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Conserved domains on  [gi|504408989|ref|WP_014596091|]
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MULTISPECIES: thioredoxin domain-containing protein [Pseudomonadota]

Protein Classification

DsbA family protein( domain architecture ID 11447254)

DsbA family protein belongs to the thioredoxin superfamily of proteins containing a redox active CXXC motif, similar to DsbA that is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  11967064|9099998|10049365|15558583|12524212
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 76-229 4.22e-23

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 91.60  E-value: 4.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989  76 TLTLYADLECPFCREYFPQLKRWVGANAD--VALQWQHQPLaaHEPAASAEARLAECAAESGghvAFWQAIEWVYAHTRS 153
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKYVDgkVRVVYRPFPL--LHPDSLRAARAALCAADQG---KFWAFHDALFANQPA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504408989 154 -DGLGLPEGLRYPGLNPA-VEQCLASERPETLIRAQAEEATKGGVTATPSLRLHDRqtsqaiLLQGPIEGDALLSAMD 229
Cdd:COG1651   78 lTDDDLREIAKEAGLDAAkFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK------LVSGAVPYEELEAALD 149
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 76-229 4.22e-23

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 91.60  E-value: 4.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989  76 TLTLYADLECPFCREYFPQLKRWVGANAD--VALQWQHQPLaaHEPAASAEARLAECAAESGghvAFWQAIEWVYAHTRS 153
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKYVDgkVRVVYRPFPL--LHPDSLRAARAALCAADQG---KFWAFHDALFANQPA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504408989 154 -DGLGLPEGLRYPGLNPA-VEQCLASERPETLIRAQAEEATKGGVTATPSLRLHDRqtsqaiLLQGPIEGDALLSAMD 229
Cdd:COG1651   78 lTDDDLREIAKEAGLDAAkFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK------LVSGAVPYEELEAALD 149
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 77-166 3.21e-12

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 61.27  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989  77 LTLYADLECPFCREYFPQLKRWVGANA-DVALQWQHQPLAAHEPAAS-AEARLAECAAESGGHVAFWQAIEWVYAHTRSD 154
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDgGVRVVYRPFPLLGGMPPNSlAAARAALAAAAQGKFEALHEALADTALARALG 80

                         90
                 ....*....|....*.
gi 504408989 155 GLGLP----EGLRYPG 166
Cdd:cd02972   81 VTGTPtfvvNGEKYSG 96
Thioredoxin_4 pfam13462
Thioredoxin;
62-229 3.18e-10

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 57.35  E-value: 3.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989   62 AGPPWQMGNAQGRFTLTLYADLECPFCR----EYFPQLKRWVGAN------ADVALQWQHQPLAAhepaasaeARLAECA 131
Cdd:pfam13462   1 TPTDPVIGNPDAPVTVVEYADLRCPHCAkfheEVLKLLEEYIDTGkvrfiiRDFPLDGEGESLLA--------AMAARCA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989  132 AESGG------HVAFWQAIEWVYAHTRSDGLGLpeglrypGLNPAVEQCLASERPETLIRAQAEEATKGGVTATPSLRLH 205
Cdd:pfam13462  73 GDQSPeyflviDKLLYSQQEEWAQDLELAALAG-------LKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIIN 145

                         170       180
                  ....*....|....*....|....
gi 504408989  206 DRQtsqailLQGPIEGDALLSAMD 229
Cdd:pfam13462 146 GKK------VDGPLTYEELKKLID 163
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 76-229 4.22e-23

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 91.60  E-value: 4.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989  76 TLTLYADLECPFCREYFPQLKRWVGANAD--VALQWQHQPLaaHEPAASAEARLAECAAESGghvAFWQAIEWVYAHTRS 153
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKYVDgkVRVVYRPFPL--LHPDSLRAARAALCAADQG---KFWAFHDALFANQPA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504408989 154 -DGLGLPEGLRYPGLNPA-VEQCLASERPETLIRAQAEEATKGGVTATPSLRLHDRqtsqaiLLQGPIEGDALLSAMD 229
Cdd:COG1651   78 lTDDDLREIAKEAGLDAAkFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK------LVSGAVPYEELEAALD 149
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 77-166 3.21e-12

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 61.27  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989  77 LTLYADLECPFCREYFPQLKRWVGANA-DVALQWQHQPLAAHEPAAS-AEARLAECAAESGGHVAFWQAIEWVYAHTRSD 154
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDgGVRVVYRPFPLLGGMPPNSlAAARAALAAAAQGKFEALHEALADTALARALG 80

                         90
                 ....*....|....*.
gi 504408989 155 GLGLP----EGLRYPG 166
Cdd:cd02972   81 VTGTPtfvvNGEKYSG 96
Thioredoxin_4 pfam13462
Thioredoxin;
62-229 3.18e-10

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 57.35  E-value: 3.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989   62 AGPPWQMGNAQGRFTLTLYADLECPFCR----EYFPQLKRWVGAN------ADVALQWQHQPLAAhepaasaeARLAECA 131
Cdd:pfam13462   1 TPTDPVIGNPDAPVTVVEYADLRCPHCAkfheEVLKLLEEYIDTGkvrfiiRDFPLDGEGESLLA--------AMAARCA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989  132 AESGG------HVAFWQAIEWVYAHTRSDGLGLpeglrypGLNPAVEQCLASERPETLIRAQAEEATKGGVTATPSLRLH 205
Cdd:pfam13462  73 GDQSPeyflviDKLLYSQQEEWAQDLELAALAG-------LKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIIN 145

                         170       180
                  ....*....|....*....|....
gi 504408989  206 DRQtsqailLQGPIEGDALLSAMD 229
Cdd:pfam13462 146 GKK------VDGPLTYEELKKLID 163
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 69-229 4.86e-04

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 39.50  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989  69 GNAQGRFTLTLYADLECPFCREYFPQLKRWVGANADVALQWQHQPLAAHEPAASAEARLAECAAESGGHVAFWQAIewvY 148
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGESSVLAARVALAVWKNGPGKYLEFHNAL---M 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989 149 AHT-RSDGLGLPEGLRYPGLNPA-VEQCLASERPETLIRAQAEEATKGGVTATPSLRLHDRqtsqaiLLQGPIEGDALLS 226
Cdd:cd03023   78 ATRgRLNEESLLRIAKKAGLDEAkLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDT------VIPGAVPADTLKE 151


                 ...
gi 504408989 227 AMD 229
Cdd:cd03023  152 AID 154
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 76-234 4.16e-03

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 37.41  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408989   76 TLTLYADLECPFCREYFPQLKRWVGANADVALQWQHQPLAAHEPaasaearlaecaaeSGGHVAFWQAIEWVYAHTRSDG 155
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLAGAKK--------------IGNVGPSNLPVKLKYMMADLER 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504408989  156 LGLPEGLrypGLNPAVEQCLASERPETLIRAQAEEatkgGVTATPSLRLHDRQTSQAILLQGPIEGDALLSAMDMLAAE 234
Cdd:pfam01323  67 WAALYGI---PLRFPANFLGNSTRANRLALAAGAE----GLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEE 138
 
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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