|
Name |
Accession |
Description |
Interval |
E-value |
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
1-1227 |
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: 2441.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1 MKKKTSALMRRLKYFSPIDRYNDNHTQETYEDREWENVYRKRWQHDKVIRSTHGVNCTGSCSWNIYVKDGIVTWEGQELN 80
Cdd:COG5013 1 MGPASSHLLDRLRFFRRGEVFSDGHGVTTEGGREWEDFYRDRWQHDKVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 81 YPTTGPDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVRGVLWNMWQEELQNNESPLEAWKSIVENREKARTYKQARGKGG 160
Cdd:COG5013 81 YPRTGPDLPNYEPRGCPRGASFSWYTYSPTRVKYPYVRGVLLELWREARARHGDPVEAWASIVEDPEKRRRYKSARGKGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 161 FIRANWDEVLQLVSASLLYTVMKYGPDRNVGFSPIPAMSMLSHAAGSRFMQLMGGPMLSFYDWYADLPPASPQIWGDQTD 240
Cdd:COG5013 161 FVRATWDEANEIIAAANVYTIKKYGPDRVAGFSPIPAMSMVSYAAGARFLSLIGGVMLSFYDWYADLPPASPQVWGEQTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 241 VPESSDWYNSGYIMTWGSNVPMTRTPDAHFLAEVRYKGTKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQE 320
Cdd:COG5013 241 VPESADWYNSGYLIMWGSNVPQTRTPDAHFMTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 321 FYVDNQVEYFTKYAKQYTDFPFFVTLKQKGDQFVADRFLNASDIG---RETKLGEWKPVLWNENTNDFATPHGTMGSRWD 397
Cdd:COG5013 321 FHVDRQVPYFTDYARRYTDLPFLVTLEERDGGYVPGRFLRASDLGgalGESNNPEWKTVVLDEATGEPVVPNGSIGFRWG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 398 NEK-KWNLRLEDeETGEKIDPRLSLLGMEEAIGTVQIPYFS--DDGNKVLERTIPVKKVMTEEGELFVTTVYDLTLANYG 474
Cdd:COG5013 401 ESEgKWNLELKD-ATGADVDPALSLLDDHDEVVEVAFPYFGgeTGGGGVLRRGVPVRRVTLADGEVLVTTVFDLMLANYG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 475 VNRGLGGQEPKDFNDDIPFTPAWQEKMTGVKRELIIQIAREFAQNAVDTNGRSMIIVGAGINHWFNSDTIYRAVLNLVLL 554
Cdd:COG5013 480 VDRGLPGNWPTGYDDDVPYTPAWQEKITGVPREQVIRVAREFAQNAEKTRGRSMIIMGAGTNHWYHSDMIYRAILNLLML 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 555 VGAQGVNGGGWAHYVGQEKLRPAEGWQTIAMAKDWQGPPKLQNGTSFFYFVTDQWRYEDTPVGHLASP-VEGNSRYQHHG 633
Cdd:COG5013 560 CGCQGVNGGGWAHYVGQEKLRPQTGWQPLAFALDWSRPPRQMNGTSFFYAHTDQWRYETLSADELLSPlADGKFWGGHLA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 634 DYNVLAARLGWLPSYPTFEKNGIELYKEAVAAGattqEEIGKYVAQKLKEKELKFAIEDPDNKNNFPRNLFVWRANLISS 713
Cdd:COG5013 640 DYNVRAARLGWLPSYPQFNRNPLDLADEAEAAG----MEPADYVVDQLKSGELKFACEDPDNPENFPRNLFVWRSNLLGS 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 714 SGKGHEYFLKHLLGTTNGLMNDDS-DSLRPEEIKWHEEAPEGKLDLLINLDFRMAGTALYSDIVLPASTWYEKHDLSSTD 792
Cdd:COG5013 716 SGKGHEYFLKHLLGTDNGVQGEELgPGLRPREVVWRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKHDLSTTD 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 793 MHPFVHPFNPAIGSPWEARSDWDIFTSLSKAVSDLAKKIdLEPMKEVVATPLLHDTPQELAQPLGKIKDWSKGECEPIPG 872
Cdd:COG5013 796 MHPFIHPFSPAVDPPWEARSDWDIFKGIAKKFSELAAGH-LGVRKDVVATPLQHDTPGELAQPFGDVKDWKKGECEPIPG 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 873 KTMPQIHVVERDYKTIYDKMTALGPNAGKQPIGTKGISWSAEKEYEQLKSKLGVVRTDSIAKGCPDIKEAINAAEAVLTL 952
Cdd:COG5013 875 KTMPKLVVVERDYPAIYEKFTSLGPLLEKLGNGGKGITWDTEEEVEELGKLNGVVREEGVAKGRPRLDTDIDAAEAILAL 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 953 SSTTNGHMAVKAWEALEKQTDLKLRDLAEEREEECFTFEQITAQPKTVITSPAFTGSEKGGRRYSPFTTNVERLIPWRTI 1032
Cdd:COG5013 955 SPETNGHVAVKAWKALEKRTGRDLAHLAAGREEEKIRFRDIQAQPRKVITSPTWSGSESGGRRYSAFTTNVEELIPWRTL 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1033 TGRQSFYLDHDMMKEFGETMATFKPILQHKPFRKSRPEVE--GKEITLNYLTPHNKWSIHSMYFDSLPMLTLFRGGPTVW 1110
Cdd:COG5013 1035 TGRQHFYLDHDWMREFGEGLPVYRPPLDMKTLFGEPGIGPngNPEIVLRYLTPHQKWGIHSTYQDNLLMLTLSRGGPTVW 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1111 MNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMHHAQDRHINVPGTKLTSNRGGTHNSPTRIHVKPTHMI 1190
Cdd:COG5013 1115 MSEEDAAKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHAQERIVNVPGSEITGKRGGIHNSVTRIVLKPTHMI 1194
|
1210 1220 1230
....*....|....*....|....*....|....*..
gi 446653436 1191 GGYGQLSYGFNYYGPTGNQRDLNVVIRKLKEVDWLED 1227
Cdd:COG5013 1195 GGYAQLSYGFNYYGPTGNQRDEVVVVRKRSQVDWLED 1231
|
|
| narG |
TIGR01580 |
respiratory nitrate reductase, alpha subunit; The Nitrate reductase enzyme complex allows ... |
6-1226 |
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: 2105.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 6 SALMRRLKYFSP-IDRYNDNHTQETYEDREWENVYRKRWQHDKVIRSTHGVNCTGSCSWNIYVKDGIVTWEGQELNYPTT 84
Cdd:TIGR01580 1 SKLLDRLRYFKQkGETFSDGHGQTLNENRDWENVYRQRWQYDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 85 GPDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVRGVLWNMWQEELQNNESPLEAWKSIVENREKARTYKQARGKGGFIRA 164
Cdd:TIGR01580 81 RPDLPNHEPRGCPRGASYSWYIYSANRLKYPMMRKRLMKLWREAKQTHSDPVEAWASIVENADKAKSYKQARGRGGFVRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 165 NWDEVLQLVSASLLYTVMKYGPDRNVGFSPIPAMSMLSHAAGSRFMQLMGGPMLSFYDWYADLPPASPQIWGDQTDVPES 244
Cdd:TIGR01580 161 SWQEVNELIAASNVYTVKNYGPDRVVGFSPIPAMSMVSYASGSRYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 245 SDWYNSGYIMTWGSNVPMTRTPDAHFLAEVRYKGTKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQEFYVD 324
Cdd:TIGR01580 241 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAALALAMGHVILREFHLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 325 NQVEYFTKYAKQYTDFPFFVTLKQKGDQFVADRFLNASDIGR---ETKLGEWKPVLWNENTnDFATPHGTMGSRWDNEKK 401
Cdd:TIGR01580 321 NPSQYFTEYAKRYTDMPMLVMLEERDGYYAAGRFLRAADLVDalgQENNPEWKTVAFDTNG-EMVAPQGSIGFRWGEKGK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 402 WNLRLEDEETGEKIDPRLSLLGMEEAIGTVQIPYFSDD---------GNKVLERTIPVKKVMTEEGEL-FVTTVYDLTLA 471
Cdd:TIGR01580 400 WNLEQRDGKTGEEIELQLSLLGSQDEIAEVGFPYFGGDgtehfnkveGENVLLRKLPVKRLQLADGSTaLVTTVFDLTLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 472 NYGVNRGLGGQE-PKDFNDDIPFTPAWQEKMTGVKRELIIQIAREFAQNAVDTNGRSMIIVGAGINHWFNSDTIYRAVLN 550
Cdd:TIGR01580 480 NYGLERGLGDVNcATSYDDVKAYTPAWQEQITGVSREQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLIN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 551 LVLLVGAQGVNGGGWAHYVGQEKLRPAEGWQTIAMAKDWQGPPKLQNGTSFFYFVTDQWRYEDTPVGHLASPVEGNSRY- 629
Cdd:TIGR01580 560 MLILCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPPRHMNGTSFFYNHSSQWRYETVTAEDLLSPMADKSRYt 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 630 QHHGDYNVLAARLGWLPSYPTFEKNGIELYKEAVAAGATTQEeigkYVAQKLKEKELKFAIEDPDNKNNFPRNLFVWRAN 709
Cdd:TIGR01580 640 GHLIDYNVRAERMGWLPSAPQLNTNPLTIAGEAEKAGMNPVD----YVVKSLQEGSLRFAAEQPDNGVNFPRNLFIWRSN 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 710 LISSSGKGHEYFLKHLLGTTNGLMNDDS---DSLRPEEIKWHEEAPEGKLDLLINLDFRMAGTALYSDIVLPASTWYEKH 786
Cdd:TIGR01580 716 LLGSSGKGHEYMLKYLLGTENGIMNKDLgqqGGVKPEEVDWQDNGLEGKLDLVVTLDFRMSSTCLYSDIVLPTATWYEKD 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 787 DLSSTDMHPFVHPFNPAIGSPWEARSDWDIFTSLSKAVSDLAKKiDLEPMKEVVATPLLHDTPQELAQPLGkIKDWSKGE 866
Cdd:TIGR01580 796 DMNTSDMHPFIHPLSAAIDPAWESKSDWEIYKAIAKAFSEVCVG-HLGKEKDIVTLPLQHDSAAELAQPFG-VKDWKKGE 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 867 CEPIPGKTMPQIHVVERDYKTIYDKMTALGPNAGKQPIGTKGISWSAEKEYEQLKSKLGVVRTDSIAKGCPDIKEAINAA 946
Cdd:TIGR01580 874 CDLIPGKTAPNIQVVERDYPAIYERFTSLGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKAEGSPAKGQPMINTAIDAA 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 947 EAVLTLSSTTNGHMAVKAWEALEKQTDLKLRDLAEEREEECFTFEQITAQPKTVITSPAFTGSEKGGRRYSPFTTNVERL 1026
