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Conserved domains on  [gi|1240939178|ref|WP_095708325|]
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DsbA family protein [Pantoea vagans]

Protein Classification

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 ...
 94-260 3.13e-35

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: 123.47  E-value: 3.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178  94 GPAGAKVIVTEFFDYECIACSMMAPVMEKMMAANAGVRFAFRDWTIFAaryPESTQASRRGLGIYrKQGADAYMEFHNGI 173
Cdd:cd03023     1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILG---ESSVLAARVALAVW-KNGPGKYLEFHNAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178 174 YRTGhneGKLTAEDIEKVAAAAGAPAASDADNAVSDAVTE---NNAALAEMLGLSGTPGIIVMpaenatpdnTTVIPGVV 250
Cdd:cd03023    77 MATR---GRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEAtidKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                         170
                  ....*....|
gi 1240939178 251 SEQVMQQAIK 260
Cdd:cd03023   145 PADTLKEAID 154
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 35-61 7.50e-05

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


:

Pssm-ID: 465704  Cd Length: 34  Bit Score: 38.91  E-value: 7.50e-05
                          10        20
                  ....*....|....*....|....*..
gi 1240939178  35 QQARIGEIAADYLVAHPDVLIEVSKKL 61
Cdd:pfam18312   1 QKAAIEAIVRDYLLENPEILVEALTAL 27
 
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 ...
 94-260 3.13e-35

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: 123.47  E-value: 3.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178  94 GPAGAKVIVTEFFDYECIACSMMAPVMEKMMAANAGVRFAFRDWTIFAaryPESTQASRRGLGIYrKQGADAYMEFHNGI 173
Cdd:cd03023     1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILG---ESSVLAARVALAVW-KNGPGKYLEFHNAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178 174 YRTGhneGKLTAEDIEKVAAAAGAPAASDADNAVSDAVTE---NNAALAEMLGLSGTPGIIVMpaenatpdnTTVIPGVV 250
Cdd:cd03023    77 MATR---GRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEAtidKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                         170
                  ....*....|
gi 1240939178 251 SEQVMQQAIK 260
Cdd:cd03023   145 PADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 99-262 1.73e-19

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 82.35  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178  99 KVIVTEFFDYECIACSMMAPVMEKMMAANAG--VRFAFRDWTIFaarYPESTQASRRGLGIYRKqgaDAYMEFHNGIYRt 176
Cdd:COG1651     1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDgkVRVVYRPFPLL---HPDSLRAARAALCAADQ---GKFWAFHDALFA- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178 177 ghNEGKLTAEDIEKVAAA----AGAPAASDADNAVSDAVtENNAALAEMLGLSGTPGIIVmpaenatpdNTTVIPGVVSE 252
Cdd:COG1651    74 --NQPALTDDDLREIAKEagldAAKFDACLNSGAVAAKV-EADTALAQALGVTGTPTFVV---------NGKLVSGAVPY 141

                         170
                  ....*....|
gi 1240939178 253 QVMQQAIKRA 262
Cdd:COG1651   142 EELEAALDAA 151
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 35-61 7.50e-05

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


Pssm-ID: 465704  Cd Length: 34  Bit Score: 38.91  E-value: 7.50e-05
                          10        20
                  ....*....|....*....|....*..
gi 1240939178  35 QQARIGEIAADYLVAHPDVLIEVSKKL 61
Cdd:pfam18312   1 QKAAIEAIVRDYLLENPEILVEALTAL 27
Thioredoxin_4 pfam13462
Thioredoxin;
91-261 2.40e-04

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 40.79  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178  91 PVKGPAGAKVIVTEFFDYECIACSMMAPVMEKMMAA--NAG-VRFAFRDwtIFAARYPESTQASrRGLGIYRKQGADAYM 167
Cdd:pfam13462   5 PVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEyiDTGkVRFIIRD--FPLDGEGESLLAA-MAARCAGDQSPEYFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178 168 EFHNGIYRTGHNEGklTAEDIEKVAAAAGAPAASDADNAVSDAVTENNAALAEMLGLSGTPGIIVmpaenatpdNTTVIP 247
Cdd:pfam13462  82 VIDKLLYSQQEEWA--QDLELAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFII---------NGKKVD 150

                         170
                  ....*....|....
gi 1240939178 248 GVVSEQVMQQAIKR 261
Cdd:pfam13462 151 GPLTYEELKKLIDD 164
 
