|
Name |
Accession |
Description |
Interval |
E-value |
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
2-1235 |
0e+00 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 2556.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 2 SKLLDRFRYFKqKGDTFADGHGQVMHSNRDWEDSYRQRWQFDKIVRSTHGVNCTGSCSWKIYVKNGLVTWEIQQTDYPRT 81
Cdd:COG5013 6 SHLLDRLRFFR-RGEVFSDGHGVTTEGGREWEDFYRDRWQHDKVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTDYPRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 82 RPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRKRLIELWREALKQHSDPVLAWASIMNDPQKSLSYKQVRGRGGFIRS 161
Cdd:COG5013 85 GPDLPNYEPRGCPRGASFSWYTYSPTRVKYPYVRGVLLELWREARARHGDPVEAWASIVEDPEKRRRYKSARGKGGFVRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 162 NWPELNQLIAAANVWTIKTYGPDRVAGFSPIPAMSMVSYAAGTRYLSLLGGTCLSFYDWYCDLPPASPMTWGEQTDVPES 241
Cdd:COG5013 165 TWDEANEIIAAANVYTIKKYGPDRVAGFSPIPAMSMVSYAAGARFLSLIGGVMLSFYDWYADLPPASPQVWGEQTDVPES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 242 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLD 321
Cdd:COG5013 245 ADWYNSGYLIMWGSNVPQTRTPDAHFMTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEFHVD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 322 NPSDYFINYCRRYSDMPMLVMLEPRdDGSYVPGRMIRASDLVDGLGESNNPQWKTVAVNTA-GELVVPNGSIGFRWGE-K 399
Cdd:COG5013 325 RQVPYFTDYARRYTDLPFLVTLEER-DGGYVPGRFLRASDLGGALGESNNPEWKTVVLDEAtGEPVVPNGSIGFRWGEsE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 400 GKWNLESI-AAGKETELSLTLLGQHDAVAGVAFPYFGGIenphfrsVKHNPVLVRQLPVKNLTLAGGsTCPVVSVYDLVL 478
Cdd:COG5013 404 GKWNLELKdATGADVDPALSLLDDHDEVVEVAFPYFGGE-------TGGGGVLRRGVPVRRVTLADG-EVLVTTVFDLML 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 479 ANYGLDRGLEDeNSAKDYAEIKPYTPAWGEQITGVPRQYIETIAREFADTAHKTHGRSMIILGAGVNHWYHMDMNYRGMI 558
Cdd:COG5013 476 ANYGVDRGLPG-NWPTGYDDDVPYTPAWQEKITGVPREQVIRVAREFAQNAEKTRGRSMIIMGAGTNHWYHSDMIYRAIL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 559 NMLIFCGCVGQSGGGWAHYVGQEKLRPQTGWLPLAFALDWNRPPRQMNSTSFFYNHSSQWRYEKVSAQELLSPLADASKY 638
Cdd:COG5013 555 NLLMLCGCQGVNGGGWAHYVGQEKLRPQTGWQPLAFALDWSRPPRQMNGTSFFYAHTDQWRYETLSADELLSPLADGKFW 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 639 SGHLIDFNVRAERMGWLPSAPQLGRNPLGIKAEADKAGLSPTEFTAQALKSGDLRMACEQPDSGSNHPRNLFVWRSNLLG 718
Cdd:COG5013 635 GGHLADYNVRAARLGWLPSYPQFNRNPLDLADEAEAAGMEPADYVVDQLKSGELKFACEDPDNPENFPRNLFVWRSNLLG 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 719 SSGKGHEYMQKYLLGTESGIQGEELGasDGIKPEEVEWQTAAIEGKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMN 798
Cdd:COG5013 715 SSGKGHEYFLKHLLGTDNGVQGEELG--PGLRPREVVWRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKHDLS 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 799 TSDMHPFIHPLSAAVDPAWESRSDWEIYKGIAKAFSQVCVGHLGKETDVVLQPLLHDSPAELSQPC-EVLDWRKGECDLS 877
Cdd:COG5013 793 TTDMHPFIHPFSPAVDPPWEARSDWDIFKGIAKKFSELAAGHLGVRKDVVATPLQHDTPGELAQPFgDVKDWKKGECEPI 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 878 PGKTAPNIVAVERDYPATYERFTSLGPLMDKLGNGGKGISWNTQDEIDFLGKLNYT-KRDGPAQGRPLIDTAIDASEVIL 956
Cdd:COG5013 873 PGKTMPKLVVVERDYPAIYEKFTSLGPLLEKLGNGGKGITWDTEEEVEELGKLNGVvREEGVAKGRPRLDTDIDAAEAIL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 957 ALAPETNGHVAVKAWQALGEITGREHTHLALHKEDEKIRFRDIQAQPRKIISSPTWSGLESDHVSYNAGYTNVHELIPWR 1036
Cdd:COG5013 953 ALSPETNGHVAVKAWKALEKRTGRDLAHLAAGREEEKIRFRDIQAQPRKVITSPTWSGSESGGRRYSAFTTNVEELIPWR 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1037 TLSGRQQLYQDHPWMRAFGESLVAYRPPIDTRSVSEMRQIPPNGFPEKALNFLTPHQKWGIHSTYSENLLMLTLSRGGPI 1116
Cdd:COG5013 1033 TLTGRQHFYLDHDWMREFGEGLPVYRPPLDMKTLFGEPGIGPNGNPEIVLRYLTPHQKWGIHSTYQDNLLMLTLSRGGPT 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1117 VWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYHAQERIMNIPGSEVTGMRGGIHNSVTRICPKPTH 1196
Cdd:COG5013 1113 VWMSEEDAAKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHAQERIVNVPGSEITGKRGGIHNSVTRIVLKPTH 1192
|
1210 1220 1230
....*....|....*....|....*....|....*....
