|
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: 2599.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 2 SKFLDRFRYFKqKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 81
Cdd:COG5013 6 SHLLDRLRFFR-RGEVFSDGHGVTTEGGREWEDFYRDRWQHDKVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTDYPRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 82 RPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRLMKMWREAKALHSDPVEAWASIIEDADKAKSFKQARGRGGFVRS 161
Cdd:COG5013 85 GPDLPNYEPRGCPRGASFSWYTYSPTRVKYPYVRGVLLELWREARARHGDPVEAWASIVEDPEKRRRYKSARGKGGFVRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 162 SWQEVNELIAASNVYTIKNYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPES 241
Cdd:COG5013 165 TWDEANEIIAAANVYTIKKYGPDRVAGFSPIPAMSMVSYAAGARFLSLIGGVMLSFYDWYADLPPASPQVWGEQTDVPES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 242 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLD 321
Cdd:COG5013 245 ADWYNSGYLIMWGSNVPQTRTPDAHFMTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEFHVD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 322 NPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRMLRAADLVDALGQENNPEWKTVAFNTN-GEMVAPNGSIGFRWGE-KG 399
Cdd:COG5013 325 RQVPYFTDYARRYTDLPFLVTLEERDGGYVPGRFLRASDLGGALGESNNPEWKTVVLDEAtGEPVVPNGSIGFRWGEsEG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 400 KWNLEQRDGkTGEETELQLSLLGSQDEIAEVGFPYFGGDgTEHfnkvelENVLLHKLPVKRLQLADGsTALVTTVYDLTL 479
Cdd:COG5013 405 KWNLELKDA-TGADVDPALSLLDDHDEVVEVAFPYFGGE-TGG------GGVLRRGVPVRRVTLADG-EVLVTTVFDLML 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 480 ANYGLERGLNDvNCATSYDDVKAYTPAWAEQITGVSRSQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLI 559
Cdd:COG5013 476 ANYGVDRGLPG-NWPTGYDDDVPYTPAWQEKITGVPREQVIRVAREFAQNAEKTRGRSMIIMGAGTNHWYHSDMIYRAIL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 560 NMLIFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAEELLSPMADKSRY 639
Cdd:COG5013 555 NLLMLCGCQGVNGGGWAHYVGQEKLRPQTGWQPLAFALDWSRPPRQMNGTSFFYAHTDQWRYETLSADELLSPLADGKFW 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 640 TGHLIDFNVRAERMGWLPSAPQLGTNPLTIAREAEKAGMNPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLG 719
Cdd:COG5013 635 GGHLADYNVRAARLGWLPSYPQFNRNPLDLADEAEAAGMEPADYVVDQLKSGELKFACEDPDNPENFPRNLFVWRSNLLG 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 720 SSGKGHEFMLKYLLGTEHGIQGKDLGqqGGVKPEEVDWQDNGLEGKLDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMN 799
Cdd:COG5013 715 SSGKGHEYFLKHLLGTDNGVQGEELG--PGLRPREVVWRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKHDLS 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 800 TSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKFSEVCVGHLGKETDIVTLPIQHDSAAELAQPL-DVKDWKKGECDLI 878
Cdd:COG5013 793 TTDMHPFIHPFSPAVDPPWEARSDWDIFKGIAKKFSELAAGHLGVRKDVVATPLQHDTPGELAQPFgDVKDWKKGECEPI 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 879 PGKTAPHIMVVERDYPATYERFTSIGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYT-KAEGPAKGQPMLNTAIDAAEMIL 957
Cdd:COG5013 873 PGKTMPKLVVVERDYPAIYEKFTSLGPLLEKLGNGGKGITWDTEEEVEELGKLNGVvREEGVAKGRPRLDTDIDAAEAIL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 958 TLAPETNGQVAVKAWAALSEFTGRDHTYLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWR 1037
Cdd:COG5013 953 ALSPETNGHVAVKAWKALEKRTGRDLAHLAAGREEEKIRFRDIQAQPRKVITSPTWSGSESGGRRYSAFTTNVEELIPWR 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1038 TLSGRQQLYQDHQWMRDFGESLLVYRPPIDTRSVKEVMGQKSNGNPEKALNFLTPHQKWGIHSTYSDNLLMLTLGRGGPV 1117
Cdd:COG5013 1033 TLTGRQHFYLDHDWMREFGEGLPVYRPPLDMKTLFGEPGIGPNGNPEIVLRYLTPHQKWGIHSTYQDNLLMLTLSRGGPT 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1118 VWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITQQRGGIHNSVTRITPKPTH 1197
Cdd:COG5013 1113 VWMSEEDAAKIGIKDNDWIEAFNRNGVVVARAVVSHRIPEGTVFMYHAQERIVNVPGSEITGKRGGIHNSVTRIVLKPTH 1192
|
1210 1220 1230
....*....|....*....|....*....|....*....
gi 1912564260 1198 MIGGYAHLAYGFNYYGTVGSNRDEFVVVRKMKNIDWLDG 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: 2573.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 2 SKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 81
Cdd:TIGR01580 1 SKLLDRLRYFKQKGETFSDGHGQTLNENRDWENVYRQRWQYDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 82 RPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRLMKMWREAKALHSDPVEAWASIIEDADKAKSFKQARGRGGFVRS 161
Cdd:TIGR01580 81 RPDLPNHEPRGCPRGASYSWYIYSANRLKYPMMRKRLMKLWREAKQTHSDPVEAWASIVENADKAKSYKQARGRGGFVRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 162 SWQEVNELIAASNVYTIKNYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPES 241
Cdd:TIGR01580 161 SWQEVNELIAASNVYTVKNYGPDRVVGFSPIPAMSMVSYASGSRYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 242 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLD 321
Cdd:TIGR01580 241 ADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAALALAMGHVILREFHLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 322 NPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRMLRAADLVDALGQENNPEWKTVAFNTNGEMVAPNGSIGFRWGEKGKW 401
Cdd:TIGR01580 321 NPSQYFTEYAKRYTDMPMLVMLEERDGYYAAGRFLRAADLVDALGQENNPEWKTVAFDTNGEMVAPQGSIGFRWGEKGKW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 402 NLEQRDGKTGEETELQLSLLGSQDEIAEVGFPYFGGDGTEHFNKVELENVLLHKLPVKRLQLADGSTALVTTVYDLTLAN 481
Cdd:TIGR01580 401 NLEQRDGKTGEEIELQLSLLGSQDEIAEVGFPYFGGDGTEHFNKVEGENVLLRKLPVKRLQLADGSTALVTTVFDLTLAN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 482 YGLERGLNDVNCATSYDDVKAYTPAWAEQITGVSRSQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLINM 561
Cdd:TIGR01580 481 YGLERGLGDVNCATSYDDVKAYTPAWQEQITGVSREQIIRIAREFADNADKTHGRSMIIVGAGLNHWYHLDMNYRGLINM 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 562 LIFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAEELLSPMADKSRYTG 641
Cdd:TIGR01580 561 LILCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPPRHMNGTSFFYNHSSQWRYETVTAEDLLSPMADKSRYTG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 642 HLIDFNVRAERMGWLPSAPQLGTNPLTIAREAEKAGMNPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLGSS 721
Cdd:TIGR01580 641 HLIDYNVRAERMGWLPSAPQLNTNPLTIAGEAEKAGMNPVDYVVKSLQEGSLRFAAEQPDNGVNFPRNLFIWRSNLLGSS 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 722 GKGHEFMLKYLLGTEHGIQGKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMNTS 801
Cdd:TIGR01580 721 GKGHEYMLKYLLGTENGIMNKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRMSSTCLYSDIVLPTATWYEKDDMNTS 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 802 DMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKFSEVCVGHLGKETDIVTLPIQHDSAAELAQPLDVKDWKKGECDLIPGK 881
Cdd:TIGR01580 801 DMHPFIHPLSAAIDPAWESKSDWEIYKAIAKAFSEVCVGHLGKEKDIVTLPLQHDSAAELAQPFGVKDWKKGECDLIPGK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 882 TAPHIMVVERDYPATYERFTSIGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKAE-GPAKGQPMLNTAIDAAEMILTLA 960
Cdd:TIGR01580 881 TAPNIQVVERDYPAIYERFTSLGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKAEgSPAKGQPMINTAIDAAEMILTLA 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 961 PETNGQVAVKAWAALSEFTGRDHTYLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTLS 1040
