|
Name |
Accession |
Description |
Interval |
E-value |
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
11-1231 |
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: 2382.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 11 GNASDALLKVGRYFTKWDETDDGRAVFRKGGRQGDVFYRDRWSHDKVVRSTHGVNCTGSCSWKVYVKDGIITWESQQTDY 90
Cdd:COG5013 2 GPASSHLLDRLRFFRRGEVFSDGHGVTTEGGREWEDFYRDRWQHDKVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 91 PSVGPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPYARGVLVEMYREAKRRLGDPVLAWADVVGDEERRRTYQRARGKGGL 170
Cdd:COG5013 82 PRTGPDLPNYEPRGCPRGASFSWYTYSPTRVKYPYVRGVLLELWREARARHGDPVEAWASIVEDPEKRRRYKSARGKGGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 171 IRISWDEATEITAAAHVHTIKTHGPDRCAGFSPIPAMSMVSHCVGTRFIQLIGGAMTSFYDWYADLPVASPQVFGDQTDV 250
Cdd:COG5013 162 VRATWDEANEIIAAANVYTIKKYGPDRVAGFSPIPAMSMVSYAAGARFLSLIGGVMLSFYDWYADLPPASPQVWGEQTDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 251 PESGDWWDSTYLMMWGSNVPVTRTPDAHWMTEVRYRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREF 330
Cdd:COG5013 242 PESADWYNSGYLIMWGSNVPQTRTPDAHFMTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 331 FVDRDVSFFSDYVRTYTDLPFLVRLRERGGDLVPGKFLTGADLGASDDED---AWKTVVLDEETGEPVVPNGSMGFRYAA 407
Cdd:COG5013 322 HVDRQVPYFTDYARRYTDLPFLVTLEERDGGYVPGRFLRASDLGGALGESnnpEWKTVVLDEATGEPVVPNGSIGFRWGE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 408 SgEGRWNLDLEG-----VNPSLTLYGG--ESAEVLLPSYGGTDGTGETLRRGVPVREV----GGQLVTTVYDLMLAQYGV 476
Cdd:COG5013 402 S-EGKWNLELKDatgadVDPALSLLDDhdEVVEVAFPYFGGETGGGGVLRRGVPVRRVtladGEVLVTTVFDLMLANYGV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 477 ARdGLPGEWPSGYDDPsTPYTPAWQESITSVPAQACIRIAREFAKNAEDSGGRSMIIMGAGICQWFHGDATYRAVLTLLL 556
Cdd:COG5013 481 DR-GLPGNWPTGYDDD-VPYTPAWQEKITGVPREQVIRVAREFAQNAEKTRGRSMIIMGAGTNHWYHSDMIYRAILNLLM 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 557 LTGCMGRNGGGWAHYVGQEKCRPITGWISLANALDWSRPPRTVPGTSYWYMHTDQWRTDGYPADALASPLADGHLAGMHT 636
Cdd:COG5013 559 LCGCQGVNGGGWAHYVGQEKLRPQTGWQPLAFALDWSRPPRQMNGTSFFYAHTDQWRYETLSADELLSPLADGKFWGGHL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 637 ADTIAASARMGWMPFYPQFDRNPLDVADDATAAVDagdspDAATYVARQLTDGDLTPAIDDVDAPQNWPRTLVLWRSNLM 716
Cdd:COG5013 639 ADYNVRAARLGWLPSYPQFNRNPLDLADEAEAAGM-----EPADYVVDQLKSGELKFACEDPDNPENFPRNLFVWRSNLL 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 717 GSSAKGSEYFQRHLLGTHANTTAEPVDESSRPRDVRWRDEAPEGKLDLLVSADFRMTSTTLLSDIVFPAATWYEKHDLSS 796
Cdd:COG5013 714 GSSGKGHEYFLKHLLGTDNGVQGEELGPGLRPREVVWRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKHDLST 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 797 TDMHPFVHAFSPAIDPPWEAKTDFETFHLIARKLSELAKTHLGVRRDLVSVPMQHDTPGQTAQPGGVARDWRDGDADPQP 876
Cdd:COG5013 794 TDMHPFIHPFSPAVDPPWEARSDWDIFKGIAKKFSELAAGHLGVRKDVVATPLQHDTPGELAQPFGDVKDWKKGECEPIP 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 877 GKTMPNFTVVERDYTAIADKLGAVGPLADELGFTVKNVTYDLEEEVRRLASHHGVM-SHGAAAGRPALDTDSKLADAILA 955
Cdd:COG5013 874 GKTMPKLVVVERDYPAIYEKFTSLGPLLEKLGNGGKGITWDTEEEVEELGKLNGVVrEEGVAKGRPRLDTDIDAAEAILA 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 956 FSGTTNGSLALQGFRTLERRVGKPLADLAEGSEERRITFADTQRGPVPVITSPEWSGSETGGRRYAPFTVNIERLKPFHT 1035
Cdd:COG5013 954 LSPETNGHVAVKAWKALEKRTGRDLAHLAAGREEEKIRFRDIQAQPRKVITSPTWSGSESGGRRYSAFTTNVEELIPWRT 1033
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1036 LTGRMHFYLDHDWMSDLGEQLPTYRPPVDMQRLFGAPPFGPNGGNQVTVRYLTPHSKWSIHSEYQDNLFMLSLSRGGPTV 1115
Cdd:COG5013 1034 LTGRQHFYLDHDWMREFGEGLPVYRPPLDMKTLFGEPGIGPNGNPEIVLRYLTPHQKWGIHSTYQDNLLMLTLSRGGPTV 1113
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1116 WMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYHAQERTIDVPKSEATGRRGGIHNSVTRLLVKPTHL 1195
Cdd:COG5013 1114 WMSEEDAAKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHAQERIVNVPGSEITGKRGGIHNSVTRIVLKPTHM 1193
|
1210 1220 1230
....*....|....*....|....*....|....*.