Cdd:TIGR01580 954 EMILTLAPETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHEL 1033
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1027 IPWRTITGRQSFYLDHDMMKEFGETMATFKPILQHKPFRKSRPEVEG--KEITLNYLTPHNKWSIHSMYFDSLPMLTLFR 1104
Cdd:TIGR01580 1034 IPWRTLTGRQQLYQDHQWMRDFGESLLVYRPPIDTRSFKEVIGQKSNgnQEIVLNFLTPHQKWGIHSTYSDNLLMLTLGR 1113
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1105 GGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMHHAQDRHINVPGTKLTSNRGGTHNSPTRIHV 1184
Cdd:TIGR01580 1114 GGPVVWLSEADAKDLGIADNDWIECFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNVPGSEITQQRGGIHNSVTRITP 1193
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|..
gi 446653436 1185 KPTHMIGGYGQLSYGFNYYGPTGNQRDLNVVIRKLKEVDWLE 1226
Cdd:TIGR01580 1194 KPTHMIGGYAQLAYGFNYYGTVGSNRDEFVVVRKMKNVDWLD 1235
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
46-824 |
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: 674.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 46 DKVIRSTHGVNCTGSCSWNIYVKDGIVTWEGQELNYPTTGPDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVRGVlwnmw 125
Cdd:cd02750 1 DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 126 qeelqnnespleawksivenrekartykqARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDRNVGFSPIPAMSMLSHAA 205
Cdd:cd02750 76 -----------------------------ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 206 GSRFMQLMGGPMLSFYDWYADLPPASPQIWGDQTDVPESSDWYNSGYIMTWGSNVPMTRTPDAHFLAEVRYKGTKVVSVS 285
Cdd:cd02750 127 GSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 286 PDFAESTKFADDWISVKQGTDGALAMAMGHVILQEFYVDNQveyftkYAKQYTDFPFFVtlkqkgdqfvadrflnasdig 365
Cdd:cd02750 207 PDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDED------YLKEYTDLPFLV--------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 366 retklgewkpvlwnentndfatphgtmgsrwdnekkwnlrledeetgekidprlsllgmeeaigtvqipyfsddgnkvle 445
Cdd:cd02750 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 446 rtipvkkvmteegelfvttvydltlanygvnrglggqepkdfnddipFTPAWQEKMTGVKRELIIQIAREFAqnavdTNG 525
Cdd:cd02750 260 -----------------------------------------------YTPAWQEAITGVPRETVIRLAREFA-----TNG 287
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 526 RSMIIVGAGINHWFNSDTIYRAVLNLVLLVGAQGVNGGGWAHYVGQeklrpaegwqtiamakdwqgppklqngtsffyfv 605
Cdd:cd02750 288 RSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQ---------------------------------- 333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 606 tdqwryedtpvghlaspvegnsryqhhgdynvlaarlgwlpsyptfekngielykeavaagattqeeigkyvaqklkeke 685
Cdd:cd02750 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 686 lkfaiedpdnknnfPRNLFVWRANLISSSGKGHEYFlkhllgttnglmnddsdslrpeeikwhEEAPEGKLDLLINLDFR 765
Cdd:cd02750 334 --------------PRVLFVWRGNLFGSSGKGHEYF---------------------------EDAPEGKLDLIVDLDFR 372
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 446653436 766 MAGTALYSDIVLPASTWYEKHDLSSTDMHPFVHPFNPAIGSPWEARSDWDIFTSLSKAV 824
Cdd:cd02750 373 MDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
1077-1217 |
3.97e-84 |
|
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: 270.02 E-value: 3.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1077 TLNYLTPHNKWSIHSMYFDSLPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMHHA 1156
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446653436 1157 QDRHINVPGTKLTSNRGGTHNSPTRIHVKPTHMIGGYGQLSYGFNYYGPTGNQRDLNVVIR 1217
Cdd:cd02776 81 QERHVNVPGSKLTGKRGGIHNSVTRVRIKPTHLVGGYGQLSYGFNYYGPTGVNRDTRVVVR 141
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
46-1163 |
5.02e-54 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 201.61 E-value: 5.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 46 DKVIRSTHgVNCTGSCSWNIYVKDGIVTWegqelnypTTG-PDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVRgvlwnm 124
Cdd:COG0243 21 TKTVKTTC-PGCGVGCGLGVKVEDGRVVR--------VRGdPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKR------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 125 wqeelqnnespleawksivenrekartyKQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDRNVGFSPIPAMSMLSHA 204
Cdd:COG0243 86 ----------------------------VGPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 205 AG---SRFMQLMGGPMlsFYDWYA-DLPP---ASPQIWGDQTDVPESSDWYNSGYIMTWGSNVPMTRTPDAHFLAE-VRY 276
Cdd:COG0243 138 AAylaQRFARALGTNN--LDDNSRlCHESavaGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 277 KGTKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQEFYVDnqveyftkyakqytdfpffvtlkqkgDQFVAd 356
Cdd:COG0243 216 RGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYD--------------------------RDFLA- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 357 rflnasdigretklgewkpvlwnENTNDFatphgtmgsrwdnekkwnlrledeetgekidprlsllgmeeaigtvqipyf 436
Cdd:COG0243 269 -----------------------RHTVGF--------------------------------------------------- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 437 sddgnkvlertipvkkvmteegELFVTTVydltlanygvnrglggqepkdfnddIPFTPAWQEKMTGVKRELIIQIAREF 516
Cdd:COG0243 275 ----------------------DELAAYV-------------------------AAYTPEWAAEITGVPAEDIRELAREF 307
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 517 AqnavdTNGRSMIIVGAGINHWFNSDTIYRAVLNLVLLVGAQGVNGGGwahyvgqeklrpaegwqtiamakdwqgppklq 596
Cdd:COG0243 308 A-----TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGG-------------------------------- 350
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 597 ngtsffyfvtdqwryedtpvghlASPVEGnsryqhhgdynvlaarlgwlpsyptfekngielykEAVAAGATTQeeigky 676
Cdd:COG0243 351 -----------------------PFSLTG-----------------------------------EAILDGKPYP------ 366
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 677 vaqklkekeLKFaiedpdnknnfprnLFVWRANLISSSGkgheyflkhllgttnglmndDSDSLRpeeikwheeapEG-- 754
Cdd:COG0243 367 ---------IKA--------------LWVYGGNPAVSAP--------------------DTNRVR-----------EAlr 392
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 755 KLDLLINLDFRMAGTALYSDIVLPASTWYEKHDLSSTDMHPFVHPFNPAIGSPWEARSDWDIFTslskavsDLAKKIDLE 834
Cdd:COG0243 393 KLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFA-------ELAKRLGFE 465
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 835 pmkevvatpllhdtpqelaqplgkikdwskgecEPIPGktmpqihvvERDYKTIYDKMTAlgpnagkqPIGTKGISWsae 914
Cdd:COG0243 466 ---------------------------------EAFPW---------GRTEEDYLRELLE--------ATRGRGITF--- 492
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 915 keyEQLKsKLGVVRtdsiakgcpdikeainaaeavltlssttnghmavkawealekqtdlklrdlAEEREEECFTFEQit 994
Cdd:COG0243 493 ---EELR-EKGPVQ---------------------------------------------------LPVPPEPAFRNDG-- 515
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 995 aqpktvitspaftgsekggrryspfttnverliPWRTITGRQSFYLdhdmmkefgETMAtFKPILQHKPFRKSRPEVEGK 1074
Cdd:COG0243 516 ---------------------------------PFPTPSGKAEFYS---------ETLA-LPPLPRYAPPYEGAEPLDAE 552
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1075 -EITLNylTPHNKWSIHSMyFDSLPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFM 1153
Cdd:COG0243 553 yPLRLI--TGRSRDQWHST-TYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFA 629
|
1130
....*....|....*.