gi 15831325 1197 MIGGYAQLAWGFNYYGTVGSNRDEFIMIRKMKNVNWLDD 1235
Cdd:COG5013 1193 MIGGYAQLSYGFNYYGPTGNQRDEVVVVRKRSQVDWLED 1231
|
|
| narG |
TIGR01580 |
respiratory nitrate reductase, alpha subunit; The Nitrate reductase enzyme complex allows ... |
2-1234 |
0e+00 |
|
respiratory nitrate reductase, alpha subunit; The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the alpha subunit for nitrate reductase I (narG) and nitrate reductase II (narZ) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model The seed members used to make the model include Nitrate reductases from Pseudomonas fluorescens (GP:11344601), E.coli (SP:P09152) and B.subtilis (SP:P42175). All seed members are experimentally characterized. Some unpublished nitrate reductases, that are shorter sequences, and probably fragments fall in between the noise and trusted cutoffs. Pfam models pfam00384 (Molybdopterin oxidoreductase) and pfam01568(Molydopterin dinucleotide binding domain) will also match the nitrate reductase, alpha subunit. [Energy metabolism, Anaerobic]
Pssm-ID: 162434 [Multi-domain] Cd Length: 1235 Bit Score: 2269.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 2 SKLLDRFRYFKQKGDTFADGHGQVMHSNRDWEDSYRQRWQFDKIVRSTHGVNCTGSCSWKIYVKNGLVTWEIQQTDYPRT 81
Cdd:TIGR01580 1 SKLLDRLRYFKQKGETFSDGHGQTLNENRDWENVYRQRWQYDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 82 RPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRKRLIELWREALKQHSDPVLAWASIMNDPQKSLSYKQVRGRGGFIRS 161
Cdd:TIGR01580 81 RPDLPNHEPRGCPRGASYSWYIYSANRLKYPMMRKRLMKLWREAKQTHSDPVEAWASIVENADKAKSYKQARGRGGFVRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 162 NWPELNQLIAAANVWTIKTYGPDRVAGFSPIPAMSMVSYAAGTRYLSLLGGTCLSFYDWYCDLPPASPMTWGEQTDVPES 241
Cdd:TIGR01580 161 SWQEVNELIAASNVYTVKNYGPDRVVGFSPIPAMSMVSYASGSRYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 242 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLD 321
Cdd:TIGR01580 241 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAALALAMGHVILREFHLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 322 NPSDYFINYCRRYSDMPMLVMLEPRDdGSYVPGRMIRASDLVDGLGESNNPQWKTVAVNTAGELVVPNGSIGFRWGEKGK 401
Cdd:TIGR01580 321 NPSQYFTEYAKRYTDMPMLVMLEERD-GYYAAGRFLRAADLVDALGQENNPEWKTVAFDTNGEMVAPQGSIGFRWGEKGK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 402 WNLESI--AAGKETELSLTLLGQHDAVAGVAFPYFGGIENPHFRSVKHNPVLVRQLPVKNLTLAGGSTCPVVSVYDLVLA 479
Cdd:TIGR01580 400 WNLEQRdgKTGEEIELQLSLLGSQDEIAEVGFPYFGGDGTEHFNKVEGENVLLRKLPVKRLQLADGSTALVTTVFDLTLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 480 NYGLDRGLEDENSAKDYAEIKPYTPAWGEQITGVPRQYIETIAREFADTAHKTHGRSMIILGAGVNHWYHMDMNYRGMIN 559
Cdd:TIGR01580 480 NYGLERGLGDVNCATSYDDVKAYTPAWQEQITGVSREQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLIN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 560 MLIFCGCVGQSGGGWAHYVGQEKLRPQTGWLPLAFALDWNRPPRQMNSTSFFYNHSSQWRYEKVSAQELLSPLADASKYS 639
Cdd:TIGR01580 560 MLILCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPPRHMNGTSFFYNHSSQWRYETVTAEDLLSPMADKSRYT 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 640 GHLIDFNVRAERMGWLPSAPQLGRNPLGIKAEADKAGLSPTEFTAQALKSGDLRMACEQPDSGSNHPRNLFVWRSNLLGS 719
Cdd:TIGR01580 640 GHLIDYNVRAERMGWLPSAPQLNTNPLTIAGEAEKAGMNPVDYVVKSLQEGSLRFAAEQPDNGVNFPRNLFIWRSNLLGS 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 720 SGKGHEYMQKYLLGTESGIQGEELGASDGIKPEEVEWQTAAIEGKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNT 799
Cdd:TIGR01580 720 SGKGHEYMLKYLLGTENGIMNKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRMSSTCLYSDIVLPTATWYEKDDMNT 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 800 SDMHPFIHPLSAAVDPAWESRSDWEIYKGIAKAFSQVCVGHLGKETDVVLQPLLHDSPAELSQPCEVLDWRKGECDLSPG 879
Cdd:TIGR01580 800 SDMHPFIHPLSAAIDPAWESKSDWEIYKAIAKAFSEVCVGHLGKEKDIVTLPLQHDSAAELAQPFGVKDWKKGECDLIPG 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 880 KTAPNIVAVERDYPATYERFTSLGPLMDKLGNGGKGISWNTQDEIDFLGKLNYTK-RDGPAQGRPLIDTAIDASEVILAL 958
Cdd:TIGR01580 880 KTAPNIQVVERDYPAIYERFTSLGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKaEGSPAKGQPMINTAIDAAEMILTL 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 959 APETNGHVAVKAWQALGEITGREHTHLALHKEDEKIRFRDIQAQPRKIISSPTWSGLESDHVSYNAGYTNVHELIPWRTL 1038
Cdd:TIGR01580 960 APETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTL 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1039 SGRQQLYQDHPWMRAFGESLVAYRPPIDTRSVSEMRQIPPNGFPEKALNFLTPHQKWGIHSTYSENLLMLTLSRGGPIVW 1118
Cdd:TIGR01580 1040 TGRQQLYQDHQWMRDFGESLLVYRPPIDTRSFKEVIGQKSNGNQEIVLNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVW 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1119 ISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYHAQERIMNIPGSEVTGMRGGIHNSVTRICPKPTHMI 1198
Cdd:TIGR01580 1120 LSEADAKDLGIADNDWIECFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNVPGSEITQQRGGIHNSVTRITPKPTHMI 1199
|
1210 1220 1230
....*....|....*....|....*....|....*.
gi 15831325 1199 GGYAQLAWGFNYYGTVGSNRDEFIMIRKMKNVNWLD 1234
Cdd:TIGR01580 1200 GGYAQLAYGFNYYGTVGSNRDEFVVVRKMKNVDWLD 1235
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
43-833 |
0e+00 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 659.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 43 DKIVRSTHGVNCTGSCSWKIYVKNGLVTWEIQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRKRlielw 122
Cdd:cd02750 1 DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 123 realkqhsdpvlawasimndpqkslsykqVRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVAGFSPIPAMSMVSYAA 202
Cdd:cd02750 76 -----------------------------ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 203 GTRYLSLLGGTCLSFYDWYCDLPPASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTIAIT 282
Cdd:cd02750 127 GSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 283 PDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLDNpsdyfiNYCRRYSDMPMLVmleprddgsyvpgrmirasdl 362
Cdd:cd02750 207 PDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDE------DYLKEYTDLPFLV--------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 363 vdglgesnnpqwktvavntagelvvpngsigfrwgekgkwnlesiaagketelsltllgqhdavagvafpyfggienphf 442
Cdd:cd02750 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 443 rsvkhnpvlvrqlpvknltlaggstcpvvsvydlvlanygldrgledensakdyaeikpYTPAWGEQITGVPRQYIETIA 522
Cdd:cd02750 260 -----------------------------------------------------------YTPAWQEAITGVPRETVIRLA 280
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 523 REFADTahkthGRSMIILGAGVNHWYHMDMNYRGMINMLIFCGCVGQSGGGWAHYVGQeklrpqtgwlplafaldwnrpp 602
Cdd:cd02750 281 REFATN-----GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQ---------------------- 333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 603 rqmnstsffynhssqwryekvsaqellspladaskysghlidfnvraermgwlpsapqlgrnplgikaeadkaglsptef 682
Cdd:cd02750 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 683 taqalksgdlrmaceqpdsgsnhPRNLFVWRSNLLGSSGKGHEYMQkyllgtesgiqgeelgasdgikpeevewqtAAIE 762
Cdd:cd02750 334 -----------------------PRVLFVWRGNLFGSSGKGHEYFE------------------------------DAPE 360
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831325 763 GKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESRSDWEIYKGIAKAF 833
Cdd:cd02750 361 GKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
1086-1225 |
8.37e-78 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 252.30 E-value: 8.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1086 LNFLTPHQKWGIHSTYSENLLMLTLSRGGPIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYHAQ 1165
Cdd:cd02776 2 LNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1166 ERIMNIPGSEVTGMRGGIHNSVTRICPKPTHMIGGYAQLAWGFNYYGTVGSNRDEFIMIR 1225
Cdd:cd02776 82 ERHVNVPGSKLTGKRGGIHNSVTRVRIKPTHLVGGYGQLSYGFNYYGPTGVNRDTRVVVR 141
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-1188 |
2.62e-54 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 202.38 E-value: 2.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 43 DKIVRSTHgVNCTGSCSWKIYVKNGLVTWeIqqtdypRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRKRLielw 122
Cdd:COG0243 21 TKTVKTTC-PGCGVGCGLGVKVEDGRVVR-V------RGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 123 realkqhsdpvlawasimndpqkslsykqvRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVAGFS---PIPAMSMVS 199
Cdd:COG0243 89 ------------------------------RGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTsggSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 200 YAAGTRYLSLLGgtCLSFYDW--YCDLP--PASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTE-VRYK 274
Cdd:COG0243 139 AYLAQRFARALG--TNNLDDNsrLCHESavAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 275 GTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEfhldnpsdyfinycrrysdmpmlvmleprddgsyvpg 354
Cdd:COG0243 217 GAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEE------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 355 rmirasDLVDglgesnnpqwktvavntagelvvpngsigfrwgekgkwnlesiaagketelsltllgqhdavagVAFpyf 434
Cdd:COG0243 260 ------GLYD----------------------------------------------------------------RDF--- 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 435 ggienphfrsvkhnpvlvrqlpvknltlaggstcpvvsvydlvLANY--GLDRgledensAKDYaeIKPYTPAWGEQITG 512
Cdd:COG0243 267 -------------------------------------------LARHtvGFDE-------LAAY--VAAYTPEWAAEITG 294
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 513 VPRQYIETIAREFAdtahkTHGRSMIILGAGVNHWYHMDMNYRGMINMLIFCGCVGQSGGGWahyvgqeklrpqtgwlpl 592
Cdd:COG0243 295 VPAEDIRELAREFA-----TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGP------------------ 351
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 593 afaldwnrpprqmnstsffynhssqwryekvsaqellspladaskysghlidFNVRAERMgwlpsapqLGRNPLGIKAea 672
Cdd:COG0243 352 ----------------------------------------------------FSLTGEAI--------LDGKPYPIKA-- 369
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 673 dkaglspteftaqalksgdlrmaceqpdsgsnhprnLFVWRSNLLGSSgkgheymqkyllgtesgiqgeelgasdgikPE 752
Cdd:COG0243 370 ------------------------------------LWVYGGNPAVSA------------------------------PD 383
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 753 evewQTAAIEG--KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESRSDWEIYKGIA 830
Cdd:COG0243 384 ----TNRVREAlrKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELA 459
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 831 KAfsqvcvghLGKETDVVLQpllhDSPAELsqpcevldWRKgecdlspgktapnIVAVERDYPATYERFTSLGPlmdklg 910
Cdd:COG0243 460 KR--------LGFEEAFPWG----RTEEDY--------LRE-------------LLEATRGRGITFEELREKGP------ 500
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 911 nggkgISWNTQDEIDFlgklnytKRDGpaqgrplidtaidasevilalapetnghvavkawqalgeitgrehthlalhke 990
Cdd:COG0243 501 -----VQLPVPPEPAF-------RNDG----------------------------------------------------- 515
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 991 dekirfrdiqaqprkiissptwsglesdhvsynagytnvheliPWRTLSGRQQLYQDHPWMRAfgesLVAYRPPIdtrsv 1070
Cdd:COG0243 516 -------------------------------------------PFPTPSGKAEFYSETLALPP----LPRYAPPY----- 543
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1071 sEMRQIPPNGFPekaLNFLTPHQKWGIHSTYSeNLLMLTLSRGGPIVWISETDARELTIVDNDWVEVFNANGALTARAVV 1150
Cdd:COG0243 544 -EGAEPLDAEYP---LRLITGRSRDQWHSTTY-NNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKV 618
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 15831325 1151 SQRVPPGMTMMYHAQerimnipGSEVTGMRGGIHNSVT 1188
Cdd:COG0243 619 TEGIRPGVVFAPHGW-------WYEPADDKGGNVNVLT 649
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-309 |
6.33e-49 |
|
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: 178.68 E-value: 6.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 47 RSTHgVNCTGSCSWKIYVKNGLVTWEiqqtdypRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRkrlielwreal 126
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRI-------EGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIR----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 127 kqhsdpvlawasimndpqkslsykqVRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVAGFSPIPAMSMVSYAAGTRy 206
Cdd:cd00368 62 -------------------------VGGRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKL- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 207 LSLLGGTCLSFYDWYCDLPPASPMTW-GEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTIAITPDY 285
Cdd:cd00368 116 LRALGSNNVDSHARLCHASAVAALKAfGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRR 195
|
250 260
....*....|....*....|....
gi 15831325 286 SEVAKLCDQWLAPKQGTDSALAMA 309
Cdd:cd00368 196 TETAAKADEWLPIRPGTDAALALA 219
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
48-833 |
8.24e-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: 168.81 E-value: 8.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 48 STHGVNCTGSCSWKIYVKNGLVTweiqqtdypRTRP-DLPNHE-PRGCPRGASYSWYLYSANRLKYPLirKRLIElwrea 125
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIV---------KVEPnEWPDKTyKRGCTRGLSHLQRVYSPDRLKYPM--KRVGE----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 126 lkqhsdpvlawasimndpqkslsykqvRGRGGFIRSNWPELNQLIAAANVWTIKTYGPdRVAGFSpipAMSMVSYAAGTR 205
Cdd:cd02765 66 ---------------------------RGEGKFERITWDEALDTIADKLTEAKREYGG-KSILWM---SSSGDGAILSYL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 206 YLSLLGGTCLSFYDWYCDLPPASPMT----WGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTIAI 281
Cdd:cd02765 115 RLALLGGGLQDALTYGIDTGVGQGFNrvtgGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 282 TPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLDNPsdyfinYCRRYSDMPMLVmlepRDDGsyvpGRMIRASD 361
Cdd:cd02765 195 DPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEA------FLKSNTSAPFLV----REDN----GTLLRQAD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 362 LVDGLGESNnpqwktvavntageLVVpngsigfrwgekgkWNLESIAAGKETElsltllgqhdavagvafpyfggienph 441
Cdd:cd02765 261 VTATPAEDG--------------YVV--------------WDTNSDSPEPVAA--------------------------- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 442 frsvkhnpvlvrqlPVKNLTLAGGSTCPVVSVYDlvlanyGLDRGLEdensakdyaEIKPYTPAWGEQITGVPRQYIETI 521
Cdd:cd02765 286 --------------TNINPALEGEYTINGVKVHT------VLTALRE---------QAASYPPKAAAEICGLEEAIIETL 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 522 AREFAdtahkTHGRSMIILGAGVNHWYHMDMNYRGMINMLIFCGCVGQSGGGwahyVGQEKlrpqtgwlplafaldwnrp 601
Cdd:cd02765 337 AEWYA-----TGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG----VGQIK------------------- 388
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 602 prqmnstsFFYN-HSSQwryekvsaqellspladaskySGHLIDFNVRAErmgWLPsapqlgrnplgikaeadkaglspt 680
Cdd:cd02765 389 --------FMYFmGSNF---------------------LGNQPDRDRWLK---VMK------------------------ 412
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 681 eftaqalksgdlrmaceqpdsgsnhprnlfvwrsnllgssgkgheymqkyllgtesgiqgeelgasdgikpeevewqtaa 760
Cdd:cd02765 --------------------------------------------------------------------------------
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831325 761 iegKLDLLVTLDFRMSSTCLFSDIVLPTATWYE-KDDMNTSDMHPFIHPLSAAVDPAWESRSDWEIYKGIAKAF 833
Cdd:cd02765 413 ---NLDFIVVVDIFHTPTVRYADIVLPAAHWFEvEDLLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERL 483
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
153-325 |
2.37e-37 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 144.47 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 153 RGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVA-GFSPIPAMSMVSYAAGTRYLSLLGGTCLSFYDWYCDLPPASPMT 231
Cdd:pfam00384 9 RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAiNGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNGDLCTAAAAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 232 WG-----EQTDVPESADWYNSSYIIAWGSNVPQTRTPD-AHFFTEVRYKGTKTIAITPDYSevAKLCDQWLAPKQGTDSA 305
Cdd:pfam00384 89 FGsdlrsNYLFNSSIADIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRLD--LTYADEHLGIKPGTDLA 166
|
170 180
....*....|....*....|
gi 15831325 306 LAMAMGHVILKEFHLDNPSD 325
Cdd:pfam00384 167 LALAGAHVFIKELKKDKDFA 186
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
57-833 |
6.90e-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: 136.20 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 57 SCSW---KIYVKNGLVTweiqqtdypRTRPDlPNHEPRGCPRGASYSWYLYSANRLKYPLIRKRlielWREALKQHSDpv 133
Cdd:cd02751 3 ACHWgpfKAHVKDGVIV---------RVEPD-DTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVG----WLGNGPGSRE-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 134 lawasimndpqkslsykqVRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRV-----AGFSP---IPAMSMVSyaagtR 205
Cdd:cd02751 67 ------------------LRGEGEFVRISWDEALDLVASELKRIREKYGNEAIfggsyGWASAgrlHHAQSLLH-----R 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 206 YLSLLGGTCLSF--YDWYCdLPPASPMTWG------EQTDVPESADwyNSSYIIAWGSNVPQTR--------TPDAHFFT 269
Cdd:cd02751 124 FLNLIGGYLGSYgtYSTGA-AQVILPHVVGsdevyeQGTSWDDIAE--HSDLVVLFGANPLKTRqgggggpdHGSYYYLK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 270 EVRYKGTKTIAITPDYSEVAK-LCDQWLAPKQGTDSALAMAMGHVILKEfhldNPSDY-FIN-YCrrysdmpmlvmlepr 346
Cdd:cd02751 201 QAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITE----DLHDQaFLArYT--------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 347 ddgsyvpgrmirasdlvdglgesnnpqwktvavntagelvvpngsIGFrwgekgkwnlesiaagkETELSLtLLGQHDAV 426
Cdd:cd02751 262 ---------------------------------------------VGF-----------------DEFKDY-LLGESDGV 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 427 agvafpyfggienphfrsvkhnpvlvrqlpvknltlaggstcpvvsvydlvlanygldrgledensakdyaeikPYTPAW 506
Cdd:cd02751 279 --------------------------------------------------------------------------PKTPEW 284
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 507 GEQITGVPRQYIETIAREFADTahkthgRSMIILGAGVNHWYHMDMNYRGMINMLIFCGCVGQSGGGWAHYVGQeklrpQ 586
Cdd:cd02751 285 AAEITGVPAETIRALAREIASK------RTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGY-----S 353
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 587 TGWLPLAFALDWNRPPRQMNSTSFFYNhSSQWryekvsAQELLSPladaskysGHLIDFNvraermgwlpsapqlGRNPL 666
Cdd:cd02751 354 NGGGPPRGGAGGPGLPQGKNPVKDSIP-VARI------ADALLNP--------GKEFTAN---------------GKLKT 403
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 667 GIkaeadkaglspteftaqalksgDLRMaceqpdsgsnhprnLFVWRSNLLGSSGKGHEYMQKYLlgtesgiqgeelgas 746
Cdd:cd02751 404 YP----------------------DIKM--------------IYWAGGNPLHHHQDLNRLIKALR--------------- 432
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 747 dgikpeevewqtaaiegKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTS--DMHPFIHPLSAAVDPAWESRSDWE 824
Cdd:cd02751 433 -----------------KDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTgnYSNRYLIAMKQAVEPLGEARSDYE 495
|
....*....
gi 15831325 825 IYKGIAKAF 833
Cdd:cd02751 496 IFAELAKRL 504
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
52-844 |
1.17e-31 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 132.45 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 52 VNCTGSCSWKIYVKNGLVTWeiQQTDypRTRPDLP-NHEPRGCPRGASYSWYLYSANRLKYPLIRKrlielwrealkqhs 130
Cdd:cd02770 6 VNCGGRCPLKAHVKDGVITR--IETD--DTGDDDPgFHQIRACLRGRSQRKRVYNPDRLKYPMKRV-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 131 dpvlAWasimndpqkslsykqvRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVagfspipamsMVSYAAGT------ 204
Cdd:cd02770 68 ----GK----------------RGEGKFVRISWDEALDTIASELKRIIEKYGNEAI----------YVNYGTGTyggvpa 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 205 ------RYLSLLGGTcLSFYDWYC--DLPPASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTR---TPDAHFFTEVRY 273
Cdd:cd02770 118 grgaiaRLLNLTGGY-LNYYGTYSwaQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRmggGGSTYYYLQAKK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 274 KGTKTIAITPDYSEVAK-LCDQWLAPKQGTDSALAMAMGHVILKEfhldNPSDY-FIN-YCrrysdmpmlvmleprddgs 350
Cdd:cd02770 197 AGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITE----NLHDQaFLDrYC------------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 351 yvpgrmirasdlvdglgesnnpqwktvavntagelvvpngsIGFrwgekgkwnlesiaagketelsltllgqhDAvagva 430
Cdd:cd02770 254 -----------------------------------------VGF-----------------------------DA----- 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 431 fpyfggienphfrsvKHNPVLVrqlPVKNltlaggstcpvvSVYDLVLanygldrGLEDENSAKdyaeikpyTPAWGEQI 510
Cdd:cd02770 259 ---------------EHLPEGA---PPNE------------SYKDYVL-------GTGYDGTPK--------TPEWASEI 293
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 511 TGVPRQYIETIAREFADTAhkthgRSMIILGAGVNHWYHMDMNYRGMINMLIFCGCVGQSGGGwahyvgqeklrpqTGWL 590
Cdd:cd02770 294 TGVPAETIRRLAREIATTK-----PAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-------------TGAR 355
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 591 PLAFALDWNRPPRQMNSTSFFYNHSSQWryekvsaqellsplaDAskysghlIDfnvRAERMgwlpsapqlgrnplgika 670
Cdd:cd02770 356 PGGSAYNGAGLPAGKNPVKTSIPCFMWT---------------DA-------IE---RGEEM------------------ 392
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 671 EADKAGLSptefTAQALKSgDLRMaceqpdsgsnhprnLFVWRSNllgssgkgheymqkYLLGTESGIQGeelgasdgik 750
Cdd:cd02770 393 TADDGGVK----GADKLKS-NIKM--------------IWNYAGN--------------TLINQHSDDNN---------- 429
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 751 peevewQTAAI---EGKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDM----NTSDMHPFIHpLSAAVDPAWESRSDW 823
Cdd:cd02770 430 ------TTRALlddESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIvltsNAGMMEYLIY-SQKAIEPLYECKSDY 502
|
810 820
....*....|....*....|.
gi 15831325 824 EIYKGIAKafsqvcvgHLGKE 844
Cdd:cd02770 503 EICAELAK--------RLGVE 515
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
54-341 |
4.69e-23 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 103.92 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 54 CTGSCSWKIYVKNGLVtWEIQQTdyprtrPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRKrlielwrealkqhsdpv 133
Cdd:cd02755 8 CSSRCGILARVEDGRV-VKIDGN------PLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 134 lawasimndpqkslsykQVRGRGGFIRSNWPELNQLIAAaNVWTIKT-YGPDRVAGFSPIPAMS---------MVSYAAG 203
Cdd:cd02755 64 -----------------GERGEGKFREASWDEALQYIAS-KLKEIKEqHGPESVLFGGHGGCYSpffkhfaaaFGSPNIF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 204 TRYlsllgGTCLSFYDWYCDLppaspMTWGEQTDVPesADWYNSSYIIAWGSNV-PQTRTPDAHFFTEVRYKGTKTIAIT 282
Cdd:cd02755 126 SHE-----STCLASKNLAWKL-----VIDSFGGEVN--PDFENARYIILFGRNLaEAIIVVDARRLMKALENGAKVVVVD 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831325 283 PDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLDnpsDYFInycRRYSDMPMLV 341
Cdd:cd02755 194 PRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYD---AAFV---EKYTNGFELL 246
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
54-331 |
1.90e-22 |
|
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: 102.38 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 54 CTGSCSWKIYVKNGLVTWEIQQTDYPRTRPdlpnhepRGCPRGASYSWYLYSANRLKYPLirKRLIElwrealkqhsdpv 133
Cdd:cd02759 7 CHSGCGVLVYVKDGKLVKVEGDPNHPTNKG-------RLCMRGLAAPEIVYHPDRLLYPL--KRVGE------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 134 lawasimndpqkslsykqvRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVAGFSPIPAMSMVSYAAGT-RYLSLLGG 212
Cdd:cd02759 65 -------------------RGENKWERISWDEALDEIAEKLAEIKAEYGPESIATAVGTGRGTMWQDSLFWiRFVRLFGS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 213 TCLSFYDWYCDLPPASPMTWGEQT-DVPESADWYNSSYIIAWGSNvPQTRTPD--AHFFTEVRYKGTKTIAITPDYSEVA 289
Cdd:cd02759 126 PNLFLSGESCYWPRDMAHALTTGFgLGYDEPDWENPECIVLWGKN-PLNSNLDlqGHWLVAAMKRGAKLIVVDPRLTWLA 204
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15831325 290 KLCDQWLAPKQGTDSALAMAMGHVILKEFHLDNpsDYFINYC 331
Cdd:cd02759 205 ARADLWLPIRPGTDAALALGMLNVIINEGLYDK--DFVENWC 244
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
53-317 |
1.45e-20 |
|
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: 96.93 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 53 NCTGSCSWKIYVKNGLVTweiqqtdypRTRPDlPNHEP-RG--CPRGASYSWYLYSANRLKYPLIRkrlielwrealkqh 129
Cdd:cd02766 7 DCPDTCSLLVTVEDGRIV---------RVEGD-PAHPYtRGfiCAKGARYVERVYSPDRLLTPLKR-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 130 sdpvlawasimndpqkslsykQVRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVAGFSPIPAMSMVSYAAGTRYLSL 209
Cdd:cd02766 63 ---------------------VGRKGGQWERISWDEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 210 LGGTclSFYDWYCDLP--PASPMTWGEQTDV-PEsaDWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTIAITPDYS 286
Cdd:cd02766 122 LGAS--ELRGTICSGAgiEAQKYDFGASLGNdPE--DMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRT 197
|
250 260 270
....*....|....*....|....*....|.
gi 15831325 287 EVAKLCDQWLAPKQGTDSALAMAMGHVILKE 317
Cdd:cd02766 198 ATAARADLHIQIRPGTDGALALGVAKVLFRE 228
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-1163 |
4.02e-19 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 93.41 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 43 DKIVRST---HGVnctgSCSWKIYVKNGLVTweiqqtdypRTRPDlPNHEP-RG--CPRGASYSWYLYSANRLKYPLIRK 116
Cdd:COG3383 4 MKKVKTVcpyCGV----GCGIDLEVKDGKIV---------KVEGD-PDHPVnRGrlCVKGRFGFEFVNSPDRLTTPLIRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 117 RlielwrealkqhsdpvlawasimndpqkslsykqvrgrGGFIRSNWPELNQLIAAANVWTIKTYGPDRVAGFSpipams 196
Cdd:COG3383 70 G--------------------------------------GEFREVSWDEALDLVAERLREIQAEHGPDAVAFYG------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 197 mvS--------YAA--------GTRYLSLLGGTCLSfydwycdlppasPMTWGEQTDVPESA------DWYNSSYIIAWG 254
Cdd:COG3383 106 --SgqltneenYLLqklargvlGTNNIDNNARLCMA------------SAVAGLKQSFGSDAppnsydDIEEADVILVIG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 255 SNVPQTRTPDAHFFTEVRYKGTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEfhldnpsdyfinycrry 334
Cdd:COG3383 172 SNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEE----------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 335 sdmpmlvmleprddgsyvpgrmirasDLVDglgesnnpqWKTVAVNTAGelvvpngsigfrwgekgkwnlesiaagkete 414
Cdd:COG3383 235 --------------------------GLVD---------EDFIAERTEG------------------------------- 248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 415 lsltllgqhdavagvafpyfggienphFRSVKhnpvlvrqlpvknltlaggstcpvvsvydlvlanygldrgledensak 494
Cdd:COG3383 249 ---------------------------FEELK------------------------------------------------ 253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 495 dyAEIKPYTPAWGEQITGVPRQYIETIAREFAdtahkTHGRSMIILGAGVNHWYHMDMNYRGMINMLIFCGCVGQSGGGw 574
Cdd:COG3383 254 --ASVAKYTPERVAEITGVPAEDIREAARLIA-----EAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTG- 325
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 575 ahyVGQekLRPQ--------TGWLPLAFAldwnrpprqmnstsffynhssqwRYEKVSAQELLSPLADAskysghlidfn 646
Cdd:COG3383 326 ---PFP--LTGQnnvqggrdMGALPNVLP-----------------------GYRDVTDPEHRAKVADA----------- 366
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 647 vraermgWlpsapqlgrnplGIKAEADKAGLSPTEfTAQALKSGDLRmaceqpdsgsnhprnlFVWrsnllgssgkghey 726
Cdd:COG3383 367 -------W------------GVPPLPDKPGLTAVE-MFDAIADGEIK----------------ALW-------------- 396
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 727 mqkyllgtesgIQGEELGASDGiKPEEVEwqtAAIEgKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDD-MNTSDMHpf 805
Cdd:COG3383 397 -----------IIGENPAVSDP-DANHVR---EALE-KLEFLVVQDIFLTETAEYADVVLPAASWAEKDGtFTNTERR-- 458
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 806 IHPLSAAVDPAWESRSDWEIYKGIAKAfsqvcvghLGketdvvlQPLLHDSPAelsqpcEVLDwrkgecdlspgktapNI 885
Cdd:COG3383 459 VQRVRKAVEPPGEARPDWEIIAELARR--------LG-------YGFDYDSPE------EVFD---------------EI 502
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 886 VAVERDY-PATYERftslgplMDKLGnggkGISWNTQDEIDFLGKLNYTKR----DGPAQGRPLidtaidasevilalap 960
Cdd:COG3383 503 ARLTPDYsGISYER-------LEALG----GVQWPCPSEDHPGTPRLFTGRfptpDGKARFVPV---------------- 555
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 961 etnghvavkAWQALGEITGREHthlalhkedekirfrdiqaqprkiissptwsglesdhvsynagytnvheliPWRTLSG 1040
Cdd:COG3383 556 ---------EYRPPAELPDEEY---------------------------------------------------PLVLTTG 575
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1041 RqQLYQDHpwmrafgeslvayrppidTRSVSemRQIPpngfpekALNFLTPHqkwgihstysenllmltlsrggPIVWIS 1120
Cdd:COG3383 576 R-LLDQWH------------------TGTRT--RRSP-------RLNKHAPE----------------------PFVEIH 605
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....
gi 15831325 1121 ETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMM-YH 1163
Cdd:COG3383 606 PEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMpFH 649
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
1086-1201 |
4.34e-19 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 83.86 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1086 LNFLTPHQKWGIHSTYsENLLMLTLSRGGP-IVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYHA 1164
Cdd:pfam01568 1 LYLITGRVLGQYHSQT-RTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 15831325 1165 QERimnipgsevtGMRGGIHNSVTRICPKPTHMIGGY 1201
Cdd:pfam01568 80 WWY----------EPRGGNANALTDDATDPLSGGPEF 106
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
43-387 |
2.39e-18 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 91.24 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 43 DKIVRSTHGVNCTGSCSWKIYVKNGlvtwEIQQTDYPRTRPDLPN--HEPRGCPRGASYSWYLYSANRLKYPLirKRLIE 120
Cdd:PRK14990 56 EKVIWSACTVNCGSRCPLRMHVVDG----EIKYVETDNTGDDNYDglHQVRACLRGRSMRRRVYNPDRLKYPM--KRVGA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 121 lwrealkqhsdpvlawasimndpqkslsykqvRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVA---GFSPIPAMSM 197
Cdd:PRK14990 130 --------------------------------RGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnyGTGTLGGTMT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 198 VSYAAGTRYLSLLGGTCLSFYDWYCDLPPAS-----PMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDA---HFFT 269
Cdd:PRK14990 178 RSWPPGNTLVARLMNCCGGYLNHYGDYSSAQiaeglNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGgvtYYLE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 270 EVRYKGT-KTIAITPDYSEV-AKLCDQWLAPKQGTDSALAMAMGHVILKEFHLDNPsdYFINYCRRYsDMPMLVMLEPRd 347
Cdd:PRK14990 258 QARQKSNaRMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQP--FLDKYCVGY-DEKTLPASAPK- 333
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15831325 348 DGSYVPGRMIRASDlvdglGESNNPQWKTVAVNTAGELVV 387
Cdd:PRK14990 334 NGHYKAYILGEGPD-----GVAKTPEWASQITGVPADKII 368
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
53-317 |
2.53e-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: 90.19 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 53 NCTGSCSWKIYVKNGLVTweiqqtdYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRK-----RLIE------L 121
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVT-------KVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgRDVDpkfvpiS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 122 WREALKQHSDPVLAwaSIMNDPQKSLSYKqvRGRGGFIRSNWPElnqliaaanvWTIKTYGPDRVAGFSPIPAMS--MVS 199
Cdd:cd02757 81 WDEALDTIADKIRA--LRKENEPHKIMLH--RGRYGHNNSILYG----------RFTKMIGSPNNISHSSVCAESekFGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 200 YAAGtrylsllggtclSFYDWycdlppaspmtwgeqtdvpESADWYNSSYIIAWGSNVPQTRTPDAHF--FTEVRYKGTK 277
Cdd:cd02757 147 YYTE------------GGWDY-------------------NSYDYANAKYILFFGADPLESNRQNPHAqrIWGGKMDQAK 195
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15831325 278 TIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKE 317
Cdd:cd02757 196 VVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTE 235
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
1094-1201 |
1.68e-17 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 78.90 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1094 KWGIHSTYSENLLMLTLSRGGPIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYHAQERimnipg 1173
Cdd:cd02775 2 RDHFHSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGH------ 75
|
90 100
....*....|....*....|....*...
gi 15831325 1174 sevTGMRGGIHNSVTRICPKPTHMIGGY 1201
Cdd:cd02775 76 ---RGGRGGNANVLTPDALDPPSGGPAY 100
|
|
| Nitr_red_alph_N |
pfam14710 |
Respiratory nitrate reductase alpha N-terminal; This is the N-terminal tail of the respiratory ... |
4-40 |
9.47e-17 |
|
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: 74.57 E-value: 9.47e-17
10 20 30
....*....|....*....|....*....|....*..
gi 15831325 4 LLDRFRYFKQKGDTFADGHGQVMHSNRDWEDSYRQRW 40
Cdd:pfam14710 1 FLDRLRFFKRKRETFADGHGETTNEDRDWEDAYRQRW 37
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
54-832 |
1.02e-15 |
|
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: 81.88 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 54 CTGSCSWKIYVKNGLVTweiqqtdYPRTRPDLPNHEPRGCPRGAsYSW-YLYSANRLKYPLIRKRLIelWREAlkqhsdp 132
Cdd:cd02753 7 CGVGCGLELWVKDNKIV-------GVEPVKGHPVNRGKLCVKGR-FGFdFVNSKDRLTKPLIRKNGK--FVEA------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 133 vlAWasimndpQKSLSYkqvrgrggfirsnwpelnqliAAANVWTIK-TYGPDRVAGFSPipamsmvsyAAGTR---YL- 207
Cdd:cd02753 70 --SW-------DEALSL---------------------VASRLKEIKdKYGPDAIAFFGS---------AKCTNeenYLf 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 208 ----SLLGGT-----CLSfydwYCDlppaSPMTWGEQTDVPESADW------YNSSYIIAWGSNvpqtrTPDAH--FFTE 270
Cdd:cd02753 111 qklaRAVGGTnnvdhCAR----LCH----SPTVAGLAETLGSGAMTnsiadiEEADVILVIGSN-----TTEAHpvIARR 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 271 VR---YKGTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEfhldnpsdyfinycrrysdmpmlvmleprd 347
Cdd:cd02753 178 IKrakRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEE------------------------------ 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 348 dgsyvpgrmirasDLVDGlgesnnpqwktvavntagelvvpngsigfrwgekgkwnlesiaagketelsltllgqhdava 427
Cdd:cd02753 228 -------------GLYDE-------------------------------------------------------------- 232
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 428 gvAFpyfggienphfrsvkhnpvlvrqlpVKNLTlaggstcpvvsvydlvlanygldrgledENSAKDYAEIKPYTPAWG 507
Cdd:cd02753 233 --EF-------------------------IEERT----------------------------EGFEELKEIVEKYTPEYA 257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 508 EQITGVPRQYIETIAREFAdtahkTHGRSMIILGAGVNHWYHMDMNYRGMINMLIFCGCVGqsgggwahyvgqeklRPQT 587
Cdd:cd02753 258 ERITGVPAEDIREAARMYA-----TAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIG---------------RPGT 317
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 588 GWLPLafaldwnrppRQMNstsffynhssqwryekvsaqellspladaskysghlidfNVR-AERMGWLPSapQLgrnPL 666
Cdd:cd02753 318 GVNPL----------RGQN---------------------------------------NVQgACDMGALPN--VL---PG 343
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 667 GIKAeadkaglspteftaqalksgdlrmaceqpdsgsnhprnLFvwrsnllgssgkgheymqkyllgtesgIQGEELGAS 746
Cdd:cd02753 344 YVKA--------------------------------------LY---------------------------IMGENPALS 358
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 747 DgikPEevewQTAAIEG--KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPfIHPLSAAVDPAWESRSDWE 824
Cdd:cd02753 359 D---PN----TNHVRKAleSLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERR-VQRVRKAVEPPGEARPDWE 430
|
....*...
gi 15831325 825 IYKGIAKA 832
Cdd:cd02753 431 IIQELANR 438
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
1086-1206 |
2.70e-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: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1086 LNFLTPHQKWGIHSTYSENLLMLTLSrGGPIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYHaq 1165
Cdd:cd02785 4 LACIQRHSRFRVHSQFSNVPWLLELQ-PEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQ-- 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15831325 1166 erimnipGSEVTGMRGGIHNSVTRICPKPTHMIGGYAQLAW 1206
Cdd:cd02785 81 -------GWWSRYFQEGSLQDLTSPFVNPVHEYIYGPNSAF 114
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1086-1163 |
3.10e-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: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1086 LNFLTPHQKWGIHSTYSENLlmlTLSRGGPI-----VWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTM 1160
Cdd:cd02777 3 LQLISPHPKRRLHSQLDNVP---WLREAYKVkgrepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVA 79
|
...
gi 15831325 1161 MYH 1163
Cdd:cd02777 80 LPE 82
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
1086-1159 |
2.04e-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: 59.22 E-value: 2.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831325 1086 LNFLTPHQKWGIHSTYSeNLLMLTLSRGGPIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMT 1159
Cdd:cd02786 3 LRLITPPAHNFLNSTFA-NLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV 75
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
54-345 |
4.24e-10 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 64.08 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 54 CTGSCSWKIYVKNGLVTweiqqtdYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRK--------RLIElWREA 125
Cdd:cd02763 7 CACRCGIRVHLRDGKVR-------YIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKgprgsgqfEEIE-WEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 126 LKQHSDPVLAWASimNDPQKSLSYKqvrGRggfirsnwpelNQLIAAANVWTIKTYGPDRVA--GFSPipamsmVSYAAG 203
Cdd:cd02763 79 FSIATKRLKAARA--TDPKKFAFFT---GR-----------DQMQALTGWFAGQFGTPNYAAhgGFCS------VNMAAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 204 TRYLslLGGtclSFYDWycdlppaspmtwGEqtdvpesADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTIAITP 283
Cdd:cd02763 137 GLYS--IGG---SFWEF------------GG-------PDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNP 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831325 284 DYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLDnpsdyfINYCRRYSDMPMLVMLEP 345
Cdd:cd02763 193 VRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLID------WEFLKRYTNAAELVDYTP 248
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
764-833 |
1.24e-09 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 62.77 E-value: 1.24e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831325 764 KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPF--IHPLSAAVDPAWESRSDWEIYKGIAKAF 833
Cdd:PRK15102 494 KLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNrgIIAMKKVVEPLFESRSDFDIFRELCRRF 565
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
764-833 |
2.11e-09 |
|
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: 61.90 E-value: 2.11e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 764 KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESRSDWEIYKGIAKAF 833
Cdd:cd02769 435 KPETVIVHEPFWTATARHADIVLPATTSLERNDIGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERL 504
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
54-342 |
2.49e-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: 61.47 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 54 CTGSCSWKIYVKNGLVtWEIqqtdypRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRkrlielwrealkqhsdpv 133
Cdd:cd02754 7 CGVGCGVEIGVKDGKV-VAV------RGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 134 lawasimndpqkslsykqvRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVAGFS----PIPAMsmvsYAA------- 202
Cdd:cd02754 62 -------------------RNGGELVPVSWDEALDLIAERFKAIQAEYGPDSVAFYGsgqlLTEEY----YAAnklakgg 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 203 -GTRYL---------SLLGGTCLSFYdwyCDLPPASpmtwgeqtdvpeSADWYNSSYIIAWGSNvpqtrTPDAH--FFTE 270
Cdd:cd02754 119 lGTNNIdtnsrlcmaSAVAGYKRSFG---ADGPPGS------------YDDIEHADCFFLIGSN-----MAECHpiLFRR 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831325 271 VR-----YKGTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLDnpSDYFINYCRRYSDMPMLVM 342
Cdd:cd02754 179 LLdrkkaNPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLID--RDFIDAHTEGFEELKAFVA 253
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
103-317 |
2.75e-09 |
|
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: 61.51 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 103 LYSANRLKYPLIRKRlielWREAlKQHSDPvlawasimndpqkslsykQVRGRGGFIRSNWPELNQLIAAANVWTIKTYG 182
Cdd:cd02769 41 VYSPTRIKYPMVRRG----WLEK-GPGSDR------------------SLRGKEEFVRVSWDEALDLVAAELKRVRKTYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 183 PDRVAG-----FSP---IPAMSMVSyaagtRYLSLLGGTCLSFYDwYCD------LP---PASPMTWGEQTDVPESADwy 245
Cdd:cd02769 98 NEAIFGgsygwSSAgrfHHAQSLLH-----RFLNLAGGYVGSVGD-YSTgaaqviLPhvvGSMEVYTEQQTSWPVIAE-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 246 NSSYIIAWGSNVPQTR------TPDaH----FFTEVRYKGTKTIAITPDYSEVAKLCD-QWLAPKQGTDSALAMAMGHVI 314
Cdd:cd02769 170 HTELVVAFGADPLKNAqiawggIPD-HqaysYLKALKDRGIRFISISPLRDDTAAELGaEWIAIRPGTDVALMLALAHTL 248
|
...
gi 15831325 315 LKE 317
Cdd:cd02769 249 VTE 251
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
764-833 |
7.73e-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: 59.93 E-value: 7.73e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831325 764 KLDLLVTLD-FRMSSTCLFSDIVLPTATWYEKDDMNTsDMHPFIHPLSAAVDPAWESRSDWEIYKGIAKAF 833
Cdd:cd02754 416 RLEFVVVQDaFADTETAEYADLVLPAASWGEKEGTMT-NSERRVSLLRAAVEPPGEARPDWWILADVARRL 485
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
43-105 |
4.44e-08 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 50.71 E-value: 4.44e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831325 43 DKIVRSTHGVnCTGSCSWKIYVKNGLVTWEIQqtdyprtRPDLPNHEPRGCPRGASYSWYLYS 105
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVRG-------DPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
764-831 |
4.83e-08 |
|
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: 56.93 E-value: 4.83e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831325 764 KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDD-MNTSDMHPFIHPLSAAVDPAWESRSDWEIYKGIAK 831
Cdd:cd02759 356 ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGlRGGFEAENFVQLRQKAVEPYGEAKSDYEIVLELGK 424
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1085-1157 |
5.00e-08 |
|
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: 53.02 E-value: 5.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831325 1085 ALNFLTPHQKWGIHSTYSENLLMLTLSRGG--PIvWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPG 1157
Cdd:cd02793 2 PLHLLSNQPATRLHSQLDHGSLSRAYKVQGrePI-RINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPG 75
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
54-317 |
7.14e-08 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 56.98 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 54 CTGSCSWKIYVKNGlvtweiqQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIR--KRLIELWREAlkqhsd 131
Cdd:PRK15488 51 CSTRCPIEARVVNG-------KNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRvgERGEGKWQEI------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 132 pvlawasimndpqkslsykqvrgrggfirsNWPELNQLIAAaNVWTIKT-YGPDRVAgfspipamsmVSYAAGtrylsll 210
Cdd:PRK15488 118 ------------------------------SWDEAYQEIAA-KLNAIKQqHGPESVA----------FSSKSG------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 211 ggtclSFYDWYCDLPPA--SPMTWGEQTDVP---ESA-----------DWYNSSYIIAWGSN------VPQTRTPdAHFF 268
Cdd:PRK15488 150 -----SLSSHLFHLATAfgSPNTFTHASTCPagyAIAakvmfggklkrDLANSKYIINFGHNlyeginMSDTRGL-MTAQ 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15831325 269 TEvryKGTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKE 317
Cdd:PRK15488 224 ME---KGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEE 269
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
49-547 |
1.55e-07 |
|
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: 55.75 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 49 THGVNCTGSCSW-KIYVKNGLVTwEIQqtdyprtrpdlPNHEP--------RGCPRGASYSWYLYSANRLKYPLIRkrli 119
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVAT-EIE-----------PNFAAedihpargRVCVKAYGLVQKTYNPNRVLQPMKR---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 120 elwrealkqhsdpvlawasimNDPQKSLSYKQvrgrgGFIRSNWPELNQLIAA------ANVWTIKTYGPDRVAGFSP-- 191
Cdd:cd02760 66 ---------------------TNPKKGRNEDP-----GFVPISWDEALDLVAAklrrvrEKGLLDEKGLPRLAATFGHgg 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 192 IPAMSMVSYAAgtrYLSLLGGTCLSFYDWYCDLPPASPMTWGE--QTDVPESADWYNSSYIIAWGSNVPQTRTPDA-HFF 268
Cdd:cd02760 120 TPAMYMGTFPA---FLAAWGPIDFSFGSGQGVKCVHSEHLYGEfwHRAFTVAADTPLANYVISFGSNVEASGGPCAvTRH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 269 TEVRYKGTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLDNpsdYFINYCRRYSDMPMLVmlepRDD 348
Cdd:cd02760 197 ADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMFAMIHVMVHEQGLGK---LDVPFLRDRTSSPYLV----GPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 349 GSYVPGRMIRASDLvdglgesnnpqWKTVAvNTAgelvVPNGSIGFRWGEKGKWNLEsiaagketelsltllGQHDAVAG 428
Cdd:cd02760 270 GLYLRDAATGKPLV-----------WDERS-GRA----VPFDTRGAVPAVAGDFAVD---------------GAVSVDAD 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 429 VAFPYFGGIEnphfrsvkhnpvlvrqlpvknltlaggstcpVVSVYDLVLANygldrgledensakdyaeIKPYTPAWGE 508
Cdd:cd02760 319 DETAIHQGVE-------------------------------GTTAFTMLVEH------------------MRKYTPEWAE 349
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15831325 509 QITGVPRQYIETIAREFADTAH-----KTHGRSM------IILGAGV-NHW 547
Cdd:cd02760 350 SICDVPAATIRRIAREFLENASigstiEVDGVTLpyrpvaVTLGKSVnNGW 400
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
1114-1163 |
1.87e-07 |
|
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: 50.97 E-value: 1.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15831325 1114 GPIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMM-YH 1163
Cdd:cd00508 34 EPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMpFH 84
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
1086-1203 |
5.95e-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: 49.60 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1086 LNFLTPHQKWGIHSTYSeNLLMLTLSRGGPiVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYHAQ 1165
Cdd:cd02794 3 LQLIGWHYKRRTHSTFD-NVPWLREAFPQE-VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 15831325 1166 ERIMNIPGSEVtgmrGGIHNSVTRicPKPTHMIGGYAQ 1203
Cdd:cd02794 81 WYEPDANGIDK----GGCINTLTG--LRPSPLAKGNPQ 112
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
1088-1163 |
4.54e-06 |
|
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: 46.88 E-value: 4.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831325 1088 FLTPHQKW--GIHSTYSENLLMLTLSRGgpiVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYH 1163
Cdd:cd02778 4 LIYGKSPVhtHGHTANNPLLHELTPENT---LWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH 78
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
141-317 |
4.87e-06 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 50.86 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 141 NDPQKsLSYKQVRGRGGFIRSNWPELNQLIAAANVWTIKTYGPDRVAGFSPIPAMSMVSYAAGTRYLSLLGGTCLSFYDW 220
Cdd:cd02762 50 NDPDR-LRTPMRRRGGSFEEIDWDEAFDEIAERLRAIRARHGGDAVGVYGGNPQAHTHAGGAYSPALLKALGTSNYFSAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 221 YCDLPP---ASPMTWGEQTDVPeSADWYNSSYII-----AWGSNVPQTRTPDA-HFFTEVRYKGTKTIAITPDYSEVAKL 291
Cdd:cd02762 129 TADQKPghfWSGLMFGHPGLHP-VPDIDRTDYLLilganPLQSNGSLRTAPDRvLRLKAAKDRGGSLVVIDPRRTETAKL 207
|
170 180
....*....|....*....|....*.
gi 15831325 292 CDQWLAPKQGTDSALAMAMGHVILKE 317
Cdd:cd02762 208 ADEHLFVRPGTDAWLLAAMLAVLLAE 233
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
1117-1163 |
1.06e-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. 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: 46.06 E-value: 1.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15831325 1117 VWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMM-YH 1163
Cdd:cd02792 37 VEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIpYH 84
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
764-832 |
1.91e-05 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 48.90 E-value: 1.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831325 764 KLDLLVTLDFRMSSTCLFSDIVLPTATWYEKD----DMntSDMHPFIHPLSAAVDPAWESRSDWEIYKGIAKA 832
Cdd:PRK15488 456 KLDLVVVCDVYLSESAAYADVVLPESTYLERDeeisDK--SGKNPAYALRQRVVEPIGDTKPSWQIFKELGEK 526
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
497-529 |
6.17e-05 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 47.35 E-value: 6.17e-05
10 20 30
....*....|....*....|....*....|...
gi 15831325 497 AEIKPYTPAWGEQITGVPRQYIETIAREFADTA 529
Cdd:PRK15488 289 ASVKEYTPEWAEAISDVPADDIRRIARELAAAA 321
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
1115-1157 |
1.17e-04 |
|
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: 42.95 E-value: 1.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15831325 1115 PIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPG 1157
Cdd:cd02791 35 PYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPG 77
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
997-1161 |
5.52e-04 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 44.25 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 997 RDIQAQPRKIISS-PTWSGL-----------ESDHVSYNAgYTNVHELIPWRTLSGRQQLYQDH------PWMRAFGEsl 1058
Cdd:PRK14990 594 RHLYAQSREAIPElPTFEEFrkqgifkkrdpQGHHVAYKA-FREDPQANPLTTPSGKIEIYSQAladiaaTWELPEGD-- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 1059 VAYRPPIDTRSVSEMRQIPPNGFPEKALNFltpHQKWGIHSTYSENLLMLTLSRGGpiVWISETDARELTIVDNDWVEVF 1138
Cdd:PRK14990 671 VIDPLPIYTPGFESYQDPLNKQYPLQLTGF---HYKSRVHSTYGNVDVLKAACRQE--MWINPLDAQKRGINNGDKVRIF 745
|
170 180
....*....|....*....|...
gi 15831325 1139 NANGALTARAVVSQRVPPGMTMM 1161
Cdd:PRK14990 746 NDRGEVHIEAKVTPRMMPGVVAL 768
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
1115-1161 |
7.00e-04 |
|
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: 40.52 E-value: 7.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15831325 1115 PIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMM 1161
Cdd:cd02779 33 PYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFM 79
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
1115-1163 |
7.63e-04 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 40.68 E-value: 7.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15831325 1115 PIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMM-YH 1163
Cdd:cd02790 35 EYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFMpFH 84
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
1115-1163 |
9.78e-04 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 40.37 E-value: 9.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15831325 1115 PIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYH 1163
Cdd:cd02781 33 PVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEH 81
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
757-878 |
1.93e-03 |
|
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: 42.38 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831325 757 QTAAIE---GKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNtsdmhpFIHPLSAA---------VDPAWESRSDWE 824
Cdd:cd02762 394 DGARLEaalGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHAT------FFNLEFPRnafryrrplFPPPPGTLPEWE 467
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15831325 825 IYKGIAKAFsqvcvghlgketDVVLQPLLHDSPAELSQPCEVLDWRKGECDLSP 878
Cdd:cd02762 468 ILARLVEAL------------DAVLRAGFYGERAGGTLLLAALLERPSGVDLGP 509
|
|
| |