gi 2320167329 1196 IGAYAQLSYAFNYLGPTGNQRDMVSTVRKRSQdVTY 1231
Cdd:COG5013 1194 IGGYAQLSYGFNYYGPTGNQRDEVVVVRKRSQ-VDW 1228
|
|
| narG |
TIGR01580 |
respiratory nitrate reductase, alpha subunit; The Nitrate reductase enzyme complex allows ... |
17-1224 |
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: 1505.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 17 LLKVGRYFTKWDET-DDGRAVFRKGGRQGDVFYRDRWSHDKVVRSTHGVNCTGSCSWKVYVKDGIITWESQQTDYPSVGP 95
Cdd:TIGR01580 3 LLDRLRYFKQKGETfSDGHGQTLNENRDWENVYRQRWQYDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 96 DRPEYEPRGCPRGAAFSWYTYSPTRVRYPYARGVLVEMYREAKRRLGDPVLAWADVVGDEERRRTYQRARGKGGLIRISW 175
Cdd:TIGR01580 83 DLPNHEPRGCPRGASYSWYIYSANRLKYPMMRKRLMKLWREAKQTHSDPVEAWASIVENADKAKSYKQARGRGGFVRSSW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 176 DEATEITAAAHVHTIKTHGPDRCAGFSPIPAMSMVSHCVGTRFIQLIGGAMTSFYDWYADLPVASPQVFGDQTDVPESGD 255
Cdd:TIGR01580 163 QEVNELIAASNVYTVKNYGPDRVVGFSPIPAMSMVSYASGSRYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPESAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 256 WWDSTYLMMWGSNVPVTRTPDAHWMTEVRYRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRD 335
Cdd:TIGR01580 243 WYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAALALAMGHVILREFHLDNP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 336 VSFFSDYVRTYTDLPFLVRLRERGGDLVPGKFLTGADLG---ASDDEDAWKTVVLDEEtGEPVVPNGSMGFRYaaSGEGR 412
Cdd:TIGR01580 323 SQYFTEYAKRYTDMPMLVMLEERDGYYAAGRFLRAADLVdalGQENNPEWKTVAFDTN-GEMVAPQGSIGFRW--GEKGK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 413 WNLDL------EGVNPSLTLYGGES--AEVLLPSYGGtDGTG--------ETLRRGVPVREV---GGQ--LVTTVYDLML 471
Cdd:TIGR01580 400 WNLEQrdgktgEEIELQLSLLGSQDeiAEVGFPYFGG-DGTEhfnkvegeNVLLRKLPVKRLqlaDGStaLVTTVFDLTL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 472 AQYGVARdGLPGEWPS-GYDDPStPYTPAWQESITSVPAQACIRIAREFAKNAEDSGGRSMIIMGAGICQWFHGDATYRA 550
Cdd:TIGR01580 479 ANYGLER-GLGDVNCAtSYDDVK-AYTPAWQEQITGVSREQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 551 VLTLLLLTGCMGRNGGGWAHYVGQEKCRPITGWISLANALDWSRPPRTVPGTSYWYMHTDQWRTDGYPADALASPLADGH 630
Cdd:TIGR01580 557 LINMLILCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPPRHMNGTSFFYNHSSQWRYETVTAEDLLSPMADKS 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 631 LAGMHTADTIAASARMGWMPFYPQFDRNPLdvADDATAAVDAGDSPDaatYVARQLTDGDLTPAIDDVDAPQNWPRTLVL 710
Cdd:TIGR01580 637 RYTGHLIDYNVRAERMGWLPSAPQLNTNPL--TIAGEAEKAGMNPVD---YVVKSLQEGSLRFAAEQPDNGVNFPRNLFI 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 711 WRSNLMGSSAKGSEYFQRHLLGTHANTTAEPVDE--SSRPRDVRWRDEAPEGKLDLLVSADFRMTSTTLLSDIVFPAATW 788
Cdd:TIGR01580 712 WRSNLLGSSGKGHEYMLKYLLGTENGIMNKDLGQqgGVKPEEVDWQDNGLEGKLDLVVTLDFRMSSTCLYSDIVLPTATW 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 789 YEKHDLSSTDMHPFVHAFSPAIDPPWEAKTDFETFHLIARKLSELAKTHLGVRRDLVSVPMQHDTPGQTAQPGGVaRDWR 868
Cdd:TIGR01580 792 YEKDDMNTSDMHPFIHPLSAAIDPAWESKSDWEIYKAIAKAFSEVCVGHLGKEKDIVTLPLQHDSAAELAQPFGV-KDWK 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 869 DGDADPQPGKTMPNFTVVERDYTAIADKLGAVGPLADELGFTVKNVTYDLEEEVRRLAS-HHGVMSHGAAAGRPALDTDS 947
Cdd:TIGR01580 871 KGECDLIPGKTAPNIQVVERDYPAIYERFTSLGPLMEKIGNGGKGIAWNTQSEMDLLRKlNYTKAEGSPAKGQPMINTAI 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 948 KLADAILAFSGTTNGSLALQGFRTLERRVGKPLADLAEGSEERRITFADTQRGPVPVITSPEWSGSETGGRRYAPFTVNI 1027
Cdd:TIGR01580 951 DAAEMILTLAPETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNV 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1028 ERLKPFHTLTGRMHFYLDHDWMSDLGEQLPTYRPPVDMQRLFGAPPFGPNGGNQVTVRYLTPHSKWSIHSEYQDNLFMLS 1107
Cdd:TIGR01580 1031 HELIPWRTLTGRQQLYQDHQWMRDFGESLLVYRPPIDTRSFKEVIGQKSNGNQEIVLNFLTPHQKWGIHSTYSDNLLMLT 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1108 LSRGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYHAQERTIDVPKSEATGRRGGIHNSVTR 1187
Cdd:TIGR01580 1111 LGRGGPVVWLSEADAKDLGIADNDWIECFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNVPGSEITQQRGGIHNSVTR 1190
|
1210 1220 1230
....*....|....*....|....*....|....*..
gi 2320167329 1188 LLVKPTHLIGAYAQLSYAFNYLGPTGNQRDMVSTVRK 1224
Cdd:TIGR01580 1191 ITPKPTHMIGGYAQLAYGFNYYGTVGSNRDEFVVVRK 1227
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
55-830 |
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: 634.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 55 DKVVRSTHGVNCTGSCSWKVYVKDGIITWESQQTDYPSVGPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPYARGvlvemy 134
Cdd:cd02750 1 DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 135 reakrrlgdpvlawadvvgdeerrrtyqRARGKGGLIRISWDEATEITAAAHVHTIKTHGPDRCAGFSPIPAMSMVSHCV 214
Cdd:cd02750 75 ----------------------------GARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 215 GTRFIQLIGGAMTSFYDWYADLPVASPQVFGDQTDVPESGDWWDSTYLMMWGSNVPVTRTPDAHWMTEVRYRGTKVVSVS 294
Cdd:cd02750 127 GSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 295 PDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRdvsffsDYVRTYTDLPFLVrlrerggdlvpgkfltgadlg 374
Cdd:cd02750 207 PDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDE------DYLKEYTDLPFLV--------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 375 asddedawktvvldeetgepvvpngsmgfryaasgegrwnldlegvnpsltlyggesaevllpsyggtdgtgetlrrgvp 454
Cdd:cd02750 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 455 vrevggqlvttvydlmlaqygvardglpgewpsgyddpstpYTPAWQESITSVPAQACIRIAREFAKNaedsgGRSMIIM 534
Cdd:cd02750 260 -----------------------------------------YTPAWQEAITGVPRETVIRLAREFATN-----GRSMIIV 293
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 535 GAGICQWFHGDATYRAVLTLLLLTGCMGRNGGGWAHYVGqekcrpitgwislanaldwsrpprtvpgtsywymhtdqwrt 614
Cdd:cd02750 294 GAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG----------------------------------------- 332
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 615 dgypadalaspladghlagmhtadtiaasarmgwmpfypqfdrnpldvaddataavdagdspdaatyvarqltdgdltpa 694
Cdd:cd02750 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 695 iddvdapqnWPRTLVLWRSNLMGSSAKGSEYFQRhllgthanttaepvdessrprdvrwrdeAPEGKLDLLVSADFRMTS 774
Cdd:cd02750 333 ---------QPRVLFVWRGNLFGSSGKGHEYFED----------------------------APEGKLDLIVDLDFRMDS 375
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2320167329 775 TTLLSDIVFPAATWYEKHDLSSTDMHPFVHAFSPAIDPPWEAKTDFETFHLIARKL 830
Cdd:cd02750 376 TALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
1083-1223 |
5.20e-72 |
|
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: 236.12 E-value: 5.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1083 TVRYLTPHSKWSIHSEYQDNLFMLSLSRGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYHA 1162
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320167329 1163 QERTIDVPKSEATGRRGGIHNSVTRLLVKPTHLIGAYAQLSYAFNYLGPTGNQRDMVSTVR 1223
Cdd:cd02776 81 QERHVNVPGSKLTGKRGGIHNSVTRVRIKPTHLVGGYGQLSYGFNYYGPTGVNRDTRVVVR 141
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
55-1186 |
5.59e-58 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 213.17 E-value: 5.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 55 DKVVRSTHgVNCTGSCSWKVYVKDGIITweSQQTDypsvgPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPyargvlveMY 134
Cdd:COG0243 21 TKTVKTTC-PGCGVGCGLGVKVEDGRVV--RVRGD-----PDHPVNRGRLCAKGAALDERLYSPDRLTYP--------MK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 135 REAKrrlgdpvlawadvvgdeerrrtyqraRGKGGLIRISWDEATEITAAAHVHTIKTHGPDRCAGFS---PIPAMSMVS 211
