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Conserved domains on  [gi|260872827|gb|EEX79896|]
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DSBA oxidoreductase [Brucella abortus bv. 9 str. C68]

Protein Classification

DsbA family protein( domain architecture ID 10603290)

DsbA family protein belonging to the thioredoxin superfamily is a thiol-disulfide oxidoreductase, similar to Wolbachia pipientis alpha-DsbA1

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_4 pfam13462
Thioredoxin;
78-242 2.08e-60

Thioredoxin;


:

Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 187.55  E-value: 2.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827   78 KDMVYGKADAPVTIVEYASLTCPHCADFKLITFpKIKEKYIDTGKARLIFRDFPFDPR--ATAAVMLARCAPEDH--YFP 153
Cdd:pfam13462   3 TDPVIGNPDAPVTVVEYADLRCPHCAKFHEEVL-KLLEEYIDTGKVRFIIRDFPLDGEgeSLLAAMAARCAGDQSpeYFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  154 MIDLFFRQQQQWATAEDgkaallQIAKLAGFTQESFEACLTNQQLLNDVRATVERGsKEFGVNATPTFFINGKKYAGDLS 233
Cdd:pfam13462  82 VIDKLLYSQQEEWAQDL------ELAALAGLKDEEFEACLEEEDFLALVMADVKEA-RAAGINFTPTFIINGKKVDGPLT 154


                  ....*....
gi 260872827  234 FEEMSGFID 242
Cdd:pfam13462 155 YEELKKLID 163
 
Name Accession Description Interval E-value
Thioredoxin_4 pfam13462
Thioredoxin;
78-242 2.08e-60

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 187.55  E-value: 2.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827   78 KDMVYGKADAPVTIVEYASLTCPHCADFKLITFpKIKEKYIDTGKARLIFRDFPFDPR--ATAAVMLARCAPEDH--YFP 153
Cdd:pfam13462   3 TDPVIGNPDAPVTVVEYADLRCPHCAKFHEEVL-KLLEEYIDTGKVRFIIRDFPLDGEgeSLLAAMAARCAGDQSpeYFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  154 MIDLFFRQQQQWATAEDgkaallQIAKLAGFTQESFEACLTNQQLLNDVRATVERGsKEFGVNATPTFFINGKKYAGDLS 233
Cdd:pfam13462  82 VIDKLLYSQQEEWAQDL------ELAALAGLKDEEFEACLEEEDFLALVMADVKEA-RAAGINFTPTFIINGKKVDGPLT 154


                  ....*....
gi 260872827  234 FEEMSGFID 242
Cdd:pfam13462 155 YEELKKLID 163
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 88-245 4.83e-47

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 153.23  E-value: 4.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  88 PVTIVEYASLTCPHCADFKLiTFPKIKEKYIDtGKARLIFRDFPF-DPRATAAVMLARCAPE-DHYFPMIDLFFRQQQQW 165
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHP-ELPELLKKYVD-GKVRVVYRPFPLlHPDSLRAARAALCAADqGKFWAFHDALFANQPAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827 166 AtaedgKAALLQIAKLAGFTQESFEACLTNQQLLNDVRATVERGSKeFGVNATPTFFINGKKYAGDLSFEEMSGFIDSAL 245
Cdd:COG1651   79 T-----DDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQA-LGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 91-230 3.01e-11

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: 58.19  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  91 IVEYASLTCPHCADFKLITFPKIkekYIDTGKARLIFRDFPFDP----RATAAVMLARCAPEdhyfpmidlffrQQQQWA 166
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLL---YADDGGVRVVYRPFPLLGgmppNSLAAARAALAAAA------------QGKFEA 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260872827 167 TAEDgkaallqiaklagftqesfeacLTNQQLLNdvratvergskEFGVNATPTFFINGKKYAG 230
Cdd:cd02972   66 LHEA----------------------LADTALAR-----------ALGVTGTPTFVVNGEKYSG 96
 
Name Accession Description Interval E-value
Thioredoxin_4 pfam13462
Thioredoxin;
78-242 2.08e-60

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 187.55  E-value: 2.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827   78 KDMVYGKADAPVTIVEYASLTCPHCADFKLITFpKIKEKYIDTGKARLIFRDFPFDPR--ATAAVMLARCAPEDH--YFP 153
Cdd:pfam13462   3 TDPVIGNPDAPVTVVEYADLRCPHCAKFHEEVL-KLLEEYIDTGKVRFIIRDFPLDGEgeSLLAAMAARCAGDQSpeYFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  154 MIDLFFRQQQQWATAEDgkaallQIAKLAGFTQESFEACLTNQQLLNDVRATVERGsKEFGVNATPTFFINGKKYAGDLS 233
Cdd:pfam13462  82 VIDKLLYSQQEEWAQDL------ELAALAGLKDEEFEACLEEEDFLALVMADVKEA-RAAGINFTPTFIINGKKVDGPLT 154


                  ....*....
gi 260872827  234 FEEMSGFID 242
Cdd:pfam13462 155 YEELKKLID 163
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 88-245 4.83e-47

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 153.23  E-value: 4.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  88 PVTIVEYASLTCPHCADFKLiTFPKIKEKYIDtGKARLIFRDFPF-DPRATAAVMLARCAPE-DHYFPMIDLFFRQQQQW 165
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHP-ELPELLKKYVD-GKVRVVYRPFPLlHPDSLRAARAALCAADqGKFWAFHDALFANQPAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827 166 AtaedgKAALLQIAKLAGFTQESFEACLTNQQLLNDVRATVERGSKeFGVNATPTFFINGKKYAGDLSFEEMSGFIDSAL 245
Cdd:COG1651   79 T-----DDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQA-LGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 91-230 3.01e-11

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: 58.19  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  91 IVEYASLTCPHCADFKLITFPKIkekYIDTGKARLIFRDFPFDP----RATAAVMLARCAPEdhyfpmidlffrQQQQWA 166
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLL---YADDGGVRVVYRPFPLLGgmppNSLAAARAALAAAA------------QGKFEA 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260872827 167 TAEDgkaallqiaklagftqesfeacLTNQQLLNdvratvergskEFGVNATPTFFINGKKYAG 230
Cdd:cd02972   66 LHEA----------------------LADTALAR-----------ALGVTGTPTFVVNGEKYSG 96
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 85-226 1.11e-07

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: 50.36  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  85 ADAPVTIVEYASLTCPHCADF--KLITFPKIKEKYIDTGKARLIFRDFPFDP--RATAAVMLArcAPEDHYfpMIDLFFR 160
Cdd:cd03019   13 PSGKPEVIEFFSYGCPHCYNFepILEAWVKKLPKDVKFEKVPVVFGGGEGEPlaRAFYAAEAL--GLEDKL--HAALFEA 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260872827 161 QQQQwATAEDGKAALLQIAKLAGFTQESFEAcltnqqLLN--DVRATVERG---SKEFGVNATPTFFINGK 226
Cdd:cd03019   89 IHEK-RKRLLDPDDIRKIFLSQGVDKKKFDA------AYNsfSVKALVAKAeklAKKYKITGVPAFVVNGK 152
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 83-242 1.47e-07

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: 49.51  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  83 GKADAPVTIVEYASLTCPHCAdfKLitFPKIKEKYIDTGKARLIFRDFPF-----DPRATAAVMLARCAPeDHYFPMIDL 157
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCK--KL--APELEKLLKEDPDVRVVFKEFPIlgessVLAARVALAVWKNGP-GKYLEFHNA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827 158 FFRQQQQwATAEdgkaALLQIAKLAGFTqesfEACLTNQQLLNDVRATVER---GSKEFGVNATPTFFINGKKYAGDLSF 234
Cdd:cd03023   76 LMATRGR-LNEE----SLLRIAKKAGLD----EAKLKKDMDDPEIEATIDKnrqLARALGITGTPAFIIGDTVIPGAVPA 146


                 ....*...
gi 260872827 235 EEMSGFID 242
Cdd:cd03023  147 DTLKEAID 154
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 90-242 9.75e-05

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: 42.03  E-value: 9.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827   90 TIVEYASLTCPHCADFKlITFPKIKEKYidtGKARLIFRDFPFDPRATAAVMLARCAPEDHYFPMIDLFFRQQQ------ 163
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAK-ERLEKLAARY---GDVKVVYRPFPLAGAKKIGNVGPSNLPVKLKYMMADLERWAALygiplr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  164 ----------------QWATAED---------------------GKAALLQIAKLAGFTQESFEACLTNQQLLNDVRATV 206
Cdd:pfam01323  77 fpanflgnstranrlaLAAGAEGlaekvvrelfnalwgegaaitDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENT 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 260872827  207 ERGsKEFGVNATPTFFINGKKYAGDLSFEEMSGFID 242
Cdd:pfam01323 157 AAA-ISLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 175-226 1.82e-04

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 41.41  E-value: 1.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 260872827 175 LLQIAKLAGFTQESFEACLTNQQLLNDVRATVERgSKEFGVNATPTFFINGK 226
Cdd:COG2761  134 LLDLAAEVGLDAEEFRADLESDEAAAAVRADEAE-ARELGVTGVPTFVFDGK 184
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 68-237 1.34e-03

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 38.84  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827  68 AIEIAKPGKLKDMVYGKADAPVTIVEYASLTCPHCADFklitfpkikEKYIDTGKARLIFRDFPF-------DPRATAAV 140
Cdd:cd03020   58 AIDLSALPLDDAIVYGKGNGKRVVYVFTDPDCPYCRKL---------EKELKPNADGVTVRIFPVpilglpdSTAKAAAI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260872827 141 MlarCAPEdhyfpmidlffrQQQQWATAEDGKAALLQIAKlagftqesfeaCltnqqlLNDVRATVERGSKeFGVNATPT 220
Cdd:cd03020  129 W---CAKD------------RAKAWTDAMSGGKVPPPAAS-----------C------DNPVAANLALGRQ-LGVNGTPT 175

                        170
                 ....*....|....*...
gi 260872827 221 -FFINGKKYAGDLSFEEM 237
Cdd:cd03020  176 iVLADGRVVPGAPPAAQL 193
 
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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