NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1434010499|gb|RDA23215|]
View 

dimethyl sulfoxide reductase subunit A [Escherichia coli]

Protein Classification

DmsA/YnfE/YnfF family dimethyl sulfoxide reductase( domain architecture ID 11493795)

DmsA/YnfE/YnfF family dimethyl sulfoxide reductase is terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds; similar to Escherichia coli dimethyl sulfoxide reductase chains, YnfE and YnfF

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
dmsA_ynfE TIGR02166
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ...
14-807 0e+00

anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.


:

Pssm-ID: 274006 [Multi-domain]  Cd Length: 797  Bit Score: 1361.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  14 ISRRSLMKTS-ALGSLALASSAFTLPFSQMVRAAEVPV--EEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDV 90
Cdd:TIGR02166   1 ISRRHFLKTSaALGGLAAASGALSLPFSVNAAAEATPTgpDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTGDDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  91 YGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGN 170
Cdd:TIGR02166  81 YGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTGGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 171 ITNSNVPY---RLMNSCGGFLSRYGSYSTAQISAAMSYMFGAN-DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYYVE 246
Cdd:TIGR02166 161 MSRSWPPTavaRLLNLCGGYLNQYGSYSTAQINEAMPYTYGISaDGSSLDDIENSKLVVMFGNNPAETRMSGGGQTYYFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 247 QARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEKTLPANAPRNAHY 326
Cdd:TIGR02166 241 QALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPKNGSY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 327 KAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGN 406
Cdd:TIGR02166 321 KDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 407 SGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTH 486
Cdd:TIGR02166 401 NGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDINRTH 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 487 EVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRL 566
Cdd:TIGR02166 481 KILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAKRL 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 567 GpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSE 646
Cdd:TIGR02166 561 G--VEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEIYSE 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 647 RLATIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARG 726
Cdd:TIGR02166 639 RLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDAQKRG 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 727 IRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:TIGR02166 719 ITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPD--KNGIDVGGCINTLTTQRPSPLAKGNPQHTNLVEVEK 796

                  .
gi 1434010499 807 V 807
Cdd:TIGR02166 797 A 797
 
Name Accession Description Interval E-value
dmsA_ynfE TIGR02166
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ...
14-807 0e+00

anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.


Pssm-ID: 274006 [Multi-domain]  Cd Length: 797  Bit Score: 1361.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  14 ISRRSLMKTS-ALGSLALASSAFTLPFSQMVRAAEVPV--EEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDV 90
Cdd:TIGR02166   1 ISRRHFLKTSaALGGLAAASGALSLPFSVNAAAEATPTgpDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTGDDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  91 YGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGN 170
Cdd:TIGR02166  81 YGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTGGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 171 ITNSNVPY---RLMNSCGGFLSRYGSYSTAQISAAMSYMFGAN-DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYYVE 246
Cdd:TIGR02166 161 MSRSWPPTavaRLLNLCGGYLNQYGSYSTAQINEAMPYTYGISaDGSSLDDIENSKLVVMFGNNPAETRMSGGGQTYYFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 247 QARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEKTLPANAPRNAHY 326
Cdd:TIGR02166 241 QALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPKNGSY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 327 KAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGN 406
Cdd:TIGR02166 321 KDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 407 SGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTH 486
Cdd:TIGR02166 401 NGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDINRTH 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 487 EVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRL 566
Cdd:TIGR02166 481 KILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAKRL 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 567 GpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSE 646
Cdd:TIGR02166 561 G--VEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEIYSE 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 647 RLATIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARG 726
Cdd:TIGR02166 639 RLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDAQKRG 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 727 IRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:TIGR02166 719 ITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPD--KNGIDVGGCINTLTTQRPSPLAKGNPQHTNLVEVEK 796

                  .
gi 1434010499 807 V 807
Cdd:TIGR02166 797 A 797
PRK14990 PRK14990
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
1-807 0e+00

anaerobic dimethyl sulfoxide reductase subunit A; Provisional


Pssm-ID: 184952 [Multi-domain]  Cd Length: 814  Bit Score: 1306.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499   1 MKIHTTEALMKAEISRRSLMKTSALGSLALASSAFTLPFSQMVRAAEV----PVEEKAVWSSCTVNCGSRCLLRLHVKDD 76
Cdd:PRK14990    1 MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSaiptKSDEKVIWSACTVNCGSRCPLRMHVVDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  77 TVYWVESDTTGDDVY-GNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGN 155
Cdd:PRK14990   81 EIKYVETDNTGDDNYdGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 156 EAVHVLYGTGVDGGNITNSNVP-----YRLMNSCGGFLSRYGSYSTAQISAAMSYMFGA-NDGNSPDDIANTKLVVMFGN 229
Cdd:PRK14990  161 ESIYLNYGTGTLGGTMTRSWPPgntlvARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGwADGNSPSDIENSKLVVLFGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 230 NPAETRMSGGGVTYYVEQARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCV 309
Cdd:PRK14990  241 NPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 310 GYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRA 389
Cdd:PRK14990  321 GYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 390 IAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWC 469
Cdd:PRK14990  401 ISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 470 YASNTLINQHGDINHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAK 549
Cdd:PRK14990  481 YAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPR 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 550 FERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDP 629
Cdd:PRK14990  561 FECKTIYEMTSELAKRLG--VEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDP 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 630 QANPLKTPSGKIEIYSERLATIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQ 709
Cdd:PRK14990  639 QANPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKA 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 710 ACPQEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPS 789
Cdd:PRK14990  719 ACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD--AKRVDKGGCINVLTTQRPS 796
                         810
                  ....*....|....*...
gi 1434010499 790 PLAKGNPSHSNLVQIEKV 807
Cdd:PRK14990  797 PLAKGNPSHTNLVQVEKV 814
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
56-675 0e+00

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: 947.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  56 WSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISW 135
Cdd:cd02770     1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 136 DEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGAND-GNS 214
Cdd:cd02770    81 DEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAAsGSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 215 PDDIANTKLVVMFGNNPAETRMSGGGVTYYVEQAReRSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLI 294
Cdd:cd02770   161 LDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAK-KAGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAAMAYVMI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 295 TENMVDQPFLDKYCVGYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQG 374
Cdd:cd02770   240 TENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGYDGTPKTPEWASEITGVPAETIRRLAREIATTKPAAILQG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 375 WGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGV 454
Cdd:cd02770   320 WGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTADDGGV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 455 RGKEKLDVPIKFLWCYASNTLINQHGDINHTHEVL-QDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESA 533
Cdd:cd02770   400 KGADKLKSNIKMIWNYAGNTLINQHSDDNNTTRALlDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNA 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 534 GNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKK 613
Cdd:cd02770   480 GMMEYLIYSQKAIEPLYECKSDYEICAELAKRLG--VEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGIYRVP 557
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1434010499 614 cPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLATIADTweLKKDEIIHPLPAYTPGFDG 675
Cdd:cd02770   558 -RALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT--LPEGDEIPAIPKYVPAWEG 616
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
45-807 0e+00

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 682.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  45 AAEVPVEEKAVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGK 124
Cdd:COG0243    14 AALEAAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVR----GDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 125 RGEGKFERISWDEALDTISDNLRRILKDYGNEAVhVLYGTGVDGGNITNSNVPY--RLMNSCG--GFLSRyGSYSTAQIS 200
Cdd:COG0243    89 RGSGKFERISWDEALDLIAEKLKAIIDEYGPEAV-AFYTSGGSAGRLSNEAAYLaqRFARALGtnNLDDN-SRLCHESAV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 201 AAMSYMFGANDG-NSPDDIANTKLVVMFGNNPAETrmsGGGVTYYVEQARERSNARMIVIDPRYNDTAAgREDEWLPIRP 279
Cdd:COG0243   167 AGLPRTFGSDKGtVSYEDLEHADLIVLWGSNPAEN---HPRLLRRLREAAKKRGAKIVVIDPRRTETAA-IADEWLPIRP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 280 GTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktlpanaprnahYKAYIlgegpdgIAKTPEWAAKITSIPAEKIIHL 359
Cdd:COG0243   243 GTDAALLLALAHVLIEEGLYDRDFLARHTVGFDE------------LAAYV-------AAYTPEWAAEITGVPAEDIREL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 360 AREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGswdlgvewfpmlenpvktqisvftwtD 439
Cdd:COG0243   304 AREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG--------------------------E 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 440 AIdhgtemtatrdgvrgKEKLDVPIKFLWCYASNtLINQHGDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDILLPDL 519
Cdd:COG0243   358 AI---------------LDGKPYPIKALWVYGGN-PAVSAPDTNRVREALR---KLDFVVVIDTFLTETARYADIVLPAT 418
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 520 MPTEQEDLIsheSAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDvyQTFTEGRSQHEWIKYLHAKTKERNpemP 599
Cdd:COG0243   419 TWLERDDIV---TNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFE--EAFPWGRTEEDYLRELLEATRGRG---I 490
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 600 DYEEMKTTGIFKKKCPEEHyvafrAFREDpqaNPLKTPSGKIEIYSERLAtiadtwelkkdeiIHPLPAYTPGFDgWDDP 679
Cdd:COG0243   491 TFEELREKGPVQLPVPPEP-----AFRND---GPFPTPSGKAEFYSETLA-------------LPPLPRYAPPYE-GAEP 548
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 680 LRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTA 758
Cdd:COG0243   549 LDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPvVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVF 628
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*....
gi 1434010499 759 IGQGAWlkadmFGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV 807
Cdd:COG0243   629 APHGWW-----YEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
114-565 2.86e-68

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 229.98  E-value: 2.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 114 RLKYPMKRvgkRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGvdGGNITNSNVPY-----RLMNSCGGFL 188
Cdd:pfam00384   1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSG--GLTDVESLYALkkllnRLGSKNGNTE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 189 SRYGSYSTAQiSAAMSYMFGAN--DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYyveQARERSNARMIVIDPRYNdt 266
Cdd:pfam00384  76 DHNGDLCTAA-AAAFGSDLRSNylFNSSIADIENADLILLIGTNPREEAPILNARIR---KAALKGKAKVIVIGPRLD-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 267 aAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKycvgydektlpanaprnahykayilgegpdgiaktpewaa 346
Cdd:pfam00384 150 -LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK---------------------------------------- 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 347 kitsipaekiihlareigsakpAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNsgvregswdlgveWFPMLEN 426
Cdd:pfam00384 189 ----------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG-------------WNGLNIL 233
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 427 PvktqisvftwTDAIDHGTEMTATRDGVRGKEKLDVP----IKFLWcYASNTLINQHGDINHTHEVLQddsKCEMIVGID 502
Cdd:pfam00384 234 Q----------GAASPVGALDLGLVPGIKSVEMINAIkkggIKVLY-LLGNNPFVTHADENRVVKALQ---KLDLFVVYD 299
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434010499 503 HFM-TASAKYCDILLPDLMPTEQEDLIShesagNM-GYVILAQPATSAKFERKPIYWMLSEVAKR 565
Cdd:pfam00384 300 GHHgDKTAKYADVILPAAAYTEKNGTYV-----NTeGRVQSTKQAVPPPGEAREDWKILRALSEV 359
Molybdop_Fe4S4 smart00926
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ...
52-111 2.38e-09

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: 53.79  E-value: 2.38e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499   52 EKAVWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNH 111
Cdd:smart00926   1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVR----GDPDHPVNRGRLCPKGRAGLEQVYS 55
 
Name Accession Description Interval E-value
dmsA_ynfE TIGR02166
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ...
14-807 0e+00

anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.


