FLTPHQKW--GIHSTYSENLLMLTLSRGgpiVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMMYH 1163
Cdd:cd02778 4 LIYGKSPVhtHGHTANNPLLHELTPENT---LWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH 78
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
1115-1171 |
6.79e-04 |
|
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: 40.68 E-value: 6.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2729246587 1115 PIVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMM-YHAQERITNI 1171
Cdd:cd02790 35 EYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFMpFHFAEAAANL 92
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
1115-1169 |
1.74e-03 |
|
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: 39.36 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2729246587 1115 PIVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMMYHAQERIT 1169
Cdd:cd02779 33 PYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHPRPG 87
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
1115-1163 |
2.19e-03 |
|
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: 39.60 E-value: 2.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2729246587 1115 PIVWMSEDDAREMGIADNDWIEAFNSNGALTARAVVSQRVPAGMTMMYH 1163
Cdd:cd02781 33 PVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEH 81
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
497-562 |
5.74e-03 |
|
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: 40.79 E-value: 5.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2729246587 497 DEVKAYSPA-WAEQiCGVPRQQIIRIAREFADtahktHGRSMIIV--GAGMnhwyHMDMNYR----GLINMLI 562
Cdd:cd02758 334 EEAFSYSLEeYAEI-CGVPEAKIIELAKEFTS-----HGRAAAVVhhGGTM----HSNGFYNayaiRMLNALI 396
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
502-573 |
8.08e-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. 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: 40.46 E-value: 8.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2729246587 502 YSPAWAEQICGVPRQQIIRIAREFADTAhkTHGRSMIIVGA-GMNHWYHMDMNYRG--LINMLIfcGCVGQTGGG 573
Cdd:cd02752 241 YTPEEVEDICGVPKEDFLKVAEMFAATG--RPDKPGTILYAmGWTQHTVGSQNIRAmcILQLLL--GNIGVAGGG 311
|
|
| |
