|
Name |
Accession |
Description |
Interval |
E-value |
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
2-1236 |
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: 2597.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 2 SKFLDRFRYFKqKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 81
Cdd:COG5013 6 SHLLDRLRFFR-RGEVFSDGHGVTTEGGREWEDFYRDRWQHDKVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTDYPRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 82 RPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRLMKMWREAKVQHSDPVEAWASIIEDADKAKSFKQARGRGGFVRS 161
Cdd:COG5013 85 GPDLPNYEPRGCPRGASFSWYTYSPTRVKYPYVRGVLLELWREARARHGDPVEAWASIVEDPEKRRRYKSARGKGGFVRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 162 SWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPMTWGEQTDVPES 241
Cdd:COG5013 165 TWDEANEIIAAANVYTIKKYGPDRVAGFSPIPAMSMVSYAAGARFLSLIGGVMLSFYDWYADLPPASPQVWGEQTDVPES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 242 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLD 321
Cdd:COG5013 245 ADWYNSGYLIMWGSNVPQTRTPDAHFMTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEFHVD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 322 KPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRTLRASDLVDSLGQENNPEWKTVAFDEK-GDMTVPNGSLGFRWGD-KG 399
Cdd:COG5013 325 RQVPYFTDYARRYTDLPFLVTLEERDGGYVPGRFLRASDLGGALGESNNPEWKTVVLDEAtGEPVVPNGSIGFRWGEsEG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 400 KWNLEQRDGkTGEEIELRLSLLGSHDEVANVGFPYFGGEgsehfnkVDLENILLHKLPAKRLQLADGsTALVTTVYDLTM 479
Cdd:COG5013 405 KWNLELKDA-TGADVDPALSLLDDHDEVVEVAFPYFGGE-------TGGGGVLRRGVPVRRVTLADG-EVLVTTVFDLML 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 480 ANYGLERGLNDeNCATGYDDMKAYTPAWAEKITGVSRAHIIRTAREFADNADKTHGRSMIIVGAGLNHWFHLDMNYRGLI 559
Cdd:COG5013 476 ANYGVDRGLPG-NWPTGYDDDVPYTPAWQEKITGVPREQVIRVAREFAQNAEKTRGRSMIIMGAGTNHWYHSDMIYRAIL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 560 NMLVFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAQELLSPMADKSRY 639
Cdd:COG5013 555 NLLMLCGCQGVNGGGWAHYVGQEKLRPQTGWQPLAFALDWSRPPRQMNGTSFFYAHTDQWRYETLSADELLSPLADGKFW 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 640 SGHLIDFNVRAERMGWLPSAPQLGVNPLRIADEAKKAGMTPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLG 719
Cdd:COG5013 635 GGHLADYNVRAARLGWLPSYPQFNRNPLDLADEAEAAGMEPADYVVDQLKSGELKFACEDPDNPENFPRNLFVWRSNLLG 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 720 SSGKGHEYMLKYLLGTENGIQGKDLGkqGGVKPEEVEWRDNGLDGKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMN 799
Cdd:COG5013 715 SSGKGHEYFLKHLLGTDNGVQGEELG--PGLRPREVVWRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKHDLS 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 800 TSDMHPFIHPLSAAVDPAWESKSDWDIYKGIAKKFSEVCVGHLGKETDVVTLPIQHDSAAEMAQPL-DVKDWKKGECDLI 878
Cdd:COG5013 793 TTDMHPFIHPFSPAVDPPWEARSDWDIFKGIAKKFSELAAGHLGVRKDVVATPLQHDTPGELAQPFgDVKDWKKGECEPI 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 879 PGKTAPHIIPVERDYPATYERFTSIGPLLETIGNGGKGIAWNTQSEMDLLRKLNYT-KAEGPAKGQPKLETAIDAAEMIL 957
Cdd:COG5013 873 PGKTMPKLVVVERDYPAIYEKFTSLGPLLEKLGNGGKGITWDTEEEVEELGKLNGVvREEGVAKGRPRLDTDIDAAEAIL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 958 TLAPETNGQVAVKAWKALSEITGREHAHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWR 1037
Cdd:COG5013 953 ALSPETNGHVAVKAWKALEKRTGRDLAHLAAGREEEKIRFRDIQAQPRKVITSPTWSGSESGGRRYSAFTTNVEELIPWR 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1038 TLSGRQSLYQDHQWMRDFGESLLVYRPPIDTRSVKAVMGEKSNGNPEKALNFLTPHQKWGIHSTYSDNLLMLTLSRGGPI 1117
Cdd:COG5013 1033 TLTGRQHFYLDHDWMREFGEGLPVYRPPLDMKTLFGEPGIGPNGNPEIVLRYLTPHQKWGIHSTYQDNLLMLTLSRGGPT 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1118 VWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITGQRGGIHNSVTRITPKPTH 1197
Cdd:COG5013 1113 VWMSEEDAAKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHAQERIVNVPGSEITGKRGGIHNSVTRIVLKPTH 1192
|
1210 1220 1230
....*....|....*....|....*....|....*....