Pssm-ID: 274006 [Multi-domain]  Cd Length: 797  Bit Score: 1361.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  14 ISRRSLMKTS-ALGSLALASSAFTLPFSQMVRAAEVPV--EEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDV 90
Cdd:TIGR02166   1 ISRRHFLKTSaALGGLAAASGALSLPFSVNAAAEATPTgpDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTGDDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  91 YGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGN 170
Cdd:TIGR02166  81 YGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTGGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 171 ITNSNVPY---RLMNSCGGFLSRYGSYSTAQISAAMSYMFGAN-DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYYVE 246
Cdd:TIGR02166 161 MSRSWPPTavaRLLNLCGGYLNQYGSYSTAQINEAMPYTYGISaDGSSLDDIENSKLVVMFGNNPAETRMSGGGQTYYFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 247 QARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEKTLPANAPRNAHY 326
Cdd:TIGR02166 241 QALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPKNGSY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 327 KAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGN 406
Cdd:TIGR02166 321 KDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 407 SGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTH 486
Cdd:TIGR02166 401 NGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDINRTH 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 487 EVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRL 566
Cdd:TIGR02166 481 KILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAKRL 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 567 GpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSE 646
Cdd:TIGR02166 561 G--VEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEIYSE 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 647 RLATIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARG 726
Cdd:TIGR02166 639 RLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDAQKRG 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 727 IRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:TIGR02166 719 ITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPD--KNGIDVGGCINTLTTQRPSPLAKGNPQHTNLVEVEK 796

                  .
gi 1434010499 807 V 807
Cdd:TIGR02166 797 A 797
PRK14990 PRK14990
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
1-807 0e+00

anaerobic dimethyl sulfoxide reductase subunit A; Provisional


Pssm-ID: 184952 [Multi-domain]  Cd Length: 814  Bit Score: 1306.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499   1 MKIHTTEALMKAEISRRSLMKTSALGSLALASSAFTLPFSQMVRAAEV----PVEEKAVWSSCTVNCGSRCLLRLHVKDD 76
Cdd:PRK14990    1 MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSaiptKSDEKVIWSACTVNCGSRCPLRMHVVDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  77 TVYWVESDTTGDDVY-GNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGN 155
Cdd:PRK14990   81 EIKYVETDNTGDDNYdGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 156 EAVHVLYGTGVDGGNITNSNVP-----YRLMNSCGGFLSRYGSYSTAQISAAMSYMFGA-NDGNSPDDIANTKLVVMFGN 229
Cdd:PRK14990  161 ESIYLNYGTGTLGGTMTRSWPPgntlvARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGwADGNSPSDIENSKLVVLFGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 230 NPAETRMSGGGVTYYVEQARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCV 309
Cdd:PRK14990  241 NPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 310 GYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRA 389
Cdd:PRK14990  321 GYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 390 IAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWC 469
Cdd:PRK14990  401 ISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 470 YASNTLINQHGDINHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAK 549
Cdd:PRK14990  481 YAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPR 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 550 FERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDP 629
Cdd:PRK14990  561 FECKTIYEMTSELAKRLG--VEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDP 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 630 QANPLKTPSGKIEIYSERLATIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQ 709
Cdd:PRK14990  639 QANPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKA 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 710 ACPQEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPS 789
Cdd:PRK14990  719 ACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD--AKRVDKGGCINVLTTQRPS 796
                         810
                  ....*....|....*...
gi 1434010499 790 PLAKGNPSHSNLVQIEKV 807
Cdd:PRK14990  797 PLAKGNPSHTNLVQVEKV 814
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
56-675 0e+00

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: 947.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  56 WSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISW 135
Cdd:cd02770     1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 136 DEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGAND-GNS 214
Cdd:cd02770    81 DEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAAsGSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 215 PDDIANTKLVVMFGNNPAETRMSGGGVTYYVEQAReRSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLI 294
Cdd:cd02770   161 LDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAK-KAGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAAMAYVMI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 295 TENMVDQPFLDKYCVGYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQG 374
Cdd:cd02770   240 TENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGYDGTPKTPEWASEITGVPAETIRRLAREIATTKPAAILQG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 375 WGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGV 454
Cdd:cd02770   320 WGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTADDGGV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 455 RGKEKLDVPIKFLWCYASNTLINQHGDINHTHEVL-QDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESA 533
Cdd:cd02770   400 KGADKLKSNIKMIWNYAGNTLINQHSDDNNTTRALlDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNA 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 534 GNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKK 613
Cdd:cd02770   480 GMMEYLIYSQKAIEPLYECKSDYEICAELAKRLG--VEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGIYRVP 557
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1434010499 614 cPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLATIADTweLKKDEIIHPLPAYTPGFDG 675
Cdd:cd02770   558 -RALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT--LPEGDEIPAIPKYVPAWEG 616
MopB_DMSOR-like cd02751
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
56-675 0e+00

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: 700.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  56 WSSCTvncgsRCLLRLHVKDDTVYWVESDTTgddvygnHQVRACLRGRSIRRRMNHPDRLKYPMKRVGK----------R 125
Cdd:cd02751     1 PTACH-----WGPFKAHVKDGVIVRVEPDDT-------DQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 126 GEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPY-RLMNSCGGFLSRYGSYSTAQISAAMS 204
Cdd:cd02751    69 GEGEFVRISWDEALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLhRFLNLIGGYLGSYGTYSTGAAQVILP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 205 YMFGA----NDGNSPDDIA-NTKLVVMFGNNPAETRMSGGGV-----TYYVEQARERsNARMIVIDPRYNDTAAGREDEW 274
Cdd:cd02751   149 HVVGSdevyEQGTSWDDIAeHSDLVVLFGANPLKTRQGGGGGpdhgsYYYLKQAKDA-GVRFICIDPRYTDTAAVLAAEW 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 275 LPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktlpanaprnahYKAYILGEgPDGIAKTPEWAAKITSIPAE 354
Cdd:cd02751   228 IPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDE------------FKDYLLGE-SDGVPKTPEWAAEITGVPAE 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 355 KIIHLAREIGSaKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEW--------FPMLEN 426
Cdd:cd02751   295 TIRALAREIAS-KRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPrggaggpgLPQGKN 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 427 PVKTQISVFTWTDAIDH-GTEMTAtrdgvRGKEKLDVPIKFLWCYASNTLINQHgDINHTHEVLQDDskcEMIVGIDHFM 505
Cdd:cd02751   374 PVKDSIPVARIADALLNpGKEFTA-----NGKLKTYPDIKMIYWAGGNPLHHHQ-DLNRLIKALRKD---ETIVVHDIFW 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 506 TASAKYCDILLPDLMPTEQEDLIShESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIK 585
Cdd:cd02751   445 TASARYADIVLPATTSLERNDIGL-TGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLG--VEEEFTEGRDEMEWLE 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 586 YLHAKTKERN----PEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLATIADTwelkkDe 661
Cdd:cd02751   522 HLYEETRAKAagpgPELPSFEEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYD-----D- 595
                         650
                  ....*....|....
gi 1434010499 662 iIHPLPAYTPGFDG 675
Cdd:cd02751   596 -CPGHPTWIEPWEG 608
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
45-807 0e+00

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 682.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  45 AAEVPVEEKAVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGK 124
Cdd:COG0243    14 AALEAAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVR----GDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 125 RGEGKFERISWDEALDTISDNLRRILKDYGNEAVhVLYGTGVDGGNITNSNVPY--RLMNSCG--GFLSRyGSYSTAQIS 200
Cdd:COG0243    89 RGSGKFERISWDEALDLIAEKLKAIIDEYGPEAV-AFYTSGGSAGRLSNEAAYLaqRFARALGtnNLDDN-SRLCHESAV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 201 AAMSYMFGANDG-NSPDDIANTKLVVMFGNNPAETrmsGGGVTYYVEQARERSNARMIVIDPRYNDTAAgREDEWLPIRP 279
Cdd:COG0243   167 AGLPRTFGSDKGtVSYEDLEHADLIVLWGSNPAEN---HPRLLRRLREAAKKRGAKIVVIDPRRTETAA-IADEWLPIRP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 280 GTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktlpanaprnahYKAYIlgegpdgIAKTPEWAAKITSIPAEKIIHL 359
Cdd:COG0243   243 GTDAALLLALAHVLIEEGLYDRDFLARHTVGFDE------------LAAYV-------AAYTPEWAAEITGVPAEDIREL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 360 AREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGswdlgvewfpmlenpvktqisvftwtD 439
Cdd:COG0243   304 AREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG--------------------------E 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 440 AIdhgtemtatrdgvrgKEKLDVPIKFLWCYASNtLINQHGDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDILLPDL 519
Cdd:COG0243   358 AI---------------LDGKPYPIKALWVYGGN-PAVSAPDTNRVREALR---KLDFVVVIDTFLTETARYADIVLPAT 418
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 520 MPTEQEDLIsheSAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDvyQTFTEGRSQHEWIKYLHAKTKERNpemP 599
Cdd:COG0243   419 TWLERDDIV---TNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFE--EAFPWGRTEEDYLRELLEATRGRG---I 490
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 600 DYEEMKTTGIFKKKCPEEHyvafrAFREDpqaNPLKTPSGKIEIYSERLAtiadtwelkkdeiIHPLPAYTPGFDgWDDP 679
Cdd:COG0243   491 TFEELREKGPVQLPVPPEP-----AFRND---GPFPTPSGKAEFYSETLA-------------LPPLPRYAPPYE-GAEP 548
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 680 LRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTA 758
Cdd:COG0243   549 LDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPvVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVF 628
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*....
gi 1434010499 759 IGQGAWlkadmFGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV 807
Cdd:COG0243   629 APHGWW-----YEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
MopB_DMSOR-BSOR-TMAOR cd02769
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
102-649 1.73e-119

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: 373.52  E-value: 1.73e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 102 GRSIRRRMNHPDRLKYPMKRVG-----------KRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHV-LYGTGvDGG 169
Cdd:cd02769    34 LDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIFGgSYGWS-SAG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 170 NITNSNVP-YRLMNSCGGFLSRYGSYSTAQISAAMSYMFGAND-----GNSPDDIA-NTKLVVMFGNNPAETRMSGGGVT 242
Cdd:cd02769   113 RFHHAQSLlHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEvyteqQTSWPVIAeHTELVVAFGADPLKNAQIAWGGI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 243 ------YYVEQARERsNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktl 316
Cdd:cd02769   193 pdhqaySYLKALKDR-GIRFISISPLRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDK--- 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 317 panaprnahYKAYILGEGpDGIAKTPEWAAKITSIPAEKIIHLAREIgSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVL 396
Cdd:cd02769   269 ---------FLPYLLGES-DGVPKTPEWAAAICGIPAETIRELARRF-ASKRTMIMAGWSLQRAHHGEQPHWMAVTLAAM 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 397 TGNVGINGG--------NSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDH-GTEMtaTRDGvrgkEKLDVP-IKF 466
Cdd:cd02769   338 LGQIGLPGGgfgfgyhySNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLNpGKPF--DYNG----KKLTYPdIKL 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 467 LWcYASNTLINQHGDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLishESAGNMGYVILAQPAT 546
Cdd:cd02769   412 VY-WAGGNPFHHHQDLNRLIRAWQ---KPETVIVHEPFWTATARHADIVLPATTSLERNDI---GGSGDNRYIVAMKQVV 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 547 SAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLH----AKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAF 622
Cdd:cd02769   485 EPVGEARDDYDIFADLAERLG--VEEQFTEGRDEMEWLRHLYeesrAQAAARGVEMPSFDEFWAQGYVELPIPEADFVRL 562
                         570       580
                  ....*....|....*....|....*..
gi 1434010499 623 RAFREDPQANPLKTPSGKIEIYSERLA 649
Cdd:cd02769   563 ADFREDPEANPLGTPSGRIEIFSETIA 589
MopB_3 cd02766
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ...
57-649 1.05e-109

