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Conserved domains on  [gi|501411924|ref|WP_012443490|]
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DsbA family protein [Erwinia tasmaniensis]

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 ...
 90-256 2.45e-42

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 cd03023:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 154  Bit Score: 141.58  E-value: 2.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  90 GPEDASVIVTEFFDYQCVYCHRDARIVEKLIQDNPKVKFVFRDWPIFAGQyplSNTAALTGIGIYReAGADAYLKYHNGI 169
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGES---SVLAARVALAVWK-NGPGKYLEFHNAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924 170 FATGhdeGKLREQDIADVAAKAMGKTPKLD---DLKSYTATIDKNDMLAKAIGANGTPLFIVMpasnptaenITVIPGAA 246
Cdd:cd03023   77 MATR---GRLNEESLLRIAKKAGLDEAKLKkdmDDPEIEATIDKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                        170
                 ....*....|
gi 501411924 247 SLDVLQTAIN 256
Cdd:cd03023  145 PADTLKEAID 154
 
Name Accession Description Interval E-value
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 90-256 2.45e-42

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: 141.58  E-value: 2.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  90 GPEDASVIVTEFFDYQCVYCHRDARIVEKLIQDNPKVKFVFRDWPIFAGQyplSNTAALTGIGIYReAGADAYLKYHNGI 169
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGES---SVLAARVALAVWK-NGPGKYLEFHNAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924 170 FATGhdeGKLREQDIADVAAKAMGKTPKLD---DLKSYTATIDKNDMLAKAIGANGTPLFIVMpasnptaenITVIPGAA 246
Cdd:cd03023   77 MATR---GRLNEESLLRIAKKAGLDEAKLKkdmDDPEIEATIDKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                        170
                 ....*....|
gi 501411924 247 SLDVLQTAIN 256
Cdd:cd03023  145 PADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 96-259 1.97e-25

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 97.76  E-value: 1.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  96 VIVTEFFDYQCVYCHRDARIVEKLIQD--NPKVKFVFRDWPIFagqYPLSNTAALtgigIYREAGA-DAYLKYHNGIFAT 172
Cdd:COG1651    2 VTVVEFFDYQCPYCARFHPELPELLKKyvDGKVRVVYRPFPLL---HPDSLRAAR----AALCAADqGKFWAFHDALFAN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924 173 ghdEGKLREQDIADVAAKAMGKTPKLD-DLKS--YTATIDKNDMLAKAIGANGTPLFIVmpasnptaeNITVIPGAASLD 249
Cdd:COG1651   75 ---QPALTDDDLREIAKEAGLDAAKFDaCLNSgaVAAKVEADTALAQALGVTGTPTFVV---------NGKLVSGAVPYE 142

                        170
                 ....*....|
gi 501411924 250 VLQTAINHAR 259
Cdd:COG1651  143 ELEAALDAAL 152
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 97-255 1.37e-12

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: 64.37  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924   97 IVTEFFDYQCVYCHRDARIVEKLIQDNPKVKFVFRDWPIFAGQYP------------------LSNTAALTGIGI----- 153
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLAGAKKIgnvgpsnlpvklkymmadLERWAALYGIPLrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  154 ---------------YREAGADAYLK-YHNGIFATGHDEGklREQDIADVAAKA-MGKTPKLDDLKS--YTATIDKNDML 214
Cdd:pfam01323  81 flgnstranrlalaaGAEGLAEKVVReLFNALWGEGAAIT--DDSVLREVAEKAgLDAEEFDEFLDSpaVKEAVRENTAA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 501411924  215 AKAIGANGTPLFIVmpasnptaeNITVIPGAASLDVLQTAI 255
Cdd:pfam01323 159 AISLGVFGVPTFVV---------GGKMVFGADRLDTLADAL 190
 
Name Accession Description Interval E-value
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 90-256 2.45e-42

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: 141.58  E-value: 2.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  90 GPEDASVIVTEFFDYQCVYCHRDARIVEKLIQDNPKVKFVFRDWPIFAGQyplSNTAALTGIGIYReAGADAYLKYHNGI 169
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGES---SVLAARVALAVWK-NGPGKYLEFHNAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924 170 FATGhdeGKLREQDIADVAAKAMGKTPKLD---DLKSYTATIDKNDMLAKAIGANGTPLFIVMpasnptaenITVIPGAA 246
Cdd:cd03023   77 MATR---GRLNEESLLRIAKKAGLDEAKLKkdmDDPEIEATIDKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                        170
                 ....*....|
gi 501411924 247 SLDVLQTAIN 256
Cdd:cd03023  145 PADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 96-259 1.97e-25