gi 749146766 1198 MIGGYGHLAYGFNYYGTVGSNRDEFVVVRKMKNINWLDG 1236
Cdd:COG5013 1193 MIGGYAQLSYGFNYYGPTGNQRDEVVVVRKRSQVDWLED 1231
|
|
| narG |
TIGR01580 |
respiratory nitrate reductase, alpha subunit; The Nitrate reductase enzyme complex allows ... |
2-1235 |
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: 2493.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 2 SKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 81
Cdd:TIGR01580 1 SKLLDRLRYFKQKGETFSDGHGQTLNENRDWENVYRQRWQYDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 82 RPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRLMKMWREAKVQHSDPVEAWASIIEDADKAKSFKQARGRGGFVRS 161
Cdd:TIGR01580 81 RPDLPNHEPRGCPRGASYSWYIYSANRLKYPMMRKRLMKLWREAKQTHSDPVEAWASIVENADKAKSYKQARGRGGFVRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 162 SWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPMTWGEQTDVPES 241
Cdd:TIGR01580 161 SWQEVNELIAASNVYTVKNYGPDRVVGFSPIPAMSMVSYASGSRYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 242 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLD 321
Cdd:TIGR01580 241 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAALALAMGHVILREFHLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 322 KPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRTLRASDLVDSLGQENNPEWKTVAFDEKGDMTVPNGSLGFRWGDKGKW 401
Cdd:TIGR01580 321 NPSQYFTEYAKRYTDMPMLVMLEERDGYYAAGRFLRAADLVDALGQENNPEWKTVAFDTNGEMVAPQGSIGFRWGEKGKW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 402 NLEQRDGKTGEEIELRLSLLGSHDEVANVGFPYFGGEGSEHFNKVDLENILLHKLPAKRLQLADGSTALVTTVYDLTMAN 481
Cdd:TIGR01580 401 NLEQRDGKTGEEIELQLSLLGSQDEIAEVGFPYFGGDGTEHFNKVEGENVLLRKLPVKRLQLADGSTALVTTVFDLTLAN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 482 YGLERGLNDENCATGYDDMKAYTPAWAEKITGVSRAHIIRTAREFADNADKTHGRSMIIVGAGLNHWFHLDMNYRGLINM 561
Cdd:TIGR01580 481 YGLERGLGDVNCATSYDDVKAYTPAWQEQITGVSREQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLINM 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 562 LVFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAQELLSPMADKSRYSG 641
Cdd:TIGR01580 561 LILCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPPRHMNGTSFFYNHSSQWRYETVTAEDLLSPMADKSRYTG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 642 HLIDFNVRAERMGWLPSAPQLGVNPLRIADEAKKAGMTPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLGSS 721
Cdd:TIGR01580 641 HLIDYNVRAERMGWLPSAPQLNTNPLTIAGEAEKAGMNPVDYVVKSLQEGSLRFAAEQPDNGVNFPRNLFIWRSNLLGSS 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 722 GKGHEYMLKYLLGTENGIQGKDLGKQGGVKPEEVEWRDNGLDGKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMNTS 801
Cdd:TIGR01580 721 GKGHEYMLKYLLGTENGIMNKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRMSSTCLYSDIVLPTATWYEKDDMNTS 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 802 DMHPFIHPLSAAVDPAWESKSDWDIYKGIAKKFSEVCVGHLGKETDVVTLPIQHDSAAEMAQPLDVKDWKKGECDLIPGK 881
Cdd:TIGR01580 801 DMHPFIHPLSAAIDPAWESKSDWEIYKAIAKAFSEVCVGHLGKEKDIVTLPLQHDSAAELAQPFGVKDWKKGECDLIPGK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 882 TAPHIIPVERDYPATYERFTSIGPLLETIGNGGKGIAWNTQSEMDLLRKLNYTKAE-GPAKGQPKLETAIDAAEMILTLA 960
Cdd:TIGR01580 881 TAPNIQVVERDYPAIYERFTSLGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKAEgSPAKGQPMINTAIDAAEMILTLA 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 961 PETNGQVAVKAWKALSEITGREHAHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTLS 1040
Cdd:TIGR01580 961 PETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTLT 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1041 GRQSLYQDHQWMRDFGESLLVYRPPIDTRSVKAVMGEKSNGNPEKALNFLTPHQKWGIHSTYSDNLLMLTLSRGGPIVWM 1120
Cdd:TIGR01580 1041 GRQQLYQDHQWMRDFGESLLVYRPPIDTRSFKEVIGQKSNGNQEIVLNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWL 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1121 SEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITGQRGGIHNSVTRITPKPTHMIG 1200
Cdd:TIGR01580 1121 SEADAKDLGIADNDWIECFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNVPGSEITQQRGGIHNSVTRITPKPTHMIG 1200
|
1210 1220 1230
....*....|....*....|....*....|....*
gi 749146766 1201 GYGHLAYGFNYYGTVGSNRDEFVVVRKMKNINWLD 1235
Cdd:TIGR01580 1201 GYAQLAYGFNYYGTVGSNRDEFVVVRKMKNVDWLD 1235
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
43-834 |
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: 685.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 43 DKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRlmkmw 122
Cdd:cd02750 1 DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 123 reakvqhsdpveawasiiedadkaksfkqARGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSMVSYAS 202
Cdd:cd02750 76 -----------------------------ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 203 GARYLSLIGGTCLSFYDWYCDLPPASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAIT 282
Cdd:cd02750 127 GSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 283 PDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYTDMPMLVmleerdgyyaagrtlrasdlv 362
Cdd:cd02750 207 PDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDE------DYLKEYTDLPFLV--------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 363 dslgqennpewktvafdekgdmtvpngslgfrwgdkgkwnleqrdgktgeeielrlsllgshdevanvgfpyfggegseh 442
Cdd:cd02750 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 443 fnkvdlenillhklpakrlqladgstalvttvydltmanyglerglndencatgyddmkaYTPAWAEKITGVSRAHIIRT 522
Cdd:cd02750 260 ------------------------------------------------------------YTPAWQEAITGVPRETVIRL 279
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 523 AREFADNadkthGRSMIIVGAGLNHWFHLDMNYRGLINMLVFCGCVGQSGGGWAHYVGQeklrpqtgwqplafaldwqrp 602
Cdd:cd02750 280 AREFATN-----GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQ--------------------- 333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 603 arhmnstsyfynhssqwryetvtaqellspmadksrysghlidfnvraermgwlpsapqlgvnplriadeakkagmtpvd 682
Cdd:cd02750 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 683 ytvkslkegsirfaaeqpengknhPRNLFIWRSNLLGSSGKGHEYmlkyllgtengiqgkdlgkqggvkpeevewRDNGL 762
Cdd:cd02750 334 ------------------------PRVLFVWRGNLFGSSGKGHEY------------------------------FEDAP 359
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749146766 763 DGKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESKSDWDIYKGIAKKF 834
Cdd:cd02750 360 EGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
1087-1226 |
6.90e-84 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 269.25 E-value: 6.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1087 LNFLTPHQKWGIHSTYSDNLLMLTLSRGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYHAQ 1166
Cdd:cd02776 2 LNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1167 ERIVNLPGSEITGQRGGIHNSVTRITPKPTHMIGGYGHLAYGFNYYGTVGSNRDEFVVVR 1226
Cdd:cd02776 82 ERHVNVPGSKLTGKRGGIHNSVTRVRIKPTHLVGGYGQLSYGFNYYGPTGVNRDTRVVVR 141
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-1189 |
1.86e-59 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 217.79 E-value: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 43 DKIVRSTHgVNCTGSCSWKIYVKNGLVTWetQQTDyprtrPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRlmkmw 122
Cdd:COG0243 21 TKTVKTTC-PGCGVGCGLGVKVEDGRVVR--VRGD-----PDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVG----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 123 reakvqhsdpveawasiiedadkaksfkqARGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFS---PIPAMSMVS 199
Cdd:COG0243 88 -----------------------------PRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTsggSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 200 YASGARYLSLIGgtCLSFYDW--YCDLP--PASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTE-VRYK 274
Cdd:COG0243 139 AYLAQRFARALG--TNNLDDNsrLCHESavAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 275 GTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYTDmpmlvmleerdgyyaagr 354
Cdd:COG0243 217 GAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYDR------DFLARHTV------------------ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 355 tlrasdlvdslgqennpewktvafdekgdmtvpngslGFrwgdkgkwnleqrdgktgeeielrlsllgshDEVAnvgfpy 434
Cdd:COG0243 273 -------------------------------------GF-------------------------------DELA------ 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 435 fggegsehfnkvdlenillhklpakrlqladgstalvttvydltmanyglerglndencatgyDDMKAYTPAWAEKITGV 514
Cdd:COG0243 279 ---------------------------------------------------------------AYVAAYTPEWAAEITGV 295
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 515 SRAHIIRTAREFAdnadkTHGRSMIIVGAGLNHWFHLDMNYRGLINMLVFCGCVGQSGGGWahyvgqeklrpqtgwqpla 594
Cdd:COG0243 296 PAEDIRELAREFA-----TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGP------------------- 351
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 595 faldwqrparhmnstsyfynhssqwryetvtaqellspmadksrysghlidFNVRAERMgwlpsapqlgvnplriadeak 674
Cdd:COG0243 352 ---------------------------------------------------FSLTGEAI--------------------- 359
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 675 kagmtpvdytvkslkegsirfaaeqpENGKNHP-RNLFIWRSNLLGSSGkgheymlkyllgtengiqgkDLGKqggvkpe 753
Cdd:COG0243 360 --------------------------LDGKPYPiKALWVYGGNPAVSAP--------------------DTNR------- 386
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 754 eveWRDnGLDgKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESKSDWDIYKGIAKK 833
Cdd:COG0243 387 ---VRE-ALR-KLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKR 461
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 834 fsevcvghLGKETDVvtlpiqhdsaaemaqpldvkDWKKGECDLIpgktaPHIIPVERDYPATYERFtsigplletigng 913
Cdd:COG0243 462 --------LGFEEAF--------------------PWGRTEEDYL-----RELLEATRGRGITFEEL------------- 495
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 914 gkgiawntqsemdllrklnytKAEGPAKgqpkletaidaaemiLTLAPETngqvavkawkalseitgrehahlalnkede 993
Cdd:COG0243 496 ---------------------REKGPVQ---------------LPVPPEP------------------------------ 509
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 994 kiRFRdiqaqprkiissptwsglEDEhvsynagytnvheliPWRTLSGRQSLYQDHQWMrdfgESLLVYRPPIDTRSVKA 1073
Cdd:COG0243 510 --AFR------------------NDG---------------PFPTPSGKAEFYSETLAL----PPLPRYAPPYEGAEPLD 550
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1074 vmgeksngnPEKALNFLTPHQKWGIHSTYsDNLLMLTLSRGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQ 1153
Cdd:COG0243 551 ---------AEYPLRLITGRSRDQWHSTT-YNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTE 620
|
1130 1140 1150
....*....|....*....|....*....|....*.
