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Conserved domains on  [gi|1092712987|ref|WP_070643111|]
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thioredoxin domain-containing protein [Corynebacterium sp. HMSC076C10]

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, ...
 75-222 5.74e-13

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


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 64.25  E-value: 5.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987  75 TIFEDFSCHYCAQMSEEgHDDELKALNDGKLVAEYRTLNFLDGQekeqrdghSTRVFAVARkiaETGDARAYWNFRTMMM 154
Cdd:COG1651     5 VEFFDYQCPYCARFHPE-LPELLKKYVDGKVRVVYRPFPLLHPD--------SLRAARAAL---CAADQGKFWAFHDALF 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092712987 155 ADQQNsvtWSDDELADRLEQLGVADEivsEVRSGIDTTEAKASANANFDDLEKrLGKVSSPHVFVDGK 222
Cdd:COG1651    73 ANQPA---LTDDDLREIAKEAGLDAA---KFDACLNSGAVAAKVEADTALAQA-LGVTGTPTFVVNGK 133
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 75-222 5.74e-13

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 64.25  E-value: 5.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987  75 TIFEDFSCHYCAQMSEEgHDDELKALNDGKLVAEYRTLNFLDGQekeqrdghSTRVFAVARkiaETGDARAYWNFRTMMM 154
Cdd:COG1651     5 VEFFDYQCPYCARFHPE-LPELLKKYVDGKVRVVYRPFPLLHPD--------SLRAARAAL---CAADQGKFWAFHDALF 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092712987 155 ADQQNsvtWSDDELADRLEQLGVADEivsEVRSGIDTTEAKASANANFDDLEKrLGKVSSPHVFVDGK 222
Cdd:COG1651    73 ANQPA---LTDDDLREIAKEAGLDAA---KFDACLNSGAVAAKVEADTALAQA-LGVTGTPTFVVNGK 133
Thioredoxin_4 pfam13462
Thioredoxin;
67-229 4.05e-05

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 42.71  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987  67 GAEGAK-TATIFEDFSCHYCAQMSEEGHDDELKALNDGKLVAEYRTLNFLdgqekeqRDGHSTRVFAVARKIAEtgDARA 145
Cdd:pfam13462   8 GNPDAPvTVVEYADLRCPHCAKFHEEVLKLLEEYIDTGKVRFIIRDFPLD-------GEGESLLAAMAARCAGD--QSPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987 146 YWNFRTMMMADQQNSVTwSDDELAdrLEQLGVADEIVSEVRSG-IDTTEAKASANANFDDLEkrlgkvSSPHVFVDGKDI 224
Cdd:pfam13462  79 YFLVIDKLLYSQQEEWA-QDLELA--ALAGLKDEEFEACLEEEdFLALVMADVKEARAAGIN------FTPTFIINGKKV 149


                  ....*
gi 1092712987 225 LENIS 229
Cdd:pfam13462 150 DGPLT 154
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 75-157 6.10e-03

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: 35.07  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987  75 TIFEDFSCHYCAQMSEEGhdDELKALNDGKLVAEYRTLNFLDGQEKEQRDGHstRVFAVArkiAETGDARAYWN-FRTMM 153
Cdd:cd02972     2 VEFFDPLCPYCYLFEPEL--EKLLYADDGGVRVVYRPFPLLGGMPPNSLAAA--RAALAA---AAQGKFEALHEaLADTA 74


                  ....
gi 1092712987 154 MADQ 157
Cdd:cd02972    75 LARA 78
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 75-222 5.74e-13

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 64.25  E-value: 5.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987  75 TIFEDFSCHYCAQMSEEgHDDELKALNDGKLVAEYRTLNFLDGQekeqrdghSTRVFAVARkiaETGDARAYWNFRTMMM 154
Cdd:COG1651     5 VEFFDYQCPYCARFHPE-LPELLKKYVDGKVRVVYRPFPLLHPD--------SLRAARAAL---CAADQGKFWAFHDALF 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092712987 155 ADQQNsvtWSDDELADRLEQLGVADEivsEVRSGIDTTEAKASANANFDDLEKrLGKVSSPHVFVDGK 222
Cdd:COG1651    73 ANQPA---LTDDDLREIAKEAGLDAA---KFDACLNSGAVAAKVEADTALAQA-LGVTGTPTFVVNGK 133
Thioredoxin_4 pfam13462
Thioredoxin;
67-229 4.05e-05

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 42.71  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987  67 GAEGAK-TATIFEDFSCHYCAQMSEEGHDDELKALNDGKLVAEYRTLNFLdgqekeqRDGHSTRVFAVARKIAEtgDARA 145
Cdd:pfam13462   8 GNPDAPvTVVEYADLRCPHCAKFHEEVLKLLEEYIDTGKVRFIIRDFPLD-------GEGESLLAAMAARCAGD--QSPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987 146 YWNFRTMMMADQQNSVTwSDDELAdrLEQLGVADEIVSEVRSG-IDTTEAKASANANFDDLEkrlgkvSSPHVFVDGKDI 224
Cdd:pfam13462  79 YFLVIDKLLYSQQEEWA-QDLELA--ALAGLKDEEFEACLEEEdFLALVMADVKEARAAGIN------FTPTFIINGKKV 149


                  ....*
gi 1092712987 225 LENIS 229
Cdd:pfam13462 150 DGPLT 154
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 75-157 6.10e-03

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: 35.07  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092712987  75 TIFEDFSCHYCAQMSEEGhdDELKALNDGKLVAEYRTLNFLDGQEKEQRDGHstRVFAVArkiAETGDARAYWN-FRTMM 153
Cdd:cd02972     2 VEFFDPLCPYCYLFEPEL--EKLLYADDGGVRVVYRPFPLLGGMPPNSLAAA--RAALAA---AAQGKFEALHEaLADTA 74


                  ....
gi 1092712987 154 MADQ 157
Cdd:cd02972    75 LARA 78
 
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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