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Conserved domains on  [gi|6066882|emb|CAB58226|]
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anaerobic dimethylsulfoxide reductase chain A, partial [Yersinia pseudotuberculosis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14990 super family cl33052
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
 1-148 3.57e-93

anaerobic dimethyl sulfoxide reductase subunit A; Provisional


The actual alignment was detected with superfamily member PRK14990:

Pssm-ID: 184952 [Multi-domain]  Cd Length: 814  Bit Score: 286.54  E-value: 3.57e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882     1 SAEYADIILPDCTASEQMDFCLDASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:PRK14990 519 SAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYA 598

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6066882    81 QSQAAIPELPSFEDFRAQGMFKKRDPAGHHVAYHDFRTDPVANPLSTPSGKIEIYSAALAEIAATWEL 148
Cdd:PRK14990 599 QSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADIAATWEL 666
 
Name Accession Description Interval E-value
PRK14990 PRK14990
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
 1-148 3.57e-93

anaerobic dimethyl sulfoxide reductase subunit A; Provisional


Pssm-ID: 184952 [Multi-domain]  Cd Length: 814  Bit Score: 286.54  E-value: 3.57e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882     1 SAEYADIILPDCTASEQMDFCLDASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:PRK14990 519 SAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYA 598

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6066882    81 QSQAAIPELPSFEDFRAQGMFKKRDPAGHHVAYHDFRTDPVANPLSTPSGKIEIYSAALAEIAATWEL 148
Cdd:PRK14990 599 QSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADIAATWEL 666
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
 1-145 3.29e-65

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: 208.72  E-value: 3.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDFCLDASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:cd02770 454 SARYADILLPDTTELEREDIVLTSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEELYG 533

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6066882   81 QSQAAIPELPSFEDFRAQGMFKKRdPAGHHVAYHDFRTDPVANPLSTPSGKIEIYSAALAEIAAT 145
Cdd:cd02770 534 QTRAKEPGLPTYEEFREKGIYRVP-RALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT 597
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
1-140 1.26e-35

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


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 129.58  E-value: 1.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDFcldASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:COG0243 407 TARYADIVLPATTWLERDDI---VTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELLE 483

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882   81 QSQaaiPELPSFEDFRAQGMFKKRDPAGHHvayhdFRTDpvaNPLSTPSGKIEIYSAALA 140
Cdd:COG0243 484 ATR---GRGITFEELREKGPVQLPVPPEPA-----FRND---GPFPTPSGKAEFYSETLA 532
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
1-56 1.18e-08

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 52.40  E-value: 1.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6066882      1 SAEYADIILPDCTASEQMDFCLDASSGNMayviFADQVIKPRFECKNIYDITSGLA 56
Cdd:pfam00384 306 TAKYADVILPAAAYTEKNGTYVNTEGRVQ----STKQAVPPPGEAREDWKILRALS 357
 
Name Accession Description Interval E-value
PRK14990 PRK14990
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
 1-148 3.57e-93

anaerobic dimethyl sulfoxide reductase subunit A; Provisional


Pssm-ID: 184952 [Multi-domain]  Cd Length: 814  Bit Score: 286.54  E-value: 3.57e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882     1 SAEYADIILPDCTASEQMDFCLDASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:PRK14990 519 SAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYA 598

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6066882    81 QSQAAIPELPSFEDFRAQGMFKKRDPAGHHVAYHDFRTDPVANPLSTPSGKIEIYSAALAEIAATWEL 148
Cdd:PRK14990 599 QSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADIAATWEL 666
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
 1-145 3.29e-65

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: 208.72  E-value: 3.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDFCLDASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:cd02770 454 SARYADILLPDTTELEREDIVLTSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEELYG 533

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6066882   81 QSQAAIPELPSFEDFRAQGMFKKRdPAGHHVAYHDFRTDPVANPLSTPSGKIEIYSAALAEIAAT 145
Cdd:cd02770 534 QTRAKEPGLPTYEEFREKGIYRVP-RALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT 597
MopB_DMSOR-like cd02751
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
 1-145 2.66e-59

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: 193.21  E-value: 2.66e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDFcLDASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:cd02751 447 SARYADIVLPATTSLERNDI-GLTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEMEWLEHLYE 525

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6066882   81 QSQAAI----PELPSFEDFRAQGMFKKRDPAGHHVAYHDFRTDPVANPLSTPSGKIEIYSAALAEIAAT 145
Cdd:cd02751 526 ETRAKAagpgPELPSFEEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYD 594
MopB_DMSOR-BSOR-TMAOR cd02769
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
 1-140 1.27e-44

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: 153.96  E-value: 1.27e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDFcldASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:cd02769 449 TARHADIVLPATTSLERNDI---GGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEMEWLRHLYE 525

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6066882   81 QSQAAI----PELPSFEDFRAQGMFKKRDPAGHHVAYHDFRTDPVANPLSTPSGKIEIYSAALA 140
Cdd:cd02769 526 ESRAQAaargVEMPSFDEFWAQGYVELPIPEADFVRLADFREDPEANPLGTPSGRIEIFSETIA 589
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
1-140 1.26e-35

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


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 129.58  E-value: 1.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDFcldASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ 80
Cdd:COG0243 407 TARYADIVLPATTWLERDDI---VTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELLE 483

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882   81 QSQaaiPELPSFEDFRAQGMFKKRDPAGHHvayhdFRTDpvaNPLSTPSGKIEIYSAALA 140
Cdd:COG0243 484 ATR---GRGITFEELREKGPVQLPVPPEPA-----FRND---GPFPTPSGKAEFYSETLA 532
PRK15102 PRK15102
trimethylamine-N-oxide reductase TorA;
4-140 6.55e-28

trimethylamine-N-oxide reductase TorA;


Pssm-ID: 237909 [Multi-domain]  Cd Length: 825  Bit Score: 107.83  E-value: 6.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882     4 YADIILPDCTASEQMDFCLDASSGNMAyVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEGRTQEEWMRHLYQ--- 80
Cdd:PRK15102 511 FADIVLPACTQFERNDIDQYGSYSNRG-IIAMKKVVEPLFESRSDFDIFRELCRRFGREKEYTRGMDEMGWLKRLYQeck 589

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6066882    81 QSQAAIPELPSFEDFRAQG--MFKKRDPAGHHVayhDFRTDPVANPLSTPSGKIEIYSAALA 140
Cdd:PRK15102 590 QQNKGKFHMPEFDEFWKKGyvEFGEGQPWVRHA---DFREDPELNPLGTPSGLIEIYSRKIA 648
MopB_4 cd02765
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ...
 1-143 5.25e-18

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: 79.45  E-value: 5.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDfcLDASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEgrTQEEWMRHLYQ 80
Cdd:cd02765 427 TVRYADIVLPAAHWFEVED--LLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFPK--TPEDYVRAFMN 502

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6066882   81 QSQAAIPELpSFEDFRAQGMFKKRD-PAGHHVAYHDfrtdpvaNPLSTPSGKIEIYSAALAEIA 143
Cdd:cd02765 503 SDDPALDGI-TWEALKEEGIIMRLAtPEDPYVAYLD-------QKFGTPSGKLEFYNEAAPELE 558
MopB_3 cd02766
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ...
 1-141 3.55e-12

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: 62.65  E-value: 3.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDfcLDASSGNmAYVIFADQVIKPRFECKNIYDITSGLARHMGVEQKFTEgRTQEEWMRhlyq 80
Cdd:cd02766 370 TARYADIVLPATTFLEHED--VYASYWH-YYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFE-ESDEEWLD---- 441

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6066882   81 qsQAAIPELPSFEDFRAQGMFKKRDPAGHHVAYHDFRtdpvanpLSTPSGKIEIYSAALAE 141
Cdd:cd02766 442 --QALDGTGLPLEGIDLERLLGPRKAGFPLVAWEDRG-------FPTPSGKFEFYSERAAK 493
PRK15488 PRK15488
thiosulfate reductase PhsA; Provisional
 1-144 1.67e-10

thiosulfate reductase PhsA; Provisional


Pssm-ID: 237973 [Multi-domain]  Cd Length: 759  Bit Score: 57.75  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882     1 SAEYADIILPDCTASEQMDFCLDASSGNMAYVIfADQVIKPRFECKNIYDITSGLARHMGVEQKFTeGRTQEEWmrHLYQ 80
Cdd:PRK15488 470 SAAYADVVLPESTYLERDEEISDKSGKNPAYAL-RQRVVEPIGDTKPSWQIFKELGEKMGLGQYYP-WQDMETL--QLYQ 545

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6066882    81 --QSQAAIPEL----------PSFedFRAQGM---FKKRDPAGHHVAyHDFRTDPVANpLSTPSGKIEIYSAALAEIAA 144
Cdd:PRK15488 546 vnGDHALLKELkkkgyvsfgvPLL--LREPKMvakFVARYPNAKAVD-EDGTYGSQLK-FKTPSGKIELFSAKLEALAP 620
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
1-56 1.18e-08

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 52.40  E-value: 1.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6066882      1 SAEYADIILPDCTASEQMDFCLDASSGNMayviFADQVIKPRFECKNIYDITSGLA 56
Cdd:pfam00384 306 TAKYADVILPAAAYTEKNGTYVNTEGRVQ----STKQAVPPPGEAREDWKILRALS 357
Molybdopterin-Binding cd00368
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
 1-59 3.43e-07

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: 48.09  E-value: 3.43e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6066882    1 SAEYADIILPDCTASEqmdfCLDASSGNMAYVIFADQVIKPRFECKNIYDITSGLARHM 59
Cdd:cd00368 320 TAAYADVVLPAATYLE----KEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
MopB_Thiosulfate-R-like cd02755
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ...
 1-141 4.52e-06

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: 44.98  E-value: 4.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDFCLDASSGNMAYVIfADQVIKPRFECKNIYDITSGLARHMGveqkftegrtqeewmrhlyq 80
Cdd:cd02755 371 TALYADVILPEATYLERDEPFSDKGGPAPAVAT-RQRAIEPLYDTRPGWDILKELARRLG-------------------- 429

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6066882   81 qsqaaipelpsfedfraqgmfkkrdpaghhvayhdfrtdpvanPLSTPSGKIEIYSAALAE 141
Cdd:cd02755 430 -------------------------------------------LFGTPSGKIELYSPILAK 447
MopB_Acetylene-hydratase cd02759
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ...
 1-142 5.93e-06

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: 44.60  E-value: 5.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDFCLDASSGNMAYVIfaDQVIKPRFECKNIYDITSGLARHMGveqkftegrtQEEWmrhlyq 80
Cdd:cd02759 370 TAMLADIVLPVAMSLERPGLRGGFEAENFVQLR--QKAVEPYGEAKSDYEIVLELGKRLG----------PEEA------ 431

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6066882   81 qsqaaipelpsfedfraqgmfkkrdpagHHVAYHDFRTDPVANP-LSTPSGKIEIYSAALAEI 142
Cdd:cd02759 432 ----------------------------EYYKYEKGLLRPDGQPgFNTPTGKVELYSTMLEEL 466
MopB_Nitrate-R-NarG-like cd02750
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ...
 1-78 2.57e-05

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: 42.69  E-value: 2.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6066882    1 SAEYADIILPDCTASEQMDfcLDASSGNmAYVIFADQVIKPRFECKNIYDITSGLARHmgVEQKFTEGRTQ----EEWMR 76
Cdd:cd02750 376 TALYSDIVLPAATWYEKHD--LSTTDMH-PFIHPFSPAVDPLWEAKSDWEIFKALAKK--VPWRTLTGRQQfyldHDWFL 450


                ..
gi 6066882   77 HL 78
Cdd:cd02750 451 EL 452
 
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.
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