Cdd:TIGR01580 961 PETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTLT 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1041 GRQQLYQDHQWMRDFGESLLVYRPPIDTRSVKEVMGQKSNGNPEKALNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWL 1120
Cdd:TIGR01580 1041 GRQQLYQDHQWMRDFGESLLVYRPPIDTRSFKEVIGQKSNGNQEIVLNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWL 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1121 SEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITQQRGGIHNSVTRITPKPTHMIG 1200
Cdd:TIGR01580 1121 SEADAKDLGIADNDWIECFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNVPGSEITQQRGGIHNSVTRITPKPTHMIG 1200
|
1210 1220 1230
....*....|....*....|....*....|....*
gi 1912564260 1201 GYAHLAYGFNYYGTVGSNRDEFVVVRKMKNIDWLD 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: 692.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 43 DKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRlmkmw 122
Cdd:cd02750 1 DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPETPPDLPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 123 reakalhsdpveawasiiedadkaksfkqARGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFSPIPAMSMVSYAS 202
Cdd:cd02750 76 -----------------------------ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 203 GARYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVT 282
Cdd:cd02750 127 GSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 283 PDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDNpsqyftDYVRRYTDMPMLVmleerdgyyaagrmlraadlv 362
Cdd:cd02750 207 PDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDE------DYLKEYTDLPFLV--------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 363 dalgqennpewktvafntngemvapngsigfrwgekgkwnleqrdgktgeetelqlsllgsqdeiaevgfpyfggdgteh 442
Cdd:cd02750 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 443 fnkvelenvllhklpvkrlqladgstalvttvydltlanyglerglndvncatsyddvkaYTPAWAEQITGVSRSQIIRI 522
Cdd:cd02750 260 ------------------------------------------------------------YTPAWQEAITGVPRETVIRL 279
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 523 AREFADNadkthGRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGWAHYVGQeklrpqtgwqplafaldwqrp 602
Cdd:cd02750 280 AREFATN-----GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQ--------------------- 333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 603 arhmnstsyfynhssqwryetvtaeellspmadksrytghlidfnvraermgwlpsapqlgtnpltiareaekagmnpvd 682
Cdd:cd02750 --------------------------------------------------------------------------------
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 683 ytvkslkegsirfaaeqpengknhPRNLFIWRSNLLGSSGKGHEFMlkyllgtehgiqgkdlgqqggvkpeevdwqDNGL 762
Cdd:cd02750 334 ------------------------PRVLFVWRGNLFGSSGKGHEYF------------------------------EDAP 359
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1912564260 763 EGKLDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKF 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 |
1.85e-83 |
|
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: 268.09 E-value: 1.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1087 LNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHAQ 1166
Cdd:cd02776 2 LNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1167 ERIVNLPGSEITQQRGGIHNSVTRITPKPTHMIGGYAHLAYGFNYYGTVGSNRDEFVVVR 1226
Cdd:cd02776 82 ERHVNVPGSKLTGKRGGIHNSVTRVRIKPTHLVGGYGQLSYGFNYYGPTGVNRDTRVVVR 141
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-1189 |
1.23e-63 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 230.12 E-value: 1.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 43 DKIVRSTHgVNCTGSCSWKIYVKNGLVTWetQQTDyprtrPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRlmkmw 122
Cdd:COG0243 21 TKTVKTTC-PGCGVGCGLGVKVEDGRVVR--VRGD-----PDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVG----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 123 reakalhsdpveawasiiedadkaksfkqARGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFS---PIPAMSMVS 199
Cdd:COG0243 88 -----------------------------PRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTsggSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 200 YASGARYLSLIGgtCLSFYDW--YCDLP--PASPQTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTE-VRYK 274
Cdd:COG0243 139 AYLAQRFARALG--TNNLDDNsrLCHESavAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 275 GTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDnpsqyfTDYVRRYTDmpmlvmleerdgyyaagr 354
Cdd:COG0243 217 GAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYD------RDFLARHTV------------------ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 355 mlraadlvdalgqennpewktvafntngemvapngsiGFrwgekgkwnleqrdgktgeetelqlsllgsqDEIAEvgfpy 434
Cdd:COG0243 273 -------------------------------------GF-------------------------------DELAA----- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 435 fggdgtehfnkvelenvllhklpvkrlqladgstalvttvydltlanyglerglndvncatsydDVKAYTPAWAEQITGV 514
Cdd:COG0243 280 ----------------------------------------------------------------YVAAYTPEWAAEITGV 295
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 515 SRSQIIRIAREFAdnadkTHGRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGwahyvgqeklrpqtgwqpla 594
Cdd:COG0243 296 PAEDIRELAREFA-----TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGG-------------------- 350
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 595 faldwqrparhmnstsYFYnhssqwryetVTAEELLspmadksrytghlidfnvraermgwlpsapqlgtnpltiareae 674
Cdd:COG0243 351 ----------------PFS----------LTGEAIL-------------------------------------------- 360
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 675 kagmnpvdytvkslkegsirfaaeqpeNGKNHP-RNLFIWRSNLLGSSGkghefmlkyllGTEHGIQGkdlgqqggvkpe 753
Cdd:COG0243 361 ---------------------------DGKPYPiKALWVYGGNPAVSAP-----------DTNRVREA------------ 390
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 754 evdWQdnglegKLDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKK 833
Cdd:COG0243 391 ---LR------KLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKR 461
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 834 fsevcvghLGKEtdivtlpiqhdsaaelaqplDVKDWKKGECDLIpgktaPHIMVVERDYPATYERFtsigplmekigng 913
Cdd:COG0243 462 --------LGFE--------------------EAFPWGRTEEDYL-----RELLEATRGRGITFEEL------------- 495
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 914 gkgiawntqsemdllrklnytKAEGPAKgqpmlntaidaaemiLTLAPETngqvavkawaalseftgrdhtylalnkede 993
Cdd:COG0243 496 ---------------------REKGPVQ---------------LPVPPEP------------------------------ 509
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 994 kiRFRdiqaqprkiissptwsglEDEhvsynagytnvheliPWRTLSGRQQLYQDHQWMrdfgESLLVYRPPIDTRSVKE 1073
Cdd:COG0243 510 --AFR------------------NDG---------------PFPTPSGKAEFYSETLAL----PPLPRYAPPYEGAEPLD 550
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1074 vmgqksngnPEKALNFLTPHQKWGIHSTYsDNLLMLTLGRGGPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQ 1153
Cdd:COG0243 551 ---------AEYPLRLITGRSRDQWHSTT-YNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTE 620
|
1130 1140 1150
....*....|....*....|....*....|....*.