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: 344.62  E-value: 1.05e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  57 SSCTVNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGeGKFERISWD 136
Cdd:cd02766     2 SVCPLDCPDTCSLLVTVEDGRIVRVE----GDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKG-GQWERISWD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 137 EALDTISDNLRRILKDYGNEAVHVLYGTGVDGgnITNSNVPYRLMNScGGFLSRYGSYSTAQISAAMSYMFGANDGNSPD 216
Cdd:cd02766    77 EALDTIAAKLKEIKAEYGPESILPYSYAGTMG--LLQRAARGRFFHA-LGASELRGTICSGAGIEAQKYDFGASLGNDPE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 217 DIANTKLVVMFGNNPAETRMSGggvTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVLITE 296
Cdd:cd02766   154 DMVNADLIVIWGINPAATNIHL---MRIIQEARKR-GAKVVVIDPYRTATAA-RADLHIQIRPGTDGALALGVAKVLFRE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 297 NMVDQPFLDKYCVGYDEktlpanaprnahYKAYILgegpdgiAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWG 376
Cdd:cd02766   229 GLYDRDFLARHTEGFEE------------LKAHLE-------TYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYG 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 377 PQRHSNGEQTSRAIAMLSVLTGNVGINGGnsGVREGSwdlgvewfpmlenpvktqisvftwtdaidhgtemtatrdgvrg 456
Cdd:cd02766   290 MQRYRNGGQNVRAIDALPALTGNIGVPGG--GAFYSN------------------------------------------- 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 457 kekLDVPIKFLWCYASNtLINQHGDINHTHEVLQDDskCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLIshesaGNM 536
Cdd:cd02766   325 ---SGPPVKALWVYNSN-PVAQAPDSNKVRKGLARE--DLFVVVHDQFMTDTARYADIVLPATTFLEHEDVY-----ASY 393
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 537 G--YVILAQPATSAKFERKPIYWMLSEVAKRLGpdvyqtFTEG---RSQHEWIKylhaktKERNPEMPdyeemKTTGIfk 611
Cdd:cd02766   394 WhyYLQYNEPAIPPPGEARSNTEIFRELAKRLG------FGEPpfeESDEEWLD------QALDGTGL-----PLEGI-- 454
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1434010499 612 kKCPEEHYVAFRAFREDPQANP-LKTPSGKIEIYSERLA 649
Cdd:cd02766   455 -DLERLLGPRKAGFPLVAWEDRgFPTPSGKFEFYSERAA 492
Molybdopterin-Binding cd00368
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
56-566 1.43e-103

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: 323.90  E-value: 1.43e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  56 WSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGegKFERISW 135
Cdd:cd00368     1 PSVCPF-CGVGCGILVYVKDGKVVRIE----GDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRG--KFVPISW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 136 DEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGniTNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGANDGNSP 215
Cdd:cd00368    74 DEALDEIAEKLKEIREKYGPDAIAFYGGGGASNE--EAYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 216 DDIANTKLVVMFGNNPAETRMSgggVTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAiawvlit 295
Cdd:cd00368   152 ADIENADLILLWGSNPAETHPV---LAARLRRAKKR-GAKLIVIDPRRTETAA-KADEWLPIRPGTDAALALA------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 296 enmvdqpfldkycvgydektlpanaprnahykayilgegpdgiaktpEWAAKITSIPAEKIIHLAREIGSAKPAYICQGW 375
Cdd:cd00368   220 -----------------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGM 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 376 GPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVRegswdlgvewfpmlENPVKTQisvftwtdaidhgtemtatrdgvr 455
Cdd:cd00368   253 GLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGPG--------------GNPLVSA------------------------ 294
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 456 gkekldvpikflwcyasntlinqhgdiNHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHesagN 535
Cdd:cd00368   295 ---------------------------PDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTN----T 343
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1434010499 536 MGYVILAQPATSAKFERKPIYWMLSEVAKRL 566
Cdd:cd00368   344 EGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
PRK15102 PRK15102
trimethylamine-N-oxide reductase TorA;
14-806 1.83e-103

trimethylamine-N-oxide reductase TorA;


Pssm-ID: 237909 [Multi-domain]  Cd Length: 825  Bit Score: 337.80  E-value: 1.83e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  14 ISRRSLMK-TSALGSLALASSAFTLPFSQMVRAAEVPvEEKAVWSSCTVNCGSrclLRLHVKDDTvyWVESDTTGDDVYG 92
Cdd:PRK15102    1 ASRRRFLKgLGGLSAAGMLGPSLLTPRSALAAQAAAA-ETTKEWILTGSHWGA---FRAKVKNGR--FVEAKPFELDKYP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  93 NHQVRAclrgrsIRRRMNHPDRLKYPMKRV-----------GKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHvl 161
Cdd:PRK15102   75 TKMING------IKGHVYNPSRIRYPMVRLdwlrkrhksdtSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALH-- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 162 ygTGVDGGNITNSnvpyrlMNSCGG-----------FLSRYGSYSTAQISAAMSYMFGAND----GNS-PDDIANTKLVV 225
Cdd:PRK15102  147 --TGQTGWQSTGQ------FHSATGhmqraigmhgnSVGTVGDYSTGAGQVILPYVLGSTEvyeqGTSwPLILENSKTIV 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 226 MFGNNP---------AETRMSGGgvtyYVEQARER---SNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVL 293
Cdd:PRK15102  219 LWGSDPvknlqvgwnCETHESYA----YLAQLKEKvakGEINVISIDPVVTKTQNYLGCEHLYVNPQTDVPLMLALAHTL 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 294 ITENMVDQPFLDKYCVGYDEkTLPanaprnahykaYILGEgPDGIAKTPEWAAKITSIPAEKIIHLAREIgSAKPAYICQ 373
Cdd:PRK15102  295 YSENLYDKKFIDNYCLGFEQ-FLP-----------YLLGE-KDGVPKTPEWAEKICGIDAETIRELARQM-AKGRTQIIA 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 374 GWGPQRHSNGEQTSRAIAMLSVLTGNVGINGG--------NS-GVRE----------GSWDLGVEwfPMLENP----VKT 430
Cdd:PRK15102  361 GWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGgisyghhySGiGVPSsggaipggfpGNLDTGQK--PKHDNSdykgYSS 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 431 QISVFTWTDAIDH-GTEMTATrdgvrGKEKLDVPIKFLwCYASNTLINQHGDINHTHEVLQddsKCEMIVGIDHFMTASA 509
Cdd:PRK15102  439 TIPVARFIDAILEpGKTINWN-----GKKVTLPPLKMM-IFSGTNPWHRHQDRNRMKEAFR---KLETVVAIDNQWTATC 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 510 KYCDILLPDLMPTEQEDLISHESAGNMGyVILAQPATSAKFERKPIYWMLSEVAKRLGPDvyQTFTEGRSQHEWIKYLHA 589
Cdd:PRK15102  510 RFADIVLPACTQFERNDIDQYGSYSNRG-IIAMKKVVEPLFESRSDFDIFRELCRRFGRE--KEYTRGMDEMGWLKRLYQ 586
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 590 KTKERNP---EMPDYEEMKTTGI--FKKKCPeehYVAFRAFREDPQANPLKTPSGKIEIYSErlaTIAD----------T 654
Cdd:PRK15102  587 ECKQQNKgkfHMPEFDEFWKKGYveFGEGQP---WVRHADFREDPELNPLGTPSGLIEIYSR---KIADmgyddcqghpM 660
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 655 WeLKKDEIIHPlpayTPGFDgwddplrkTYPLQLTGFHYKARTHSsygnidvlqQACPQE-------------VWINPID 721
Cdd:PRK15102  661 W-FEKIERSHG----GPGSD--------KYPLWLQSVHPDKRLHS---------QLCESEelretytvqgrepVYINPQD 718
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 722 AQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADMFGD--RVDHGGSINILTSHRP-SPLAKGNPSH 798
Cdd:PRK15102  719 AKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEigALCTYGDPNTLTLDIGtSQLAQATSAH 798

                  ....*...
gi 1434010499 799 SNLVQIEK 806
Cdd:PRK15102  799 TCLVEIEK 806
MopB_Acetylene-hydratase cd02759
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ...
58-671 1.36e-99

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: 317.33  E-value: 1.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  58 SCTVnCGSRCLLRLHVKDDTVYWVESDTTGDDVYGnhqvRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDE 137
Cdd:cd02759     3 TCPG-CHSGCGVLVYVKDGKLVKVEGDPNHPTNKG----RLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 138 ALDTISDNLRRILKDYGNEAVHVLYGTGvDGGNITNS---NVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGANDGNS 214
Cdd:cd02759    78 ALDEIAEKLAEIKAEYGPESIATAVGTG-RGTMWQDSlfwIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLGYDEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 215 pdDIANTKLVVMFGNNPAETrmSGGGVTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVLI 294
Cdd:cd02759   157 --DWENPECIVLWGKNPLNS--NLDLQGHWLVAAMKRG-AKLIVVDPRLTWLAA-RADLWLPIRPGTDAALALGMLNVII 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 295 TENMVDQPFLDKYCVGYDEKtlpanAPRNAHYkayilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQG 374
Cdd:cd02759   231 NEGLYDKDFVENWCYGFEEL-----AERVQEY--------------TPEKVAEITGVPAEKIRKAARLYATAKPACIQWG 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 375 WGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSgvregswdlgveWFPMlenpvktqisvftwtdaidhgtemtatrdgv 454
Cdd:cd02759   292 LAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL------------LIPY------------------------------- 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 455 rgkekldvPIKFLWCYASNTLINQHGDINhtheVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAG 534
Cdd:cd02759   329 --------PVKMLIVFGTNPLASYADTAP----VLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAE 396
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 535 NMGYVI--LAQPAtsakFERKPIYWMLSEVAKRLGPDvyqtftegrsQHEWIKYlhaKTKERnpempdyeemkttgifkk 612
Cdd:cd02759   397 NFVQLRqkAVEPY----GEAKSDYEIVLELGKRLGPE----------EAEYYKY---EKGLL------------------ 441
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1434010499 613 kcpeehyvafrafREDPQAnPLKTPSGKIEIYSERLatiadtWELKKDeiihPLPAYTP 671
Cdd:cd02759   442 -------------RPDGQP-GFNTPTGKVELYSTML------EELGYD----PLPYYRE 476
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
63-793 4.08e-93

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 306.43  E-value: 4.08e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  63 CGSRCLLRLHVKDDTVYWVESDTtgddvygNHQV---RACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISWDEAL 139
Cdd:COG3383    14 CGVGCGIDLEVKDGKIVKVEGDP-------DHPVnrgRLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREVSWDEAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 140 DTISDNLRRILKDYGNEAVHVLYgtgvdGGNITNSNvpYRLMNS-CGGFL--------SRYGSYSTAqisAAMSYMFGAn 210
Cdd:COG3383    83 DLVAERLREIQAEHGPDAVAFYG-----SGQLTNEE--NYLLQKlARGVLgtnnidnnARLCMASAV---AGLKQSFGS- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 211 DG--NSPDDIANTKLVVMFGNNPAETrmsgggVTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACA 288
Cdd:COG3383   152 DAppNSYDDIEEADVILVIGSNPAEAhp---vLARRIKKAKKN-GAKLIVVDPRRTETAR-LADLHLQIKPGTDLALLNG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 289 IAWVLITENMVDQPFLDKYCVGYDEktlpanaprnahYKAYILGEgpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKP 368
Cdd:COG3383   227 LLHVIIEEGLVDEDFIAERTEGFEE------------LKASVAKY-------TPERVAEITGVPAEDIREAARLIAEAKR 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 369 AYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGgnSGV---RE-----GSWDLGV--EWFP---MLENP-VKTQISV 434
Cdd:COG3383   288 AMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPG--TGPfplTGqnnvqGGRDMGAlpNVLPgyrDVTDPeHRAKVAD 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 435 FTWTDAIDHGTEMTATR--DGVRGKEkldvpIKFLWCYASNTLInQHGDINHTHEVLqddSKCEMIVGIDHFMTASAKYC 512
Cdd:COG3383   366 AWGVPPLPDKPGLTAVEmfDAIADGE-----IKALWIIGENPAV-SDPDANHVREAL---EKLEFLVVQDIFLTETAEYA 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 513 DILLPDLMPTEQED-LISHEsagnmGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDV-YQT----FTEGRSqhewiky 586
Cdd:COG3383   437 DVVLPAASWAEKDGtFTNTE-----RRVQRVRKAVEPPGEARPDWEIIAELARRLGYGFdYDSpeevFDEIAR------- 504
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 587 lhaktkernpEMPD-----YEEMKTTGIFKKKCP-EEHYVAFRAFREDpqanpLKTPSGKIeiyserlatiadtwelkkd 660
Cdd:COG3383   505 ----------LTPDysgisYERLEALGGVQWPCPsEDHPGTPRLFTGR-----FPTPDGKA------------------- 550
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 661 eIIHPLPAYTPgfdgwDDPLRKTYPLQL-TG---FHYKARTHSsyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRV 735
Cdd:COG3383   551 -RFVPVEYRPP-----AELPDEEYPLVLtTGrllDQWHTGTRT--RRSPRLNKHAPEPfVEIHPEDAARLGIKDGDLVRV 622
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1434010499 736 FNNNGEMLIAAKVTPRILPGVTAIgqgawlkADMFGDrvdhgGSINILTSHRPSPLAK 793
Cdd:COG3383   623 SSRRGEVVLRARVTDRVRPGTVFM-------PFHWGE-----GAANALTNDALDPVSK 668
MopB_4 cd02765
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ...
57-649 7.53e-87