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 ...
 94-260 3.13e-35

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: 123.47  E-value: 3.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178  94 GPAGAKVIVTEFFDYECIACSMMAPVMEKMMAANAGVRFAFRDWTIFAaryPESTQASRRGLGIYrKQGADAYMEFHNGI 173
Cdd:cd03023     1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILG---ESSVLAARVALAVW-KNGPGKYLEFHNAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178 174 YRTGhneGKLTAEDIEKVAAAAGAPAASDADNAVSDAVTE---NNAALAEMLGLSGTPGIIVMpaenatpdnTTVIPGVV 250
Cdd:cd03023    77 MATR---GRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEAtidKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                         170
                  ....*....|
gi 1240939178 251 SEQVMQQAIK 260
Cdd:cd03023   145 PADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 99-262 1.73e-19

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 82.35  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178  99 KVIVTEFFDYECIACSMMAPVMEKMMAANAG--VRFAFRDWTIFaarYPESTQASRRGLGIYRKqgaDAYMEFHNGIYRt 176
Cdd:COG1651     1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDgkVRVVYRPFPLL---HPDSLRAARAALCAADQ---GKFWAFHDALFA- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178 177 ghNEGKLTAEDIEKVAAA----AGAPAASDADNAVSDAVtENNAALAEMLGLSGTPGIIVmpaenatpdNTTVIPGVVSE 252
Cdd:COG1651    74 --NQPALTDDDLREIAKEagldAAKFDACLNSGAVAAKV-EADTALAQALGVTGTPTFVV---------NGKLVSGAVPY 141

                         170
                  ....*....|
gi 1240939178 253 QVMQQAIKRA 262
Cdd:COG1651   142 EELEAALDAA 151
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 102-171 9.31e-07

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: 46.24  E-value: 9.31e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240939178 102 VTEFFDYECIACSMMAPVMEKMMAANAG-VRFAFRDWTIFAARYPESTQASRrglGIYRKQGADAYMEFHN 171
Cdd:cd02972     1 IVEFFDPLCPYCYLFEPELEKLLYADDGgVRVVYRPFPLLGGMPPNSLAAAR---AALAAAAQGKFEALHE 68
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 35-61 7.50e-05

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


Pssm-ID: 465704  Cd Length: 34  Bit Score: 38.91  E-value: 7.50e-05
                          10        20
                  ....*....|....*....|....*..
gi 1240939178  35 QQARIGEIAADYLVAHPDVLIEVSKKL 61
Cdd:pfam18312   1 QKAAIEAIVRDYLLENPEILVEALTAL 27
Thioredoxin_4 pfam13462
Thioredoxin;
91-261 2.40e-04

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 40.79  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178  91 PVKGPAGAKVIVTEFFDYECIACSMMAPVMEKMMAA--NAG-VRFAFRDwtIFAARYPESTQASrRGLGIYRKQGADAYM 167
Cdd:pfam13462   5 PVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEyiDTGkVRFIIRD--FPLDGEGESLLAA-MAARCAGDQSPEYFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178 168 EFHNGIYRTGHNEGklTAEDIEKVAAAAGAPAASDADNAVSDAVTENNAALAEMLGLSGTPGIIVmpaenatpdNTTVIP 247
Cdd:pfam13462  82 VIDKLLYSQQEEWA--QDLELAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFII---------NGKKVD 150

                         170
                  ....*....|....
gi 1240939178 248 GVVSEQVMQQAIKR 261
Cdd:pfam13462 151 GPLTYEELKKLIDD 164
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 93-232 8.45e-03

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: 36.11  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939178  93 KGPAGAKVIVTEFFDYECIACSMMAPVMEKMMAAN-AGVRF-----AFRD-WTIFAARypestqasrrglgIYRKQGADA 165
Cdd:cd03019    10 PPIPSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLpKDVKFekvpvVFGGgEGEPLAR-------------AFYAAEALG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1240939178 166 YME-FHNGIYRTGHNEGK--LTAEDIEKVAAAAGAPAASDADNAVSDAVT---ENNAALAEMLGLSGTPGIIV 232
Cdd:cd03019    77 LEDkLHAALFEAIHEKRKrlLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKalvAKAEKLAKKYKITGVPAFVV 149
 
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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