gi 446653436 1154 HH------AQDRHINV 1163
Cdd:COG0243 630 PHgwwyepADDKGGNV 645
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
50-824 |
2.38e-52 |
|
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: 188.69 E-value: 2.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 50 RSTHgVNCTGSCSWNIYVKDGIVTWEGQELNYPTTgpdmpdfEPRGCPRGASFSWYIYSPLRVKYPYVRGvlwnmwqeel 129
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRIEGDPNHPVN-------EGRLCDKGRAGLDGLYSPDRLKYPLIRV---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 130 qnnespleawksivenrekartykqaRGKGGFIRANWDEVLQLVSASLLYTVMKYGPDRNVGFSPIPAMSMLSHAAGSrF 209
Cdd:cd00368 63 --------------------------GGRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQK-L 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 210 MQLMGGPMLSFYDWYADLPPASPQIW-GDQTDVPESSDWYNSGYIMTWGSNVPMTRTPDAHFLAEVRYKGTKVVSVSPDF 288
Cdd:cd00368 116 LRALGSNNVDSHARLCHASAVAALKAfGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 289 AESTKFADDWISVKQGTDGALAMAmghvilqefyvdnqveyftkyakqytdfpffvtlkqkgdqfvadrflnasdigret 368
Cdd:cd00368 196 TETAAKADEWLPIRPGTDAALALA-------------------------------------------------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 369 klgewkpvlwnentndfatphgtmgsrwdnekkwnlrledeetgekidprlsllgmeeaigtvqipyfsddgnkvlerti 448
Cdd:cd00368 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 449 pvkkvmteegelfvttvydltlanygvnrglggqepkdfnddipftpAWQEKMTGVKRELIIQIAREFAqnavdTNGRSM 528
Cdd:cd00368 220 -----------------------------------------------EWAAEITGVPAETIRALAREFA-----AAKRAV 247
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 529 IIVGAGINHWFNSDTIYRAVLNLVLLVGAQGVNGGGWAHyvgqeklrpaegwqtiamakdwqgppklqngtsffyfvtdq 608
Cdd:cd00368 248 ILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP----------------------------------------- 286
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 609 wryedtpvghlaspvegnsryqhhgdynvlaarlgwlpsyptfekngielykeavaagattqeeigkyvaqklkekelkf 688
Cdd:cd00368 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 689 aiedpdnknnfprnlfvwRANLISSSGKGHEYFlkhllgttnglmnddsdslrpeeikwheeAPEGKLDLLINLDFRMAG 768
Cdd:cd00368 287 ------------------GGNPLVSAPDANRVR-----------------------------AALKKLDFVVVIDIFMTE 319
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 446653436 769 TALYSDIVLPASTWYEKHDLsSTDMHPFVHPFNPAIGSPWEARSDWDIFTSLSKAV 824
Cdd:cd00368 320 TAAYADVVLPAATYLEKEGT-YTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
156-823 |
4.79e-49 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 178.75 E-value: 4.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 156 RGKGGFIRANWDEVLQLVSASLLYTVMKYGPDRN-VGFSPIPAMSMLSHAAGSRFMQLMGGPMLSFYDWYADLPPASPQ- 233
Cdd:pfam00384 9 RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIaINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNGDLCTAAAAa 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 234 IWGDQTDV----PESSDWYNSGYIMTWGSNVPMTRTPD-AHFLAEVRYKGTKVVSVSPDFaeSTKFADDWISVKQGTDGA 308
Cdd:pfam00384 89 FGSDLRSNylfnSSIADIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRL--DLTYADEHLGIKPGTDLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 309 LAMAMGHVILQEFyvdnqveyftKYAKqytdfpffvtlkqkgdqfvadrflnasdigretklgewkpvlwnentndfatp 388
Cdd:pfam00384 167 LALAGAHVFIKEL----------KKDK----------------------------------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 389 hgtmgsrwdnekkwnlrledeetgekidprlsllgmeeaigtvqipyfsddgnkvlertipvkkvmteegelfvttvydl 468
Cdd:pfam00384 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 469 tlanygvnrglggqepkdfnddipftpawqekmtgvkreliiqiarefaqnavDTNGRSMIIVGAGINHWFNSDTIYRAV 548
Cdd:pfam00384 184 -----------------------------------------------------DFAPKPIIIVGAGVLQRQDGEAIFRAI 210
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 549 LNLVLLVGAQGVNGGGWAHYVgqeklrpaegwqtiamakdwqgppKLQNGTSFfyfvtdqwryedtpvghlaspvegnsr 628
Cdd:pfam00384 211 ANLADLTGNIGRPGGGWNGLN------------------------ILQGAASP--------------------------- 239
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 629 yqhhgdynVLAARLGwlpsyptfekngielykeavaagattqeeigkyvaqklkekelkfaiedpdnknNFPRNLFVWRA 708
Cdd:pfam00384 240 --------VGALDLG------------------------------------------------------LVPGIKSVEMI 257
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 709 NLISSSGKGHEYFLKHllgttnglmnddSDSLRPEEIKWHEEAPEgKLDLLINLDFRM-AGTALYSDIVLPASTWYEKHD 787
Cdd:pfam00384 258 NAIKKGGIKVLYLLGN------------NPFVTHADENRVVKALQ-KLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNG 324
|
650 660 670
....*....|....*....|....*....|....*.