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: 286.30  E-value: 7.53e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  57 SSCTVNCGSRCLLRLHVKDDTVYWVESDttgdDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWD 136
Cdd:cd02765     2 TACPPNCGGRCPLKCHVRDGKIVKVEPN----EWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 137 EALDTISDNLRRILKDYGNEAVHVLYGTGVDGgniTNSNVPYRLMNScGGFLSRYGSYSTAQ---ISAAMSYMFGANdGN 213
Cdd:cd02765    78 EALDTIADKLTEAKREYGGKSILWMSSSGDGA---ILSYLRLALLGG-GLQDALTYGIDTGVgqgFNRVTGGGFMPP-TN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 214 SPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVL 293
Cdd:cd02765   153 EITDWVNAKTIIIWGSNILETQFQD---AEFFLDARENG-AKIVVIDPVYSTTAA-KADQWVPIRPGTDPALALGMINYI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 294 ITENMVDQPFLDKYC-----VGYDEKTL--PANAPRNAHYKAYIL---------------------GEGP---------- 335
Cdd:cd02765   228 LEHNWYDEAFLKSNTsapflVREDNGTLlrQADVTATPAEDGYVVwdtnsdspepvaatninpaleGEYTingvkvhtvl 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 336 ----DGIAK-TPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVr 410
Cdd:cd02765   308 talrEQAASyPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ- 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 411 egswdlgvewfpmlenpvktqisvftwtdaidhgtemtatrdgvrgkekldvpIKFLWCYASNtLINQHGDINHTHEVLq 490
Cdd:cd02765   387 -----------------------------------------------------IKFMYFMGSN-FLGNQPDRDRWLKVM- 411
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 491 ddSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNmgYVILAQPATSAKFERKPIYWMLSEVAKRLGPDV 570
Cdd:cd02765   412 --KNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP--HVLLQQKAIEPLFESKSDFEIEKGLAERLGLGD 487
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 571 YQTFTEgrsqHEWIKyLHAKTKERNPEMPDYEEMKTTGIFKKK-CPEEHYVAF--RAFredpqanplKTPSGKIEIYSER 647
Cdd:cd02765   488 YFPKTP----EDYVR-AFMNSDDPALDGITWEALKEEGIIMRLaTPEDPYVAYldQKF---------GTPSGKLEFYNEA 553

                  ..
gi 1434010499 648 LA 649
Cdd:cd02765   554 AP 555
MopB_Thiosulfate-R-like cd02755
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ...
55-575 1.52e-81

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: 268.78  E-value: 1.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  55 VWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERIS 134
Cdd:cd02755     1 VPSICEM-CSSRCGILARVEDGRVVKID----GNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREAS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 135 WDEALDTISDNLRRILKDYGNEAVhvLYGTGVDGG--------------NITNSnvpyrlMNSCggFLSRygsystaqiS 200
Cdd:cd02755    76 WDEALQYIASKLKEIKEQHGPESV--LFGGHGGCYspffkhfaaafgspNIFSH------ESTC--LASK---------N 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 201 AAMSYMFGANDGNSPDDIANTKLVVMFGNNPAEtrmsGGGVTYYVEQARERSN-ARMIVIDPRYNDTAAgREDEWLPIRP 279
Cdd:cd02755   137 LAWKLVIDSFGGEVNPDFENARYIILFGRNLAE----AIIVVDARRLMKALENgAKVVVVDPRFSELAS-KADEWIPIKP 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 280 GTDGALACAIAWVLITENMVDQPFLDKYCVGYDEKTlpanaprnAHYKAYilgegpdgiakTPEWAAKITSIPAEKIIHL 359
Cdd:cd02755   212 GTDLAFVLALIHVLISENLYDAAFVEKYTNGFELLK--------AHVKPY-----------TPEWAAQITDIPADTIRRI 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 360 AREIG-SAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGnsgvregswdlgveWFPmlenpvktqisvftwt 438
Cdd:cd02755   273 AREFAaAAPHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRGG--------------LYY---------------- 322
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 439 daidhgtemtatrdgvrGKEKLDVPIKFLWCYASNTLINQHgDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDILLPD 518
Cdd:cd02755   323 -----------------AGSAKPYPIKALFIYRTNPFHSMP-DRARLIKALK---NLDLVVAIDILPSDTALYADVILPE 381
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1434010499 519 LMPTEQEDLISHESAGNMGYVIlAQPATSAKFERKPIYWMLSEVAKRLGPdvYQTFT 575
Cdd:cd02755   382 ATYLERDEPFSDKGGPAPAVAT-RQRAIEPLYDTRPGWDILKELARRLGL--FGTPS 435
PRK15488 PRK15488
thiosulfate reductase PhsA; Provisional
13-807 1.25e-79

thiosulfate reductase PhsA; Provisional


Pssm-ID: 237973 [Multi-domain]  Cd Length: 759  Bit Score: 271.93  E-value: 1.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  13 EISRRSLMKTSALGSLALASSAFtLPFS-QMVRAAEVPVEEKAVWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttgddvy 91
Cdd:PRK15488    2 SLSRRDFLKGAGAGCAACALGSL-LPGAlAANEIAQLKGKTKLTPSICEM-CSTRCPIEARVVNGKNVFIQ--------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  92 GNHQV-----RACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGV 166
Cdd:PRK15488   71 GNPKAksfgtKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSGS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 167 DGGNITNsnvpyrlmnscggFLSRYGS------YSTAQISAAM--SYMFGandGNSPDDIANTKLVVMFGNNPAE-TRMS 237
Cdd:PRK15488  151 LSSHLFH-------------LATAFGSpntfthASTCPAGYAIaaKVMFG---GKLKRDLANSKYIINFGHNLYEgINMS 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 238 gggVTYYVEQARERSNARMIVIDPRYNdTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktLP 317
Cdd:PRK15488  215 ---DTRGLMTAQMEKGAKLVVFEPRFS-VVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEE--LA 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 318 ANAprnahyKAYilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQgWGPQRHSNGE--QTSRAIAMLSV 395
Cdd:PRK15488  289 ASV------KEY-----------TPEWAEAISDVPADDIRRIARELAAAAPHAIVD-FGHRATFTPEefDMRRAIFAANV 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 396 LTGNVGINGGNSGVREGSWD---LGVEWFPMLENPVKTQISVFTWT--DAIDHGTEMTATRDGVRGK------EKLDVPI 464
Cdd:PRK15488  351 LLGNIERKGGLYFGKNASVYnklAGEKVAPTLAKPGVKGMPKPTAKriDLVGEQFKYIAAGGGVVQSiidatlTQKPYQI 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 465 KFLWCYASNTLINQhgdiNHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVIlAQP 544
Cdd:PRK15488  431 KGWVMSRHNPMQTV----TDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYAL-RQR 505
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 545 ATSAKFERKPIYWMLSEVAKRLGPDVYQTFtegrsqhEWIKYLHAKTKERNPEMpdYEEMKTTGIFKKKCP----EEHYV 620
Cdd:PRK15488  506 VVEPIGDTKPSWQIFKELGEKMGLGQYYPW-------QDMETLQLYQVNGDHAL--LKELKKKGYVSFGVPlllrEPKMV 576
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 621 AfrAFRED-PQANP------------LKTPSGKIEIYSERLATIAdtwelkkdeiihplPAY-TPGFDgwDDPLRKTYPL 686
Cdd:PRK15488  577 A--KFVARyPNAKAvdedgtygsqlkFKTPSGKIELFSAKLEALA--------------PGYgVPRYR--DVALKKEDEL 638
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 687 QLTGFHYKARTHSSYGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWL 765
Cdd:PRK15488  639 YFIQGKVAVHTNGATQNVPLLANLMSDNaVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLFAYMGFGS 718
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 1434010499 766 KADMFGDRVDHGGSINILTSHRPSPLAkGNPSHSNLVQIEKV 807
Cdd:PRK15488  719 KNKELTRATGKGIHCGNLLPHVTSPVS-GTNVHTTGVTLSKA 759
MopB_Nitrate-R-NarG-like cd02750
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ...
53-583 3.18e-79

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: 262.64  E-value: 3.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  53 KAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDT----TGDDvYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEG 128
Cdd:cd02750     2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATdypeTPPD-LPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 129 KFERISWDEALDTISDNLRRILKDYGNEAV----------HVLYGTGvdggnitnsnvpYRLMNSCGG----FLSRYGSY 194
Cdd:cd02750    81 KWKRISWDEALELIADAIIDTIKKYGPDRVigfspipamsMVSYAAG------------SRFASLIGGvslsFYDWYGDL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 195 STAQisaamSYMFG-ANDGNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSnARMIVIDPRYNDTAAgREDE 273
Cdd:cd02750   149 PPGS-----PQTWGeQTDVPESADWYNADYIIMWGSNVPVTRTPD---AHFLTEARYNG-AKVVVVSPDYSPSAK-HADL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 274 WLPIRPGTDGALACAIAWVLITENMVDQPFLDKYcvgydeKTLPanaprnahYKAYilgegpdgiakTPEWAAKITSIPA 353
Cdd:cd02750   219 WVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEY------TDLP--------FLVY-----------TPAWQEAITGVPR 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 354 EKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGswdlgvewfpmlenpvktQIS 433
Cdd:cd02750   274 ETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG------------------QPR 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 434 VFtwtdaidhgtemtatrdgvrgkekldvpikFLWcyaSNTLINQHgdiNHTHEVLQD--DSKCEMIVGIDHFMTASAKY 511
Cdd:cd02750   336 VL------------------------------FVW---RGNLFGSS---GKGHEYFEDapEGKLDLIVDLDFRMDSTALY 379
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434010499 512 CDILLPDLMPTEQEDLISheSAGNMgYVILAQPATSAKFERKPIYWMLSEVAKRLgpdVYQTFTeGRSQ----HEW 583
Cdd:cd02750   380 SDIVLPAATWYEKHDLST--TDMHP-FIHPFSPAVDPLWEAKSDWEIFKALAKKV---PWRTLT-GRQQfyldHDW 448
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
114-565 2.86e-68

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 229.98  E-value: 2.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 114 RLKYPMKRvgkRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGvdGGNITNSNVPY-----RLMNSCGGFL 188
Cdd:pfam00384   1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSG--GLTDVESLYALkkllnRLGSKNGNTE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 189 SRYGSYSTAQiSAAMSYMFGAN--DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYyveQARERSNARMIVIDPRYNdt 266
Cdd:pfam00384  76 DHNGDLCTAA-AAAFGSDLRSNylFNSSIADIENADLILLIGTNPREEAPILNARIR---KAALKGKAKVIVIGPRLD-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 267 aAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKycvgydektlpanaprnahykayilgegpdgiaktpewaa 346
Cdd:pfam00384 150 -LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK---------------------------------------- 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 347 kitsipaekiihlareigsakpAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNsgvregswdlgveWFPMLEN 426
Cdd:pfam00384 189 ----------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG-------------WNGLNIL 233
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 427 PvktqisvftwTDAIDHGTEMTATRDGVRGKEKLDVP----IKFLWcYASNTLINQHGDINHTHEVLQddsKCEMIVGID 502
Cdd:pfam00384 234 Q----------GAASPVGALDLGLVPGIKSVEMINAIkkggIKVLY-LLGNNPFVTHADENRVVKALQ---KLDLFVVYD 299
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434010499 503 HFM-TASAKYCDILLPDLMPTEQEDLIShesagNM-GYVILAQPATSAKFERKPIYWMLSEVAKR 565
Cdd:pfam00384 300 GHHgDKTAKYADVILPAAAYTEKNGTYV-----NTeGRVQSTKQAVPPPGEAREDWKILRALSEV 359
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
63-640 5.42e-67