gi 1912564260 1154 RVPAGMTMMYHAQerivnlpGSEITQQRGGIHNSVT 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 |
3.13e-53 |
|
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: 191.39 E-value: 3.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 47 RSTHgVNCTGSCSWKIYVKNGLVTWEtqqtdypRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRlmkmwreak 126
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRI-------EGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVG--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 127 alhsdpveawasiiedadkaksfkqarGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFSPIPAMSMVSYASGARY 206
Cdd:cd00368 64 ---------------------------GRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 207 LSLIGGTcLSFYDWYCDLPPASPQTW-GEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTPDY 285
Cdd:cd00368 117 RALGSNN-VDSHARLCHASAVAALKAfGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 286 AEIAKLCDLWLAPKQGTdaamalamghvmlrefhldnpsqyftdyvrrytdmpmlvmleerdgyyaagrmlraadlvdal 365
Cdd:cd00368 196 TETAAKADEWLPIRPGT--------------------------------------------------------------- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 366 gqennpewktvafntngemvapngsigfrwgekgkwnleqrdgktgeetelqlsllgsqdeiaevgfpyfggdgtehfnk 445
Cdd:cd00368 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 446 velenvllhklpvkrlqladgstalvttvyDLTLANYglerglndvncatsyddvkaytpAWAEQITGVSRSQIIRIARE 525
Cdd:cd00368 213 ------------------------------DAALALA-----------------------EWAAEITGVPAETIRALARE 239
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 526 FAdnadkTHGRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGWAHyvgqeklrpqtgwqplafaldwqrparh 605
Cdd:cd00368 240 FA-----AAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP---------------------------- 286
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 606 mnstsyfynhssqwryetvtaeellspmadksrytghlidfnvraermgwlpsapqlGTNPLTIAREAEKAgmnpvdytv 685
Cdd:cd00368 287 ---------------------------------------------------------GGNPLVSAPDANRV--------- 300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 686 kslkegsirFAAEQpengknhprnlfiwrsnllgssgkghefmlkyllgtehgiqgkdlgqqggvkpeevdwqdnglegK 765
Cdd:cd00368 301 ---------RAALK-----------------------------------------------------------------K 306
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1912564260 766 LDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMNTSdMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKF 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 |
1.34e-45 |
|
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: 174.20 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 48 STHGVNCTGSCSWKIYVKNGLVTWETQQtdyprtrpDLPNHE-PRGCPRGASYSWYLYSANRLKYPMmrKRLMKmwreak 126
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPN--------EWPDKTyKRGCTRGLSHLQRVYSPDRLKYPM--KRVGE------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 127 alhsdpveawasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAASNVYTIKNYGPdRVAGFSpipAMSMVSYASGARY 206
Cdd:cd02765 66 --------------------------RGEGKFERITWDEALDTIADKLTEAKREYGG-KSILWM---SSSGDGAILSYLR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 207 LSLIGGTCLSFYDWYCDLPPASPQT----WGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVT 282
Cdd:cd02765 116 LALLGGGLQDALTYGIDTGVGQGFNrvtgGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVID 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 283 PDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDnpsqyfTDYVRRYTDMPMLVmlEERDgyyaaGRMLRAADLV 362
Cdd:cd02765 196 PVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYD------EAFLKSNTSAPFLV--REDN-----GTLLRQADVT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 363 DALGQennpewktvafntNGEMVapngsigfrwgekgkWNLEQRDGKTGEETELQLSLLGSqdeiaevgfpyFGGDGTEh 442
Cdd:cd02765 263 ATPAE-------------DGYVV---------------WDTNSDSPEPVAATNINPALEGE-----------YTINGVK- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 443 fnkvelenvllhklpvkrlqladgstalVTTVYDLTLanyglerglndvncatsyDDVKAYTPAWAEQITGVSRSQIIRI 522
Cdd:cd02765 303 ----------------------------VHTVLTALR------------------EQAASYPPKAAAEICGLEEAIIETL 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 523 AREFAdnadkTHGRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGwahyVGQEKlrpqtgwqplafaldwqrp 602
Cdd:cd02765 337 AEWYA-----TGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG----VGQIK------------------- 388
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 603 arhmnstSYFYNHSSQwryetvtaeellspmadksryTGHLIDFNVraermgWLpsapqlgtnpltiareaekagmnpvd 682
Cdd:cd02765 389 -------FMYFMGSNF---------------------LGNQPDRDR------WL-------------------------- 408
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 683 ytvkslkegsirfaaeqpengknhprnlfiwrsnllgssgkghefmlkyllgtehgiqgkdlgqqggvkpeevDWQDNgl 762
Cdd:cd02765 409 -------------------------------------------------------------------------KVMKN-- 413
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1912564260 763 egkLDLVVTLDFRLSSTCLYSDIILPTATWYE-KDDMNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKF 834
Cdd:cd02765 414 ---LDFIVVVDIFHTPTVRYADIVLPAAHWFEvEDLLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERL 483
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
108-324 |
1.19e-40 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 154.10 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 108 RLKYPMMRkrlmkmwreakalhsdpveawasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVA 187
Cdd:pfam00384 1 RLKYPMVR-------------------------------------RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 188 -GFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPQTWG-----EQTDVPESADWYNSSYIIAWGSNVPQTR 261
Cdd:pfam00384 44 iNGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNGDLCTAAAAAFGsdlrsNYLFNSSIADIENADLILLIGTNPREEA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1912564260 262 TPD-AHFFTEVRYKGTKTVAVTPDYAeiAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDNPS 324
Cdd:pfam00384 124 PILnARIRKAALKGKAKVIVIGPRLD--LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDF 185
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
57-834 |
1.02e-38 |
|
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: 153.92 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 57 SCSW---KIYVKNGLVTwetqqtdypRTRPDlPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRlmkmWREAKALHSDpv 133
Cdd:cd02751 3 ACHWgpfKAHVKDGVIV---------RVEPD-DTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVG----WLGNGPGSRE-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 134 eawasiiedadkaksfkqARGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRV-----AGFSP---IPAMSMVsyasgAR 205
Cdd:cd02751 67 ------------------LRGEGEFVRISWDEALDLVASELKRIREKYGNEAIfggsyGWASAgrlHHAQSLL-----HR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 206 YLSLIGGTCLSF--YDWYCdLPPASPQTWG------EQTDVPESADwyNSSYIIAWGSNVPQTR--------TPDAHFFT 269
Cdd:cd02751 124 FLNLIGGYLGSYgtYSTGA-AQVILPHVVGsdevyeQGTSWDDIAE--HSDLVVLFGANPLKTRqgggggpdHGSYYYLK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 270 EVRYKGTKTVAVTPDYAEIAK-LCDLWLAPKQGTDAAMALAMGHVMLREfhldnpSQYFTDYVRRYTdmpmlvmleerdg 348
Cdd:cd02751 201 QAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITE------DLHDQAFLARYT------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 349 yyaagrmlraadlvdalgqennpewktvafntngemvapngsigfrwgekgkwnleqrdgktgeetelqlsllgsqdeia 428
Cdd:cd02751 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 429 eVGFPYFggdgtehfnkvelenvllhklpvkrlqladgstalvttvydltlANYGLERglndvncatsyDDVKAYTPAWA 508
Cdd:cd02751 262 -VGFDEF--------------------------------------------KDYLLGE-----------SDGVPKTPEWA 285
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 509 EQITGVSRSQIIRIAREFADNadkthgRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGWAHYVGQeklrpQT 588
Cdd:cd02751 286 AEITGVPAETIRALAREIASK------RTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGY-----SN 354
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 589 GWQPLAFALDWQRPARHMNSTSYFYNhSSQWryetvtAEELLSPmadksrytGHLIDFNVRAE-----RMGWlpsapqlg 663
Cdd:cd02751 355 GGGPPRGGAGGPGLPQGKNPVKDSIP-VARI------ADALLNP--------GKEFTANGKLKtypdiKMIY-------- 411
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 664 tnpltiareaeKAGMNPvdytvkslkegsirFAAEQPENgknhpRNLFIWRsnllgssgkghefmlkyllgtehgiqgkd 743
Cdd:cd02751 412 -----------WAGGNP--------------LHHHQDLN-----RLIKALR----------------------------- 432
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 744 lgqqggvkpeevdwqdnglegKLDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMNTS--DMHPFIHPLSAAVDPAWEAK 821
Cdd:cd02751 433 ---------------------KDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTgnYSNRYLIAMKQAVEPLGEAR 491
|
810
....*....|...
gi 1912564260 822 SDWEIYKAIAKKF 834
Cdd:cd02751 492 SDYEIFAELAKRL 504
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
52-373 |
1.20e-32 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 135.53 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 52 VNCTGSCSWKIYVKNGLVTW-ETQQTdyprTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKrlmkmwreakalhs 130
Cdd:cd02770 6 VNCGGRCPLKAHVKDGVITRiETDDT----GDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRV-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 131 dpveawasiiedadkaksfkQARGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVagfspipamsMVSYASGA------ 204
Cdd:cd02770 68 --------------------GKRGEGKFVRISWDEALDTIASELKRIIEKYGNEAI----------YVNYGTGTyggvpa 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 205 ------RYLSLIGGTcLSFYDWYC--DLPPASPQTWGEQTDVPESADWYNSSYIIAWGSNVPQTR---TPDAHFFTEVRY 273
Cdd:cd02770 118 grgaiaRLLNLTGGY-LNYYGTYSwaQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRmggGGSTYYYLQAKK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 274 KGTKTVAVTPDYAEIAK-LCDLWLAPKQGTDAAMALAMGHVMLREFHLDnpsQYFTDyvrRYT------DMPMLVMLEER 346
Cdd:cd02770 197 AGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHD---QAFLD---RYCvgfdaeHLPEGAPPNES 270
|
330 340
....*....|....*....|....*..
gi 1912564260 347 dgyYAAGRMLRAADlvdalGQENNPEW 373
Cdd:cd02770 271 ---YKDYVLGTGYD-----GTPKTPEW 289
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
54-336 |
2.76e-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: 111.24 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 54 CTGSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP---RGCPRGASYSWYLYSANRLKYPMMRKrlmkmwreakalhs 130
Cdd:cd02759 7 CHSGCGVLVYVKDGKLV---------KVEGD-PNHPTnkgRLCMRGLAAPEIVYHPDRLLYPLKRV-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 131 dpveawasiiedadkaksfkQARGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFSPIP--AMSMVSYASgARYLS 208
Cdd:cd02759 63 --------------------GERGENKWERISWDEALDEIAEKLAEIKAEYGPESIATAVGTGrgTMWQDSLFW-IRFVR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 209 LIGGTCLSFYDWYCDLPPASPQTWGEQT-DVPESADWYNSSYIIAWGSNvPQTRTPD--AHFFTEVRYKGTKTVAVTPDY 285
Cdd:cd02759 122 LFGSPNLFLSGESCYWPRDMAHALTTGFgLGYDEPDWENPECIVLWGKN-PLNSNLDlqGHWLVAAMKRGAKLIVVDPRL 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1912564260 286 AEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDNpsqyftDYVRRYTD 336
Cdd:cd02759 201 TWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDK------DFVENWCY 245
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
54-341 |
7.64e-25 |
|
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: 109.31 E-value: 7.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 54 CTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLpnheprgCPRGASYSWYLYSANRLKYPMMRkrlmkmwreakalhsdpV 133
Cdd:cd02755 8 CSSRCGILARVEDGRVVKIDGNPLSPLSRGKL-------CARGNAGIQLLYDPDRLKKPLIR-----------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 134 EAwasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAaSNVYTIK-NYGPDRVAGFSPIPAMSmvSYASgaRYLSLIG- 211
Cdd:cd02755 64 GE-----------------RGEGKFREASWDEALQYIA-SKLKEIKeQHGPESVLFGGHGGCYS--PFFK--HFAAAFGs 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 212 -------GTCLSFYDWYCDLppaspQTWGEQTDVPesADWYNSSYIIAWGSNV-PQTRTPDAHFFTEVRYKGTKTVAVTP 283
Cdd:cd02755 122 pnifsheSTCLASKNLAWKL-----VIDSFGGEVN--PDFENARYIILFGRNLaEAIIVVDARRLMKALENGAKVVVVDP 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1912564260 284 DYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREfhldnpSQYFTDYVRRYTDMPMLV 341
Cdd:cd02755 195 RFSELASKADEWIPIKPGTDLAFVLALIHVLISE------NLYDAAFVEKYTNGFELL 246
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
53-336 |
2.17e-23 |
|
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: 105.79 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 53 NCTGSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP-RG--CPRGASYSWYLYSANRLKYPMMRkrlmkmwreakalh 129
Cdd:cd02766 7 DCPDTCSLLVTVEDGRIV---------RVEGD-PAHPYtRGfiCAKGARYVERVYSPDRLLTPLKR-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 130 sdpveawasiiedadkaksfkQARGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFSPIPAMSMVSYASGARYLSL 209
Cdd:cd02766 63 ---------------------VGRKGGQWERISWDEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 210 IGGTclSFYDWYCDLP--PASPQTWGEQTDV-PEsaDWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTPDYA 286
Cdd:cd02766 122 LGAS--ELRGTICSGAgiEAQKYDFGASLGNdPE--DMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRT 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1912564260 287 EIAKLCDLWLAPKQGTDAAMALAMGHVMLREfhldnpSQYFTDYVRRYTD 336
Cdd:cd02766 198 ATAARADLHIQIRPGTDGALALGVAKVLFRE------GLYDRDFLARHTE 241
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-834 |
2.03e-22 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 103.81 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 43 DKIVRST---HGVnctgSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP-RG--CPRGASYSWYLYSANRLKYPMMRK 116
Cdd:COG3383 4 MKKVKTVcpyCGV----GCGIDLEVKDGKIV---------KVEGD-PDHPVnRGrlCVKGRFGFEFVNSPDRLTTPLIRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 117 RlmkmwreakalhsdpveawasiiedadkaksfkqargrGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFSpipams 196
Cdd:COG3383 70 G--------------------------------------GEFREVSWDEALDLVAERLREIQAEHGPDAVAFYG------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 197 mvsyasGAR------YL------SLIGgTclSFYDwYCDLPPASPQTWGEQTDVPESA------DWYNSSYIIAWGSNVP 258
Cdd:COG3383 106 ------SGQltneenYLlqklarGVLG-T--NNID-NNARLCMASAVAGLKQSFGSDAppnsydDIEEADVILVIGSNPA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 259 QTRTPDAHFFTEVRYKGTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDnpsqyfTDYVRRYTDmp 338
Cdd:COG3383 176 EAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVD------EDFIAERTE-- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 339 mlvmleerdgyyaagrmlraadlvdalgqennpewktvafntngemvapngsiGFrwgekgkwnleqrdgktgeetelql 418
Cdd:COG3383 248 -----------------------------------------------------GF------------------------- 249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 419 sllgsqDEIAEVgfpyfggdgtehfnkvelenvllhklpvkrlqladgstalvttvydltlanyglerglndvncatsyd 498
Cdd:COG3383 250 ------EELKAS-------------------------------------------------------------------- 255
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 499 dVKAYTPAWAEQITGVSRSQIIRIAREFAdnadkTHGRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGqsgggwahy 578
Cdd:COG3383 256 -VAKYTPERVAEITGVPAEDIREAARLIA-----EAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIG--------- 320
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 579 vgqeklRPQTGWQPLafaldwqrparhmnstsyfynhssqwryetvtaeellspmadksryTGHlidFNVR-AERMGWLP 657
Cdd:COG3383 321 ------RPGTGPFPL----------------------------------------------TGQ---NNVQgGRDMGALP 345
