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Conserved domains on  [gi|15596179|ref|NP_249673|]
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hypothetical protein PA0982 [Pseudomonas aeruginosa PAO1]

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, ...
 20-176 4.50e-29

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


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 105.08  E-value: 4.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  20 TINEYADLECPFCKVYTPRLKRWVDSHTD--VNLVWRHLPLqmHGEAARHQARLVECAGIQGgakAFWSAIDAIFAQSAG 97
Cdd:COG1651   3 TVVEFFDYQCPYCARFHPELPELLKKYVDgkVRVVYRPFPL--LHPDSLRAARAALCAADQG---KFWAFHDALFANQPA 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596179  98 NGGGLPGGTLDFPDLDQARLEKCAKDMDlVDQLIKTDIDTARSNGITATPTLVIQDnqtgrsVKLEGMADETTLLSAID 176
Cdd:COG1651  78 LTDDDLREIAKEAGLDAAKFDACLNSGA-VAAKVEADTALAQALGVTGTPTFVVNG------KLVSGAVPYEELEAALD 149
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 20-176 4.50e-29

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 105.08  E-value: 4.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  20 TINEYADLECPFCKVYTPRLKRWVDSHTD--VNLVWRHLPLqmHGEAARHQARLVECAGIQGgakAFWSAIDAIFAQSAG 97
Cdd:COG1651   3 TVVEFFDYQCPYCARFHPELPELLKKYVDgkVRVVYRPFPL--LHPDSLRAARAALCAADQG---KFWAFHDALFANQPA 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596179  98 NGGGLPGGTLDFPDLDQARLEKCAKDMDlVDQLIKTDIDTARSNGITATPTLVIQDnqtgrsVKLEGMADETTLLSAID 176
Cdd:COG1651  78 LTDDDLREIAKEAGLDAAKFDACLNSGA-VAAKVEADTALAQALGVTGTPTFVVNG------KLVSGAVPYEELEAALD 149
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 21-153 1.49e-13

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: 63.19  E-value: 1.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  21 INEYADLECPFCKVYTPRLKRWVDSHT-DVNLVWRHLPL-QMHGEAARHQARLVECAGIQGGAKAFWSAIDaifaqsagn 98
Cdd:cd02972   1 IVEFFDPLCPYCYLFEPELEKLLYADDgGVRVVYRPFPLlGGMPPNSLAAARAALAAAAQGKFEALHEALA--------- 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15596179  99 ggglpggtldfpdldqarlekcakdmdlvdqliktDIDTARSNGITATPTLVIQD 153
Cdd:cd02972  72 -----------------------------------DTALARALGVTGTPTFVVNG 91
Thioredoxin_4 pfam13462
Thioredoxin;
12-176 1.29e-12

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 62.36  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179    12 YGDAKARWTINEYADLECPFCKVYT----PRLKRWVDShTDVNLVWRHLPLQMHGEAARhQARLVECAGIQgGAKAFWSA 87
Cdd:pfam13462   7 IGNPDAPVTVVEYADLRCPHCAKFHeevlKLLEEYIDT-GKVRFIIRDFPLDGEGESLL-AAMAARCAGDQ-SPEYFLVI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179    88 IDAIFAQSAGNGGGLPGGTLDFpdLDQARLEKCAKDMDLvDQLIKTDIDTARSNGITATPTLVIQDnqtgrsVKLEGMAD 167
Cdd:pfam13462  84 DKLLYSQQEEWAQDLELAALAG--LKDEEFEACLEEEDF-LALVMADVKEARAAGINFTPTFIING------KKVDGPLT 154


                  ....*....
gi 15596179   168 ETTLLSAID 176
Cdd:pfam13462 155 YEELKKLID 163
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 20-176 4.50e-29

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 105.08  E-value: 4.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  20 TINEYADLECPFCKVYTPRLKRWVDSHTD--VNLVWRHLPLqmHGEAARHQARLVECAGIQGgakAFWSAIDAIFAQSAG 97
Cdd:COG1651   3 TVVEFFDYQCPYCARFHPELPELLKKYVDgkVRVVYRPFPL--LHPDSLRAARAALCAADQG---KFWAFHDALFANQPA 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596179  98 NGGGLPGGTLDFPDLDQARLEKCAKDMDlVDQLIKTDIDTARSNGITATPTLVIQDnqtgrsVKLEGMADETTLLSAID 176
Cdd:COG1651  78 LTDDDLREIAKEAGLDAAKFDACLNSGA-VAAKVEADTALAQALGVTGTPTFVVNG------KLVSGAVPYEELEAALD 149
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 21-153 1.49e-13

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: 63.19  E-value: 1.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  21 INEYADLECPFCKVYTPRLKRWVDSHT-DVNLVWRHLPL-QMHGEAARHQARLVECAGIQGGAKAFWSAIDaifaqsagn 98
Cdd:cd02972   1 IVEFFDPLCPYCYLFEPELEKLLYADDgGVRVVYRPFPLlGGMPPNSLAAARAALAAAAQGKFEALHEALA--------- 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15596179  99 ggglpggtldfpdldqarlekcakdmdlvdqliktDIDTARSNGITATPTLVIQD 153
Cdd:cd02972  72 -----------------------------------DTALARALGVTGTPTFVVNG 91
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 13-176 7.70e-13

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: 62.61  E-value: 7.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  13 GDAKARWTINEYADLECPFCKVYTPRLKRWVDSHTDVNLVWRHLPLQmhGEAARHQARLVECAGIQGGAKaFWSAIDAIF 92
Cdd:cd03023   1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPIL--GESSVLAARVALAVWKNGPGK-YLEFHNALM 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  93 AQSAGNGGGLPGGTLDFPDLDQARLEKCAKDMDlVDQLIKTDIDTARSNGITATPTLVIqdnqtGRSVkLEGMADETTLL 172
Cdd:cd03023  78 ATRGRLNEESLLRIAKKAGLDEAKLKKDMDDPE-IEATIDKNRQLARALGITGTPAFII-----GDTV-IPGAVPADTLK 150


                ....
gi 15596179 173 SAID 176
Cdd:cd03023 151 EAID 154
Thioredoxin_4 pfam13462
Thioredoxin;
12-176 1.29e-12

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 62.36  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179    12 YGDAKARWTINEYADLECPFCKVYT----PRLKRWVDShTDVNLVWRHLPLQMHGEAARhQARLVECAGIQgGAKAFWSA 87
Cdd:pfam13462   7 IGNPDAPVTVVEYADLRCPHCAKFHeevlKLLEEYIDT-GKVRFIIRDFPLDGEGESLL-AAMAARCAGDQ-SPEYFLVI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179    88 IDAIFAQSAGNGGGLPGGTLDFpdLDQARLEKCAKDMDLvDQLIKTDIDTARSNGITATPTLVIQDnqtgrsVKLEGMAD 167
Cdd:pfam13462  84 DKLLYSQQEEWAQDLELAALAG--LKDEEFEACLEEEDF-LALVMADVKEARAAGINFTPTFIING------KKVDGPLT 154


                  ....*....
gi 15596179   168 ETTLLSAID 176
Cdd:pfam13462 155 YEELKKLID 163
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 20-153 3.66e-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: 42.42  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179    20 TINEYADLECPFCKVYTPRLKRWVDSHTDVNLVWRHLPL-------------------QMHGEAARHQA----------- 69
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLagakkignvgpsnlpvklkYMMADLERWAAlygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179    70 ---------RLVECAGIQG-GAKAFWSAIDAIFAQSAgnggglpggtldfPDLDQARLEKCAKDM-------------DL 126
Cdd:pfam01323  81 flgnstranRLALAAGAEGlAEKVVRELFNALWGEGA-------------AITDDSVLREVAEKAgldaeefdefldsPA 147

                         170       180
                  ....*....|....*....|....*..
gi 15596179   127 VDQLIKTDIDTARSNGITATPTLVIQD 153
Cdd:pfam01323 148 VKEAVRENTAAAISLGVFGVPTFVVGG 174
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 26-171 1.20e-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: 38.07  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  26 DLECPFCKVYTPRLKRWVDshtDVNLVWRHLPLQMHGEAARhQARLVECAGIQggAKAFWSAIDAifaqsagnggglpgg 105
Cdd:cd03020  86 DPDCPYCRKLEKELKPNAD---GVTVRIFPVPILGLPDSTA-KAAAIWCAKDR--AKAWTDAMSG--------------- 144

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596179 106 tldfpDLDQARLEKCAKDMDLVDQLiktdidtARSNGITATPTLVIQDnqtGRsvKLEGMADETTL 171
Cdd:cd03020 145 -----GKVPPPAASCDNPVAANLAL-------GRQLGVNGTPTIVLAD---GR--VVPGAPPAAQL 193
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 70-176 1.26e-03

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: 37.94  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596179  70 RLVECAGIQGGAKAFWSAI-DAIFAQSAgnggglpggtldfpDL-DQARLEKCAK----DMDLVDQL---------IKTD 134
Cdd:COG2761  99 RLLKAAELQGKQDALLEALfEAYFTEGR--------------DIgDREVLLDLAAevglDAEEFRADlesdeaaaaVRAD 164

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15596179 135 IDTARSNGITATPTLVIqdnqtGRSVKLEGMADETTLLSAID 176
Cdd:COG2761 165 EAEARELGVTGVPTFVF-----DGKYAVSGAQPYEVFEQALR 201
 
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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