gi 446653436 788 LSSTDMHPFVHpFNPAIGSPWEARSDWDIFTSLSKA 823
Cdd:pfam00384 325 TYVNTEGRVQS-TKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
51-567 |
1.08e-36 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 147.24 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 51 STHGVNCTGSCSWNIYVKDG-IVTWEGQELnypttgPDmPDFePRGCPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeel 129
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGkIVKVEPNEW------PD-KTY-KRGCTRGLSHLQRVYSPDRLKYPMKR----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 130 qnnespleawksivenrekartyKQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPdRNVGFSpipAMSMLSHAAGSRF 209
Cdd:cd02765 63 -----------------------VGERGEGKFERITWDEALDTIADKLTEAKREYGG-KSILWM---SSSGDGAILSYLR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 210 MQLMGGPMLSFYDWYADLPPASPQ--IWGDQTDVP--ESSDWYNSGYIMTWGSNVPMTRTPDAHFLAEVRYKGTKVVSVS 285
Cdd:cd02765 116 LALLGGGLQDALTYGIDTGVGQGFnrVTGGGFMPPtnEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVID 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 286 PDFAESTKFADDWISVKQGTDGALAMAMGHVILQEFYVDnqveyfTKYAKQYTDFPFFVtlkQKGDQfvadRFLNASDIG 365
Cdd:cd02765 196 PVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYD------EAFLKSNTSAPFLV---REDNG----TLLRQADVT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 366 RETKLGEWkpVLWNENTNDFATPHGTMGsrwdnekkwNLRLEDEetgekidprlsllgmeeaigtvqipyFSDDGNKvle 445
Cdd:cd02765 263 ATPAEDGY--VVWDTNSDSPEPVAATNI---------NPALEGE--------------------------YTINGVK--- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 446 rtipvkkvmteegelfVTTVYDltlanygvnrglggqepkDFNDDIP-FTPAWQEKMTGVKRELIIQIAREFAqnavdTN 524
Cdd:cd02765 303 ----------------VHTVLT------------------ALREQAAsYPPKAAAEICGLEEAIIETLAEWYA-----TG 343
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446653436 525 GRSMIIVGAGINHWFNSDTIYRAVLNLVLLVGAQGVNGGGWAH 567
Cdd:cd02765 344 KPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ 386
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
60-822 |
9.91e-33 |
|
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: 135.82 E-value: 9.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 60 SCSW---NIYVKDGIVTWegqelnyptTGPDMPDfEPRGCPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnnespl 136
Cdd:cd02751 3 ACHWgpfKAHVKDGVIVR---------VEPDDTD-QPRPCPRGRSVRDRVYSPDRIKYPMKR------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 137 eawKSIVENREKARtykQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDR---NVGFSPIPAMSMLSHAAGSRFMQLM 213
Cdd:cd02751 55 ---VGWLGNGPGSR---ELRGEGEFVRISWDEALDLVASELKRIREKYGNEAifgGSYGWASAGRLHHAQSLLHRFLNLI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 214 GGpMLSFYDWY--ADLPPASPQIWGDQTDVPESSDW----YNSGYIMTWGSNVPMTR--------TPDAHFLAEVRYKGT 279
Cdd:cd02751 129 GG-YLGSYGTYstGAAQVILPHVVGSDEVYEQGTSWddiaEHSDLVVLFGANPLKTRqgggggpdHGSYYYLKQAKDAGV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 280 KVVSVSPDFAESTK-FADDWISVKQGTDGALAMAMGHVILQEfyvdnqveyftkyaKQYtdfpffvtlkqkgDQfvadRF 358
Cdd:cd02751 208 RFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITE--------------DLH-------------DQ----AF 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 359 LNASDIGretklgewkpvlwnentndfatphgtmgsrWDNEKKWnlrledeetgekidprlsLLGmeeaigtvqipyfSD 438
Cdd:cd02751 257 LARYTVG------------------------------FDEFKDY------------------LLG-------------ES 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 439 DGnkvlertipvkkvmteegelfvttvydltlanygvnrglggqepkdfnddIPFTPAWQEKMTGVKRELIIQIAREFAQ 518
Cdd:cd02751 276 DG--------------------------------------------------VPKTPEWAAEITGVPAETIRALAREIAS 305
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 519 NavdtngRSMIIVGAGINHWFNSDTIYRAVLNLVLLVGAQGVNGGG---WAHYVGqeklrpaeGWQTIAMAKDWQGPPKL 595
Cdd:cd02751 306 K------RTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGfgfGYGYSN--------GGGPPRGGAGGPGLPQG 371
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 596 QNGTSFFyfvtdqwryedTPVGHLASPVEgnsryqHHGdynvlaarlgwlpsyPTFEKNGielykeavaagattqeeigk 675
Cdd:cd02751 372 KNPVKDS-----------IPVARIADALL------NPG---------------KEFTANG-------------------- 399
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 676 yvaqklkekelkFAIEDPDNKnnfprnlFVWRAnlisssgkGHEYFLKHllgttnglmNDDSDSLRpeeiKWHeeapegK 755
Cdd:cd02751 400 ------------KLKTYPDIK-------MIYWA--------GGNPLHHH---------QDLNRLIK----ALR------K 433
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446653436 756 LDLLINLDFRMAGTALYSDIVLPASTWYEKHDL--SSTDMHPFVHPFNPAIGSPWEARSDWDIFTSLSK 822
Cdd:cd02751 434 DETIVVHDIFWTASARYADIVLPATTSLERNDIglTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAK 502
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
55-835 |
2.13e-32 |
|
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: 134.76 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 55 VNCTGSCSWNIYVKDGIVTWEGQElnypTTGPDMPDF-EPRGCPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnne 133
Cdd:cd02770 6 VNCGGRCPLKAHVKDGVITRIETD----DTGDDDPGFhQIRACLRGRSQRKRVYNPDRLKYPMKR--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 134 spleawksivenrekartyKQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDR---NVGfSPIPAMSMLSHAAGSRFM 210
Cdd:cd02770 67 -------------------VGKRGEGKFVRISWDEALDTIASELKRIIEKYGNEAiyvNYG-TGTYGGVPAGRGAIARLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 211 QLMGGpMLSFYDWY--ADLPPASPQIWGdqTDVPESS--DWYNSGYIMTWGSNVPMTR---TPDAHFLAEVRYKGTKVVS 283
Cdd:cd02770 127 NLTGG-YLNYYGTYswAQITTATPYTYG--AAASGSSldDLKDSKLVVLFGHNPAETRmggGGSTYYYLQAKKAGAKFIV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 284 VSPDFAESTK-FADDWISVKQGTDGALAMAMGHVILQEFYVDNqveyftkyakqytdfpffvtlkqkgdqfvadRFLNAS 362
Cdd:cd02770 204 IDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQ-------------------------------AFLDRY 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 363 DIGretklgewkpvlwnentndFatphgtmgsrwdnekkwnlrleDEETgekidprlsllgmeeaigtvqipyfsddgnk 442
Cdd:cd02770 253 CVG-------------------F----------------------DAEH------------------------------- 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 443 vLERTIPVKKvmteegelfvttvydltlaNYgVNRGLGGQEpkdfnDDIPFTPAWQEKMTGVKRELIIQIAREFAqnavd 522
Cdd:cd02770 261 -LPEGAPPNE-------------------SY-KDYVLGTGY-----DGTPKTPEWASEITGVPAETIRRLAREIA----- 309
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 523 TNGRSMIIVGAGINHWFNSDTIYRAVLNLVLLVGAQGVNGGGWAHYVGQEKLRPAegwqtiamakdwqGPPKLQNgtsff 602
Cdd:cd02770 310 TTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGA-------------GLPAGKN----- 371
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 603 yfvtdqwryedtpvghlasPVEGnsryqhhgdynvlaarlgwlpSYPTFE-KNGIELYKEavaagaTTQEEIGKYVAQKL 681
Cdd:cd02770 372 -------------------PVKT---------------------SIPCFMwTDAIERGEE------MTADDGGVKGADKL 405
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 682 KEKelkfaIEdpdnknnfprnlFVWranlisssgkgheyflkHLLGttNGLMNDDSDSLRPEEIkwHEEAPEgKLDLLIN 761
Cdd:cd02770 406 KSN-----IK------------MIW-----------------NYAG--NTLINQHSDDNNTTRA--LLDDES-KCEFIVV 446
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446653436 762 LDFRMAGTALYSDIVLPASTWYEKHDL---SSTDMHPFVHPFNPAIGSPWEARSDWDIftslskaVSDLAKKIDLEP 835
Cdd:cd02770 447 IDNFMTPSARYADILLPDTTELEREDIvltSNAGMMEYLIYSQKAIEPLYECKSDYEI-------CAELAKRLGVED 516
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
57-338 |
2.37e-26 |
|
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: 113.93 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 57 CTGSCSWNIYVKDGIVTW-EGQelnypttgPDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnnesp 135
Cdd:cd02755 8 CSSRCGILARVEDGRVVKiDGN--------PLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIR----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 136 leawksiVEnrekartykqARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDRNVGFSPIPAMSMLSHAagsrFMQLMGG 215
Cdd:cd02755 63 -------VG----------ERGEGKFREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKH----FAAAFGS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 216 PMlsfYDWYADLPPASPQI-WGDQTDVPESS---DWYNSGYIMTWGSNV-PMTRTPDAHFLAEVRYKGTKVVSVSPDFAE 290
Cdd:cd02755 122 PN---IFSHESTCLASKNLaWKLVIDSFGGEvnpDFENARYIILFGRNLaEAIIVVDARRLMKALENGAKVVVVDPRFSE 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446653436 291 STKFADDWISVKQGTDGALAMAMGHVILQE-FYVDNQVEYFT-------KYAKQYT 338
Cdd:cd02755 199 LASKADEWIPIKPGTDLAFVLALIHVLISEnLYDAAFVEKYTngfellkAHVKPYT 254
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
57-320 |
2.72e-24 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 108.16 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 57 CTGSCSWNIYVKDG-IVTWEGQELNYPTTGpdmpdfepRGCPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnnesp 135
Cdd:cd02759 7 CHSGCGVLVYVKDGkLVKVEGDPNHPTNKG--------RLCMRGLAAPEIVYHPDRLLYPLKR----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 136 leawksivenrekartyKQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDRNVGFSPIPAMSMLSHAAGS-RFMQLMG 214
Cdd:cd02759 62 -----------------VGERGENKWERISWDEALDEIAEKLAEIKAEYGPESIATAVGTGRGTMWQDSLFWiRFVRLFG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 215 GP--MLSFYDWYA--DLPPASPQIWGDQTDVPessDWYNSGYIMTWGSNvPMTRTPD--AHFLAEVRYKGTKVVSVSPDF 288
Cdd:cd02759 125 SPnlFLSGESCYWprDMAHALTTGFGLGYDEP---DWENPECIVLWGKN-PLNSNLDlqGHWLVAAMKRGAKLIVVDPRL 200
|
250 260 270
....*....|....*....|....*....|..