gi 749146766 1154 RVPAGMTMMYHAQerivnlpGSEITGQRGGIHNSVT 1189
Cdd:COG0243 621 GIRPGVVFAPHGW-------WYEPADDKGGNVNVLT 649
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-834 |
1.47e-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: 180.60 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 47 RSTHgVNCTGSCSWKIYVKNGLVTWEtqqtdypRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRlmkmwreak 126
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRI-------EGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVG--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 127 vqhsdpveawasiiedadkaksfkqarGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSMVSYASGARY 206
Cdd:cd00368 64 ---------------------------GRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 207 LSLIGGTcLSFYDWYCDLPPASPMTW-GEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDY 285
Cdd:cd00368 117 RALGSNN-VDSHARLCHASAVAALKAfGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 286 AEIAKLCDLWLAPKQGtdaamalamghvmlrefhldkpsqyfTDYVrrytdmpmlvmleerdgyyaagrtlrasdlvdsl 365
Cdd:cd00368 196 TETAAKADEWLPIRPG--------------------------TDAA---------------------------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 366 gqennpewktvafdekgdmtvpngslgfrwgdkgkwnleqrdgktgeeielrlsllgshdevanvgfpyfggegsehfnk 445
Cdd:cd00368 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 446 vdlenillhklpakrlqLADGstalvttvydltmanyglerglndencatgyddmkaytpAWAEKITGVSRAHIIRTARE 525
Cdd:cd00368 216 -----------------LALA---------------------------------------EWAAEITGVPAETIRALARE 239
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 526 FAdnadkTHGRSMIIVGAGLNHWFHLDMNYRGLINMLVFCGCVGQSGGGWAHyvgqeklrpqtgwqplafaldwqrparh 605
Cdd:cd00368 240 FA-----AAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP---------------------------- 286
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 606 mnstsyfynhssqwryetvtaqellspmadksrysghlidfnvraermgwlpsapqlGVNPLRIADEAKKAgmtpvdytv 685
Cdd:cd00368 287 ---------------------------------------------------------GGNPLVSAPDANRV--------- 300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 686 kslkegsirFAAEQpengknhprnlfiwrsnllgssgkgheymlkyllgtengiqgkdlgkqggvkpeevewrdngldgK 765
Cdd:cd00368 301 ---------RAALK-----------------------------------------------------------------K 306
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749146766 766 LDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMNTSdMHPFIHPLSAAVDPAWESKSDWDIYKGIAKKF 834
Cdd:cd00368 307 LDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTN-TEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
48-834 |
1.19e-42 |
|
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: 165.34 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 48 STHGVNCTGSCSWKIYVKNGLVTWETQQtdyprtrpDLPNHE-PRGCPRGASYSWYLYSANRLKYPLmrKRLMKmwreak 126
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPN--------EWPDKTyKRGCTRGLSHLQRVYSPDRLKYPM--KRVGE------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 127 vqhsdpveawasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAASNVYTVKTYGPdRVAGFSpipAMSMVSYASGARY 206
Cdd:cd02765 66 --------------------------RGEGKFERITWDEALDTIADKLTEAKREYGG-KSILWM---SSSGDGAILSYLR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 207 LSLIGGTCLSFYDWYCDLPPASPMT----WGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAIT 282
Cdd:cd02765 116 LALLGGGLQDALTYGIDTGVGQGFNrvtgGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVID 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 283 PDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDkpsqyfTDYVRRYTDMPMLVmlEERDGYYaagrtLRASDLV 362
Cdd:cd02765 196 PVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYD------EAFLKSNTSAPFLV--REDNGTL-----LRQADVT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 363 DSLGQENnpewkTVAFDEKGDMTVPNGSLGFRWGDKGKWNLeqrdgktgeeielrlsllgshdevanvgfpyfggegseh 442
Cdd:cd02765 263 ATPAEDG-----YVVWDTNSDSPEPVAATNINPALEGEYTI--------------------------------------- 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 443 fnkvdlenillhklpakrlqlaDGSTalVTTVYDLTManyglerglndencatgyDDMKAYTPAWAEKITGVSRAHIIRT 522
Cdd:cd02765 299 ----------------------NGVK--VHTVLTALR------------------EQAASYPPKAAAEICGLEEAIIETL 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 523 AREFAdnadkTHGRSMIIVGAGLNHWFHLDMNYRGLINMLVFCGCVGQSGGGwahyVGQEKlrpqtgwqplafaldwqrp 602
Cdd:cd02765 337 AEWYA-----TGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG----VGQIK------------------- 388
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 603 arhmnstSYFYNHSSQwryetvtaqellspmadksrySGHLIDFNVraermgWLpsapqlgvnplriadeakkagmtpvd 682
Cdd:cd02765 389 -------FMYFMGSNF---------------------LGNQPDRDR------WL-------------------------- 408
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 683 ytvkslkegsirfaaeqpengknhprnlfiwrsnllgssgkgheymlkyllgtengiqgkdlgkqggvkpeevEWRDNgl 762
Cdd:cd02765 409 -------------------------------------------------------------------------KVMKN-- 413
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749146766 763 dgkLDLVVTLDFRLSSTCLYSDIVLPTATWYE-KDDMNTSDMHPFIHPLSAAVDPAWESKSDWDIYKGIAKKF 834
Cdd:cd02765 414 ---LDFIVVVDIFHTPTVRYADIVLPAAHWFEvEDLLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERL 483
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
153-324 |
4.24e-40 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 152.55 E-value: 4.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 153 RGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVA-GFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPMT 231
Cdd:pfam00384 9 RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAiNGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNGDLCTAAAAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 232 WG-----EQTDVPESADWYNSSYIIAWGSNVPQTRTPD-AHFFTEVRYKGTKTVAITPDYAeiAKLCDLWLAPKQGTDAA 305
Cdd:pfam00384 89 FGsdlrsNYLFNSSIADIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRLD--LTYADEHLGIKPGTDLA 166
|
170
....*....|....*....