Cdd:COG0243 85 RVGP--------------------------RGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTsggSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 212 HCVGTRFIQLIGGAMtsFYDW----YADLPVASPQVFGDQTDVPESGDWWDSTYLMMWGSNVPVTRTPDAHWMTE-VRYR 286
Cdd:COG0243 139 AYLAQRFARALGTNN--LDDNsrlcHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 287 GTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRdvsffsDYVRTYTDlpflvrlrerggdlvpgk 366
Cdd:COG0243 217 GAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYDR------DFLARHTV------------------ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 367 fltgadlgasddedawktvvldeetgepvvpngsmGFryaasgegrwnldlegvnpsltlyggesaevllpsyggtdgtg 446
Cdd:COG0243 273 -----------------------------------GF------------------------------------------- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 447 ETLRRGVpvrevggqlvttvydlmlaqygvardglpgewpsgyddpsTPYTPAWQESITSVPAQACIRIAREFAKNAeds 526
Cdd:COG0243 275 DELAAYV----------------------------------------AAYTPEWAAEITGVPAEDIRELAREFATAK--- 311
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 527 ggRSMIIMGAGICQWFHGDATYRAVLTLLLLTGCMGRNGGGwahyvgqekCRPITGwislanaldwsrpprtvpgtsywy 606
Cdd:COG0243 312 --PAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGG---------PFSLTG------------------------ 356
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 607 mhtdqwrtdgypadalaspladghlagmhtadtiaasarmgwmpfypqfdrnpldvaddataavdagdspdaatyvaRQL 686
Cdd:COG0243 357 -----------------------------------------------------------------------------EAI 359
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 687 TDGDLTPAiddvdapqnwpRTLVLWRSNLMGSsakgseyfqrhllgtHANTTaepvdessrprdvRWRdeapEG--KLDL 764
Cdd:COG0243 360 LDGKPYPI-----------KALWVYGGNPAVS---------------APDTN-------------RVR----EAlrKLDF 396
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 765 LVSADFRMTSTTLLSDIVFPAATWYEKHDLSSTDMHPFVHAFSPAIDPPWEAKTDFETFHLIARKLselakthlgvrrdl 844
Cdd:COG0243 397 VVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRL-------------- 462
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 845 vsvpmqhdtpgqtaqpgGVARDWRDGDAdpqpgktmpnftvvERDYtaiadklgavgpladelgftvknvtydleeevrr 924
Cdd:COG0243 463 -----------------GFEEAFPWGRT--------------EEDY---------------------------------- 477
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 925 lashhgvmshgaaagrpaldtdskladailafsgttngslalqgfrtlerrvgkpLADLAEGSEERRITFAD-TQRGPVP 1003
Cdd:COG0243 478 -------------------------------------------------------LRELLEATRGRGITFEElREKGPVQ 502
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1004 VITSPEwsgsetggrryAPFTVNierlKPFHTLTGRMHFYLDHDWMSDlgeqLPTYRPPVDMQR-LFGAPPFgpnggnqv 1082
Cdd:COG0243 503 LPVPPE-----------PAFRND----GPFPTPSGKAEFYSETLALPP----LPRYAPPYEGAEpLDAEYPL-------- 555
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1083 tvRYLTPHSKWSIHSEYQDNLFMLSLsRGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYHA 1162
Cdd:COG0243 556 --RLITGRSRDQWHSTTYNNPRLREI-GPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHG 632
|
1130 1140
....*....|....*....|....
gi 2320167329 1163 QERtidvpksEATGRRGGIHNSVT 1186
Cdd:COG0243 633 WWY-------EPADDKGGNVNVLT 649
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
59-830 |
3.22e-47 |
|
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: 173.67 E-value: 3.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 59 RSTHgVNCTGSCSWKVYVKDGIITWESQQtdypsvgPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPYARGvlvemyreak 138
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRIEGD-------PNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRV---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 139 rrlgdpvlawadvvgdeerrrtyqraRGKGGLIRISWDEATEITAAAHVHTIKTHGPDRCAGFSPIPAMSMVSHCVGTRF 218
Cdd:cd00368 63 --------------------------GGRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 219 iQLIGGAMTSFYDWYADLP-VASPQVFGDQTDVPESGDWWDSTYLMMWGSNVPVTRTPDAHWMTEVRYRGTKVVSVSPDY 297
Cdd:cd00368 117 -RALGSNNVDSHARLCHASaVAALKAFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 298 ADNTKFADEWLPAQAGTDAALAMAmghvmlreffvdrdvsffsdyvrtytdlpflvrlrerggdlvpgkfltgadlgasd 377
Cdd:cd00368 196 TETAAKADEWLPIRPGTDAALALA-------------------------------------------------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 378 dedawktvvldeetgepvvpngsmgfryaasgegrwnldlegvnpsltlyggesaevllpsyggtdgtgetlrrgvpvre 457
Cdd:cd00368 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 458 vggqlvttvydlmlaqygvardglpgewpsgyddpstpytpAWQESITSVPAQACIRIAREFAKNaedsgGRSMIIMGAG 537
Cdd:cd00368 220 -----------------------------------------EWAAEITGVPAETIRALAREFAAA-----KRAVILWGMG 253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 538 ICQWFHGDATYRAVLTLLLLTGCMGRNGGGWAHyvgqekcrpitgwislanaldwsrpprtvpgtsywymhtdqwrtdgy 617
Cdd:cd00368 254 LTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP----------------------------------------------- 286
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 618 padalaspladghlagmhtadtiaasarmgwmpfypqfdrnpldvaddataavdagdspdaatyvarqltdgdltpaidd 697
Cdd:cd00368 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 698 vdapqnwprtlvlwRSNLMGSSAKGSEYFqrhllgthanttaepvdessrprdvrwrdeAPEGKLDLLVSADFRMTSTTL 777
Cdd:cd00368 287 --------------GGNPLVSAPDANRVR------------------------------AALKKLDFVVVIDIFMTETAA 322
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 2320167329 778 LSDIVFPAATWYEKHDLsSTDMHPFVHAFSPAIDPPWEAKTDFETFHLIARKL 830
Cdd:cd00368 323 YADVVLPAATYLEKEGT-YTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
60-570 |
1.76e-44 |
|
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: 170.74 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 60 STHGVNCTGSCSWKVYVKDGIITWESQQtdypsVGPDrPEYePRGCPRGAAFSWYTYSPTRVRYPYARgvlvemyreakr 139
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPN-----EWPD-KTY-KRGCTRGLSHLQRVYSPDRLKYPMKR------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 140 rlgdpvlawadvVGDeerrrtyqraRGKGGLIRISWDEATEITAAAHVHTIKTHGPdRCAGFSpipAMSMVSHCVGTRFI 219
Cdd:cd02765 63 ------------VGE----------RGEGKFERITWDEALDTIADKLTEAKREYGG-KSILWM---SSSGDGAILSYLRL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 220 QLIGGAMTSFYDWYADLPVASPQ--VFGDQTDVP--ESGDWWDSTYLMMWGSNVPVTRTPDAHWMTEVRYRGTKVVSVSP 295
Cdd:cd02765 117 ALLGGGLQDALTYGIDTGVGQGFnrVTGGGFMPPtnEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 296 DYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDrdvsffSDYVRTYTDLPFLVRLRErggdlvpGKFLTGADLGA 375
Cdd:cd02765 197 VYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYD------EAFLKSNTSAPFLVREDN-------GTLLRQADVTA 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 376 SDDEDAWktVVLDEETGEPVVPNGSmgfryaasgegrwnldleGVNPSLtlyggesaevllpsyggtdgTGETLRRGVPv 455
Cdd:cd02765 264 TPAEDGY--VVWDTNSDSPEPVAAT------------------NINPAL--------------------EGEYTINGVK- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 456 revggqlVTTVYDLMLAQygvardglpgewpsgyddpSTPYTPAWQESITSVPAQACIRIAREFAknaedSGGRSMIIMG 535
Cdd:cd02765 303 -------VHTVLTALREQ-------------------AASYPPKAAAEICGLEEAIIETLAEWYA-----TGKPSGIWGF 351
|
490 500 510
....*....|....*....|....*....|....*
gi 2320167329 536 AGICQWFHGDATYRAVLTLLLLTGCMGRNGGGWAH 570
Cdd:cd02765 352 GGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ 386
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