gi 446653436 289 AESTKFADDWISVKQGTDGALAMAMGHVILQE 320
Cdd:cd02759 201 TWLAARADLWLPIRPGTDAALALGMLNVIINE 232
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
1078-1193 |
7.30e-23 |
|
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: 94.65 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1078 LNYLTPHNKWSIHSMYfDSLPMLTLFRGGP-TVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMHHA 1156
Cdd:pfam01568 1 LYLITGRVLGQYHSQT-RTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 446653436 1157 QDRhinvpgtkltSNRGGTHNSPTRIHVKPTHMIGGY 1193
Cdd:pfam01568 80 WWY----------EPRGGNANALTDDATDPLSGGPEF 106
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
56-338 |
1.44e-22 |
|
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: 103.10 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 56 NCTGSCSWNIYVKDG-IVTWEGQELNYPTtgpdmpdfepRG--CPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnn 132
Cdd:cd02766 7 DCPDTCSLLVTVEDGrIVRVEGDPAHPYT----------RGfiCAKGARYVERVYSPDRLLTPLKR-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 133 espleawksivenrekartykQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDR--------NVGFSPIPAMSMLSHA 204
Cdd:cd02766 63 ---------------------VGRKGGQWERISWDEALDTIAAKLKEIKAEYGPESilpysyagTMGLLQRAARGRFFHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 205 AGSrfMQLMGGPMLS------FYDWYADLPPAspqiwgdqtdvPEssDWYNSGYIMTWGSNVPMTRTPDAHFLAEVRYKG 278
Cdd:cd02766 122 LGA--SELRGTICSGagieaqKYDFGASLGND-----------PE--DMVNADLIVIWGINPAATNIHLMRIIQEARKRG 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446653436 279 TKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQE-----FYVDNQV---EYFTKYAKQYT 338
Cdd:cd02766 187 AKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREglydrDFLARHTegfEELKAHLETYT 254
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
1086-1193 |
8.01e-21 |
|
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: 88.53 E-value: 8.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1086 KWSIHSMYFDSLPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMHHAQDRHInvpg 1165
Cdd:cd02775 2 RDHFHSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRG---- 77
|
90 100
....*....|....*....|....*...
gi 446653436 1166 tkltsNRGGTHNSPTRIHVKPTHMIGGY 1193
Cdd:cd02775 78 -----GRGGNANVLTPDALDPPSGGPAY 100
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
56-320 |
8.56e-18 |
|
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: 88.27 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 56 NCTGSCSWNIYVKDG-IVTWEGQelnypttgPDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVR-----GVLWN------ 123
Cdd:cd02757 8 GCTAWCGLQAYVEDGrVTKVEGN--------PLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRtnprkGRDVDpkfvpi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 124 MWQEELQnnesplEAWKSIVENREKARTYKQA--RGKGGFIranwdevlqlvSASLLYTVMK-YGPDRNVGFSPIPAMSm 200
Cdd:cd02757 80 SWDEALD------TIADKIRALRKENEPHKIMlhRGRYGHN-----------NSILYGRFTKmIGSPNNISHSSVCAES- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 201 lshaagSRFmqlmggpmlsfydwyadlppaSPQIWGDQTDVPeSSDWYNSGYIMTWGSNVPMTRTPDAHFLA--EVRYKG 278
Cdd:cd02757 142 ------EKF---------------------GRYYTEGGWDYN-SYDYANAKYILFFGADPLESNRQNPHAQRiwGGKMDQ 193
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446653436 279 TKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQE 320
Cdd:cd02757 194 AKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTE 235
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
46-339 |
4.90e-17 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 86.62 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 46 DKVIRSTHGVNCTGSCSWNIYVKDGIVTWegqeLNYPTTGPDMPD--FEPRGCPRGASFSWYIYSPLRVKYPYVRgvlwn 123
Cdd:PRK14990 56 EKVIWSACTVNCGSRCPLRMHVVDGEIKY----VETDNTGDDNYDglHQVRACLRGRSMRRRVYNPDRLKYPMKR----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 124 mwqeelqnnespleawksivenrekartyKQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDR---NVGFSPIPAMSM 200
Cdd:PRK14990 127 -----------------------------VGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESiylNYGTGTLGGTMT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 201 LSHAAG----SRFMQLMGGPMLSFYDWY-ADLPPASPQIWGDQTDVPESSDWYNSGYIMTWGSNVPMTRTPDA---HFLA 272
Cdd:PRK14990 178 RSWPPGntlvARLMNCCGGYLNHYGDYSsAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGgvtYYLE 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446653436 273 EVRYKGT-KVVSVSPDFAES-TKFADDWISVKQGTDGALAMAMGHVILQEFYVDNqvEYFTKYAKQYTD 339
Cdd:PRK14990 258 QARQKSNaRMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQ--PFLDKYCVGYDE 324
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
46-1171 |
2.97e-16 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 84.17 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 46 DKVIRST---HGVnctgSCSWNIYVKDG-IVTWEGQElNYPTTgpdmpdfepRG--CPRGAsFSW-YIYSPLRVKYPYVR 118
Cdd:COG3383 4 MKKVKTVcpyCGV----GCGIDLEVKDGkIVKVEGDP-DHPVN---------RGrlCVKGR-FGFeFVNSPDRLTTPLIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 119 GvlwnmwqeelqnnespleawksivenrekartykqargKGGFIRANWDEVLQLVSASLLYTVMKYGPDRnVGF--SP-- 194
Cdd:COG3383 69 R--------------------------------------GGEFREVSWDEALDLVAERLREIQAEHGPDA-VAFygSGql 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 195 --------------------IPAMSMLSHA-AGSRFMQLMGGPMLSFYdwYADLppaspqiwgDQTDVpessdwynsgyI 253
Cdd:COG3383 110 tneenyllqklargvlgtnnIDNNARLCMAsAVAGLKQSFGSDAPPNS--YDDI---------EEADV-----------I 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 254 MTWGSNvpmtrTPDAH-----FLAEVRYKGTKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQEFYVDnqve 328
Cdd:COG3383 168 LVIGSN-----PAEAHpvlarRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVD---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 329 yftkyakqytdfpffvtlkqkgDQFVADRflnasdigretklgewkpvlwnenTNDFatphgtmgsrwdnekkwnlrled 408
Cdd:COG3383 239 ----------------------EDFIAER------------------------TEGF----------------------- 249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 409 eetgekidprlsllgmEEAIGTVQipyfsddgnkvlertipvkkvmteegelfvttvydltlanygvnrglggqepkdfn 488
Cdd:COG3383 250 ----------------EELKASVA-------------------------------------------------------- 257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 489 ddiPFTPAWQEKMTGVKRELIIQIAREFAqnavdTNGRSMIIVGAGIN-HWFNSDTIyRAVLNLVLLVGAQGVNGGGwah 567
Cdd:COG3383 258 ---KYTPERVAEITGVPAEDIREAARLIA-----EAKRAMILWGMGVNqHTQGTDNV-NAIINLALATGNIGRPGTG--- 325
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 568 yvgqeklrpaegwqtiamakdwqgppklqngtsfFYFVTDQwryedtpvghlaspvegNsryqhhgdyNVLAARL----- 642
Cdd:COG3383 326 ----------------------------------PFPLTGQ-----------------N---------NVQGGRDmgalp 345
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 643 GWLPSYPTFEKNGIELYKEAVAAGATTQEEIGkyvaqkLKEKELKFAIEDPDnknnfPRNLFVwranlisssgkgheyfl 722
Cdd:COG3383 346 NVLPGYRDVTDPEHRAKVADAWGVPPLPDKPG------LTAVEMFDAIADGE-----IKALWI----------------- 397
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 723 khlLGTtNGLMND-DSDSLRpeeikwheEAPEgKLDLLINLDFRMAGTALYSDIVLPASTWYEKhDLSSTDMHPFVHPFN 801
Cdd:COG3383 398 ---IGE-NPAVSDpDANHVR--------EALE-KLEFLVVQDIFLTETAEYADVVLPAASWAEK-DGTFTNTERRVQRVR 463
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 802 PAIGSPWEARSDWDIFtslskavSDLAKKIDLepmkevvatPLLHDTPQElaqplgkikdwskgecepipgktmpqihvv 881
Cdd:COG3383 464 KAVEPPGEARPDWEII-------AELARRLGY---------GFDYDSPEE------------------------------ 497
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 882 erdyktIYDKMTALGPNAGkqpigtkGISwsaekeYEQLKsklgvvRTDSIAKGCPDikeainaaeavltlssttnghma 961
Cdd:COG3383 498 ------VFDEIARLTPDYS-------GIS------YERLE------ALGGVQWPCPS----------------------- 529
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 962 vkawealekqtdlklrdlaEEREEECFTFEQitaqpktvitspAF-TGSEKG---GRRYSPFTTNVERLIPWRTITGRqs 1037
Cdd:COG3383 530 -------------------EDHPGTPRLFTG------------RFpTPDGKArfvPVEYRPPAELPDEEYPLVLTTGR-- 576
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1038 fyldhdmmkefgetmatfkpILQHkpfrksrpevegkeitlnyltphnkWSIHSMYFDSlPMLTLFRGGPTVWMNKEDAA 1117
Cdd:COG3383 577 --------------------LLDQ-------------------------WHTGTRTRRS-PRLNKHAPEPFVEIHPEDAA 610
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*.
gi 446653436 1118 EAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFM--HHAqDRHINVpgtkLTSN 1171
Cdd:COG3383 611 RLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMpfHWG-EGAANA----LTND 661
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
52-563 |
2.22e-15 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 81.17 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 52 THGVNCTGSCSW-NIYVKDGIVTweGQELNypttgPDMPDFEP---RGCPRGASFSWYIYSPLRVKYPYVRgvlwnmwqe 127
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVAT--EIEPN-----FAAEDIHPargRVCVKAYGLVQKTYNPNRVLQPMKR--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 128 elqnnespleawksivENREKARTYKQargkgGFIRANWDEVLQLVSASLLYTVMKYGPDR--------NVGFSPIPAMS 199
Cdd:cd02760 66 ----------------TNPKKGRNEDP-----GFVPISWDEALDLVAAKLRRVREKGLLDEkglprlaaTFGHGGTPAMY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 200 MLSHAAgsrFMQLMGGPMLSFYDWYADLPPASPQIWGD--QTDVPESSDWYNSGYIMTWGSNVPMTRTPDAHFL-AEVRY 276
Cdd:cd02760 125 MGTFPA---FLAAWGPIDFSFGSGQGVKCVHSEHLYGEfwHRAFTVAADTPLANYVISFGSNVEASGGPCAVTRhADARV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 277 KGTKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQEFYVDnqvEYFTKYAKQYTDFPFFVtlkqkGDQfvaD 356
Cdd:cd02760 202 RGYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMFAMIHVMVHEQGLG---KLDVPFLRDRTSSPYLV-----GPD---G 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 357 RFLNASDIGretklgewKPVLWNENTNDfATPHGTMGSrwdnekkwnlrledeetGEKIDPRLSLLGmeeaigtvqipyf 436
Cdd:cd02760 271 LYLRDAATG--------KPLVWDERSGR-AVPFDTRGA-----------------VPAVAGDFAVDG------------- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 437 sddgnkvlERTIPVKKVMTEEGELFVTTVYDLTLANYGvnrglggqepkdfnddiPFTPAWQEKMTGVKRELIIQIAREF 516
Cdd:cd02760 312 --------AVSVDADDETAIHQGVEGTTAFTMLVEHMR-----------------KYTPEWAESICDVPAATIRRIAREF 366
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446653436 517 AQNA-----VDTNGRSM------IIVGAGINHWFNSDTIYRAVLNLVLLVGAQGVNGG 563
Cdd:cd02760 367 LENAsigstIEVDGVTLpyrpvaVTLGKSVNNGWGAFECCWARTLLATLVGALEVPGG 424
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
60-320 |
1.16e-14 |
|
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: 78.84 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 60 SCSWNIY---VKDGIVT----WEgqELNYPTtgpdmpdfeprgcPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnn 132
Cdd:cd02769 3 ASHWGAFrarVKDGRIVgvrpFE--EDPDPS-------------PLLDGVPDAVYSPTRIKYPMVR-------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 133 espleawKSIVENREKARTykQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPdrnvgfSPIPAMS-------MLSHAA 205
Cdd:cd02769 54 -------RGWLEKGPGSDR--SLRGKEEFVRVSWDEALDLVAAELKRVRKTYGN------EAIFGGSygwssagRFHHAQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 206 G--SRFMQLMGG-----------------PM-LSFYDWYADLPPASPQIwgdqtdvPESSDwynsgYIMTWGSNVPMTR- 264
Cdd:cd02769 119 SllHRFLNLAGGyvgsvgdystgaaqvilPHvVGSMEVYTEQQTSWPVI-------AEHTE-----LVVAFGADPLKNAq 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446653436 265 -----TPDaH----FLAEVRYKGTKVVSVSPDFAESTKFAD-DWISVKQGTDGALAMAMGHVILQE 320
Cdd:cd02769 187 iawggIPD-HqaysYLKALKDRGIRFISISPLRDDTAAELGaEWIAIRPGTDVALMLALAHTLVTE 251
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
1078-1150 |
2.58e-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: 65.08 E-value: 2.58e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446653436 1078 LNYLTPHNKWSIHSMyFDSLPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGM 1150
Cdd:cd02785 4 LACIQRHSRFRVHSQ-FSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGV 75
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1078-1155 |
3.96e-11 |
|
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: 61.83 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1078 LNYLTPHNKWSIHSMYfDSLPMLTL---FRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMH 1154
Cdd:cd02777 3 LQLISPHPKRRLHSQL-DNVPWLREaykVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALP 81
|
.
gi 446653436 1155 H 1155
Cdd:cd02777 82 E 82
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
57-344 |
6.28e-11 |
|
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: 66.78 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 57 CTGSCSWNIYVKDGIVTwegqelnYPTTGPDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnnespl 136
Cdd:cd02763 7 CACRCGIRVHLRDGKVR-------YIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLR------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 137 eawksivenrekartyKQARGKGGFIRANWDEVLQlVSASLLYTVMKYGPDRNVGFSPIPAMSMLSHAAGSRFmqlmGGP 216
Cdd:cd02763 62 ----------------KGPRGSGQFEEIEWEEAFS-IATKRLKAARATDPKKFAFFTGRDQMQALTGWFAGQF----GTP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 217 MLSFYDWYADLPPASPQIWGDQTDVPE--SSDWYNSGYIMTWGSNVPMTRTPDAHFLAEVRYKGTKVVSVSPDFAESTKF 294
Cdd:cd02763 121 NYAAHGGFCSVNMAAGGLYSIGGSFWEfgGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAI 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446653436 295 ADDWISVKQGTDGALAMAMGHVILQEFYVDNQveyftkYAKQYTDFPFFV 344
Cdd:cd02763 201 ADEWVPIKPGTDGAFILALAHELLKAGLIDWE------FLKRYTNAAELV 244
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
57-823 |
1.26e-10 |
|
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: 65.31 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 57 CTGSCSWNIYVKDG-IVTWEGQelnypttgPDMPDFEPRGCPRGAsFSW-YIYSPLRVKYPYVRGvlwnmwqeelqnnes 134
Cdd:cd02753 7 CGVGCGLELWVKDNkIVGVEPV--------KGHPVNRGKLCVKGR-FGFdFVNSKDRLTKPLIRK--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 135 pleawksivenrekartykqargKGGFIRANWDEVLQLVSASLLYTVMKYGPDRnVGFspipamsmLSHAAGS------- 207
Cdd:cd02753 63 -----------------------NGKFVEASWDEALSLVASRLKEIKDKYGPDA-IAF--------FGSAKCTneenylf 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 208 -RFMQLMGGPmlSFYDWYADLPpASPQIWGDQTDVPESSDW------YNSGYIMTWGSNvpmtrTPDAHFLAEVRYK--- 277
Cdd:cd02753 111 qKLARAVGGT--NNVDHCARLC-HSPTVAGLAETLGSGAMTnsiadiEEADVILVIGSN-----TTEAHPVIARRIKrak 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 278 --GTKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQEFYVDnqveyftkyakqytdfpffvtlkqkgDQFVA 355
Cdd:cd02753 183 rnGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYD--------------------------EEFIE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 356 DRflnasdigretklgewkpvlwnenTNDFatphgtmgsrwdnekkwnlrledeetgekidprlsllgmEEAIGTVQipy 435
Cdd:cd02753 237 ER------------------------TEGF---------------------------------------EELKEIVE--- 250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 436 fsddgnkvlertipvkkvmteegelfvttvydltlanygvnrglggqepkdfnddiPFTPAWQEKMTGVKRELIIQIARE 515
Cdd:cd02753 251 --------------------------------------------------------KYTPEYAERITGVPAEDIREAARM 274
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 516 FAqnavdTNGRSMIIVGAGINHWFN-SDTIyRAVLNLVLLVGAQGVNGGGwahyvgqeklrpaegwqtiamakdwqgppk 594
Cdd:cd02753 275 YA-----TAKSAAILWGMGVTQHSHgTDNV-MALSNLALLTGNIGRPGTG------------------------------ 318
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 595 lqngtsffyfvtdqwryedtpvghlASPVEGNSRYQHHGDYNVLAarlGWLPSYptfekngielykeaVAAGATTQEEIg 674
Cdd:cd02753 319 -------------------------VNPLRGQNNVQGACDMGALP---NVLPGY--------------VKALYIMGENP- 355
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 675 kyvaqklkekelkfAIEDPDnknnfprnlfvwranlisssgkgheyfLKHLlgttnglmnddsdslrpeeikwhEEAPEg 754
Cdd:cd02753 356 --------------ALSDPN---------------------------TNHV-----------------------RKALE- 370
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 755 KLDLLINLDFRMAGTALYSDIVLPASTWYEKH-DLSSTDMHpfVHPFNPAIGSPWEARSDWDIFTSLSKA 823
Cdd:cd02753 371 SLEFLVVQDIFLTETAELADVVLPAASFAEKDgTFTNTERR--VQRVRKAVEPPGEARPDWEIIQELANR 438
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
57-338 |
2.10e-10 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 65.07 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 57 CTGSCSWNIYVKDG-IVTWEGQelnypttgPDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnnesp 135
Cdd:PRK15488 51 CSTRCPIEARVVNGkNVFIQGN--------PKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKR----------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 136 leawksivenrekartyKQARGKGGFIRANWDEVLQLVSASLLYTVMKYGPDrNVGFSpipAMSMLSHAAGSRFMQLMGG 215
Cdd:PRK15488 106 -----------------VGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPE-SVAFS---SKSGSLSSHLFHLATAFGS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 216 PMLsFYdwYADLPPASPQIWGDQTDVPE-SSDWYNSGYIMTWGSN------VPMTRTPdAHFLAEvryKGTKVVSVSPDF 288
Cdd:PRK15488 165 PNT-FT--HASTCPAGYAIAAKVMFGGKlKRDLANSKYIINFGHNlyeginMSDTRGL-MTAQME---KGAKLVVFEPRF 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446653436 289 AESTKFADDWISVKQGTDGALAMAMGHVILQE-----FYVDNQVEYFTKYA---KQYT 338
Cdd:PRK15488 238 SVVASKADEWHAIRPGTDLAVVLALCHVLIEEnlydkAFVERYTSGFEELAasvKEYT 295
|
|
| Nitr_red_alph_N |
pfam14710 |
Respiratory nitrate reductase alpha N-terminal; This is the N-terminal tail of the respiratory ... |
8-43 |
2.44e-10 |
|
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: 56.47 E-value: 2.44e-10
10 20 30
....*....|....*....|....*....|....*..
gi 446653436 8 LMRRLKYFSPI-DRYNDNHTQETYEDREWENVYRKRW 43
Cdd:pfam14710 1 FLDRLRFFKRKrETFADGHGETTNEDRDWEDAYRQRW 37
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
1098-1156 |
8.02e-10 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 57.52 E-value: 8.02e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446653436 1098 PMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFM--HHA 1156
Cdd:cd00508 26 PRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMpfHWG 86
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
1094-1192 |
8.52e-10 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 57.68 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 1094 FDSLPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFmhhaqdrhinVPGT--KLTSN 1171
Cdd:cd02786 18 FANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVV----------AEGGwwREHSP 87
|
90 100
....*....|....*....|.
gi 446653436 1172 RGGTHNSPTriHVKPTHMIGG 1192
Cdd:cd02786 88 DGRGVNALT--SARLTDLGGG 106
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
156-320 |
3.21e-09 |
|
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: 60.87 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 156 RGKGGFIRANWDEVLQLVSASLLYTVMKYGPDRnVGF---SPiPAMSMLSHAAGSRFMQLMGGPMLsFYDWYADLPP--- 229
Cdd:cd02762 61 RRGGSFEEIDWDEAFDEIAERLRAIRARHGGDA-VGVyggNP-QAHTHAGGAYSPALLKALGTSNY-FSAATADQKPghf 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 230 ASPQIWGDQTDVPeSSDWYNSGYIMT-----WGSNVPMTRTPDA-HFLAEVRYKGTKVVSVSPDFAESTKFADDWISVKQ 303
Cdd:cd02762 138 WSGLMFGHPGLHP-VPDIDRTDYLLIlganpLQSNGSLRTAPDRvLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRP 216
|
170
....*....|....*..
gi 446653436 304 GTDGALAMAMGHVILQE 320
Cdd:cd02762 217 GTDAWLLAAMLAVLLAE 233
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
57-344 |
8.93e-09 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 59.55 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 57 CTGSCSWNIYVKDG-IVTWEGQElNYPTTgpdmpdfepRG--CPRGASFSWYIYSPLRVKYPYVRgvlwnmwqeelqnne 133
Cdd:cd02754 7 CGVGCGVEIGVKDGkVVAVRGDP-EHPVN---------RGrlCIKGLNLHKTLNGPERLTRPLLR--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 134 spleawksivenrekartykqaRGKGGFIRANWDEVLQLVSASLLYTVMKYGPDrNVGF-----SPIPAMSMLSH----- 203
Cdd:cd02754 62 ----------------------RNGGELVPVSWDEALDLIAERFKAIQAEYGPD-SVAFygsgqLLTEEYYAANKlakgg 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 204 ---------------AAGSRFMQLMG--GPMLSfydwYADLppaspqiwgDQTDVpessdwynsgyIMTWGSN------V 260
Cdd:cd02754 119 lgtnnidtnsrlcmaSAVAGYKRSFGadGPPGS----YDDI---------EHADC-----------FFLIGSNmaechpI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 261 PMTRTPDAHFLAEvrykGTKVVSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVILQEFYVDNqvEYFTKYAKQYTDF 340
Cdd:cd02754 175 LFRRLLDRKKANP----GAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDR--DFIDAHTEGFEEL 248
|
....