gi 749146766 306 MALAMGHVMLREFHLDKPS 324
Cdd:pfam00384 167 LALAGAHVFIKELKKDKDF 185
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
57-834 |
6.80e-39 |
|
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: 154.69 E-value: 6.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 57 SCSW---KIYVKNGLVTwetqqtdypRTRPDlPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRlmkmWREAKVQHSDpv 133
Cdd:cd02751 3 ACHWgpfKAHVKDGVIV---------RVEPD-DTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVG----WLGNGPGSRE-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 134 eawasiiedadkaksfkqARGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRV-----AGFSP---IPAMSMVsyasgAR 205
Cdd:cd02751 67 ------------------LRGEGEFVRISWDEALDLVASELKRIREKYGNEAIfggsyGWASAgrlHHAQSLL-----HR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 206 YLSLIGGTCLSF--YDWYCdLPPASPMTWG------EQTDVPESADwyNSSYIIAWGSNVPQTR--------TPDAHFFT 269
Cdd:cd02751 124 FLNLIGGYLGSYgtYSTGA-AQVILPHVVGsdevyeQGTSWDDIAE--HSDLVVLFGANPLKTRqgggggpdHGSYYYLK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 270 EVRYKGTKTVAITPDYAEIAK-LCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYtdmpmlvmleerdg 348
Cdd:cd02751 201 QAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITEDLHDQ------AFLARY-------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 349 yyaagrtlrasdlvdslgqennpewkTVAFDEKGDmtvpngslgfrwgdkgkwnleqrdgktgeeielrlSLLGSHDEVA 428
Cdd:cd02751 261 --------------------------TVGFDEFKD-----------------------------------YLLGESDGVP 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 429 NvgfpyfggegsehfnkvdlenillhklpakrlqladgstalvttvydltmanyglerglndencatgyddmkayTPAWA 508
Cdd:cd02751 280 K--------------------------------------------------------------------------TPEWA 285
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 509 EKITGVSRAHIIRTAREFADNadkthgRSMIIVGAGLNHWFHLDMNYRGLINMLVFCGCVGQSGGGwahyvgqeklrpqT 588
Cdd:cd02751 286 AEITGVPAETIRALAREIASK------RTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGG-------------F 346
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 589 GwqplafaldwqrparhmnstsyfynhssqwryetvtaqellspmadksrYSGHLIDFNVRAERMGWLPSAPQlGVNP-- 666
Cdd:cd02751 347 G-------------------------------------------------FGYGYSNGGGPPRGGAGGPGLPQ-GKNPvk 376
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 667 -----LRIADEAKKAGmTPVDYTVKSLKEGSIRFaaeqpengknhprnLFIWRSNLLGSsgkgHEymlkyllGTENGIQG 741
Cdd:cd02751 377 dsipvARIADALLNPG-KEFTANGKLKTYPDIKM--------------IYWAGGNPLHH----HQ-------DLNRLIKA 430
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 742 kdlgkqggvkpeeveWRdngldgKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMNTS--DMHPFIHPLSAAVDPAWE 819
Cdd:cd02751 431 ---------------LR------KDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTgnYSNRYLIAMKQAVEPLGE 489
|
810
....*....|....*
gi 749146766 820 SKSDWDIYKGIAKKF 834
Cdd:cd02751 490 ARSDYEIFAELAKRL 504
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
52-833 |
1.06e-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: 132.83 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 52 VNCTGSCSWKIYVKNGLVTW-ETQQTdyprTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKrlmkmwreakvqhs 130
Cdd:cd02770 6 VNCGGRCPLKAHVKDGVITRiETDDT----GDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRV-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 131 dpveawasiiedadkaksfkQARGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVagfspipamsMVSYASGA------ 204
Cdd:cd02770 68 --------------------GKRGEGKFVRISWDEALDTIASELKRIIEKYGNEAI----------YVNYGTGTyggvpa 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 205 ------RYLSLIGGTcLSFYDWYC--DLPPASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTR---TPDAHFFTEVRY 273
Cdd:cd02770 118 grgaiaRLLNLTGGY-LNYYGTYSwaQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRmggGGSTYYYLQAKK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 274 KGTKTVAITPDYAEIAK-LCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYtdmpmlvmleerdgyyaa 352
Cdd:cd02770 197 AGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQ------AFLDRY------------------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 353 grtlrasdlvdslgqennpewkTVAFDEKG--DMTVPNGSLgfrwgdkgkwnleqRDgktgeeielrlsllgshdevanv 430
Cdd:cd02770 253 ----------------------CVGFDAEHlpEGAPPNESY--------------KD----------------------- 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 431 gfpYFGGEGsehfnkvdlenillhklpakrlqladgstalvttvydltmanyglerglndencatgyDDMKAYTPAWAEK 510
Cdd:cd02770 274 ---YVLGTG----------------------------------------------------------YDGTPKTPEWASE 292
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 511 ITGVSRAHIIRTAREFAdnadkTHGRSMIIVGAGLNHWFHLDMNYRGLINMLVFCGCVGQSGGGWAHYVGQEKL---RPQ 587
Cdd:cd02770 293 ITGVPAETIRRLAREIA-----TTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYngaGLP 367
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 588 TGWQPLAFALDwqrparhmnstsyfynhSSQWrYETVtaqellspmadksrysghlidfnVRAERMgwlpsapqlgvnpl 667
Cdd:cd02770 368 AGKNPVKTSIP-----------------CFMW-TDAI-----------------------ERGEEM-------------- 392
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 668 rIADEAKKAGMTPVDYTVKslkegsirfaaeqpengknhprnlFIWrsnllgsSGKGHeymlkYLLGTENGIQgkdlgkQ 747
Cdd:cd02770 393 -TADDGGVKGADKLKSNIK------------------------MIW-------NYAGN-----TLINQHSDDN------N 429
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 748 GGVKPEEVEwrdngldGKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDM----NTSDMHPFIHpLSAAVDPAWESKSD 823
Cdd:cd02770 430 TTRALLDDE-------SKCEFIVVIDNFMTPSARYADILLPDTTELEREDIvltsNAGMMEYLIY-SQKAIEPLYECKSD 501
|
810
....*....|
gi 749146766 824 WDIYKGIAKK 833
Cdd:cd02770 502 YEICAELAKR 511
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
54-341 |
1.40e-26 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 114.70 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 54 CTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLpnheprgCPRGASYSWYLYSANRLKYPLMRkrlmkmwreakvqhsdpV 133
Cdd:cd02755 8 CSSRCGILARVEDGRVVKIDGNPLSPLSRGKL-------CARGNAGIQLLYDPDRLKKPLIR-----------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 134 EAwasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSmvSYASgaRYLSLIG-- 211
Cdd:cd02755 64 GE-----------------RGEGKFREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYS--PFFK--HFAAAFGsp 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 212 ------GTCLSFYDWYCDLppaspMTWGEQTDVPesADWYNSSYIIAWGSNV-PQTRTPDAHFFTEVRYKGTKTVAITPD 284
Cdd:cd02755 123 nifsheSTCLASKNLAWKL-----VIDSFGGEVN--PDFENARYIILFGRNLaEAIIVVDARRLMKALENGAKVVVVDPR 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 749146766 285 YAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYTDMPMLV 341
Cdd:cd02755 196 FSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDA------AFVEKYTNGFELL 246
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
54-336 |
1.36e-25 |
|
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: 112.01 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 54 CTGSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP---RGCPRGASYSWYLYSANRLKYPLMRKrlmkmwreakvqhs 130
Cdd:cd02759 7 CHSGCGVLVYVKDGKLV---------KVEGD-PNHPTnkgRLCMRGLAAPEIVYHPDRLLYPLKRV-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 131 dpveawasiiedadkaksfkQARGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSPIP--AMSMVSYASgARYLS 208
Cdd:cd02759 63 --------------------GERGENKWERISWDEALDEIAEKLAEIKAEYGPESIATAVGTGrgTMWQDSLFW-IRFVR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 209 LIGGTCLSFYDWYCDLPPASPMTWGEQT-DVPESADWYNSSYIIAWGSNvPQTRTPD--AHFFTEVRYKGTKTVAITPDY 285
Cdd:cd02759 122 LFGSPNLFLSGESCYWPRDMAHALTTGFgLGYDEPDWENPECIVLWGKN-PLNSNLDlqGHWLVAAMKRGAKLIVVDPRL 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 749146766 286 AEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYTD 336
Cdd:cd02759 201 TWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDK------DFVENWCY 245
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
53-336 |
6.17e-24 |
|
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: 107.33 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 53 NCTGSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP-RG--CPRGASYSWYLYSANRLKYPLMRkrlmkmwreakvqh 129
Cdd:cd02766 7 DCPDTCSLLVTVEDGRIV---------RVEGD-PAHPYtRGfiCAKGARYVERVYSPDRLLTPLKR-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 130 sdpveawasiiedadkaksfkQARGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSMVSYASGARYLSL 209
Cdd:cd02766 63 ---------------------VGRKGGQWERISWDEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 210 IGGTclSFYDWYCDLP--PASPMTWGEQTDV-PEsaDWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYA 286
Cdd:cd02766 122 LGAS--ELRGTICSGAgiEAQKYDFGASLGNdPE--DMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRT 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 749146766 287 EIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYTD 336
Cdd:cd02766 198 ATAARADLHIQIRPGTDGALALGVAKVLFREGLYDR------DFLARHTE 241
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
1087-1206 |
1.01e-20 |
|
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: 88.48 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1087 LNFLTPHQKWGIHSTYsDNLLMLTLSRGGP-IVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYHA 1165
Cdd:pfam01568 1 LYLITGRVLGQYHSQT-RTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 749146766 1166 QERivnlpgseitGQRGGIHNSVTRITPKPTHMIGGYGHLA 1206
Cdd:pfam01568 80 WWY----------EPRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-834 |
1.35e-20 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 98.03 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 43 DKIVRST---HGVnctgSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP-RG--CPRGASYSWYLYSANRLKYPLMRK 116
Cdd:COG3383 4 MKKVKTVcpyCGV----GCGIDLEVKDGKIV---------KVEGD-PDHPVnRGrlCVKGRFGFEFVNSPDRLTTPLIRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 117 RlmkmwreakvqhsdpveawasiiedadkaksfkqargrGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSpipams 196
Cdd:COG3383 70 G--------------------------------------GEFREVSWDEALDLVAERLREIQAEHGPDAVAFYG------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 197 mvsyasGAR------YL------SLIGgTclSFYDwYCDLPPASPMTWGEQTDVPESA------DWYNSSYIIAWGSNVP 258
Cdd:COG3383 106 ------SGQltneenYLlqklarGVLG-T--NNID-NNARLCMASAVAGLKQSFGSDAppnsydDIEEADVILVIGSNPA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 259 QTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYTDmp 338
Cdd:COG3383 176 EAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDE------DFIAERTE-- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 339 mlvmleerdgyyaagrtlrasdlvdslgqennpewktvafdekgdmtvpngslgfrwgdkgkwnleqrdgktgeeielrl 418
Cdd:COG3383 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 419 sllgshdevanvgfpyfggegsehfnkvdlenillhklpakrlqladgstalvttvydltmanyglerglndencatGYD 498
Cdd:COG3383 248 -----------------------------------------------------------------------------GFE 250
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 499 DMKA----YTPAWAEKITGVSRAHIIRTAREFAdnadkTHGRSMIIVGAGLNHWFHLDMNYRGLINMLVFCGCVGQSGGG 574
Cdd:COG3383 251 ELKAsvakYTPERVAEITGVPAEDIREAARLIA-----EAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTG 325
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 575 wahyVGQekLRPQTGWQplafaldwqrPARHMNSTSYFynhssqwryetvtaqellspmadksrYSGH--LIDFNVRAEr 652
Cdd:COG3383 326 ----PFP--LTGQNNVQ----------GGRDMGALPNV--------------------------LPGYrdVTDPEHRAK- 362
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 653 mgwlpSAPQLGVNPLriadeAKKAGMTPVDyTVKSLKEGSIRFaaeqpengknhprnLFIWRSNLLGSSgkgheymlkyl 732
Cdd:COG3383 363 -----VADAWGVPPL-----PDKPGLTAVE-MFDAIADGEIKA--------------LWIIGENPAVSD----------- 406
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 733 lgtengiqgkdlgkqggvkPEEVEWRDnGLDgKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDD-MNTSDMHpfIHPLS 811
Cdd:COG3383 407 -------------------PDANHVRE-ALE-KLEFLVVQDIFLTETAEYADVVLPAASWAEKDGtFTNTERR--VQRVR 463
|
810 820
....*....|....*....|...
gi 749146766 812 AAVDPAWESKSDWDIYKGIAKKF 834
Cdd:COG3383 464 KAVEPPGEARPDWEIIAELARRL 486
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
1095-1202 |
3.79e-19 |
|
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: 83.52 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1095 KWGIHSTYSDNLLMLTLSRGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYHAQERivnlpg 1174
Cdd:cd02775 2 RDHFHSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGH------ 75
|
90 100
....*....|....*....|....*...