70-830 |
2.65e-44 |
|
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: 170.87 E-value: 2.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 70 CSWKVYVKDGIITWesqqtdypsVGPDrPEYEPRGCPRGAAFSWYTYSPTRVRYPYARgvlvemyreakrrlgdpvlawa 149
Cdd:cd02751 7 GPFKAHVKDGVIVR---------VEPD-DTDQPRPCPRGRSVRDRVYSPDRIKYPMKR---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 150 dvVGDEERRRTYQRARGKGGLIRISWDEATEITAAAHVHTIKTHGPD---------RCAGFSPiPAMSMVShcvgtRFIQ 220
Cdd:cd02751 55 --VGWLGNGPGSRELRGEGEFVRISWDEALDLVASELKRIREKYGNEaifggsygwASAGRLH-HAQSLLH-----RFLN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 221 LIGGAMTSF--YDWyADLPVASPQVFGDqTDVPESGDWWD-----STYLMMWGSNVPVTR--------TPDAHWMTEVRY 285
Cdd:cd02751 127 LIGGYLGSYgtYST-GAAQVILPHVVGS-DEVYEQGTSWDdiaehSDLVVLFGANPLKTRqgggggpdHGSYYYLKQAKD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 286 RGTKVVSVSPDYADNTK-FADEWLPAQAGTDAALAMAMGHVMLREFFVDRdvsffsDYVRTYTdlpflvrlrerggdlvp 364
Cdd:cd02751 205 AGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITEDLHDQ------AFLARYT----------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 365 gkflTGAdlgasddeDAWKTVVLdeetgepvvpngsmgfryaasgegrwnldlegvnpsltlyggesaevllpsyGGTDG 444
Cdd:cd02751 262 ----VGF--------DEFKDYLL----------------------------------------------------GESDG 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 445 tgetlrrgvpvrevggqlvttvydlmlaqygvardglpgewpsgyddpsTPYTPAWQESITSVPAQACIRIAREFAKNae 524
Cdd:cd02751 278 -------------------------------------------------VPKTPEWAAEITGVPAETIRALAREIASK-- 306
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 525 dsggRSMIIMGAGICQWFHGDATYRAVLTLLLLTGCMGRNGGG---WAHY----VGQEKCRPITGWISLANALDWSRPpr 597
Cdd:cd02751 307 ----RTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGfgfGYGYsnggGPPRGGAGGPGLPQGKNPVKDSIP-- 380
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 598 tvpgTSYWymhtdqwrtdgypADALASPladGHlagmhtadtiaasarmgwmpfypQFDRNpldvaddataavdagdspd 677
Cdd:cd02751 381 ----VARI-------------ADALLNP---GK-----------------------EFTAN------------------- 398
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 678 aatyvarqlTDGDLTPAIDdvdapqnwprtLVLWrsnlmgssaKGSEYFQRHllgthanttaepvdeSSRPRDVR-WRde 756
Cdd:cd02751 399 ---------GKLKTYPDIK-----------MIYW---------AGGNPLHHH---------------QDLNRLIKaLR-- 432
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2320167329 757 apegKLDLLVSADFRMTSTTLLSDIVFPAATWYEKHDL--SSTDMHPFVHAFSPAIDPPWEAKTDFETFHLIARKL 830
Cdd:cd02751 433 ----KDETIVVHDIFWTASARYADIVLPATTSLERNDIglTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRL 504
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
64-830 |
3.22e-39 |
|
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: 155.56 E-value: 3.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 64 VNCTGSCSWKVYVKDGIITWesQQTDypSVGPDRPEY-EPRGCPRGAAFSWYTYSPTRVRYPyargvlveMYREAKrrlg 142
Cdd:cd02770 6 VNCGGRCPLKAHVKDGVITR--IETD--DTGDDDPGFhQIRACLRGRSQRKRVYNPDRLKYP--------MKRVGK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 143 dpvlawadvvgdeerrrtyqraRGKGGLIRISWDEATEITAAAHVHTIKTHGP----------DRCAGFSPIPAMSmvsh 212
Cdd:cd02770 70 ----------------------RGEGKFVRISWDEALDTIASELKRIIEKYGNeaiyvnygtgTYGGVPAGRGAIA---- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 213 cvgtRFIQLIGGAMTSF--YDWyADLPVASPQVFGDQTDVPESGDWWDSTYLMMWGSNVPVTR---TPDAHWMTEVRYRG 287
Cdd:cd02770 124 ----RLLNLTGGYLNYYgtYSW-AQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRmggGGSTYYYLQAKKAG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 288 TKVVSVSPDYADNTK-FADEWLPAQAGTDAALAMAMGHVMLREFFVDRDvsffsdyvrtytdlpFLVRlrerggdlvpgk 366
Cdd:cd02770 199 AKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQA---------------FLDR------------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 367 fltgadlgasddedawKTVVLDEETGEPVVPNGSmgfryaasgegrwnldlegvnpsltlyggesaevllpSYggtdgtg 446
Cdd:cd02770 252 ----------------YCVGFDAEHLPEGAPPNE-------------------------------------SY------- 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 447 etlrrgvpvrevggqlvttvydlmlaqygvaRDGLPGEWPSGyddpsTPYTPAWQESITSVPAQACIRIAREFAknaedS 526
Cdd:cd02770 272 -------------------------------KDYVLGTGYDG-----TPKTPEWASEITGVPAETIRRLAREIA-----T 310
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 527 GGRSMIIMGAGICQWFHGDATYRAVLTLLLLTGCMGRNGGGWAHYVGQeKCRPITGWISLANALDWSRPprtvpgTSYWy 606
Cdd:cd02770 311 TKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGG-SAYNGAGLPAGKNPVKTSIP------CFMW- 382
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 607 mhtdqwrTDGYPADALASPLADGHLagmhTADTIAASARMGWmpfypqfdrnpldvaddataavdagdspdaatyvarql 686
Cdd:cd02770 383 -------TDAIERGEEMTADDGGVK----GADKLKSNIKMIW-------------------------------------- 413
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 687 tdgdltpaiddvdapqnwprtlvlwrsNLMGSSakgseyfqrhLLGTHA---NTTAEPVDESSrprdvrwrdeapegKLD 763
Cdd:cd02770 414 ---------------------------NYAGNT----------LINQHSddnNTTRALLDDES--------------KCE 442
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 764 LLVSADFRMTSTTLLSDIVFPAATWYEKHDL---SSTDMHPFVHAFSPAIDPPWEAKTDFETFHLIARKL 830
Cdd:cd02770 443 FIVVIDNFMTPSARYADILLPDTTELEREDIvltSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRL 512
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
165-832 |
3.08e-34 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 135.61 E-value: 3.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 165 RGKGGLIRISWDEATEITAAAHVHTIKTHGPDRCA-GFSPIPAMSMVSHCVGTRFIQLIGGAMTSFYDWYADLPVASPQV 243
Cdd:pfam00384 9 RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAiNGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNGDLCTAAAAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 244 FG-DQTDVPESG----DWWDSTYLMMWGSNVPVTRTPD-AHWMTEVRYRGTKVVSVSPDYadNTKFADEWLPAQAGTDAA 317
Cdd:pfam00384 89 FGsDLRSNYLFNssiaDIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRL--DLTYADEHLGIKPGTDLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 318 LAMAMGHVMLREFFVDRDvsffsdyvrtytdlpflvrlrerggdlvpgkfltgadlgasddedawktvvldeetgepvvp 397
Cdd:pfam00384 167 LALAGAHVFIKELKKDKD-------------------------------------------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 398 ngsmgfryaasgegrwnldlegvnpsltlyggesaevllpsyggtdgtgetlrrgvpvrevggqlvttvydlmlaqygva 477
Cdd:pfam00384 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 478 rdglpgewpsgyddpstpytpawqesitsvpaqaciriareFAKNAedsggrsMIIMGAGICQWFHGDATYRAVLTLLLL 557
Cdd:pfam00384 185 -----------------------------------------FAPKP-------IIIVGAGVLQRQDGEAIFRAIANLADL 216
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 558 TGCMGRNGGGWAHYVgqekcrpitgwislanaldwsrpprtvpgtsywymhtdqwrtdgypadalaspladgHLAGmhta 637
Cdd:pfam00384 217 TGNIGRPGGGWNGLN---------------------------------------------------------ILQG---- 235
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 638 dtiaasarmgwmpfypqfdrnpldvaddataavdagdspdAATYVARqLTDGdltpaiddvdapqNWPRTLVLWRSNLMG 717
Cdd:pfam00384 236 ----------------------------------------AASPVGA-LDLG-------------LVPGIKSVEMINAIK 261
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 718 SSAKGSEYFQRH-LLGTHANTTaepvdessrprdvrWRDEAPEgKLDLLVSADFRMTSTTLL-SDIVFPAATWYEKHDLS 795
Cdd:pfam00384 262 KGGIKVLYLLGNnPFVTHADEN--------------RVVKALQ-KLDLFVVYDGHHGDKTAKyADVILPAAAYTEKNGTY 326
|
650 660 670
....*....|....*....|....*....|....*..