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 97.76  E-value: 1.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  96 VIVTEFFDYQCVYCHRDARIVEKLIQD--NPKVKFVFRDWPIFagqYPLSNTAALtgigIYREAGA-DAYLKYHNGIFAT 172
Cdd:COG1651    2 VTVVEFFDYQCPYCARFHPELPELLKKyvDGKVRVVYRPFPLL---HPDSLRAAR----AALCAADqGKFWAFHDALFAN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924 173 ghdEGKLREQDIADVAAKAMGKTPKLD-DLKS--YTATIDKNDMLAKAIGANGTPLFIVmpasnptaeNITVIPGAASLD 249
Cdd:COG1651   75 ---QPALTDDDLREIAKEAGLDAAKFDaCLNSgaVAAKVEADTALAQALGVTGTPTFVV---------NGKLVSGAVPYE 142

                        170
                 ....*....|
gi 501411924 250 VLQTAINHAR 259
Cdd:COG1651  143 ELEAALDAAL 152
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 97-255 1.37e-12

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: 64.37  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924   97 IVTEFFDYQCVYCHRDARIVEKLIQDNPKVKFVFRDWPIFAGQYP------------------LSNTAALTGIGI----- 153
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLAGAKKIgnvgpsnlpvklkymmadLERWAALYGIPLrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  154 ---------------YREAGADAYLK-YHNGIFATGHDEGklREQDIADVAAKA-MGKTPKLDDLKS--YTATIDKNDML 214
Cdd:pfam01323  81 flgnstranrlalaaGAEGLAEKVVReLFNALWGEGAAIT--DDSVLREVAEKAgLDAEEFDEFLDSpaVKEAVRENTAA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 501411924  215 AKAIGANGTPLFIVmpasnptaeNITVIPGAASLDVLQTAI 255
Cdd:pfam01323 159 AISLGVFGVPTFVV---------GGKMVFGADRLDTLADAL 190
Thioredoxin_4 pfam13462
Thioredoxin;
87-256 2.72e-12

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 63.13  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924   87 PHAGPEDASVIVTEFFDYQCVYCHRDARIVEKLIQ---DNPKVKFVFRDWPIFAGQYPLSntAALTgigiyreagADAYL 163
Cdd:pfam13462   5 PVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEeyiDTGKVRFIIRDFPLDGEGESLL--AAMA---------ARCAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  164 KYHNGIFATGHD----EGKLREQDiADVAAKAMGKTPKLDDL---KSYTATIDKNDMLAKAIGANGTPLFIVmpasnpta 236
Cdd:pfam13462  74 DQSPEYFLVIDKllysQQEEWAQD-LELAALAGLKDEEFEACleeEDFLALVMADVKEARAAGINFTPTFII-------- 144

                         170       180
                  ....*....|....*....|
gi 501411924  237 eNITVIPGAASLDVLQTAIN 256
Cdd:pfam13462 145 -NGKKVDGPLTYEELKKLID 163
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 91-228 2.67e-11

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: 60.77  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  91 PEDASVIVTEFFDYQCVYCHRDARIVEKLIQDNPK-VKFVF------RDWPIFAGQyplsntaaltgigIYREAGADAYL 163
Cdd:cd03019   12 IPSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPKdVKFEKvpvvfgGGEGEPLAR-------------AFYAAEALGLE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501411924 164 -KYHNGIFATGHDEGK--LREQDIADVAAKAMGKTPKLDDL---KSYTATIDKNDMLAKAIGANGTPLFIV 228
Cdd:cd03019   79 dKLHAALFEAIHEKRKrlLDPDDIRKIFLSQGVDKKKFDAAynsFSVKALVAKAEKLAKKYKITGVPAFVV 149
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 98-228 4.66e-10

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: 55.10  E-value: 4.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501411924  98 VTEFFDYQCVYCHRDARIVEKLIQ-DNPKVKFVFRDWPIFAGQYPLSNTAAltgIGIYREAGADAYLKYHNGIfatghde 176
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYaDDGGVRVVYRPFPLLGGMPPNSLAAA---RAALAAAAQGKFEALHEAL------- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501411924 177 gklreqdiadvaakamgktpklddlksytatidKNDMLAKAIGANGTPLFIV 228
Cdd:cd02972   71 ---------------------------------ADTALARALGVTGTPTFVV 89
 
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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