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: 232.50  E-value: 5.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  63 CGSRCLLRLHVKDDTVYWVesdtTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRvgkRGEGKFERISWDEALDTI 142
Cdd:cd02754     7 CGVGCGVEIGVKDGKVVAV----RGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR---RNGGELVPVSWDEALDLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 143 SDNLRRILKDYGNEAVHVlYGTGvdggNITNSNvpYRLMNSC--GGFLSRYGSYSTAQI--SAAMSYM--FGAnDG--NS 214
Cdd:cd02754    80 AERFKAIQAEYGPDSVAF-YGSG----QLLTEE--YYAANKLakGGLGTNNIDTNSRLCmaSAVAGYKrsFGA-DGppGS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 215 PDDIANTKLVVMFGNNPAETR---MSgggvtyYVEQARE-RSNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIA 290
Cdd:cd02754   152 YDDIEHADCFFLIGSNMAECHpilFR------RLLDRKKaNPGAKIIVVDPRRTRTAD-IADLHLPIRPGTDLALLNGLL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 291 WVLITENMVDQPFLDKYCVGYDEKTlpanaprnAHYKAYilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKPAY 370
Cdd:cd02754   225 HVLIEEGLIDRDFIDAHTEGFEELK--------AFVADY-----------TPEKVAEITGVPEADIREAARLFGEARKVM 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 371 ICQGWGPQRHSNGEQTSRAIAMLSVLTGNVG--------ING-GNS-GVREGSWD---LGvewFPM-LENPVKTQISVFT 436
Cdd:cd02754   286 SLWTMGVNQSTQGTAANNAIINLHLATGKIGrpgsgpfsLTGqPNAmGGREVGGLanlLP---GHRsVNNPEHRAEVAKF 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 437 WtdAIDHGTEMTAT-RDGVRGKEKL-DVPIKFLWCYASN---TLINQhgdiNHTHEVLQddsKCEMIVGIDHF-MTASAK 510
Cdd:cd02754   363 W--GVPEGTIPPKPgLHAVEMFEAIeDGEIKALWVMCTNpavSLPNA----NRVREALE---RLEFVVVQDAFaDTETAE 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 511 YCDILLPDLMPTEQEdlishesaGNMG----YVILAQPATSAKFERKPIYWMLSEVAKRLGPDVYQTFTegrSQHEWIKY 586
Cdd:cd02754   434 YADLVLPAASWGEKE--------GTMTnserRVSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYT---SPEEVFEE 502
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1434010499 587 LHAKTKERNPEMP--DYEEMKTTGIfKKKCPEEHYVAFRAFREDPQANplkTPSGK 640
Cdd:cd02754   503 YRRLSRGRGADLSglSYERLRDGGV-QWPCPDGPPEGTRRLFEDGRFP---TPDGR 554
MopB_Arsenate-R cd02757
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ...
54-659 6.20e-67

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: 231.56  E-value: 6.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  54 AVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRG----EGK 129
Cdd:cd02757     1 WVPSTCQ-GCTAWCGLQAYVEDGRVTKVE----GNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKgrdvDPK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 130 FERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPyRLMNSCGGFlsrygSYSTAQISA---AMSYM 206
Cdd:cd02757    76 FVPISWDEALDTIADKIRALRKENEPHKIMLHRGRYGHNNSILYGRFT-KMIGSPNNI-----SHSSVCAESekfGRYYT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 207 FGANDGNSPDdIANTKLVVMFGNNPAETrmsgggvTYYVEQARE-----RSNARMIVIDPRYNDTAAgREDEWLPIRPGT 281
Cdd:cd02757   150 EGGWDYNSYD-YANAKYILFFGADPLES-------NRQNPHAQRiwggkMDQAKVVVVDPRLSNTAA-KADEWLPIKPGE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 282 DGALACAIAWVLITENMVDQPFLDKYCVGYD----EKTLPANAPR-----------NAHYKAYilgegpdgiakTPEWAA 346
Cdd:cd02757   221 DGALALAIAHVILTEGLWDKDFVGDFVDGKNyfkaGETVDEESFKeksteglvkwwNLELKDY-----------TPEWAA 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 347 KITSIPAEKIIHLAREIGSAKPAYICQGW-GPQRHSNGEQTSRAIAMLSVLTGNVGINGG-NSGVREGSWDLGVEWFpml 424
Cdd:cd02757   290 KISGIPAETIERVAREFATAAPAAAAFTWrGATMQNRGSYNSMACHALNGLVGSIDSKGGlCPNMGVPKIKVYFTYL--- 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 425 ENPVKTQISVFTWTDAIDhgtemtatrdgvrgkeklDVPIkflwcyasntlinqhgdinHTHevlqddskcemivgIDHF 504
Cdd:cd02757   367 DNPVFSNPDGMSWEEALA------------------KIPF-------------------HVH--------------LSPF 395
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 505 MTASAKYCDILLPDLMPTEQEDLISHESAGNmGYVILAQPATSAKFERK---PIYWMLsevAKRLGPDvyqtftegrsqh 581
Cdd:cd02757   396 MSETTYFADIVLPDGHHFERWDVMSQENNLH-PWLSIRQPVVKSLGEVReetEILIEL---AKKLDPK------------ 459
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434010499 582 ewikylhaktkernpempDYEEMKTTGIFKKKCPEEHYVAFRAFredpqANPLKTPSGKIEIYSERLATIADTWELKK 659
Cdd:cd02757   460 ------------------GSDGMKRYAPGQFKDPETGKNNRWEF-----ENVFPTETGKFEFYSETLKKYLQNHADKK 514
MopB_Formate-Dh-H cd02753
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
63-567 5.41e-65

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: 225.56  E-value: 5.41e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  63 CGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVgkrgEGKFERISWDEALDTI 142
Cdd:cd02753     7 CGVGCGLELWVKDNKIVGVE----PVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRK----NGKFVEASWDEALSLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 143 SDNLRRILKDYGNEAVHVLygTGVDGGN-------------ITNSNVpyrlmNSCggflSRYGSYSTAqisAAMSYMFGA 209
Cdd:cd02753    79 ASRLKEIKDKYGPDAIAFF--GSAKCTNeenylfqklaravGGTNNV-----DHC----ARLCHSPTV---AGLAETLGS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 210 N-DGNSPDDIANTKLVVMFGNNPAETRMSGGgvtYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACA 288
Cdd:cd02753   145 GaMTNSIADIEEADVILVIGSNTTEAHPVIA---RRIKRAKRNG-AKLIVADPRRTELAR-FADLHLQLRPGTDVALLNA 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 289 IAWVLITENMVDQPFLDKYCVGYDE--KTLPANaprnahykayilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSA 366
Cdd:cd02753   220 MAHVIIEEGLYDEEFIEERTEGFEElkEIVEKY---------------------TPEYAERITGVPAEDIREAARMYATA 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 367 KPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGnsGVregswdlgvewfpmleNPVKTQISVftwTDAIDHGTe 446
Cdd:cd02753   279 KSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGT--GV----------------NPLRGQNNV---QGACDMGA- 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 447 mtatrdgvrgkekldVP------IKFLWCYASNTLINqHGDINHTHEVLqddSKCEMIVGIDHFMTASAKYCDILLP--- 517
Cdd:cd02753   337 ---------------LPnvlpgyVKALYIMGENPALS-DPNTNHVRKAL---ESLEFLVVQDIFLTETAELADVVLPaas 397
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1434010499 518 ------DLMPTEQEdlishesagnmgyVILAQPATSAKFERKPIYWMLSEVAKRLG 567
Cdd:cd02753   398 faekdgTFTNTERR-------------VQRVRKAVEPPGEARPDWEIIQELANRLG 440
MopB_CT_DmsA-EC cd02794
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
684-806 3.01e-63

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: 207.53  E-value: 3.01e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGA 763
Cdd:cd02794     1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1434010499 764 WLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:cd02794    81 WYEPD--ANGIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
MopB_CT_DMSOR-like cd02777
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
684-806 6.97e-53

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: 179.70  E-value: 6.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACP----QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI 759
Cdd:cd02777     1 YPLQLISPHPKRRLHSQLDNVPWLREAYKvkgrEPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1434010499 760 GQGAWLKADmFGDRVDHGGSINILTSHRPSP-LAKGNPSHSNLVQIEK 806
Cdd:cd02777    81 PEGAWYDPD-DNGGLDKGGNPNVLTSDIPTSkLAQGNPANTCLVEIEK 127
MopB_1 cd02762
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
59-527 6.75e-47

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: 175.66  E-value: 6.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  59 CTVNCGsrclLRLHVKDDTVYWVESDTtgDDVYGNHQVraCLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISWDEA 138
Cdd:cd02762     7 CEANCG----LVVTVEDGRVASIRGDP--DDPLSKGYI--CPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDWDEA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 139 LDTISDNLRRILKDYGNEAVHVlYGTGVDG---GNITNSNVPYRLMNScggflSRYGSYSTAQI---SAAMSYMFGANDG 212
Cdd:cd02762    75 FDEIAERLRAIRARHGGDAVGV-YGGNPQAhthAGGAYSPALLKALGT-----SNYFSAATADQkpgHFWSGLMFGHPGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 213 NSPDDIANTKLVVMFGNNPAETR---MSGGGVTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAI 289
Cdd:cd02762   149 HPVPDIDRTDYLLILGANPLQSNgslRTAPDRVLRLKAAKDRG-GSLVVIDPRRTETAK-LADEHLFVRPGTDAWLLAAM 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 290 AWVLITENMVDQPFLDKYCVGYDEkTLPANAPRnahykayilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKPA 369
Cdd:cd02762   227 LAVLLAEGLTDRRFLAEHCDGLDE-VRAALAEF------------------TPEAYAPRCGVPAETIRRLAREFAAAPSA 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 370 YICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGN---------------SGVREGSWDLGVEWFPmlenPVKTQISV 434
Cdd:cd02762   288 AVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAmfttpaldlvgqtsgRTIGRGEWRSRVSGLP----EIAGELPV 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 435 FTWTDAIDhgtemtatRDGvrgkeklDVPIKFLWCYASNTLINQhGDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDI 514
Cdd:cd02762   364 NVLAEEIL--------TDG-------PGRIRAMIVVAGNPVLSA-PDGARLEAALG---GLEFMVSVDVYMTETTRHADY 424
                         490
                  ....*....|...
gi 1434010499 515 LLPDLMPTEQEDL 527
Cdd:cd02762   425 ILPPASQLEKPHA 437
MopB_2 cd02763
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
63-567 1.12e-41

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: 162.69  E-value: 1.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  63 CGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTI 142
Cdd:cd02763     7 CACRCGIRVHLRDGKVRYIK----GNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWEEAFSIA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 143 SDNLRRILKdygNEAVHVLYGTGVDGgnitnsnvpyrlMNSCGGFLSR---------YGSYSTAQISAAMSYMFGAN--D 211
Cdd:cd02763    83 TKRLKAARA---TDPKKFAFFTGRDQ------------MQALTGWFAGqfgtpnyaaHGGFCSVNMAAGGLYSIGGSfwE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 212 GNSPdDIANTKLVVMFG------NNPAETRMsgggvtyyveQARERSNARMIVIDP---RYNDTAagreDEWLPIRPGTD 282
Cdd:cd02763   148 FGGP-DLEHTKYFMMIGvaedhhSNPFKIGI----------QKLKRRGGKFVAVNPvrtGYAAIA----DEWVPIKPGTD 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 283 GALACAIAWVLITENMVDQPFLDKYcvgydektlpANAPRNAHYkayilgegpdgiakTPEWAAKITSIPAEKIIHLARE 362
Cdd:cd02763   213 GAFILALAHELLKAGLIDWEFLKRY----------TNAAELVDY--------------TPEWVEKITGIPADTIRRIAKE 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 363 IGSAK-------PAYICQGWGPQR------------------HSNGEQTSRAIAMLSVLTGNVGINGGN----------- 406
Cdd:cd02763   269 LGVTArdqpielPIAWTDVWGRKHekitgrpvsfhamrgiaaHSNGFQTIRALFVLMMLLGTIDRPGGFrhkppyprhip 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 407 ---------SGVREGS--------WDLGVEWFPMLENPVKTQIS-VFTWTDAID-HGTEMTATRDGVRGKEkldVPIKFL 467
Cdd:cd02763   349 plpkppkipSADKPFTplygpplgWPASPDDLLVDEDGNPLRIDkAYSWEYPLAaHGCMQNVITNAWRGDP---YPIDTL 425
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 468 WCYASNTLINQHGDINHTHEVLQD-----DSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLIS------HESAGNM 536
Cdd:cd02763   426 MIYMANMAWNSSMNTPEVREMLTDkdasgNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSlldrpiSEADGPV 505
                         570       580       590
                  ....*....|....*....|....*....|.
gi 1434010499 537 GYVilAQPATSAKFERKPIYWMLSEVAKRLG 567
Cdd:cd02763   506 DAI--RVPIVEPKGDVKPFQEVLIELGTRLG 534
MopB_Tetrathionate-Ra cd02758
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ...
97-651 1.49e-38

