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Conserved domains on  [gi|2274802560|ref|WP_254901087|]
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DsbA family protein, partial [Salmonella enterica]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 22-138 4.95e-40

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member PRK10954:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 207  Bit Score: 132.91  E-value: 4.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  22 QEWESITPPVADAPAVVEFFSFYCPPCYAFSQTMGVDQAIRHVLPQGDRMVKYHVSLLGPLGHELTRAWALAMVMKETDV 101
Cdd:PRK10954   26 KQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYHVSDNVKKKLPEGTKMTKYHVEFLGPLGKELTQAWAVAMALGVEDK 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2274802560 102 VEKAFFTAGMVEKRLHSPDDVRRVFMSAtGISRAEYD 138
Cdd:PRK10954  106 VTPPLFEGVQKTQTIQSAADIRDVFIKA-GVKGEDYD 141
 
Name Accession Description Interval E-value
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
22-138 4.95e-40

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 132.91  E-value: 4.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  22 QEWESITPPVADAPAVVEFFSFYCPPCYAFSQTMGVDQAIRHVLPQGDRMVKYHVSLLGPLGHELTRAWALAMVMKETDV 101
Cdd:PRK10954   26 KQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYHVSDNVKKKLPEGTKMTKYHVEFLGPLGKELTQAWAVAMALGVEDK 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2274802560 102 VEKAFFTAGMVEKRLHSPDDVRRVFMSAtGISRAEYD 138
Cdd:PRK10954  106 VTPPLFEGVQKTQTIQSAADIRDVFIKA-GVKGEDYD 141
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 22-138 1.97e-32

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 112.77  E-value: 1.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  22 QEWESITPPVADA-PAVVEFFSFYCPPCYAFSQTMGVDQAIrhvLPQGDRMVKYHVSLLGPLGHELTRAWALAMVM-KET 99
Cdd:cd03019     3 KDYTVLSPPIPSGkPEVIEFFSYGCPHCYNFEPILEAWVKK---LPKDVKFEKVPVVFGGGEGEPLARAFYAAEALgLED 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2274802560 100 DVVEKAFFTAGMVEKRLHSPDDVRRVFMSAtGISRAEYD 138
Cdd:cd03019    80 KLHAALFEAIHEKRKRLLDPDDIRKIFLSQ-GVDKKKFD 117
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 36-138 7.46e-11

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: 57.05  E-value: 7.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  36 AVVEFFSFYCPPCYAFSQTMGVDQAIRHVLpqgdRMVKYHVSLLGPL--------------------------------- 82
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDV----KVVYRPFPLAGAKkignvgpsnlpvklkymmadlerwaalygiplr 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274802560  83 -----GHELTRAWALAMVMKETDVVEK---AFFTAGMVEKRLHSPDDVRRVFMSATGISRAEYD 138
Cdd:pfam01323  77 fpanfLGNSTRANRLALAAGAEGLAEKvvrELFNALWGEGAAITDDSVLREVAEKAGLDAEEFD 140
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 37-138 9.83e-08

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 48.07  E-value: 9.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  37 VVEFFSFYCPPCYAFSQTMgvdQAIRHVLPQGD-RMVKYHVSLLGPLGHELTRA-WALAMVMKETDVVEkAFFTAgmveK 114
Cdd:COG1651     4 VVEFFDYQCPYCARFHPEL---PELLKKYVDGKvRVVYRPFPLLHPDSLRAARAaLCAADQGKFWAFHD-ALFAN----Q 75

                          90       100
                  ....*....|....*....|....
gi 2274802560 115 RLHSPDDVRRvFMSATGISRAEYD 138
Cdd:COG1651    76 PALTDDDLRE-IAKEAGLDAAKFD 98
 
Name Accession Description Interval E-value
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
22-138 4.95e-40

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 132.91  E-value: 4.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  22 QEWESITPPVADAPAVVEFFSFYCPPCYAFSQTMGVDQAIRHVLPQGDRMVKYHVSLLGPLGHELTRAWALAMVMKETDV 101
Cdd:PRK10954   26 KQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYHVSDNVKKKLPEGTKMTKYHVEFLGPLGKELTQAWAVAMALGVEDK 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2274802560 102 VEKAFFTAGMVEKRLHSPDDVRRVFMSAtGISRAEYD 138
Cdd:PRK10954  106 VTPPLFEGVQKTQTIQSAADIRDVFIKA-GVKGEDYD 141
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 22-138 1.97e-32

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 112.77  E-value: 1.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  22 QEWESITPPVADA-PAVVEFFSFYCPPCYAFSQTMGVDQAIrhvLPQGDRMVKYHVSLLGPLGHELTRAWALAMVM-KET 99
Cdd:cd03019     3 KDYTVLSPPIPSGkPEVIEFFSYGCPHCYNFEPILEAWVKK---LPKDVKFEKVPVVFGGGEGEPLARAFYAAEALgLED 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2274802560 100 DVVEKAFFTAGMVEKRLHSPDDVRRVFMSAtGISRAEYD 138
Cdd:cd03019    80 KLHAALFEAIHEKRKRLLDPDDIRKIFLSQ-GVDKKKFD 117
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 36-138 7.46e-11

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: 57.05  E-value: 7.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  36 AVVEFFSFYCPPCYAFSQTMGVDQAIRHVLpqgdRMVKYHVSLLGPL--------------------------------- 82
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDV----KVVYRPFPLAGAKkignvgpsnlpvklkymmadlerwaalygiplr 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274802560  83 -----GHELTRAWALAMVMKETDVVEK---AFFTAGMVEKRLHSPDDVRRVFMSATGISRAEYD 138
Cdd:pfam01323  77 fpanfLGNSTRANRLALAAGAEGLAEKvvrELFNALWGEGAAITDDSVLREVAEKAGLDAEEFD 140
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 37-138 9.83e-08

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 48.07  E-value: 9.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274802560  37 VVEFFSFYCPPCYAFSQTMgvdQAIRHVLPQGD-RMVKYHVSLLGPLGHELTRA-WALAMVMKETDVVEkAFFTAgmveK 114
Cdd:COG1651     4 VVEFFDYQCPYCARFHPEL---PELLKKYVDGKvRVVYRPFPLLHPDSLRAARAaLCAADQGKFWAFHD-ALFAN----Q 75

                          90       100
                  ....*....|....*....|....
gi 2274802560 115 RLHSPDDVRRvFMSATGISRAEYD 138
Cdd:COG1651    76 PALTDDDLRE-IAKEAGLDAAKFD 98
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 37-105 1.58e-04

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: 38.54  E-value: 1.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274802560  37 VVEFFSFYCPPCYAFSQTMgvdQAIRHVLPQGDRMVKYHVSLLGPLGHELTRA----WALAMVMKETDVVEKA 105
Cdd:cd02972     1 IVEFFDPLCPYCYLFEPEL---EKLLYADDGGVRVVYRPFPLLGGMPPNSLAAaraaLAAAAQGKFEALHEAL 70
 
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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