gi 446653436 341 PFFV 344
Cdd:cd02754 249 KAFV 252
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
1098-1154 |
1.43e-08 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 54.12 E-value: 1.43e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446653436 1098 PMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAF--MH 1154
Cdd:cd02791 26 PRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFvpMH 84
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1078-1154 |
2.18e-07 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 51.10 E-value: 2.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446653436 1078 LNYLTPHNKWSIHSMY-FDSLPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMH 1154
Cdd:cd02793 3 LHLLSNQPATRLHSQLdHGSLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
46-108 |
5.17e-07 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 47.63 E-value: 5.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446653436 46 DKVIRSTHGVnCTGSCSWNIYVKDGIVTWegqelnypTTG-PDMPDFEPRGCPRGASFSWYIYS 108
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVR--------VRGdPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
1078-1155 |
9.97e-07 |
|
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: 48.83 E-value: 9.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446653436 1078 LNYLTPHNKWSIHSMyFDSLPMLTlfRGGP-TVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMHH 1155
Cdd:cd02794 3 LQLIGWHYKRRTHST-FDNVPWLR--EAFPqEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQ 78
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
755-823 |
1.31e-06 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 52.61 E-value: 1.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446653436 755 KLDLLINLD-FRMAGTALYSDIVLPASTWYEKH------DLSSTDMHPFVHPfnpaigsPWEARSDWDIFTSLSKA 823
Cdd:cd02754 416 RLEFVVVQDaFADTETAEYADLVLPAASWGEKEgtmtnsERRVSLLRAAVEP-------PGEARPDWWILADVARR 484
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
1087-1153 |
3.35e-06 |
|
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: 47.23 E-value: 3.35e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446653436 1087 WSIHSMYFDSlPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFM 1153
Cdd:cd02790 16 YHTGTMTRRA-EGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFM 81
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
755-822 |
3.40e-06 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 51.60 E-value: 3.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446653436 755 KLDLLINLDFRMAGTALYSDIVLPASTWYEKHDLSS---------TDMHPFVHPFnpaigspWEARSDWDIFTSLSK 822
Cdd:PRK15102 494 KLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQygsysnrgiIAMKKVVEPL-------FESRSDFDIFRELCR 563
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
1087-1155 |
2.35e-05 |
|
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: 45.38 E-value: 2.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446653436 1087 WSIHSMYFdSLPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMHH 1155
Cdd:cd02781 14 YYFHSEHR-QLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEH 81
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
96-320 |
3.35e-05 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 48.11 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 96 CPRGASFSWYIYSPLRVKYPYVR----GVlwNMWQEElqnneSPLEAWKSIVEnrekartykqargkGGFIRANwDEVLQ 171
Cdd:cd02758 68 CARGNAGLQYLYDPYRVLQPLKRvgprGS--GKWKPI-----SWEQLIEEVVE--------------GGDLFGE-GHVEG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 172 LVSASLLYTVM-----KYGPDRN----VGFSPIPAMSMLShaagsRFM-QLMGGPMLSFYDWYADLP-PASPQIW-GDQT 239
Cdd:cd02758 126 LKAIRDLDTPIdpdhpDLGPKANqllyTFGRDEGRTPFIK-----RFAnQAFGTVNFGGHGSYCGLSyRAGNGALmNDLD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 240 DVPE-SSDWYNSGYIMTWG-----SNVPMTRTpdAHFLAEVRYKGT-KVVSVSPDFAESTKFADD---WISVKQGTDGAL 309
Cdd:cd02758 201 GYPHvKPDFDNAEFALFIGtspaqAGNPFKRQ--ARRLAEARTEGNfKYVVVDPVLPNTTSAAGEnirWVPIKPGGDGAL 278
|
250
....*....|.
gi 446653436 310 AMAMGHVILQE 320
Cdd:cd02758 279 AMAMIRWIIEN 289
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
246-365 |
3.75e-05 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 48.07 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 246 DWYNSGYIMTWG-----SNVPMTRTpdAHFLAEVRYKGT-KVVSVSPDF-AESTKFADD---WISVKQGTDGALAMAMGH 315
Cdd:PRK14991 282 DWDNVEFALFIGtspaqSGNPFKRQ--ARQLANARTRGNfEYVVVAPALpLSSSLAAGDnnrWLPIRPGTDSALAMGMIR 359
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446653436 316 VILqefyvDNQveyftKYAKQYTDFPFFVTLKQKGDQ--------FVAD-------RFLNASDIG 365
Cdd:PRK14991 360 WII-----DNQ-----RYNADYLAQPGVAAMQAAGEAswtnathlVIADpghprygQFLRASDLG 414
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
57-318 |
4.78e-05 |
|
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: 47.78 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 57 CTGSCSWNIYVKDGIvtWEGQELNypttgPDMPDFEPRGCPRGASFSWYIYSPLRVKYPYVRGVLWNMWQEelqnnespl 136
Cdd:cd02752 7 CSVGCGLIAYVQNGV--WVHQEGD-----PDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 137 EAWKSIVEnrEKARTYKQARGKgGFIRANWDEVlqlvsasllyTVmkYGPDrnvgfspipAMSMLSHAAGS--------R 208
Cdd:cd02752 71 ISWDEALD--EIARKMKDIRDA-SFVEKNAAGV----------VV--NRPD---------SIAFLGSAKLSneecylirK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 209 FMQLMGgpmLSFYDWYADLPPAS-----PQIWGDQTDVPESSDWYNSGYIMTWGSNvPMTRTPDA--HFLAEVRYKGTKV 281
Cdd:cd02752 127 FARALG---TNNLDHQARIUHSPtvaglANTFGRGAMTNSWNDIKNADVILVMGGN-PAEAHPVSfkWILEAKEKNGAKL 202
|
250 260 270
....*....|....*....|....*....|....*..
gi 446653436 282 VSVSPDFAESTKFADDWISVKQGTDGALAMAMGHVIL 318
Cdd:cd02752 203 IVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYII 239
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
1108-1155 |
7.50e-05 |
|
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: 43.42 E-value: 7.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446653436 1108 TVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMHH 1155
Cdd:cd02778 31 TLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH 78
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
106-320 |
3.91e-04 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 44.66 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 106 IYSPLRVKYPYVRgVLWnmwqeelqnnespleawksiVENREKARTykQARGKGGFIRANWDEVLQLVSASLLYTVMKYG 185
Cdd:PRK15102 85 VYNPSRIRYPMVR-LDW--------------------LRKRHKSDT--SQRGDNRFVRVSWDEALDLFYEELERVQKTYG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 186 PDR----NVGFSpipAMSMLsHAAGSRFMQLMG--GPMLSFYDWYAD------LP--PASPQIWGDQTDVPESSDwyNSG 251
Cdd:PRK15102 142 PSAlhtgQTGWQ---STGQF-HSATGHMQRAIGmhGNSVGTVGDYSTgagqviLPyvLGSTEVYEQGTSWPLILE--NSK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 252 YIMTWGS----------NVPmTRTPDAHF--LAE-VRYKGTKVVSVSPDFAESTKFAD-DWISVKQGTDGALAMAMGHVI 317
Cdd:PRK15102 216 TIVLWGSdpvknlqvgwNCE-THESYAYLaqLKEkVAKGEINVISIDPVVTKTQNYLGcEHLYVNPQTDVPLMLALAHTL 294
|
...
gi 446653436 318 LQE 320
Cdd:PRK15102 295 YSE 297
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
1109-1154 |
1.16e-03 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 43.12 E-value: 1.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446653436 1109 VWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFMH 1154
Cdd:PRK15102 712 VYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIH 757
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
1080-1153 |
1.17e-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: 40.13 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446653436 1080 YLTPHNkwsihSMYFDSLPMltlfrggPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFM 1153
Cdd:cd02779 18 YHDQNN-----SEIAERVPL-------PYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFM 79
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
1096-1153 |
1.56e-03 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 39.90 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446653436 1096 SLPMLTLFRGGPTVWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFM 1153
Cdd:cd02792 24 NSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGI 81
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
489-570 |
3.38e-03 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 41.58 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 489 DDIPFTPAWQEKMTGVKRELIiqiaREFAQnaVDTNGRSMIIVGAGINHWFNSDTIYRAVLNLVLLVGAQGVNGGGWA-- 566
Cdd:PRK15102 324 DGVPKTPEWAEKICGIDAETI----RELAR--QMAKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISyg 397
|
....*
gi 446653436 567 -HYVG 570
Cdd:PRK15102 398 hHYSG 402
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
1109-1153 |
3.90e-03 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 38.18 E-value: 3.90e-03
10 20 30 40
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gi 446653436 1109 VWMNKEDAAEAGVADNDWIECFNRNGVVVARAVVTHRIPRGMAFM 1153
Cdd:cd02789 33 CEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFI 77
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| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
750-821 |
5.92e-03 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 40.84 E-value: 5.92e-03
10 20 30 40 50 60 70
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gi 446653436 750 EAPEGKLDLLINLDFRMAGTALYSDIVLPASTWYEKhDLSSTDMHPFVHPFNPAIGSP-WEARSDWDIFTSLS 821
Cdd:cd02771 359 EAALDAAEFVVVLDHFLTETAERADVVLPAASFAEK-SGTFVNYEGRAQRFFKAYDDPaGDARSDWRWLHALA 430
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| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
754-879 |
7.87e-03 |
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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: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446653436 754 GKLDLLINLDFRMAGTALYSD-------------IVLPASTWYEKhDLSSTDMHPFVHPFNPAIGSPWEARSDWDIFTSL 820
Cdd:cd02752 358 DKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEK-EGSITNSGRWLQWRYKVVEPPGEAKSDGDILVEL 436
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446653436 821 SKAVSDLAKK---IDLEPMKEVVATPLLHDTPQELAQPLGKiKDWSKGECEPIPG---KTMPQIH 879
Cdd:cd02752 437 AKRLGFLYEKeggAFPEPITKWNYGYGDEPTPEEIAREING-GALTDGYTGQSPErlkAHGQNVH 500
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