The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239159 [Multi-domain]  Cd Length: 735  Bit Score: 153.65  E-value: 1.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  97 RACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLR-------------RILK--------DYGN 155
Cdd:cd02758    66 TACARGNAGLQYLYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVVEGGDlfgeghveglkaiRDLDtpidpdhpDLGP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 156 EAVHVLYGTGVDGGNITNSNvpyRLMNSCGGFL--SRYGSYSTAQISAAMSYMFGANDGNsPD---DIANTKLVVMFGNN 230
Cdd:cd02758   146 KANQLLYTFGRDEGRTPFIK---RFANQAFGTVnfGGHGSYCGLSYRAGNGALMNDLDGY-PHvkpDFDNAEFALFIGTS 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 231 PAE-----TRMSGggvtyYVEQARERSNARMIVIDPRY--NDTAAGREDEWLPIRPGTDGALACA-IAWvlITENMvdqp 302
Cdd:cd02758   222 PAQagnpfKRQAR-----RLAEARTEGNFKYVVVDPVLpnTTSAAGENIRWVPIKPGGDGALAMAmIRW--IIENE---- 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 303 fldkycvGYDEKTLpANAPRNAHYKA---------------------YILGEgpDGIAKTPEWAAKITSIPAEKIIHLAR 361
Cdd:cd02758   291 -------RYNAEYL-SIPSKEAAKAAgepswtnathlvitvrvksalQLLKE--EAFSYSLEEYAEICGVPEAKIIELAK 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 362 EIGSA--KPAYICQgwGPQRHSNGEQTSRAIAMLSVLTGNV----GINGGNSGVREGSWDLGVEW--FPMLENP------ 427
Cdd:cd02758   361 EFTSHgrAAAVVHH--GGTMHSNGFYNAYAIRMLNALIGNLnwkgGLLMSGGGFADNSAGPRYDFkkFFGEVKPwgvpid 438
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 428 ---------------VKTQISVF----TWTD-AIDHGTEM-TATRDGvrgkekLDVPIKFLWCYASNTLINQHGDINHTH 486
Cdd:cd02758   439 rskkayektseykrkVAAGENPYpakrPWYPlTPELYTEViASAAEG------YPYKLKALILWMANPVYGAPGLVKQVE 512
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 487 EVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEqedliSHESAGNMGYVI-LAQ--------PATSAKFERKPIYW 557
Cdd:cd02758   513 EKLKDPKKLPLFIAIDAFINETSAYADYIVPDTTYYE-----SWGFSTPWGGVPtKAStarwpviaPLTEKTANGHPVSM 587
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 558 --MLSEVAKRLG---------PDVYqtfteGRS---QHEWIKYLH-----AKTKERNPEMPDYEEMKTTG-------IFK 611
Cdd:cd02758   588 esFLIDLAKALGlpgfgpnaiKDGQ-----GNKfplNRAEDYYLRvaaniAYDGKAPVPDASEEELKLTGvnrpipaLKR 662
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 612 KKCPEE-HYVAF------------RAFREDPQANPLKTPsgkIEIYSERLATI 651
Cdd:cd02758   663 TLKPEEwRKVAYilarggrfapyeESYDGDNLRNRWGKT---LQIWNEKLAKS 712
MopB_Formate-Dh-Na-like cd02752
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
59-420 5.82e-38

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: 151.01  E-value: 5.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  59 CTVNCGsrclLRLHVKDDTVYWVESDTTGDDVYGNHqvraCLRGRSIRRRMNHPDRLKYPMKRVGkrGEGKFERISWDEA 138
Cdd:cd02752     7 CSVGCG----LIAYVQNGVWVHQEGDPDHPVNRGSL----CPKGAALRDFVHSPKRLKYPMYRAP--GSGKWEEISWDEA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 139 LDTISDNLRRILKD---YGNEAVHVLYGTgvDG----GNITNSNVPYRLMNSCGGFLSRYGSYSTAQI-------SAAMS 204
Cdd:cd02752    77 LDEIARKMKDIRDAsfvEKNAAGVVVNRP--DSiaflGSAKLSNEECYLIRKFARALGTNNLDHQARIuhsptvaGLANT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 205 YMFGANDgNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSNARMIVIDPRYNDTAAgREDEWLPIRPGTDGA 284
Cdd:cd02752   155 FGRGAMT-NSWNDIKNADVILVMGGNPAEAHPVS---FKWILEAKEKNGAKLIVVDPRFTRTAA-KADLYVPIRSGTDIA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 285 LACAIAWVLItenmvdqpfldKYcvgydektlpanaprnahykayilgegpdgiakTPEWAAKITSIPAEKIIHLAREIG 364
Cdd:cd02752   230 FLGGMINYII-----------RY---------------------------------TPEEVEDICGVPKEDFLKVAEMFA 265
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434010499 365 S----AKPAYI--CQGWgpQRHSNGEQTSRAIAMLSVLTGNVGING-------GNSGVrEGSWDLGVEW 420
Cdd:cd02752   266 AtgrpDKPGTIlyAMGW--TQHTVGSQNIRAMCILQLLLGNIGVAGggvnalrGHSNV-QGATDLGLLS 331
PRK14991 PRK14991
tetrathionate reductase subunit TtrA;
98-762 1.43e-30

tetrathionate reductase subunit TtrA;


Pssm-ID: 237883 [Multi-domain]  Cd Length: 1031  Bit Score: 129.73  E-value: 1.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499   98 ACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTIS-----------DNLRRI--LK--------DYGNE 156
Cdd:PRK14991   141 ACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVVeggdlfgeghvDGLRAIrdLDtpidaknpEYGPK 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  157 AVHVLYGTGVDGGNitnSNVPYRLMNSCGGFL--SRYGSYSTAQISAAMSYMFGANDGNS---PDdIANTKLVVMFGNNP 231
Cdd:PRK14991   221 ANQLLVTNASDEGR---DAFIKRFAFNSFGTRnfGNHGSYCGLAYRAGSGALMGDLDKNPhvkPD-WDNVEFALFIGTSP 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  232 AEtrmSGGGvtyYVEQARERSNARM------IVIDPR---YNDTAAGREDEWLPIRPGTDGALACA-IAWvlITEN---- 297
Cdd:PRK14991   297 AQ---SGNP---FKRQARQLANARTrgnfeyVVVAPAlplSSSLAAGDNNRWLPIRPGTDSALAMGmIRW--IIDNqryn 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  298 --------------------------MVDQP-------FL------------------DKYCV-GYDEKTLPANAPRNAH 325
Cdd:PRK14991   369 adylaqpgvaamqaageaswtnathlVIADPghprygqFLrasdlglpfegeargdgeDTLVVdAADGELVPATQAQPAR 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  326 --YKAYILGEGPDGIA--------------KTPEWAAKITSIPAEKIIHLAREIGS--AKPAYICQGwGpQRHSNGEQTS 387
Cdd:PRK14991   449 lfVEQYVTLADGQRVRvksslqllkeaarkLSLAEYSEQCGVPEAQIIALAEEFTShgRKAAVISHG-G-TMSGNGFYNA 526
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  388 RAIAMLSVLTGNVGINGG---NSG-------------------VREGSWDLGVEWFPML------------ENPVKTQIS 433
Cdd:PRK14991   527 WAIMMLNALIGNLNLKGGvvvGGGkfpgfgdgprynlasfagkVKPKGVSLSRSKFPYEksseyrrkveagQSPYPAKAP 606
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  434 VFTWTDAIdhGTEM-TATRDGvrgkekLDVPIKFLWCYASNTLINQHGDINHTHEVLQDDSKCEMIVGIDHFMTASAKYC 512
Cdd:PRK14991   607 WYPFVAGL--LTEMlTAALEG------YPYPLKAWINHMSNPIYGVPGLRAVIEEKLKDPKKLPLFISIDAFINETTALA 678
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  513 DILLPDLMPTEQ-------EDLISHESAGNMGYVilaQPATSAKFERKPIYW--MLSEVAKRL-----GPDVYQTfTEGR 578
Cdd:PRK14991   679 DYIVPDTHTYESwgftapwGGVPTKASTARWPVV---EPRTAKTADGQPVCMesFLIAVAKRLqlpgfGDNAIKD-AQGN 754
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  579 -----SQHEWikYLHAKT------KERNPEMPDyEEMKTTG-------IFKKKCPEE-HYVAF------------RAFRE 627
Cdd:PRK14991   755 thplnRAEDF--YLRGAAniaylgKTPVADASD-EDIALTGvsrilpaLQATLKPDEvRRVAFiyarggrfapaeSAYDE 831
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  628 DPQANPLKTPsgkIEIYSERLATIADTwelKKDEIIHPLPA-YTPGF-DGwdDPLRKTY-----PLQLTGFhyKARTHSS 700
Cdd:PRK14991   832 ERMGNRWKKP---LQIWNEDVAAARHS---MTGERYSGCPTwYPPRLaDG--TPLREQFpesqwPLLLISF--KSNLMSS 901
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434010499  701 YGN-IDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 762
Cdd:PRK14991   902 MSIaSPRLRQVKPANpVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHG 965
MopB_CT_DMSOR-BSOR-TMAOR cd02793
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
684-806 2.75e-30

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: 115.81  E-value: 2.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACPQ---EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIG 760
Cdd:cd02793     1 YPLHLLSNQPATRLHSQLDHGSLSRAYKVQgrePIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1434010499 761 QGAWLkaDMFGDRVDHG----GSINILTSHRP-SPLAKGNPSHSNLVQIEK 806
Cdd:cd02793    81 TGAWY--DPDDPGEPGPlckhGNPNVLTLDIGtSSLAQGCSAQTCLVQIEK 129
Molydop_binding pfam01568
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ...
686-801 3.32e-29

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: 111.98  E-value: 3.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 686 LQLTGFHYKARTHSSYGNIDVLQQACPQE--VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGA 763
Cdd:pfam01568   1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPevVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1434010499 764 WlkadmfgdRVDHGGSINILTSHRPSPLAKGNPSHSNL 801
Cdd:pfam01568  81 W--------YEPRGGNANALTDDATDPLSGGPEFKTCA 110
MopB_Phenylacetyl-CoA-OR cd02760
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ...
57-567 1.81e-27