gi 749146766 1175 seiTGQRGGIHNSVTRITPKPTHMIGGY 1202
Cdd:cd02775 76 ---RGGRGGNANVLTPDALDPPSGGPAY 100
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
43-375 |
5.22e-19 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 93.17 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 43 DKIVRSTHGVNCTGSCSWKIYVKNGLVTW-ETQQT---DYPRTrpdlpnHEPRGCPRGASYSWYLYSANRLKYPLmrKRL 118
Cdd:PRK14990 56 EKVIWSACTVNCGSRCPLRMHVVDGEIKYvETDNTgddNYDGL------HQVRACLRGRSMRRRVYNPDRLKYPM--KRV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 119 MKmwreakvqhsdpveawasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVA---GFSPIPAM 195
Cdd:PRK14990 128 GA--------------------------------RGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnyGTGTLGGT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 196 SMVSYASGARYLSLIGGTCLSFYDWYCDLPPAS-----PMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDA---HF 267
Cdd:PRK14990 176 MTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQiaeglNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGgvtYY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 268 FTEVRYKGT-KTVAITPDYAEI-AKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKPsqYFTDYVRRYtDMPMLVMLEE 345
Cdd:PRK14990 256 LEQARQKSNaRMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQP--FLDKYCVGY-DEKTLPASAP 332
|
330 340 350
....*....|....*....|....*....|
gi 749146766 346 RDGYYAAGRTLRASDlvdslGQENNPEWKT 375
Cdd:PRK14990 333 KNGHYKAYILGEGPD-----GVAKTPEWAS 357
|
|
| Nitr_red_alph_N |
pfam14710 |
Respiratory nitrate reductase alpha N-terminal; This is the N-terminal tail of the respiratory ... |
4-40 |
7.31e-18 |
|
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: 78.04 E-value: 7.31e-18
10 20 30
....*....|....*....|....*....|....*..
gi 749146766 4 FLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRW 40
Cdd:pfam14710 1 FLDRLRFFKRKRETFADGHGETTNEDRDWEDAYRQRW 37
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
53-336 |
4.02e-17 |
|
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: 86.34 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 53 NCTGSCSWKIYVKNGLVTwetqqtdYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRLMKMWREAK--VQHS 130
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVT-------KVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKGRDVDPkfVPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 131 -DpvEAWASIIEDADKAKSFKQA------RGRGGFVRSSWQEvneliaasnvYTVKTYGPDRVAGFSPIpamsmvsYASG 203
Cdd:cd02757 81 wD--EALDTIADKIRALRKENEPhkimlhRGRYGHNNSILYG----------RFTKMIGSPNNISHSSV-------CAES 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 204 ARYlsliggtclsfydwycdlppaSPMTWGEQTDVPeSADWYNSSYIIAWGSNVPQTRTPDAHF--FTEVRYKGTKTVAI 281
Cdd:cd02757 142 EKF---------------------GRYYTEGGWDYN-SYDYANAKYILFFGADPLESNRQNPHAqrIWGGKMDQAKVVVV 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 749146766 282 TPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKPsqyftdYVRRYTD 336
Cdd:cd02757 200 DPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKD------FVGDFVD 248
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
103-834 |
8.07e-16 |
|
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: 82.31 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 103 LYSANRLKYPLMRKrlmkmwreakvqhsdpveawaSIIEDADKAKsfKQARGRGGFVRSSWQEVNELIAASNVYTVKTYG 182
Cdd:cd02769 41 VYSPTRIKYPMVRR---------------------GWLEKGPGSD--RSLRGKEEFVRVSWDEALDLVAAELKRVRKTYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 183 PDRVAG-----FSP---IPAMSMVsyasgARYLSLIGGTCLSFYDwYCD------LP---PASPMTWGEQTDVPESADwy 245
Cdd:cd02769 98 NEAIFGgsygwSSAgrfHHAQSLL-----HRFLNLAGGYVGSVGD-YSTgaaqviLPhvvGSMEVYTEQQTSWPVIAE-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 246 NSSYIIAWGSNVPQTR------TPDaH----FFTEVRYKGTKTVAITPDYAEIAKLCDL-WLAPKQGTDAAMALAMGHVM 314
Cdd:cd02769 170 HTELVVAFGADPLKNAqiawggIPD-HqaysYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALAHTL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 315 LREfhldkpSQYFTDYVRRYTdmpmlvmleerdgyyaagrtlrasdlvdslgqennpewktVAFDEkgdmtvpngslgFR 394
Cdd:cd02769 249 VTE------GLHDKAFLARYT----------------------------------------VGFDK------------FL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 395 wgdkgkwnleqrdgktgeeielrlsllgshdevanvgfPYFGGEgsehfnkvdlenillhklpakrlqladgstalvttv 474
Cdd:cd02769 271 --------------------------------------PYLLGE------------------------------------ 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 475 ydltmanyglerglndencatgyDDMKAYTPAWAEKITGVSrAHIIRT-AREFADNadkthgRSMIIVGAGLNHWFHLDM 553
Cdd:cd02769 277 -----------------------SDGVPKTPEWAAAICGIP-AETIRElARRFASK------RTMIMAGWSLQRAHHGEQ 326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 554 NYRGLINMLVFCGCVGQSGGGwahyvgqeklrpqtgwqplaFALDWQrparhmnstsyfynhssqwryetvtaqellspm 633
Cdd:cd02769 327 PHWMAVTLAAMLGQIGLPGGG--------------------FGFGYH--------------------------------- 353
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 634 adksrYSGHlidfNVRAERMGWLPSAPQlGVNPL-------RIADEAKKAGmTPVDYTVKSLKEGSIRFAAEQPENGKNH 706
Cdd:cd02769 354 -----YSNG----GGPPRGAAPPPALPQ-GRNPVssfipvaRIADMLLNPG-KPFDYNGKKLTYPDIKLVYWAGGNPFHH 422
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 707 PRNLfiwrsNLLgssgkgheymlkyllgtengIQGkdlgkqggvkpeeveWRdngldgKLDLVVTLDFRLSSTCLYSDIV 786
Cdd:cd02769 423 HQDL-----NRL--------------------IRA---------------WQ------KPETVIVHEPFWTATARHADIV 456
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 749146766 787 LPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESKSDWDIYKGIAKKF 834
Cdd:cd02769 457 LPATTSLERNDIGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERL 504
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
54-317 |
3.87e-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: 79.95 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 54 CTGSCSWKIYVKNGLVTwetqqtdYPRTRPDLPNHEPRGCPRGAsYSW-YLYSANRLKYPLMRKRlmkmwreakvqhsdp 132