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 658 S---APQLGTNPLTIAREAE---------KAGMNPVDyTVKSLKEGSIRFaaeqpengknhprnLFIWRSNLLGSsgkgh 725
Cdd:COG3383 346 NvlpGYRDVTDPEHRAKVADawgvpplpdKPGLTAVE-MFDAIADGEIKA--------------LWIIGENPAVS----- 405
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 726 efmlkyllgtehgiqgkdLGQQGGVKpeevdwqdNGLEgKLDLVVTLDFRLSSTCLYSDIILPTATWYEKDD-MNTSDMH 804
Cdd:COG3383 406 ------------------DPDANHVR--------EALE-KLEFLVVQDIFLTETAEYADVVLPAASWAEKDGtFTNTERR 458
|
810 820 830
....*....|....*....|....*....|
gi 1912564260 805 pfIHPLSAAVDPAWEAKSDWEIYKAIAKKF 834
Cdd:COG3383 459 --VQRVRKAVEPPGEARPDWEIIAELARRL 486
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
1087-1206 |
2.45e-21 |
|
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: 90.41 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1087 LNFLTPHQKWGIHSTYsDNLLMLTLGRGGP-VVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHA 1165
Cdd:pfam01568 1 LYLITGRVLGQYHSQT-RTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1912564260 1166 QERivnlpgseitQQRGGIHNSVTRITPKPTHMIGGYAHLA 1206
Cdd:pfam01568 80 WWY----------EPRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
43-375 |
1.52e-19 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 95.10 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 43 DKIVRSTHGVNCTGSCSWKIYVKNGLVTW-ETQQT---DYPRTrpdlpnHEPRGCPRGASYSWYLYSANRLKYPMmrKRL 118
Cdd:PRK14990 56 EKVIWSACTVNCGSRCPLRMHVVDGEIKYvETDNTgddNYDGL------HQVRACLRGRSMRRRVYNPDRLKYPM--KRV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 119 MKmwreakalhsdpveawasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRV---AGFSPIPAM 195
Cdd:PRK14990 128 GA--------------------------------RGEGKFERISWEEAYDIIATNMQRLIKEYGNESIylnYGTGTLGGT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 196 SMVSYASGARYLSLIGGTCLSFYDWYCDLPPAS-----PQTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDA---HF 267
Cdd:PRK14990 176 MTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQiaeglNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGgvtYY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 268 FTEVRYKG-TKTVAVTPDYAEI-AKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDNPsqYFTDYVRRYtDMPMLVMLEE 345
Cdd:PRK14990 256 LEQARQKSnARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQP--FLDKYCVGY-DEKTLPASAP 332
|
330 340 350
....*....|....*....|....*....|
gi 1912564260 346 RDGYYAAGRMLRAADlvdalGQENNPEWKT 375
Cdd:PRK14990 333 KNGHYKAYILGEGPD-----GVAKTPEWAS 357
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
1095-1202 |
2.22e-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: 84.29 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1095 KWGIHSTYSDNLLMLTLGRGGPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHAQERivnlpg 1174
Cdd:cd02775 2 RDHFHSGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGH------ 75
|
90 100
....*....|....*....|....*...
gi 1912564260 1175 seiTQQRGGIHNSVTRITPKPTHMIGGY 1202
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 |
6.07e-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: 6.07e-18
10 20 30
....*....|....*....|....*....|....*..
gi 1912564260 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 |
3.41e-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: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 53 NCTGSCSWKIYVKNGLVTwetqqtdYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRlmkmwrEAKALHSDP 132
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVT-------KVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTN------PRKGRDVDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 133 V-------EAWASIIEDADKAKSFKQA------RGRGGFVRSSWQEvneliaasnvYTIKNYGPDRVAGFSPIPAMS--M 197
Cdd:cd02757 75 KfvpiswdEALDTIADKIRALRKENEPhkimlhRGRYGHNNSILYG----------RFTKMIGSPNNISHSSVCAESekF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 198 VSYASGArylsliggtclsFYDWycdlppaspqtwgeqtdvpESADWYNSSYIIAWGSNVPQTRTPDAHF--FTEVRYKG 275
Cdd:cd02757 145 GRYYTEG------------GWDY-------------------NSYDYANAKYILFFGADPLESNRQNPHAqrIWGGKMDQ 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1912564260 276 TKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREfhldnpSQYFTDYVRRYTD 336
Cdd:cd02757 194 AKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTE------GLWDKDFVGDFVD 248
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
54-833 |
1.37e-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: 81.49 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 54 CTGSCSWKIYVKNGLVTwetqqtdYPRTRPDLPNHEPRGCPRGAsYSW-YLYSANRLKYPMMRKRlmkmwreakalhsdp 132
Cdd:cd02753 7 CGVGCGLELWVKDNKIV-------GVEPVKGHPVNRGKLCVKGR-FGFdFVNSKDRLTKPLIRKN--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 133 veawasiiedadkaksfkqargrGGFVRSSWQEVNELIAaSNVYTIK-NYGPDRVAGFSpipamsmvsyasGAR------ 205
Cdd:cd02753 64 -----------------------GKFVEASWDEALSLVA-SRLKEIKdKYGPDAIAFFG------------SAKctneen 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 206 YL-----SLIGGT-----CLSfydwYCDlppaSPQTWGEQTDVPESADW------YNSSYIIAWGSNvpqtrTPDAH--F 267
Cdd:cd02753 108 YLfqklaRAVGGTnnvdhCAR----LCH----SPTVAGLAETLGSGAMTnsiadiEEADVILVIGSN-----TTEAHpvI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 268 FTEVR---YKGTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREfhldnpsqyftdyvrrytdmpmlvmle 344
Cdd:cd02753 175 ARRIKrakRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEE--------------------------- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 345 erdgyyaagrmlraaDLVDAlgqennpewktvAFntngemvapngsigfrwgekgkwnLEQRdgktgeetelqlsllgsq 424
Cdd:cd02753 228 ---------------GLYDE------------EF------------------------IEER------------------ 238
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 425 deiaevgfpyfggdgTEHFNKVELEnvllhklpvkrlqladgstalvttvydltlanyglerglndvncatsyddVKAYT 504
Cdd:cd02753 239 ---------------TEGFEELKEI--------------------------------------------------VEKYT 253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 505 PAWAEQITGVSRSQIIRIAREFAdnadkTHGRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGqsgggwahyvgqekl 584
Cdd:cd02753 254 PEYAERITGVPAEDIREAARMYA-----TAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIG--------------- 313
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 585 RPQTGWQPLafaldwqrpaRHMNstsyfynhssqwryetvtaeellspmadksrytghlidfNVR-AERMGWLPsapqlg 663
Cdd:cd02753 314 RPGTGVNPL----------RGQN---------------------------------------NVQgACDMGALP------ 338
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 664 tnpltiareaekaGMNPvDYtVKSLkegsirfaaeqpengknhprnlfiwrsnllgssgkghefmlkYLLG--------- 734
Cdd:cd02753 339 -------------NVLP-GY-VKAL------------------------------------------YIMGenpalsdpn 361
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 735 TEHGIQgkdlgqqggvkpeevdwqdnGLEgKLDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMNTSDMHPfIHPLSAAV 814
Cdd:cd02753 362 TNHVRK--------------------ALE-SLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERR-VQRVRKAV 419
|
810
....*....|....*....
gi 1912564260 815 DPAWEAKSDWEIYKAIAKK 833
Cdd:cd02753 420 EPPGEARPDWEIIQELANR 438
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
103-834 |
9.19e-15 |
|
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: 79.23 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 103 LYSANRLKYPMMRKrlmkmwreakalhsdpveawaSIIEDADKAKsfKQARGRGGFVRSSWQEVNELIAASNVYTIKNYG 182
Cdd:cd02769 41 VYSPTRIKYPMVRR---------------------GWLEKGPGSD--RSLRGKEEFVRVSWDEALDLVAAELKRVRKTYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 183 PDRVAG-----FSP---IPAMSMVsyasgARYLSLIGGTCLSFYDwYCD------LP---PASPQTWGEQTDVPESADwy 245
Cdd:cd02769 98 NEAIFGgsygwSSAgrfHHAQSLL-----HRFLNLAGGYVGSVGD-YSTgaaqviLPhvvGSMEVYTEQQTSWPVIAE-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 246 NSSYIIAWGSNVPQTR------TPDaH----FFTEVRYKGTKTVAVTPDYAEIAKLCDL-WLAPKQGTDAAMALAMGHVM 314
Cdd:cd02769 170 HTELVVAFGADPLKNAqiawggIPD-HqaysYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALAHTL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 315 LREfhldnpSQYFTDYVRRYTDmpmlvmleerdgyyaagrmlraadlvdalgqennpewktvafntngemvapngsiGFr 394
Cdd:cd02769 249 VTE------GLHDKAFLARYTV-------------------------------------------------------GF- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 395 wgekgkwnleqrdgktgeetelqlsllgsqDEIAevgfPYFGGDgtehfnkvelenvllhklpvkrlqlADGstalvttv 474
Cdd:cd02769 267 ------------------------------DKFL----PYLLGE-------------------------SDG-------- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 475 ydltlanyglerglndvncatsyddvKAYTPAWAEQITGVSRSQIIRIAREFADNadkthgRSMIIVGAGLNHWYHLDMN 554
Cdd:cd02769 280 --------------------------VPKTPEWAAAICGIPAETIRELARRFASK------RTMIMAGWSLQRAHHGEQP 327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 555 YRGLINMLIFCGCVGQSGGGwahyvgqeklrpqtgwqplaFALDWqrparhmnstsyfynhssqwryetvtaeellspma 634
Cdd:cd02769 328 HWMAVTLAAMLGQIGLPGGG--------------------FGFGY----------------------------------- 352
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 635 dksrytgHLIDFNVRAERMGWLPSAPQlGTNPLT----IAREAEkAGMNP---VDYTVKSLKEGSIRFAAEQPENGKNHP 707
Cdd:cd02769 353 -------HYSNGGGPPRGAAPPPALPQ-GRNPVSsfipVARIAD-MLLNPgkpFDYNGKKLTYPDIKLVYWAGGNPFHHH 423
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 708 RNLfiwrsNLLgssgkghefmlkyllgtehgIQGkdlgqqggvkpeevdWQdnglegKLDLVVTLDFRLSSTCLYSDIIL 787
Cdd:cd02769 424 QDL-----NRL--------------------IRA---------------WQ------KPETVIVHEPFWTATARHADIVL 457
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1912564260 788 PTATWYEKDDMNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKF 834
Cdd:cd02769 458 PATTSLERNDIGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERL 504
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
1087-1197 |
6.33e-14 |
|
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: 69.70 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1087 LNFLTPHQKWGIHSTYSDNLLMLTLgRGGPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMtmmyhaq 1166
Cdd:cd02785 4 LACIQRHSRFRVHSQFSNVPWLLEL-QPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGV------- 75
|
90 100 110
....*....|....*....|....*....|..
gi 1912564260 1167 eriVNLP-GSEITQQRGGIHNSVTRITPKPTH 1197
Cdd:cd02785 76 ---VTAEqGWWSRYFQEGSLQDLTSPFVNPVH 104
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
54-335 |
7.45e-12 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 70.08 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 54 CTGSCSWKIYVKNGlvtwetqQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMR--KRLMKMWREAkalhsd 131
Cdd:PRK15488 51 CSTRCPIEARVVNG-------KNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRvgERGEGKWQEI------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 132 pveawasiiedadkaksfkqargrggfvrsSWQEVNELIAAsNVYTIK-NYGPDRVAgfspipamsmVSYASGarylsli 210
Cdd:PRK15488 118 ------------------------------SWDEAYQEIAA-KLNAIKqQHGPESVA----------FSSKSG------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 211 ggtclSFYDWYCDLPPA--SPQTWGEQTDVP---ESA-----------DWYNSSYIIAWGSN------VPQTRTPdAHFF 268
Cdd:PRK15488 150 -----SLSSHLFHLATAfgSPNTFTHASTCPagyAIAakvmfggklkrDLANSKYIINFGHNlyeginMSDTRGL-MTAQ 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1912564260 269 TEvryKGTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREfhldnpSQYFTDYVRRYT 335
Cdd:PRK15488 224 ME---KGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEE------NLYDKAFVERYT 281
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
49-530 |
1.11e-11 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 69.23 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 49 THGVNCTGSCSW-KIYVKNGLVTWETQQTDYPRTRPDlpnhEPRGCPRGASYSWYLYSANRLKYPMMRKRlmkmwrEAKA 127
Cdd:cd02760 2 TYCYNCVAGPDFmAVKVVDGVATEIEPNFAAEDIHPA----RGRVCVKAYGLVQKTYNPNRVLQPMKRTN------PKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 128 LHSDPveawasiiedadkaksfkqargrgGFVRSSWQEVNELIAAsNVYTIKNYG-------PDRVAGFSP--IPAMSMV 198
Cdd:cd02760 72 RNEDP------------------------GFVPISWDEALDLVAA-KLRRVREKGlldekglPRLAATFGHggTPAMYMG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 199 SYASgarYLSLIGGTCLSFYDWYCDLPPASPQTWGE--QTDVPESADWYNSSYIIAWGSNVPQTRTPDA-HFFTEVRYKG 275
Cdd:cd02760 127 TFPA---FLAAWGPIDFSFGSGQGVKCVHSEHLYGEfwHRAFTVAADTPLANYVISFGSNVEASGGPCAvTRHADARVRG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 276 TKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDnpsQYFTDYVRRYTDMPMLVmleERDGYYaagrm 355
Cdd:cd02760 204 YKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMFAMIHVMVHEQGLG---KLDVPFLRDRTSSPYLV---GPDGLY----- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 356 LRAAdlvdALGqennpewKTVAFNTNGEMVAPNGSIGFrwgekgkwnleqrdgktGEETELQLSLLGSQDEIAEVGFPYF 435
Cdd:cd02760 273 LRDA----ATG-------KPLVWDERSGRAVPFDTRGA-----------------VPAVAGDFAVDGAVSVDADDETAIH 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 436 GGdgtehfnkvelenvllhklpvkrlqlADGSTALVTTVydltlanyglerglndvncatsyDDVKAYTPAWAEQITGVS 515
Cdd:cd02760 325 QG--------------------------VEGTTAFTMLV-----------------------EHMRKYTPEWAESICDVP 355
|
490
....*....|....*
gi 1912564260 516 RSQIIRIAREFADNA 530
Cdd:cd02760 356 AATIRRIAREFLENA 370
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1087-1164 |
1.85e-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: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1087 LNFLTPHQKWGIHSTYsDNLLMLTLG---RGGPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMY 1163
Cdd:cd02777 3 LQLISPHPKRRLHSQL-DNVPWLREAykvKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALP 81
|
.
gi 1912564260 1164 H 1164
Cdd:cd02777 82 E 82
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
479-834 |
3.53e-11 |
|
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: 67.25 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 479 LANYGLERGLND---VNCATS-YDDVKA----YTPAWAEQITGVSRSQIIRIAREFADNadkthGRSMIIVGAGLNHWYH 550
Cdd:cd02754 223 LLHVLIEEGLIDrdfIDAHTEgFEELKAfvadYTPEKVAEITGVPEADIREAARLFGEA-----RKVMSLWTMGVNQSTQ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 551 LDMNYRGLINMLIFCGCVGQSGGGwahyvgqeklrpqtgwqplAFALDWQrparhmnstsyfynhssqwryetvtaeell 630
Cdd:cd02754 298 GTAANNAIINLHLATGKIGRPGSG-------------------PFSLTGQ------------------------------ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 631 sPMADKSRYTGhlidfnvraeRMGWLPSAPQLGTNPLTIAREAEKAGMNPVDytvKSLKEGsiRFAAEQP---ENGKnhP 707
Cdd:cd02754 329 -PNAMGGREVG----------GLANLLPGHRSVNNPEHRAEVAKFWGVPEGT---IPPKPG--LHAVEMFeaiEDGE--I 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 708 RNLFIWRSNLLGSSgkghefmlkyllgtehgiqgkdlgqqggvkPEEVDWQDnGLEgKLDLVVTLD-FRLSSTCLYSDII 786
Cdd:cd02754 391 KALWVMCTNPAVSL------------------------------PNANRVRE-ALE-RLEFVVVQDaFADTETAEYADLV 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1912564260 787 LPTATWYEKDDMNTsDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKF 834
Cdd:cd02754 439 LPAASWGEKEGTMT-NSERRVSLLRAAVEPPGEARPDWWILADVARRL 485
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
1087-1160 |
2.84e-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: 58.83 E-value: 2.84e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1912564260 1087 LNFLTPHQKWGIHSTYSdNLLMLTLGRGGPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMT 1160
Cdd:cd02786 3 LRLITPPAHNFLNSTFA-NLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV 75
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
54-341 |
5.82e-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: 63.70 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 54 CTGSCSWKIYVKNGLVTwetqqtdYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKrlmkmwreakalhsdpv 133
Cdd:cd02763 7 CACRCGIRVHLRDGKVR-------YIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRK----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 134 eawasiiedadkaksfkQARGRGGFVRSSWQEVNElIAASNVYTIKNYGPDRVAGFSPIPAMSMVSyasgARYLSLIGGT 213
Cdd:cd02763 63 -----------------GPRGSGQFEEIEWEEAFS-IATKRLKAARATDPKKFAFFTGRDQMQALT----GWFAGQFGTP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 214 CLSFYDWYCDLPPASPQTWGEQTDVPE--SADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTP---DYAEI 288
Cdd:cd02763 121 NYAAHGGFCSVNMAAGGLYSIGGSFWEfgGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPvrtGYAAI 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1912564260 289 AklcDLWLAPKQGTDAAMALAMGHVMLREFHLDNpsqyftDYVRRYTDMPMLV 341
Cdd:cd02763 201 A---DEWVPIKPGTDGAFILALAHELLKAGLIDW------EFLKRYTNAAELV 244
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
54-336 |
2.08e-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: 61.86 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 54 CTGSCSWKIYVKNGLVTwetqqtdypRTRPDlPNHEP---RGCPRGASYSWYLYSANRLKYPMMRkrlmkmwreakalhs 130
Cdd:cd02754 7 CGVGCGVEIGVKDGKVV---------AVRGD-PEHPVnrgRLCIKGLNLHKTLNGPERLTRPLLR--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 131 dpveawasiiedadkaksfkqaRGRGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAgFspipamsmvsYASG-----AR 205
Cdd:cd02754 62 ----------------------RNGGELVPVSWDEALDLIAERFKAIQAEYGPDSVA-F----------YGSGqllteEY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 206 YL-----------------------SLIGGTCLSFYdwyCDLPPASPQTWgEQTDVpesadwynssyIIAWGSNvpqtrT 262
Cdd:cd02754 109 YAanklakgglgtnnidtnsrlcmaSAVAGYKRSFG---ADGPPGSYDDI-EHADC-----------FFLIGSN-----M 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 263 PDAH--FFTEVR-----YKGTKTVAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDnpsqyfTDYVRRYT 335
Cdd:cd02754 169 AECHpiLFRRLLdrkkaNPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLID------RDFIDAHT 242
|
.
gi 1912564260 336 D 336
Cdd:cd02754 243 E 243
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
765-834 |
1.08e-08 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 59.68 E-value: 1.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1912564260 765 KLDLVVTLDFRLSSTCLYSDIILPTATWYEKDDMNTSDMHPF--IHPLSAAVDPAWEAKSDWEIYKAIAKKF 834
Cdd:PRK15102 494 KLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNrgIIAMKKVVEPLFESRSDFDIFRELCRRF 565
|
|
| 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 1912564260 43 DKIVRSTHGVnCTGSCSWKIYVKNGLVTWETQqtdyprtRPDLPNHEPRGCPRGASYSWYLYS 105
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVRG-------DPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
765-833 |
7.65e-08 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 56.98 E-value: 7.65e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1912564260 765 KLDLVVTLDFRLSSTCLYSDIILPTATWYEKD----DMntSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKK 833
Cdd:PRK15488 456 KLDLVVVCDVYLSESAAYADVVLPESTYLERDeeisDK--SGKNPAYALRQRVVEPIGDTKPSWQIFKELGEK 526
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
765-833 |
9.74e-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: 56.16 E-value: 9.74e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 765 KLDLVVTLDFRLSSTCLYSDIILPTATWYEKDD-MNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKK 833
Cdd:cd02759 356 ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGlRGGFEAENFVQLRQKAVEPYGEAKSDYEIVLELGKR 425
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
1089-1227 |
2.49e-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: 50.74 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1089 FLTPHQKWGIHSTYSDNLLMLTLgRGGPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHaqer 1168
Cdd:cd02778 4 LIYGKSPVHTHGHTANNPLLHEL-TPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH---- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1912564260 1169 ivnlpgseitqqrGGIHNSvTRITPKPTHMIGGYAHLAYGFNYYGTVGSNRDEFVVVRK 1227
Cdd:cd02778 79 -------------GFGHWA-PALSRAYGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
1115-1172 |
2.51e-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: 50.58 E-value: 2.51e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1912564260 1115 GPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMM-YH----AQERIVNL 1172
Cdd:cd00508 34 EPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMpFHwggeVSGGAANA 96
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
1087-1164 |
3.63e-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: 49.98 E-value: 3.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1912564260 1087 LNFLTPHQKWGIHSTYsDNLLMLTlgRGGP-VVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYH 1164
Cdd:cd02794 3 LQLIGWHYKRRTHSTF-DNVPWLR--EAFPqEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQ 78
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
1086-1158 |
4.11e-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: 50.33 E-value: 4.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1912564260 1086 ALNFLTPHQKWGIHSTYSDNLLMLTLGRGG-PVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAG 1158
Cdd:cd02793 2 PLHLLSNQPATRLHSQLDHGSLSRAYKVQGrEPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPG 75
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
67-317 |
2.61e-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: 51.63 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 67 GLVTwETQQTDYPRTRPDlPNHE-PRG--CPRGASYSWYLYSANRLKYPMMRKRlmkmwreakalhsdpveawasiieda 143
Cdd:cd02762 12 GLVV-TVEDGRVASIRGD-PDDPlSKGyiCPKAAALGDYQNDPDRLRTPMRRRG-------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 144 dkaksfkqargrGGFVRSSWQEVNELIAASNVYTIKNYGPDRVAGFSPIPAMSmvSYASGARYLSLIG--GTCLSFYDWY 221
Cdd:cd02762 64 ------------GSFEEIDWDEAFDEIAERLRAIRARHGGDAVGVYGGNPQAH--THAGGAYSPALLKalGTSNYFSAAT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 222 CDLPP---ASPQTWGEQTDVPeSADWYNSSYII-----AWGSNVPQTRTPDA-HFFTEVRYKGTKTVAVTPDYAEIAKLC 292
Cdd:cd02762 130 ADQKPghfWSGLMFGHPGLHP-VPDIDRTDYLLilganPLQSNGSLRTAPDRvLRLKAAKDRGGSLVVIDPRRTETAKLA 208
|
250 260
....*....|....*....|....*
gi 1912564260 293 DLWLAPKQGTDAAMALAMGHVMLRE 317
Cdd:cd02762 209 DEHLFVRPGTDAWLLAAMLAVLLAE 233
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
1116-1172 |
2.41e-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: 44.92 E-value: 2.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1912564260 1116 PVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMM-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 ... |
1116-1166 |
3.84e-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: 44.49 E-value: 3.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1912564260 1116 PVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAG---MTMMYHAQ 1166
Cdd:cd02791 35 PYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGevfVPMHWGDQ 88
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
1118-1158 |
7.88e-05 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 46.97 E-value: 7.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1912564260 1118 VWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAG 1158
Cdd:PRK15102 712 VYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPG 752
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
1116-1164 |
1.52e-04 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. 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: 42.60 E-value: 1.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1116 PVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMM-YH 1164
Cdd:cd02792 35 MFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIpYH 84
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
1116-1193 |
2.14e-04 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 45.71 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1116 PVVWLSEADAKELGIADNDWIEVFNSNGALTaravvsqrVPAGMTMMyhaQERIV----NLPGSEITQQRGGIHNSVTRI 1191
Cdd:PRK07860 718 PVARLSAATAAEIGVADGDAVTVSTERGSIT--------LPLAITDM---PDRVVwlplNSPGSTVRRTLGATAGAVVRI 786
|
..
gi 1912564260 1192 TP 1193
Cdd:PRK07860 787 AA 788
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
1116-1164 |
4.90e-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: 41.53 E-value: 4.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1912564260 1116 PVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYH 1164
Cdd:cd02781 33 PVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEH 81
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
54-367 |
4.99e-04 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 44.31 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 54 CTGSCSWKIYVKNGlvTWETQQTDyprtrPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRLMKMWREAkalhsdpv 133
Cdd:cd02752 7 CSVGCGLIAYVQNG--VWVHQEGD-----PDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEI-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 134 eAWASIIED-ADKAKSFKQA----RGRGGFVRSSWQEVNELIAA--SN--VYTIKNYgpdrvagfspIPAMSMVSYASGA 204
Cdd:cd02752 72 -SWDEALDEiARKMKDIRDAsfveKNAAGVVVNRPDSIAFLGSAklSNeeCYLIRKF----------ARALGTNNLDHQA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 205 RylsLIGGTCLSfydwycdlppASPQTWGEQTDVPESADWYNSSYIIAWGSNvpqtrTPDAH-----FFTEVRYK-GTKT 278
Cdd:cd02752 141 R---IUHSPTVA----------GLANTFGRGAMTNSWNDIKNADVILVMGGN-----PAEAHpvsfkWILEAKEKnGAKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 279 VAVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLRefhldnpsqYFTDYVRRYTDMPMLVMLEERDGYYAAGRMLRA 358
Cdd:cd02752 203 IVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYIIR---------YTPEEVEDICGVPKEDFLKVAEMFAATGRPDKP 273
|
....*....
gi 1912564260 359 ADLVDALGQ 367
Cdd:cd02752 274 GTILYAMGW 282
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
1116-1162 |
2.49e-03 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 38.98 E-value: 2.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1912564260 1116 PVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMM 1162
Cdd:cd02779 33 PYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFM 79
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
1098-1215 |
3.66e-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: 39.20 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912564260 1098 IHSTYSDNLLMLTLGRGGPVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHAQER--------- 1168
Cdd:cd02780 12 LNSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEHGYGHwaygavast 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1912564260 1169 IVNLPGSEITQQRGGIHNSV------TRITPKPTHMIGGYAHlaygfnYYGTV 1215
Cdd:cd02780 92 IDGKDLPGDAWRGAGVNINDiglvdpSRGGWSLVDWVGGAAA------RYDTP 138
|
|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
1116-1158 |
5.56e-03 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain, is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 37.67 E-value: 5.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1912564260 1116 PVVWLSEADAKELGIADNDWIEVFNSNGALTARAVVSQRVPAG 1158
Cdd:cd02788 29 PYARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAG 71
|
|
| |