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: 119.30  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  57 SSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNhQVRACLRGRSIRRRMNHPDRLKYPMKRVG-KRGEGK---FER 132
Cdd:cd02760     2 TYCYNCVAGPDFMAVKVVDGVATEIEPNFAAEDIHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRTNpKKGRNEdpgFVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 133 ISWDEALDTISDNLRRIL-KDYGNEAVHVLYGTGVDGGNItnsnvPYRLMNSCGGFLSRYG----SYSTAQI--SAAMSY 205
Cdd:cd02760    81 ISWDEALDLVAAKLRRVReKGLLDEKGLPRLAATFGHGGT-----PAMYMGTFPAFLAAWGpidfSFGSGQGvkCVHSEH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 206 MFGANDGNSPDDIANTKL---VVMFGNNpaeTRMSGG--GVTYYVEqARERSnARMIVIDPRYNDTAAgREDEWLPIRPG 280
Cdd:cd02760   156 LYGEFWHRAFTVAADTPLanyVISFGSN---VEASGGpcAVTRHAD-ARVRG-YKRVQVEPHLSVTGA-CSAEWVPIRPK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 281 TDGALACAIAWVLITE---NMVDQPFL-DK----YCVG----------------YDEKT-----------LPANAPRNAH 325
Cdd:cd02760   230 TDPAFMFAMIHVMVHEqglGKLDVPFLrDRtsspYLVGpdglylrdaatgkplvWDERSgravpfdtrgaVPAVAGDFAV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 326 YKAY-ILGEGP-----------------DGIAK-TPEWAAKITSIPAEKIIHLARE------IGSA----------KPAY 370
Cdd:cd02760   310 DGAVsVDADDEtaihqgvegttaftmlvEHMRKyTPEWAESICDVPAATIRRIAREflenasIGSTievdgvtlpyRPVA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 371 ICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSG---------------VREGSWDLGVEWF-----------PML 424
Cdd:cd02760   390 VTLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTLGttvrlnrphddrlasVKPGEDGFMAQGFnptdkehwvvkPTG 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 425 ENPVKTQISVF---TWTDAIDHGTEMTATRDGVRGKEKLDVPIK--FLWCYASNTLINqhgdINHTHEVLQDDSKCEMIV 499
Cdd:cd02760   470 RNAHRTLVPIVgnsAWSQALGPTQLAWMFLREVPLDWKFELPTLpdVWFNYRTNPAIS----FWDTATLVDNIAKFPFTV 545
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434010499 500 GIDHFMTASAKYCDILLPDLMPTEQEDLISH------ESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLG 567
Cdd:cd02760   546 SFAYTEDETNWMADVLLPEATDLESLQMIKVggtkfvEQFWEHRGVVLRQPAVEPQGEARDFTWISTELAKRTG 619
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
114-577 5.91e-26

The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239168 [Multi-domain]  Cd Length: 574  Bit Score: 113.17  E-value: 5.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 114 RLKYPMKRvgKRGEGKFERISWDEALDTISDNLRRILKD----Y-----GNEAVHVL------YGTgvdggnitnSNVPy 178
Cdd:cd02767    64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALDPDraafYtsgraSNEAAYLYqlfaraYGT---------NNLP- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 179 rlmnSCggflSRYGSYSTaqiSAAMSYMFGANDGN-SPDDIANTKLVVMFGNNPAET--RMsgggvTYYVEQARERSnAR 255
Cdd:cd02767   132 ----DC----SNMCHEPS---SVGLKKSIGVGKGTvSLEDFEHTDLIFFIGQNPGTNhpRM-----LHYLREAKKRG-GK 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 256 MIVIDP-------RYNDTAAGRE---------DEWLPIRPGTDGALACAIAWVLI-----TENMVDQPFLDKYCVGYDEk 314
Cdd:cd02767   195 IIVINPlrepgleRFANPQNPESmltggtkiaDEYFQVRIGGDIALLNGMAKHLIerddePGNVLDHDFIAEHTSGFEE- 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 315 tlpanaprnahYKAYIlgegpdgiaKTPEWA--AKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAM 392
Cdd:cd02767   274 -----------YVAAL---------RALSWDeiERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVN 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 393 LSVLTGNVGING-------GNSGVrEGSWDLGVEWFPMLENpvKTQIS-VFTWTDAIDHG-TEMTATRDGVRGKekldvp 463
Cdd:cd02767   334 LALLRGNIGRPGaglmpirGHSNV-QGDRTMGITEKPFPEF--LDALEeVFGFTPPRDPGlDTVEAIEAALEGK------ 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 464 IKFLWCYASNtLINQHGDINHTHEVLqddSKCEMIVGID------HFMTASakyCDILLPDLMPTEQ------------E 525
Cdd:cd02767   405 VKAFISLGGN-FAEAMPDPAATEEAL---RRLDLTVHVAtklnrsHLVHGE---EALILPCLGRTEIdmqaggaqavtvE 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 526 DLIS--HESAG---NMGYVILAQPATSAK-----FERKPIYW-MLSEVAKRLGPDVYQTFTEG 577
Cdd:cd02767   478 DSMSmtHTSRGrlkPASRVLLSEEAIVAGiagarLGEAKPEWeILVEDYDRIRDEIAAVIYEG 540
MopB_CT cd02775
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ...
693-798 1.68e-23

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: 95.46  E-value: 1.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 693 YKARTHSSY-GNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWlkadmf 770
Cdd:cd02775     1 LRDHFHSGTrTRNPWLRELAPEPvVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWG------ 74
                          90       100
                  ....*....|....*....|....*...
gi 1434010499 771 gDRVDHGGSINILTSHRPSPLAKGNPSH 798
Cdd:cd02775    75 -HRGGRGGNANVLTPDALDPPSGGPAYK 101
MopB_CT_4 cd02785
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ...
684-807 4.69e-23

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: 95.13  E-value: 4.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 762
Cdd:cd02785     2 YPLACIQRHSRFRVHSQFSNVPWLLELQPEpRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1434010499 763 AWlkadmfgDRVDHGGSINILTS----HRPSPLAKGNPSHSN-LVQIEKV 807
Cdd:cd02785    82 WW-------SRYFQEGSLQDLTSpfvnPVHEYIYGPNSAFYDtLVEVRKA 124
MopB_CT_3 cd02786
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
684-804 3.08e-20

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: 86.57  E-value: 3.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACP-QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 762
Cdd:cd02786     1 YPLRLITPPAHNFLNSTFANLPELRAKEGePTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1434010499 763 AWLKAdmFGDrvdhGGSINILTSHRPSPLAKGNPSHSNLVQI 804
Cdd:cd02786    81 WWREH--SPD----GRGVNALTSARLTDLGGGSTFHDTRVEV 116
MopB_CT_Acetylene-hydratase cd02781
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ...
684-806 1.65e-14

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: 70.80  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTgfhYKART----HSSYGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVtA 758
Cdd:cd02781     2 YPLILT---TGARSyyyfHSEHRQLPSLRELHPDpVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGV-V 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 759 IGQGAWLKADMFGDRVDHGG----SINILTSHRPS-PLAKGNPSHSNLVQIEK 806
Cdd:cd02781    78 RAEHGWWYPEREAGEPALGGvwesNANALTSDDWNdPVSGSSPLRSMLCKIYK 130
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
13-360 2.07e-14

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 77.25  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  13 EISRRSLMKTSALGSLAlASSAFTLPfsqmVRAAEVPVEEKAVW----SSCTVnCGSRCLLRLHVKDDTVYWVESDTTGD 88
Cdd:PRK13532    2 KLSRRDFMKANAAAAAA-AAAGLSLP----AVANAVVGSAQTAIkwdkAPCRF-CGTGCGVLVGTKDGRVVATQGDPDAP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  89 DVYG-NhqvraCLRGRSIRRRMNHPDRLKYPMKRVgKRGE----GKFERISWDEALDTISDNLRRILKDYGNEAVHVlYG 163
Cdd:PRK13532   76 VNRGlN-----CIKGYFLSKIMYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGM-FG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 164 TG---VDGGnitnsnvpY---RLMNscGGFLS-------RYgsystAQISAAMSYM--FGANDgnsP----DDIANTKLV 224
Cdd:PRK13532  149 SGqwtIWEG--------YaasKLMK--AGFRSnnidpnaRH-----CMASAVVGFMrtFGIDE---PmgcyDDIEAADAF 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 225 VMFGNNPAE------TRMSGggvtyyveqaRERSN--ARMIVIDP---RYNDTAagreDEWLPIRPGTDGALACAIAWVL 293
Cdd:PRK13532  211 VLWGSNMAEmhpilwSRVTD----------RRLSNpdVKVAVLSTfehRSFELA----DNGIIFTPQTDLAILNYIANYI 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 294 ITENMVDQPFLDKYCV--------GY-----DEKTLPANAPRNA---------HYKAYilgegpdgIAK-TPEWAAKITS 350
Cdd:PRK13532  277 IQNNAVNWDFVNKHTNfrkgatdiGYglrptHPLEKAAKNPGTAgksepisfeEFKKF--------VAPyTLEKTAKMSG 348
                         410
                  ....*....|
gi 1434010499 351 IPAEKIIHLA 360
Cdd:PRK13532  349 VPKEQLEQLA 358
NarG COG5013
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ...
53-308 4.51e-14

Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 444037 [Multi-domain]  Cd Length: 1231  Bit Score: 76.40  E-value: 4.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499   53 KAVWSSCTVNC-GSrCLLRLHVKDDTVYWvESD-----TTGDDvYGNHQVRACLRGRSIRRRMNHPDRLKYPMKR----- 121
Cdd:COG5013     47 KVVRSTHGVNCtGS-CSWKVYVKDGIITW-ETQqtdypRTGPD-LPNYEPRGCPRGASFSWYTYSPTRVKYPYVRgvlle 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  122 -----------------------------VGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVH----------VLY 162
Cdd:COG5013    124 lwreararhgdpveawasivedpekrrryKSARGKGGFVRATWDEANEIIAAANVYTIKKYGPDRVAgfspipamsmVSY 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  163 GTGVdggnitnsnvpyRLMNSCGG-FLSRYGSYstAQISAAMSYMFG-ANDGNSPDDIANTKLVVMFGNNPAETRmsggg 240
Cdd:COG5013    204 AAGA------------RFLSLIGGvMLSFYDWY--ADLPPASPQVWGeQTDVPESADWYNSGYLIMWGSNVPQTR----- 264
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434010499  241 vT----YYVEqARERSnARMIVIDPRYNDtAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQ--PFLDKYC 308
Cdd:COG5013    265 -TpdahFMTE-ARYKG-TKVVVVSPDYAE-NTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDRqvPYFTDYA 334
Molybdop_Fe4S4 pfam04879
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ...
52-111 2.14e-13

Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.


Pssm-ID: 428168 [Multi-domain]  Cd Length: 55  Bit Score: 65.01  E-value: 2.14e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  52 EKAVWSSCTvNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGnhqvRACLRGRSIRRRMNH 111
Cdd:pfam04879   1 MKVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEG----RLCVKGRFGYERVYN 55
MopB_CT_Nitrate-R-NarG-like cd02776
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ...
685-791 2.27e-13

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: 67.79  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 685 PLQLTGFHYKARTHSSYGN---IDVLQQACPqEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI-- 759
Cdd:cd02776     1 PLNYLTPHGKWSIHSTYRDnllMLRLQRGGP-VVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMyh 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1434010499 760 GQGAWLKADMFGDRVDHGGSINILTSHRPSPL 791
Cdd:cd02776    80 AQERHVNVPGSKLTGKRGGIHNSVTRVRIKPT 111
MopB_CT_Fdh-Nap-like cd00508
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ...
682-793 9.82e-13

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: 65.61  E-value: 9.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 682 KTYPLQL-TG-----FHYKARThssyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILP 754
Cdd:cd00508     1 EEYPLVLtTGrllehWHTGTMT----RRSPRLAALAPEPfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRP 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1434010499 755 GVTAIGqgawlkadM-FGDRVDhGGSINILTSHRPSPLAK 793
Cdd:cd00508    77 GTVFMP--------FhWGGEVS-GGAANALTNDALDPVSG 107
MopB_CT_Tetrathionate_Arsenate-R cd02780
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ...
684-795 6.92e-12

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: 63.85  E-value: 6.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI--G 760
Cdd:cd02780     1 YPFILVTFKSNLNSHRS-ANAPWLKEIKPENpVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIehG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1434010499 761 QGAW----LKADMFGDRVDH------GGSINILTSHRPSPLAKGN 795
Cdd:cd02780    80 YGHWaygaVASTIDGKDLPGdawrgaGVNINDIGLVDPSRGGWSL 124
MopB_Arsenite-Ox cd02756
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ...
92-572 9.82e-12