gi 2320167329 796 STDMHPFVHAFsPAIDPPWEAKTDFEtfhlIARKLSE 832
Cdd:pfam00384 327 VNTEGRVQSTK-QAVPPPGEAREDWK----ILRALSE 358
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
66-358 |
1.07e-26 |
|
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: 115.48 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 66 CTGSCSWKVYVKDGiiTWESQQTDypsvgPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPYargvlvemyreakRRLGDpv 145
Cdd:cd02759 7 CHSGCGVLVYVKDG--KLVKVEGD-----PNHPTNKGRLCMRGLAAPEIVYHPDRLLYPL-------------KRVGE-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 146 lawadvvgdeerrrtyqraRGKGGLIRISWDEATEITAAAHVHTIKTHGPDRCAGFSPIPA-MSMVSHCVGTRFIQLIG- 223
Cdd:cd02759 65 -------------------RGENKWERISWDEALDEIAEKLAEIKAEYGPESIATAVGTGRgTMWQDSLFWIRFVRLFGs 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 224 ----GAMTSFYdWYADLPVASPQVFGDQTDVPesgDWWDSTYLMMWGSNvPVTRTPD--AHWMTEVRYRGTKVVSVSPDY 297
Cdd:cd02759 126 pnlfLSGESCY-WPRDMAHALTTGFGLGYDEP---DWENPECIVLWGKN-PLNSNLDlqGHWLVAAMKRGAKLIVVDPRL 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320167329 298 ADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRdvsffsDYVRTYTDLPFlvRLRER 358
Cdd:cd02759 201 TWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDK------DFVENWCYGFE--ELAER 253
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
66-353 |
1.86e-22 |
|
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: 101.99 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 66 CTGSCSWKVYVKDGIITWESQQtdypsvgPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPYARgvlvemyreakrrlgdpv 145
Cdd:cd02755 8 CSSRCGILARVEDGRVVKIDGN-------PLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIR------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 146 lawadvVGdeerrrtyqrARGKGGLIRISWDEA-TEItaAAHVHTIKT-HGPDRCAGFSPIPAMSMVSHcvgtRFIQLIG 223
Cdd:cd02755 63 ------VG----------ERGEGKFREASWDEAlQYI--ASKLKEIKEqHGPESVLFGGHGGCYSPFFK----HFAAAFG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 224 gamTSFYDWYADLPVASPQVFGDQTDVPESG----DWWDSTYLMMWGSNV-PVTRTPDAHWMTEVRYRGTKVVSVSPDYA 298
Cdd:cd02755 121 ---SPNIFSHESTCLASKNLAWKLVIDSFGGevnpDFENARYIILFGRNLaEAIIVVDARRLMKALENGAKVVVVDPRFS 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2320167329 299 DNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDrdvsffSDYVRTYTDLPFLV 353
Cdd:cd02755 198 ELASKADEWIPIKPGTDLAFVLALIHVLISENLYD------AAFVEKYTNGFELL 246
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
55-830 |
8.67e-20 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 95.34 E-value: 8.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 55 DKVVRST---HGVnctgSCSWKVYVKDGIITWESQQTDYPSvgpdrpeYEPRGCPRGAAFSWYTYSPTRVRYPyargvlv 131
Cdd:COG3383 4 MKKVKTVcpyCGV----GCGIDLEVKDGKIVKVEGDPDHPV-------NRGRLCVKGRFGFEFVNSPDRLTTP------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 132 eMYREakrrlgdpvlawadvvgdeerrrtyqrargKGGLIRISWDEATEITAAAHVHTIKTHGPDRCAGFSpipamsmvs 211
Cdd:COG3383 66 -LIRR------------------------------GGEFREVSWDEALDLVAERLREIQAEHGPDAVAFYG--------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 212 hcvGTR--------FIQLIGGAM-TSFYDWYADLPVAS-----PQVFGdqTDVPeSG---DWWDSTYLMMWGSNV----P 270
Cdd:COG3383 106 ---SGQltneenylLQKLARGVLgTNNIDNNARLCMASavaglKQSFG--SDAP-PNsydDIEEADVILVIGSNPaeahP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 271 VTrtpdAHWMTEVRYRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRDvsffsdYVRTYTDlp 350
Cdd:COG3383 180 VL----ARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDED------FIAERTE-- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 351 flvrlrerggdlvpgkfltgadlgasdDEDAWKTVVLDeetgepvvpngsmgfryaasgegrwnldlegvnpsltlygge 430
Cdd:COG3383 248 ---------------------------GFEELKASVAK------------------------------------------ 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 431 saevllpsyggtdgtgetlrrgvpvrevggqlvttvydlmlaqygvardglpgewpsgyddpstpYTPAWQESITSVPAQ 510
Cdd:COG3383 259 -----------------------------------------------------------------YTPERVAEITGVPAE 273
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 511 ACIRIAREFAKnaedsGGRSMIIMGAGICQWFHGDATYRAVLTLLLLTGCMGRNGGGWAhyvgqekcrPITGwisLAN-- 588
Cdd:COG3383 274 DIREAARLIAE-----AKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPF---------PLTG---QNNvq 336
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 589 -ALDWSRPPRTVPGtsywYMHtdqwrtdgypadaLASPLADGHLAGMHTADTIaasarmgwmpfypqfdrnpldvaddat 667
Cdd:COG3383 337 gGRDMGALPNVLPG----YRD-------------VTDPEHRAKVADAWGVPPL--------------------------- 372
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 668 aavdagdsPDAATYVARQLTDGDLTPAIDdvdapqnwprtlVLWrsnLMGSsakgseyfqrhllgthanttaEPVDESSR 747
Cdd:COG3383 373 --------PDKPGLTAVEMFDAIADGEIK------------ALW---IIGE---------------------NPAVSDPD 408
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 748 PRDVRwrdEAPEgKLDLLVSADFRMTSTTLLSDIVFPAATWYEKhDLSSTDMHPFVHAFSPAIDPPWEAKTDFETFHLIA 827
Cdd:COG3383 409 ANHVR---EALE-KLEFLVVQDIFLTETAEYADVVLPAASWAEK-DGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELA 483
|
...
gi 2320167329 828 RKL 830
Cdd:COG3383 484 RRL 486
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
69-348 |
1.11e-19 |
|
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: 94.64 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 69 SCSWKVY---VKDGIITwesqqtdypSVGPDRPEYEPRgcPRGAAFSWYTYSPTRVRYPYAR-GVLvemyreaKRRLGDP 144
Cdd:cd02769 3 ASHWGAFrarVKDGRIV---------GVRPFEEDPDPS--PLLDGVPDAVYSPTRIKYPMVRrGWL-------EKGPGSD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 145 vlawadvvgdeerrrtyQRARGKGGLIRISWDEATEITAAAHVHTIKTHGPD---------RCAGfspipamsMVSHCVG 215
Cdd:cd02769 65 -----------------RSLRGKEEFVRVSWDEALDLVAAELKRVRKTYGNEaifggsygwSSAG--------RFHHAQS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 216 T--RFIQLIGGAMTSFYDW-YADLPVASPQVFGDQTDVPESGDWWD-----STYLMMWGSNVPVTR------TPDaH--- 278
Cdd:cd02769 120 LlhRFLNLAGGYVGSVGDYsTGAAQVILPHVVGSMEVYTEQQTSWPviaehTELVVAFGADPLKNAqiawggIPD-Hqay 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2320167329 279 -WMTEVRYRGTKVVSVSPDYADNTKFAD-EWLPAQAGTDAALAMAMGHVMLREFFVDRdvsffsDYVRTYTD 348
Cdd:cd02769 199 sYLKALKDRGIRFISISPLRDDTAAELGaEWIAIRPGTDVALMLALAHTLVTEGLHDK------AFLARYTV 264
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
53-348 |
1.98e-18 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 91.24 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 53 SHDKVVRSTHGVNCTGSCSWKVYVKDGIITWesQQTDypSVGPDRPE--YEPRGCPRGAAFSWYTYSPTRVRYPYARgvl 130
Cdd:PRK14990 54 SDEKVIWSACTVNCGSRCPLRMHVVDGEIKY--VETD--NTGDDNYDglHQVRACLRGRSMRRRVYNPDRLKYPMKR--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 131 vemyreakrrlgdpvlawadvVGdeerrrtyqrARGKGGLIRISWDEATEITAAAHVHTIKTHGPDR------------C 198
Cdd:PRK14990 127 ---------------------VG----------ARGEGKFERISWEEAYDIIATNMQRLIKEYGNESiylnygtgtlggT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 199 AGFSPIPAMSMVShcvgtRFIQLIGGAMTSFYDWY-ADLPVASPQVFGDQTDVPESGDWWDSTYLMMWGSNVPVTRTPDA 277
Cdd:PRK14990 176 MTRSWPPGNTLVA-----RLMNCCGGYLNHYGDYSsAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGG 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2320167329 278 ---HWMTEVRYRGT-KVVSVSPDYADN-TKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRdvSFFSDYVRTYTD 348
Cdd:PRK14990 251 gvtYYLEQARQKSNaRMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQ--PFLDKYCVGYDE 324
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
65-335 |
3.71e-18 |
|
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: 89.23 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 65 NCTGSCSWKVYVKDGIITwesqqtdypSVGPDRPEYEPRG--CPRGAAFSWYTYSPTRVRYPYARGVlvemyreakrrlg 142
Cdd:cd02766 7 DCPDTCSLLVTVEDGRIV---------RVEGDPAHPYTRGfiCAKGARYVERVYSPDRLLTPLKRVG------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 143 dpvlawadvvgdeerrrtyqraRGKGGLIRISWDEATEITAAAHVHTIKTHG-----PDRCAGFspipaMSMVSHCVGTR 217
Cdd:cd02766 65 ----------------------RKGGQWERISWDEALDTIAAKLKEIKAEYGpesilPYSYAGT-----MGLLQRAARGR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 218 FIQLiGGAMTSFYD--WYADLPvASPQVFGDQTDV-PEsgDWWDSTYLMMWGSNVPVTRTPDAHWMTEVRYRGTKVVSVS 294
Cdd:cd02766 118 FFHA-LGASELRGTicSGAGIE-AQKYDFGASLGNdPE--DMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVID 193
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2320167329 295 PDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRD 335
Cdd:cd02766 194 PYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRD 234
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
1085-1199 |
1.99e-17 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 79.24 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1085 RYLTPHSKWSIHSEYQdNLFMLSLSRGGP-TVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYHAQ 1163
Cdd:pfam01568 2 YLITGRVLGQYHSQTR-TRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 2320167329 1164 ERTidvpkseatgRRGGIHNSVTRLLVKPTHLIGAY 1199
Cdd:pfam01568 81 WYE----------PRGGNANALTDDATDPLSGGPEF 106
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
61-852 |
9.73e-17 |
|
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: 85.79 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 61 THGVNCTGSCSW-KVYVKDGIITWESQQTDYPSVGPDRPeyepRGCPRGAAFSWYTYSPTRVRYPYARGvlvemyREAKR 139
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVATEIEPNFAAEDIHPARG----RVCVKAYGLVQKTYNPNRVLQPMKRT------NPKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 140 RLGDPvlawadvvgdeerrrtyqrargkgGLIRISWDEATEITAAaHVHTIKTHG-------PDRCAGFSP--IPAMSMV 210
Cdd:cd02760 72 RNEDP------------------------GFVPISWDEALDLVAA-KLRRVREKGlldekglPRLAATFGHggTPAMYMG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 211 SHCVgtrFIQLIGGAMTSFYDWYADLPVASPQVFGD--QTDVPESGDWWDSTYLMMWGSNVPVTRTPDA-HWMTEVRYRG 287
Cdd:cd02760 127 TFPA---FLAAWGPIDFSFGSGQGVKCVHSEHLYGEfwHRAFTVAADTPLANYVISFGSNVEASGGPCAvTRHADARVRG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 288 TKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDR-DVSFfsdyVRTYTDLPFLVrlrerGGDlvpGK 366
Cdd:cd02760 204 YKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMFAMIHVMVHEQGLGKlDVPF----LRDRTSSPYLV-----GPD---GL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 367 FLTgadlgasdDEDAWKTVVLDEETGEPVvpngsmgfryaasgegrwNLDLEGVNPSltlyggESAEVLLPSYGGTDGTG 446
Cdd:cd02760 272 YLR--------DAATGKPLVWDERSGRAV------------------PFDTRGAVPA------VAGDFAVDGAVSVDADD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 447 ETlrrgvpvREVGGQLVTTVYDLMlaqygvaRDGLpgewpsgyddpsTPYTPAWQESITSVPAQACIRIAREFAKNAedS 526
Cdd:cd02760 320 ET-------AIHQGVEGTTAFTML-------VEHM------------RKYTPEWAESICDVPAATIRRIAREFLENA--S 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 527 GGRSMIIMGAGIcqwfhgdaTYRAVLTLLlltgcmGRN-GGGWAHYvgqEKCRPITGWISLANALDwsrpprtVPGTSYW 605
Cdd:cd02760 372 IGSTIEVDGVTL--------PYRPVAVTL------GKSvNNGWGAF---ECCWARTLLATLVGALE-------VPGGTLG 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 606 YmhtdQWRTDGYPADALAS--PLADGHLA-GMHTADtiaasaRMGWmpfypqfdrnPLDVADDATAAVDAGDSPDAATYV 682
Cdd:cd02760 428 T----TVRLNRPHDDRLASvkPGEDGFMAqGFNPTD------KEHW----------VVKPTGRNAHRTLVPIVGNSAWSQ 487
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 683 ARQLTDGDL----TPAIDDVDAPQNWPRTLVLWRSNLMGSSAKgseyfqrhllgthantTAEPVDESSrprdvrwrdeap 758
Cdd:cd02760 488 ALGPTQLAWmflrEVPLDWKFELPTLPDVWFNYRTNPAISFWD----------------TATLVDNIA------------ 539
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 759 egKLDLLVSADFRMTSTTLLSDIVFPAATWYEKHDLSSTDMHPFVHAF---------SPAIDPPWEAKtDFETFHL-IAR 828
Cdd:cd02760 540 --KFPFTVSFAYTEDETNWMADVLLPEATDLESLQMIKVGGTKFVEQFwehrgvvlrQPAVEPQGEAR-DFTWISTeLAK 616
|
810 820
....*....|....*....|....
gi 2320167329 829 KLSELAKTHLGVRRDLVSVPMQHD 852
Cdd:cd02760 617 RTGLLADYNAALNRGAGGAPLKGE 640
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
1091-1199 |
3.13e-16 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 75.43 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1091 SKWSIHSEYQDNLFMLSLSRGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYHAQERTIDvp 1170
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGG-- 78
|
90 100
....*....|....*....|....*....
gi 2320167329 1171 kseatgrRGGIHNSVTRLLVKPTHLIGAY 1199
Cdd:cd02775 79 -------RGGNANVLTPDALDPPSGGPAY 100
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
150-830 |
2.18e-13 |
|
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: 74.17 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 150 DVVGDEERRrTYQRARGKGGLIRISWDEATEITAAAHVHTIKTHGPDRCAGFSP-----------------IPAMSMVSH 212
Cdd:cd02753 47 DFVNSKDRL-TKPLIRKNGKFVEASWDEALSLVASRLKEIKDKYGPDAIAFFGSakctneenylfqklaraVGGTNNVDH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 213 CvgTRF---------IQLIG-GAMTSFYDwyaDLpvaspqvfgDQTDVpesgdwwdstyLMMWGSNvpvtrTPDAH---- 278
Cdd:cd02753 126 C--ARLchsptvaglAETLGsGAMTNSIA---DI---------EEADV-----------ILVIGSN-----TTEAHpvia 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 279 -WMTEVRYRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDrdvsffSDYVRTYTDlpflvrlre 357
Cdd:cd02753 176 rRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYD------EEFIEERTE--------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 358 rggdlvpgkfltgadlgasddedawktvvldeetgepvvpngsmGFryaasgegrwnldlegvnpsltlyggesaevllp 437
Cdd:cd02753 241 --------------------------------------------GF---------------------------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 438 syggtdgtgETLRRGVPvrevggqlvttvydlmlaqygvardglpgewpsgyddpstPYTPAWQESITSVPAQACIRIAR 517
Cdd:cd02753 243 ---------EELKEIVE----------------------------------------KYTPEYAERITGVPAEDIREAAR 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 518 EFAknaedSGGRSMIIMGAGICQWFHGDATYRAVLTLLLLTGCMGRNGGGWAHYVGQEkcrpitgwislanaldwsrppr 597
Cdd:cd02753 274 MYA-----TAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQN---------------------- 326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 598 TVPGTSYwymhtdqwrtdgypadalaspladghlagmhtadtiaasarMGWMP-FYPQFDRnpldvaddataavdagdsp 676
Cdd:cd02753 327 NVQGACD-----------------------------------------MGALPnVLPGYVK------------------- 346
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 677 daATYVarqltdgdltpaiddvdapqnwprtlvlwrsnlMGSSakgseyfqrhLLGTHANTtaepvdessrpRDVRwrdE 756
Cdd:cd02753 347 --ALYI---------------------------------MGEN----------PALSDPNT-----------NHVR---K 367
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2320167329 757 APEgKLDLLVSADFRMTSTTLLSDIVFPAATWYEKH-DLSSTDMHpfVHAFSPAIDPPWEAKTDFETFHLIARKL 830
Cdd:cd02753 368 ALE-SLEFLVVQDIFLTETAELADVVLPAASFAEKDgTFTNTERR--VQRVRKAVEPPGEARPDWEIIQELANRL 439
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
65-343 |
2.20e-13 |
|
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: 74.40 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 65 NCTGSCSWKVYVKDGIIT-WESQqtdypsvgPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPyargvlveMYREAKRRLGD 143
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVTkVEGN--------PLHPGSRGRLCAKGHLGLQQVYDPDRILYP--------MKRTNPRKGRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 144 PVLAWadvvgdeerrrtyqrargkgglIRISWDEATEITAAAHVHTIKTHGPdrcagfspipamsmvshcvgTRFIQLIG 223
Cdd:cd02757 72 VDPKF----------------------VPISWDEALDTIADKIRALRKENEP--------------------HKIMLHRG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 224 GAMTSFYDWYADLP--VASPQVFGdQTDVPESG-----------------DWWDSTYLMMWGSNVPVT--RTPDAHWMTE 282
Cdd:cd02757 110 RYGHNNSILYGRFTkmIGSPNNIS-HSSVCAESekfgryyteggwdynsyDYANAKYILFFGADPLESnrQNPHAQRIWG 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320167329 283 VRYRGTKVVSVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRDvsFFSDYV 343
Cdd:cd02757 189 GKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKD--FVGDFV 247
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
66-353 |
3.38e-13 |
|
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: 74.10 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 66 CTGSCSWKVYVKDGIITwesqqtdYPSVGPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPYARgvlvemyreakrrlgdpv 145
Cdd:cd02763 7 CACRCGIRVHLRDGKVR-------YIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLR------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 146 lawadvvgdeerrrtyQRARGKGGLIRISWDEATEItAAAHVHTIKTHGPDRCAGFSPIPAMSMVSHCVGTRFIQLIGGA 225
Cdd:cd02763 62 ----------------KGPRGSGQFEEIEWEEAFSI-ATKRLKAARATDPKKFAFFTGRDQMQALTGWFAGQFGTPNYAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 226 MTSFydwyADLPVASPQVFGDQTDVPESG--DWWDSTYLMMWGSNVPVTRTPDAHWMTEVRYRGTKVVSVSPDYADNTKF 303
Cdd:cd02763 125 HGGF----CSVNMAAGGLYSIGGSFWEFGgpDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAI 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2320167329 304 ADEWLPAQAGTDAALAMAMGHVMLREFFVDRdvsffsDYVRTYTDLPFLV 353
Cdd:cd02763 201 ADEWVPIKPGTDGAFILALAHELLKAGLIDW------EFLKRYTNAAELV 244
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
146-336 |
4.04e-13 |
|
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: 73.59 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 146 LAWADVVGDEERRRTYQRARGkGGLIRISWDEATEITAAAHVHTIKTHGPDRCAGFSPIPAMSmvSHCVGTRFIQLIGGA 225
Cdd:cd02762 43 AALGDYQNDPDRLRTPMRRRG-GSFEEIDWDEAFDEIAERLRAIRARHGGDAVGVYGGNPQAH--THAGGAYSPALLKAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 226 MTS--FYDWYAD-LP--VASPQVFGDQTDVPeSGDWWDSTYLMM-----WGSNVPVTRTPDA-HWMTEVRYRGTKVVSVS 294
Cdd:cd02762 120 GTSnyFSAATADqKPghFWSGLMFGHPGLHP-VPDIDRTDYLLIlganpLQSNGSLRTAPDRvLRLKAAKDRGGSLVVID 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2320167329 295 PDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRDV 336
Cdd:cd02762 199 PRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAEGLTDRRF 240
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
1086-1194 |
2.81e-11 |
|
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: 62.00 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 1086 YLTPHSKWSIHSEYQDNLFMLSLSrGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVfvyhaqer 1165
Cdd:cd02785 6 CIQRHSRFRVHSQFSNVPWLLELQ-PEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVV-------- 76
|
90 100 110
....*....|....*....|....*....|
gi 2320167329 1166 tiDVPKS-EATGRRGGIHNSVTRLLVKPTH 1194
Cdd:cd02785 77 --TAEQGwWSRYFQEGSLQDLTSPFVNPVH 104
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
158-348 |
5.45e-10 |
|
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: 63.40 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 158 RRTYQRARGKGG-LIRISWDEATEITAAAHVHTIKTHGPDRCAGFS----PIPAMSMVSH----CVGTRFIQ-------- 220
Cdd:cd02754 54 RLTRPLLRRNGGeLVPVSWDEALDLIAERFKAIQAEYGPDSVAFYGsgqlLTEEYYAANKlakgGLGTNNIDtnsrlcma 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 221 -LIGGAMTSFYdwyADLPVASPQVFgDQTDVpesgdwwdstyLMMWGSNvpvtrTPDAH-----WMTEVR--YRGTKVVS 292
Cdd:cd02754 134 sAVAGYKRSFG---ADGPPGSYDDI-EHADC-----------FFLIGSN-----MAECHpilfrRLLDRKkaNPGAKIIV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2320167329 293 VSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLREFFVDRdvsffsDYVRTYTD 348
Cdd:cd02754 194 VDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDR------DFIDAHTE 243
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
66-345 |
4.61e-09 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 60.84 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 66 CTGSCSWKVYVKDGiitwesqQTDYPSVGPDRPEYEPRGCPRGAAFSWYTYSPTRVRYPYARgvlvemyreakrrlgdpv 145
Cdd:PRK15488 51 CSTRCPIEARVVNG-------KNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKR------------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 146 lawadvVGDeerrrtyqraRGKGGLIRISWDEA-TEItaAAHVHTIKT-HGPDRCAgFSPiPAMSMVSHCVgtRFIQLIG 223
Cdd:PRK15488 106 ------VGE----------RGEGKWQEISWDEAyQEI--AAKLNAIKQqHGPESVA-FSS-KSGSLSSHLF--HLATAFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 224 GAMTsFYDW------YAdlpVASPQVFGdqTDVPEsgDWWDSTYLMMWGSN------VPVTRTpdahWMTEVRYRGTKVV 291
Cdd:PRK15488 164 SPNT-FTHAstcpagYA---IAAKVMFG--GKLKR--DLANSKYIINFGHNlyeginMSDTRG----LMTAQMEKGAKLV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2320167329 292 SVSPDYADNTKFADEWLPAQAGTDAALAMAMGHVMLRE-----FFVDRDVSFFSDYVRT 345
Cdd:PRK15488 232 VFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEEnlydkAFVERYTSGFEELAAS 290
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1087-1161 |
2.34e-07 |
|
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: 50.66 E-value: 2.34e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2320167329 1087 LTPHSKWSIHSEYqDNLFMLSLS---RGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYH 1161
Cdd:cd02777 6 ISPHPKRRLHSQL-DNVPWLREAykvKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALPE 82
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
55-117 |
2.85e-07 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 48.40 E-value: 2.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2320167329 55 DKVVRSTHGVnCTGSCSWKVYVKDGIITWESQQTDYPSvgpdrpeYEPRGCPRGAAFSWYTYS 117
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVRGDPDHPV-------NRGRLCPKGRAGLEQVYS 55
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
761-830 |
2.08e-06 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 52.37 E-value: 2.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2320167329 761 KLDLLVSADFRMTSTTLLSDIVFPAATWYEKHDLSSTDMHPF--VHAFSPAIDPPWEAKTDFETFHLIARKL 830
Cdd:PRK15102 494 KLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNrgIIAMKKVVEPLFESRSDFDIFRELCRRF 565
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
1111-1159 |
3.23e-06 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 47.28 E-value: 3.23e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2320167329 1111 GGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFV 1159
Cdd:cd02786 29 GEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVA 77
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| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
1113-1159 |
5.32e-06 |
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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: 46.80 E-value: 5.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2320167329 1113 PTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFV 1159
Cdd:cd02791 35 PYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFV 81
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| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
495-523 |
5.63e-06 |
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thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 50.82 E-value: 5.63e-06
10 20
....*....|....*....|....*....
gi 2320167329 495 PYTPAWQESITSVPAQACIRIAREFAKNA 523
Cdd:PRK15488 293 EYTPEWAEAISDVPADDIRRIARELAAAA 321
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| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
1105-1161 |
7.77e-06 |
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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: 46.35 E-value: 7.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2320167329 1105 MLSLSRGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFV-YH 1161
Cdd:cd00508 27 RLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMpFH 84
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| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
1085-1161 |
2.37e-04 |
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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: 42.26 E-value: 2.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2320167329 1085 RYLTPHSKWSIHSEYQDNLFMLSLsRGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYH 1161
Cdd:cd02778 3 RLIYGKSPVHTHGHTANNPLLHEL-TPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH 78
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| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
494-573 |
9.58e-04 |
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trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 43.51 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 494 TPYTPAWQESITSVPAQacirIAREFAKNAedSGGRSMIIMGAGICQWFHGDATYRAVLTLLLLTGCMGRNGGGWA---H 570
Cdd:PRK15102 326 VPKTPEWAEKICGIDAE----TIRELARQM--AKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISyghH 399
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...
gi 2320167329 571 YVG 573
Cdd:PRK15102 400 YSG 402
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| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
85-322 |
2.30e-03 |
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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: 42.33 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 85 SQQTDYPSVGPDRPEYEPRG----------CPRGAAFSWYTYSPTRVRYPYARgvlvemyreakrrlgdpvlawadvVGd 154
Cdd:cd02758 38 APSLPYNTPLKESLYLSLVGenglkarataCARGNAGLQYLYDPYRVLQPLKR------------------------VG- 92
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 155 eerrrtyqrARGKGGLIRISWDEA-TEITAAAHVHT----------------IKTHGPDrcagFSPIPAMSMVSHCVG-- 215
Cdd:cd02758 93 ---------PRGSGKWKPISWEQLiEEVVEGGDLFGeghveglkairdldtpIDPDHPD----LGPKANQLLYTFGRDeg 159
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320167329 216 -----TRFI-QLIGGAMTSFYDWYADLP--VASPQVFGDQTDVPE-SGDWWDSTYLMMWG-----SNVPVTRTpdAHWMT 281
Cdd:cd02758 160 rtpfiKRFAnQAFGTVNFGGHGSYCGLSyrAGNGALMNDLDGYPHvKPDFDNAEFALFIGtspaqAGNPFKRQ--ARRLA 237
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250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2320167329 282 EVRYRGT-KVVSVSPDYADNTKFADE---WLPAQAGTDAALAMAM 322
Cdd:cd02758 238 EARTEGNfKYVVVDPVLPNTTSAAGEnirWVPIKPGGDGALAMAM 282
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| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
1115-1183 |
3.34e-03 |
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This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 39.20 E-value: 3.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2320167329 1115 VWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYHAQERT---------IDVPKSEATGRRGGIHN 1183
Cdd:cd02780 32 VWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEHGYGHWaygavastiDGKDLPGDAWRGAGVNI 109
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1087-1157 |
4.41e-03 |
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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: 38.77 E-value: 4.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2320167329 1087 LTPHSKWSIHSEYqDN--LFMLSLSRGGPTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVV 1157
Cdd:cd02793 6 LSNQPATRLHSQL-DHgsLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVV 77
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| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
1088-1157 |
4.93e-03 |
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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: 38.43 E-value: 4.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320167329 1088 TPHSKWSIHSEYqDNLFMLSlsRGGP-TVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVV 1157
Cdd:cd02794 7 GWHYKRRTHSTF-DNVPWLR--EAFPqEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVV 74
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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 ... |
756-830 |
5.36e-03 |
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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: 5.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2320167329 756 EAPEGKLDLLVSADFRMTSTTLLSDIVFPAATWYEKhDLSSTDMHPFVHAFSPAID-PPWEAKTDFETFHLIARKL 830
Cdd:cd02771 359 EAALDAAEFVVVLDHFLTETAERADVVLPAASFAEK-SGTFVNYEGRAQRFFKAYDdPAGDARSDWRWLHALAAKL 433
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| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
1113-1161 |
6.83e-03 |
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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: 38.06 E-value: 6.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2320167329 1113 PTVWMSPADADAIEVADNDWVECVNPNGVLVGRAIVSHRMPTGVVFVYH 1161
Cdd:cd02781 33 PVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEH 81
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