Cdd:cd02753 7 CGVGCGLELWVKDNKIV-------GVEPVKGHPVNRGKLCVKGR-FGFdFVNSKDRLTKPLIRKN--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 133 veawasiiedadkaksfkqargrGGFVRSSWQEVNELIAaSNVYTVK-TYGPDRVAGFSpipamsmvsyasGAR------ 205
Cdd:cd02753 64 -----------------------GKFVEASWDEALSLVA-SRLKEIKdKYGPDAIAFFG------------SAKctneen 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 206 YL-----SLIGGT-----CLSfydwYCDlppaSPMTWGEQTDVPESADW------YNSSYIIAWGSNvpqtrTPDAH--F 267
Cdd:cd02753 108 YLfqklaRAVGGTnnvdhCAR----LCH----SPTVAGLAETLGSGAMTnsiadiEEADVILVIGSN-----TTEAHpvI 174
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 749146766 268 FTEVR---YKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLRE 317
Cdd:cd02753 175 ARRIKrakRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEE 227
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
49-530 |
2.50e-14 |
|
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: 78.09 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 49 THGVNCTGSCSW-KIYVKNGLVTWETQQTDYPRTRPDlpnhEPRGCPRGASYSWYLYSANRLKYPLMRKRlmkmwrEAKV 127
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVATEIEPNFAAEDIHPA----RGRVCVKAYGLVQKTYNPNRVLQPMKRTN------PKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 128 QHSDPveawasiiedadkaksfkqargrgGFVRSSWQEVNELIAAsNVYTVKTYG-------PDRVAGFSP--IPAMSMV 198
Cdd:cd02760 72 RNEDP------------------------GFVPISWDEALDLVAA-KLRRVREKGlldekglPRLAATFGHggTPAMYMG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 199 SYASgarYLSLIGGTCLSFYDWYCDLPPASPMTWGE--QTDVPESADWYNSSYIIAWGSNVPQTRTPDA-HFFTEVRYKG 275
Cdd:cd02760 127 TFPA---FLAAWGPIDFSFGSGQGVKCVHSEHLYGEfwHRAFTVAADTPLANYVISFGSNVEASGGPCAvTRHADARVRG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 276 TKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqYFTDYVRRYTDMPMLVmleERDGYYaagrt 355
Cdd:cd02760 204 YKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMFAMIHVMVHEQGLGK---LDVPFLRDRTSSPYLV---GPDGLY----- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 356 LRasdlvdslgqeNNPEWKTVAFDEKGDMTVPNGSLGFrwgdkgkwnleqrdgktGEEIELRLSLLGSHDEVANVGFPYF 435
Cdd:cd02760 273 LR-----------DAATGKPLVWDERSGRAVPFDTRGA-----------------VPAVAGDFAVDGAVSVDADDETAIH 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 436 GGegsehfnkvdlenillhklpakrlqlADGSTALVTTVydltmanyglerglndencatgyDDMKAYTPAWAEKITGVS 515
Cdd:cd02760 325 QG--------------------------VEGTTAFTMLV-----------------------EHMRKYTPEWAESICDVP 355
|
490
....*....|....*
gi 749146766 516 RAHIIRTAREFADNA 530
Cdd:cd02760 356 AATIRRIAREFLENA 370
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
479-834 |
6.65e-13 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 73.03 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 479 MANYGLERGLNDE----NCATGYDDMKA----YTPAWAEKITGVSRAHIIRTAREFADNadkthGRSMIIVGAGLNHWFH 550
Cdd:cd02754 223 LLHVLIEEGLIDRdfidAHTEGFEELKAfvadYTPEKVAEITGVPEADIREAARLFGEA-----RKVMSLWTMGVNQSTQ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 551 LDMNYRGLINMLVFCGCVGQSGGGwahyvgqeklrpqtgwqplAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAqell 630
Cdd:cd02754 298 GTAANNAIINLHLATGKIGRPGSG-------------------PFSLTGQPNAMGGREVGGLANLLPGHRSVNNPE---- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 631 spmadksrysgHlidfnvRAErmgwlpSAPQLGVNPLRIADEakkagmTPVDYT--VKSLKEGSIRFaaeqpengknhpr 708
Cdd:cd02754 355 -----------H------RAE------VAKFWGVPEGTIPPK------PGLHAVemFEAIEDGEIKA------------- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 709 nLFIWRSNLLGSSgkgheymlkyllgtengiqgkdlgkqggvkPEEVEWRDNGLdgKLDLVVTLD-FRLSSTCLYSDIVL 787
Cdd:cd02754 393 -LWVMCTNPAVSL------------------------------PNANRVREALE--RLEFVVVQDaFADTETAEYADLVL 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 749146766 788 PTATWYEKDDMNTsDMHPFIHPLSAAVDPAWESKSDWDIYKGIAKKF 834
Cdd:cd02754 440 PAASWGEKEGTMT-NSERRVSLLRAAVEPPGEARPDWWILADVARRL 485
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
1087-1197 |
2.45e-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: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1087 LNFLTPHQKWGIHSTYSDNLLMLTLSrGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMtmmyhaq 1166
Cdd:cd02785 4 LACIQRHSRFRVHSQFSNVPWLLELQ-PEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGV------- 75
|
90 100 110
....*....|....*....|....*....|..
gi 749146766 1167 eriVNLP-GSEITGQRGGIHNSVTRITPKPTH 1197
Cdd:cd02785 76 ---VTAEqGWWSRYFQEGSLQDLTSPFVNPVH 104
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
54-368 |
1.58e-11 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 68.70 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 54 CTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLpnheprgCPRGASYSWYLYSANRLKYPLMRKrlmkmwreakvqhsdpv 133
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIKGNPDHPLNKGVI-------CAKGSSGIMKQYSPARLTKPLLRK----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 134 eawasiiedadkaksfkQARGRGGFVRSSWQEVNElIAASNVYTVKTYGPDRVAGFSPIPAMSMVSyasgARYLSLIGGT 213
Cdd:cd02763 63 -----------------GPRGSGQFEEIEWEEAFS-IATKRLKAARATDPKKFAFFTGRDQMQALT----GWFAGQFGTP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 214 CLSFYDWYCDLPPASPMTWGEQTDVPE--SADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITP---DYAEI 288
Cdd:cd02763 121 NYAAHGGFCSVNMAAGGLYSIGGSFWEfgGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPvrtGYAAI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 289 AklcDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYTDMPMLVMLEERdgyYAAGRTLRASDLVDSLGQE 368
Cdd:cd02763 201 A---DEWVPIKPGTDGAFILALAHELLKAGLIDW------EFLKRYTNAAELVDYTPE---WVEKITGIPADTIRRIAKE 268
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1087-1164 |
1.84e-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: 62.60 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1087 LNFLTPHQKWGIHSTYsDNLLMLTLS---RGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMY 1163
Cdd:cd02777 3 LQLISPHPKRRLHSQL-DNVPWLREAykvKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALP 81
|
.
gi 749146766 1164 H 1164
Cdd:cd02777 82 E 82
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
54-335 |
3.18e-11 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 67.77 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 54 CTGSCSWKIYVKNGlvtwetqQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMR--KRLMKMWREAkvqhsd 131
Cdd:PRK15488 51 CSTRCPIEARVVNG-------KNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRvgERGEGKWQEI------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 132 pveawasiiedadkaksfkqargrggfvrsSWQEVNELIAASNVYTVKTYGPDRVAgfspipamsmVSYASGarylslig 211
Cdd:PRK15488 118 ------------------------------SWDEAYQEIAAKLNAIKQQHGPESVA----------FSSKSG-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 212 gtclSFYDWYCDLPPA--SPMTWGEQTDVP---ESA-----------DWYNSSYIIAWGSN------VPQTRTPdAHFFT 269
Cdd:PRK15488 150 ----SLSSHLFHLATAfgSPNTFTHASTCPagyAIAakvmfggklkrDLANSKYIINFGHNlyeginMSDTRGL-MTAQM 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749146766 270 EvryKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYT 335
Cdd:PRK15488 225 E---KGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDK------AFVERYT 281
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
765-834 |
1.04e-09 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 63.15 E-value: 1.04e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749146766 765 KLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMNTSDMHPF--IHPLSAAVDPAWESKSDWDIYKGIAKKF 834
Cdd:PRK15102 494 KLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNrgIIAMKKVVEPLFESRSDFDIFRELCRRF 565
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
1087-1160 |
2.31e-09 |
|
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: 56.14 E-value: 2.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749146766 1087 LNFLTPHQKWGIHSTYSdNLLMLTLSRGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMT 1160
Cdd:cd02786 3 LRLITPPAHNFLNSTFA-NLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV 75
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
54-336 |
5.93e-09 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 60.32 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 54 CTGSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP---RGCPRGASYSWYLYSANRLKYPLMRkrlmkmwreakvqhs 130
Cdd:cd02754 7 CGVGCGVEIGVKDGKVV---------AVRGD-PEHPVnrgRLCIKGLNLHKTLNGPERLTRPLLR--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 131 dpveawasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAgFspipamsmvsYASG-----AR 205
Cdd:cd02754 62 ----------------------RNGGELVPVSWDEALDLIAERFKAIQAEYGPDSVA-F----------YGSGqllteEY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 206 YL-----------------------SLIGGTCLSFYdwyCDLPPASpmtwgeqtdvpeSADWYNSSYIIAWGSNvpqtrT 262
Cdd:cd02754 109 YAanklakgglgtnnidtnsrlcmaSAVAGYKRSFG---ADGPPGS------------YDDIEHADCFFLIGSN-----M 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 263 PDAH--FFTEVR-----YKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKpsqyftDYVRRYT 335
Cdd:cd02754 169 AECHpiLFRRLLdrkkaNPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDR------DFIDAHT 242
|
.
gi 749146766 336 D 336
Cdd:cd02754 243 E 243
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
43-105 |
2.67e-08 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 51.10 E-value: 2.67e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749146766 43 DKIVRSTHGVnCTGSCSWKIYVKNGLVTWETQqtdyprtRPDLPNHEPRGCPRGASYSWYLYS 105
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVRG-------DPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1086-1158 |
1.45e-07 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 51.48 E-value: 1.45e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749146766 1086 ALNFLTPHQKWGIHSTYsDNLlmlTLSRGGPI-----VWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAG 1158
Cdd:cd02793 2 PLHLLSNQPATRLHSQL-DHG---SLSRAYKVqgrepIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPG 75
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
765-833 |
1.83e-07 |
|
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: 55.39 E-value: 1.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 765 KLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDD-MNTSDMHPFIHPLSAAVDPAWESKSDWDIYKGIAKK 833
Cdd:cd02759 356 ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGlRGGFEAENFVQLRQKAVEPYGEAKSDYEIVLELGKR 425
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
1115-1172 |
3.92e-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: 50.20 E-value: 3.92e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749146766 1115 GPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMM-YH----AQERIVNL 1172
Cdd:cd00508 34 EPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMpFHwggeVSGGAANA 96
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
1089-1227 |
5.20e-07 |
|
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: 49.58 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 1089 FLTPHQKWGIHSTYSDNLLMLTLsRGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYHAQEr 1168
Cdd:cd02778 4 LIYGKSPVHTHGHTANNPLLHEL-TPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGFG- 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 749146766 1169 iVNLPGSEITGQRGGihnSVTRITPkpthmiggyghlaYGFNYYGTVGSNRDEFVVVRK 1227
Cdd:cd02778 82 -HWAPALSRAYGGGV---NDNNLLP-------------GSTEPVSGGAGLQEFTVTVRK 123
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
765-833 |
1.14e-06 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 53.13 E-value: 1.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749146766 765 KLDLVVTLDFRLSSTCLYSDIVLPTATWYEKD----DMntSDMHPFIHPLSAAVDPAWESKSDWDIYKGIAKK 833
Cdd:PRK15488 456 KLDLVVVCDVYLSESAAYADVVLPESTYLERDeeisDK--SGKNPAYALRQRVVEPIGDTKPSWQIFKELGEK 526
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
1087-1164 |
2.57e-06 |
|
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: 47.67 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749146766 1087 LNFLTPHQKWGIHSTYsDNLLMLTLSRGGPiVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYH 1164
Cdd:cd02794 3 LQLIGWHYKRRTHSTF-DNVPWLREAFPQE-VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQ 78
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
67-317 |
3.52e-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: 51.24 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 67 GLVTwETQQTDYPRTRPDlPNHE-PRG--CPRGASYSWYLYSANRLKYPLMRKRlmkmwreakvqhsdpveawasiieda 143
Cdd:cd02762 12 GLVV-TVEDGRVASIRGD-PDDPlSKGyiCPKAAALGDYQNDPDRLRTPMRRRG-------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 144 dkaksfkqargrGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSmvSYASGARYLSLIG--GTCLSFYDWY 221
Cdd:cd02762 64 ------------GSFEEIDWDEAFDEIAERLRAIRARHGGDAVGVYGGNPQAH--THAGGAYSPALLKalGTSNYFSAAT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749146766 222 CDLPP---ASPMTWGEQTDVPeSADWYNSSYII-----AWGSNVPQTRTPDA-HFFTEVRYKGTKTVAITPDYAEIAKLC 292
Cdd:cd02762 130 ADQKPghfWSGLMFGHPGLHP-VPDIDRTDYLLilganPLQSNGSLRTAPDRvLRLKAAKDRGGSLVVIDPRRTETAKLA 208
|
250 260
....*....|....*....|....*
gi 749146766 293 DLWLAPKQGTDAAMALAMGHVMLRE 317
Cdd:cd02762 209 DEHLFVRPGTDAWLLAAMLAVLLAE 233
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
1118-1164 |
3.40e-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: 44.52 E-value: 3.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 749146766 1118 VWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMM-YH 1164
Cdd:cd02792 37 VEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIpYH 84
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
1116-1172 |
3.91e-05 |
|
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: 44.15 E-value: 3.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 749146766 1116 PIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMM-YHAQERIVNL 1172
Cdd:cd02790 35 EYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFMpFHFAEAAANL 92
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
1116-1158 |
8.64e-05 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 43.33 E-value: 8.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 749146766 1116 PIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAG 1158
Cdd:cd02791 35 PYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPG 77
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
1116-1162 |
1.93e-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: 42.06 E-value: 1.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 749146766 1116 PIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMM 1162
Cdd:cd02779 33 PYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFM 79
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
1116-1164 |
8.23e-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: 40.75 E-value: 8.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 749146766 1116 PIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYH 1164
Cdd:cd02781 33 PVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEH 81
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
1098-1158 |
5.40e-03 |
|
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: 38.81 E-value: 5.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749146766 1098 IHSTYSDNLLMLTLSRGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAG 1158
Cdd:cd02780 12 LNSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPG 72
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