Arsenite oxidase (Arsenite-Ox) 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. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239157 [Multi-domain]  Cd Length: 676  Bit Score: 68.66  E-value: 9.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  92 GNHQVRACLRGRSIRRRMNHP--DRLKYPMKRVGkrgeGKFERISWDEALDTISDNLRRILKDYGNE---AVHVLYGTGV 166
Cdd:cd02756    93 GNYSTRGGTNAERIWSPDNRVgeTRLTTPLVRRG----GQLQPTTWDDAIDLVARVIKGILDKDGNDdavFASRFDHGGG 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 167 DGGNITNSNVpyrlmnscGGFLsrYGSYSTAQIS------------AAMSYMFGAnDGNSPDDIANTKLVVMFGNNPAET 234
Cdd:cd02756   169 GGGFENNWGV--------GKFF--FMALQTPFVRihnrpaynsevhATREMGVGE-LNNSYEDARLADTIVLWGNNPYET 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 235 RmsgggVTYYVE---------------QARERSN----ARMIVIDPRYNDT------AAGREDEW-LPIRPGTDGALACA 288
Cdd:cd02756   238 Q-----TVYFLNhwlpnlrgatvsekqQWFPPGEpvppGRIIVVDPRRTETvhaaeaAAGKDRVLhLQVNPGTDTALANA 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 289 IAWVlITEnmvdqpfldkycvGYDEktlpanaprnahykayILGEgpdgiaktpewAAKITSIPAEKIIHLA-----REI 363
Cdd:cd02756   313 IARY-IYE-------------SLDE----------------VLAE-----------AEQITGVPRAQIEKAAdwiakPKE 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 364 GSAKPAYIC---QG--WGPQRHsngeQTSRAIAMLSVLTGNVGINGGN----SGVREG---SWDLGVEWFPMLENPVKT- 430
Cdd:cd02756   352 GGYRKRVMFeyeKGiiWGNDNY----RPIYSLVNLAIITGNIGRPGTGcvrqGGHQEGyvrPPPPPPPWYPQYQYAPYId 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 431 ------QISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTHEVLQDDSKceMIVGIDHF 504
Cdd:cd02756   428 qllisgKGKVLWVIGCDPYKTTPNAQRLRETINHRSKLVTDAVEAALYAGTYDREAMVCLIGDAIQPGGL--FIVVQDIY 505
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434010499 505 MTASAKYCDILLPDLMPTEQEDLishESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLgPDVYQ 572
Cdd:cd02756   506 PTKLAEDAHVILPAAANGEMNET---SMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRI-YELYQ 569
MopB_CT_Formate-Dh_H cd02790
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
684-757 1.93e-10

Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. 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: 58.79  E-value: 1.93e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434010499 684 YPLQL-TG---FHYKARTHSsyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVT 757
Cdd:cd02790     3 YPLVLtTGrvlYHYHTGTMT--RRAEGLDAIAPEEyVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
MopB_CT_Nitrate-R-NapA-like cd02791
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
683-807 2.32e-10

Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. 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: 58.74  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 683 TYPLQL-TG-----FHYKARThssyGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPG 755
Cdd:cd02791     2 EYPLWLnTGrvrdqWHTMTRT----GRVPRLNAHVPEpYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 756 VtaigqgawLKADMF-GDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV 807
Cdd:cd02791    78 E--------VFVPMHwGDQFGRSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
53-151 1.79e-09

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 60.62  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  53 KAVWSSCTvNCGSRCLLRLHVKDDTVYWVESdttGDDVYGNHqVRACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFER 132
Cdd:COG1034   216 KKTPSICP-HCSVGCNIRVDVRGGKVYRVLP---RENEAVNE-EWLCDKGRFGYDGLNSPDRLTRPLVRKD----GELVE 286
                          90
                  ....*....|....*....
gi 1434010499 133 ISWDEALDTISDNLRRILK 151
Cdd:COG1034   287 ASWEEALAAAAEGLKALKK 305
Molybdop_Fe4S4 smart00926
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ...
52-111 2.38e-09

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: 53.79  E-value: 2.38e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499   52 EKAVWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNH 111
Cdd:smart00926   1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVR----GDPDHPVNRGRLCPKGRAGLEQVYS 55
MopB_CT_1 cd02782
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
717-807 2.58e-09

The MopB_CT_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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239183 [Multi-domain]  Cd Length: 129  Bit Score: 55.86  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 717 INPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADMFGDRVDHGG-SINILTSHRP-SPLAkG 794
Cdd:cd02782    37 IHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYPGVSGAGSRPGvNVNDLTDDTQrDPLS-G 115
                          90
                  ....*....|....
gi 1434010499 795 NPSHSNL-VQIEKV 807
Cdd:cd02782   116 NAAHNGVpVRLARV 129
MopB_CT_Thiosulfate-R-like cd02778
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ...
697-806 3.72e-09

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: 55.36  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 697 THSSYGNIDVLQQACP-QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI--GQGAWLKADMFGDR 773
Cdd:cd02778    13 THGHTANNPLLHELTPeNTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMphGFGHWAPALSRAYG 92
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1434010499 774 vdHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:cd02778    93 --GGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
FwdB COG1029
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
59-289 6.42e-09

Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];


Pssm-ID: 440652 [Multi-domain]  Cd Length: 428  Bit Score: 59.09  E-value: 6.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  59 CTVnCGSRCllrlhvkDDTVYWVEsdttgddvyGNHQV---RACLRGRSIRRRMNHPDRLKYPMKRvgkrgegkFERISW 135
Cdd:COG1029    10 CPF-CGCLC-------DDLEVEVE---------GGKIVvvkNACAIGAAKFERAVSDHRITSPRIR--------GKEVSL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 136 DEALDTISdnlrRILKdygnEAVHVLYGtgvdGGNITNSN---VPYRLMNSCGGFLSrygsySTAQISAAMSYMFGANDG 212
Cdd:COG1029    65 EEAIDKAA----EILA----NAKRPLIY----GLSSTDCEamrAGLALAERVGAVVD-----NTASVCHGPSLLALQDVG 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 213 NSPDDIANTK----LVVMFGNNPAET------RMSGGGVTYYVEQARERSnaRMIVIDPRYNDTAAgREDEWLPIRPGTD 282
Cdd:COG1029   128 WPTCTLGEVKnradVIIYWGCNPVHAhprhmsRYSVFPRGFFTPKGRKDR--TVIVVDPRPTDTAK-VADLHLQVKPGRD 204

                  ....*..
gi 1434010499 283 GALACAI 289
Cdd:COG1029   205 YEVLSAL 211
MopB_PHLH cd02764
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ...
112-554 6.87e-09

The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.


Pssm-ID: 239165 [Multi-domain]  Cd Length: 524  Bit Score: 59.04  E-value: 6.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 112 PDRLKYPMKRVGKRGEGKferISWDEALDTISDNLRRIlKDYGNEAVHvlygTGVDGGNITNSNVpyrlmnscGGFLSRY 191
Cdd:cd02764    97 PDRAQGPLRRGIDGAYVA---SDWADFDAKVAEQLKAV-KDGGKLAVL----SGNVNSPTTEALI--------GDFLKKY 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 192 GSYSTAQISA--------AMSYMFGaNDGNSPDDIANTKLVVMFGNNPAETRMSG-GGVTYYVEQARERSNA---RMIVI 259
Cdd:cd02764   161 PGAKHVVYDPlsaedvneAWQASFG-KDVVPGYDFDKAEVIVSIDADFLGSWISAiRHRHDFAAKRRLGAEEpmsRLVAA 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 260 DPRYNDTAAGrEDEWLPIRPGTDGALACAIAWVLItenmvdqpfldkycvgydEKTLPANAPRNahYKAYILgegpdgiA 339
Cdd:cd02764   240 ESVYTLTGAN-ADVRLAIRPSQEKAFALGLAHKLI------------------KKGAGSSLPDF--FRALNL-------A 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 340 KTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGwgpQRHSNGEQTSRAIAM--LSVLTGNVGinggnSGVREGSwdlg 417
Cdd:cd02764   292 FKPAKVAELTVDLDKALAALAKALAAAGKSLVVAG---SELSQTAGADTQVAVnaLNSLLGNDG-----KTVDHAR---- 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 418 vewfPMLENPVKTQISVFTWTDAIDHGTemtatrdgvrgkekldvpikflwcyASNTLINqhgDINHTHEVLQDD----- 492
Cdd:cd02764   360 ----PIKGGELGNQQDLKALASRINAGK-------------------------VSALLVY---DVNPVYDLPQGLgfaka 407
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 493 -SKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDlishESAGNMGYVILAQPATSAKFERKP 554
Cdd:cd02764   408 lEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESWG----DAETPDGTYSICQPVIAPLFDTRS 466
MopB_CT_Formate-Dh-Na-like cd02792
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
682-806 7.10e-07

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: 48.76  E-value: 7.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 682 KTYPLQLTG------FHYKARTHSSYGnidvLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILP 754
Cdd:cd02792     1 EEFPLVLTTgrltehFHGGNMTRNSPY----LAELQPEMfVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKP 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1434010499 755 GVTAIgqgAWLKADMFGDRvdhGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:cd02792    77 HEVGI---PYHWGGMGLVI---GDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
MopB_NADH-Q-OR-NuoG2 cd02768
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ...
61-234 1.36e-06

MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.


Pssm-ID: 239169 [Multi-domain]  Cd Length: 386  Bit Score: 51.51  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  61 VNCGSRCLLRLHVKDDTVYWVESDTtgddvygNHQVRACL---RGR----SIrrrmNHPDRLKYPMKRVGkrgeGKFERI 133
Cdd:cd02768     5 VHDALGSNIRVDVRGGEVMRILPRE-------NEAINEEWisdKGRfgydGL----NSRQRLTQPLIKKG----GKLVPV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 134 SWDEALDTIsdnlRRILKDYGNEAVHVLYGTGVDggniTNSNVPY-RLMNSCG----GFLSRYGSYSTAQISAAMSYMfg 208
Cdd:cd02768    70 SWEEALKTV----AEGLKAVKGDKIGGIAGPRAD----LESLFLLkKLLNKLGsnniDHRLRQSDLPADNRLRGNYLF-- 139
                         170       180
                  ....*....|....*....|....*.
gi 1434010499 209 andGNSPDDIANTKLVVMFGNNPAET 234
Cdd:cd02768   140 ---NTSIAEIEEADAVLLIGSNLRKE 162
MopB_NDH-1_NuoG2-N7 cd02771
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ...
57-149 6.39e-06

MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239172 [Multi-domain]  Cd Length: 472  Bit Score: 49.69  E-value: 6.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499  57 SSCTvNCGSRCLLRLHVKDDTVYWVESDTTGD-DVYGNhqvraCLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISW 135
Cdd:cd02771     2 SICH-HCSVGCNISLGERYGELRRVENRYNGAvNHYFL-----CDRGRFGYGYVNSRDRLTQPLIRRG----GTLVPVSW 71
                          90
                  ....*....|....
gi 1434010499 136 DEALDTISDNLRRI 149
Cdd:cd02771    72 NEALDVAAARLKEA 85
MopB_NDH-1_NuoG2 cd02772
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ...
109-161 3.31e-05

MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239173 [Multi-domain]  Cd Length: 414  Bit Score: 46.96  E-value: 3.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 109 MNHPDRLKYPMKRVGkrgeGKFERISWDEALDTISDNLRRILKDYGNEAVHVL 161
Cdd:cd02772    49 LNSEDRLTKPMIKKD----GQWQEVDWETALEYVAEGLSAIIKKHGADQIGAL 97
FwdD COG1153
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
716-764 8.69e-05

Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];


Pssm-ID: 440767 [Multi-domain]  Cd Length: 127  Bit Score: 42.92  E-value: 8.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1434010499 716 WINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAW 764
Cdd:COG1153    34 ELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGPW 82
MopB_CT_FmdC-FwdD cd02789
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ...
715-796 1.63e-04

The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239190 [Multi-domain]  Cd Length: 106  Bit Score: 41.64  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 715 VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWlkADMFGDRVDHGGSiniltshrpSPLAKG 794
Cdd:cd02789    33 CEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPW--ANVVVDPYTDSTG---------SPIFKG 101

                  ..
gi 1434010499 795 NP 796
Cdd:cd02789   102 VP 103
MopB_CT_Arsenite-Ox cd02779
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ...
717-764 3.46e-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: 38.21  E-value: 3.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1434010499 717 INPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAW 764
Cdd:cd02779    37 VNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHP 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH