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Conserved domains on  [gi|1467773860|ref|WP_116994117|]
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MULTISPECIES: DsbA family protein [Enterobacteriaceae]

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 ...
134-313 3.16e-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 cd03023:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 154  Bit Score: 138.11  E-value: 3.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 134 GPDNADVAVIEFFDYMCHFCQQSSPVLEKAIAENKNVRTFFKDFTIFADRtpiSGMGAKIGLYIfNKYGQEKYYEFHNKL 213
Cdd:cd03023     1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGES---SVLAARVALAV-WKNGPGKYLEFHNAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 214 MSEAGRAMKDRkdytpsnLAALVNGLGYKEildqqgNFLLTVEMRDQLQNVLDANMMLADKLNYSGTPVFIVMnmknpqn 293
Cdd:cd03023    77 MATRGRLNEES-------LLRIAKKAGLDE------AKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIG------- 136
                         170       180
                  ....*....|....*....|
gi 1467773860 294 ktTTIMPGAPDFYRLQQAID 313
Cdd:cd03023   137 --DTVIPGAVPADTLKEAID 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 ...
134-313 3.16e-40

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: 138.11  E-value: 3.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 134 GPDNADVAVIEFFDYMCHFCQQSSPVLEKAIAENKNVRTFFKDFTIFADRtpiSGMGAKIGLYIfNKYGQEKYYEFHNKL 213
Cdd:cd03023     1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGES---SVLAARVALAV-WKNGPGKYLEFHNAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 214 MSEAGRAMKDRkdytpsnLAALVNGLGYKEildqqgNFLLTVEMRDQLQNVLDANMMLADKLNYSGTPVFIVMnmknpqn 293
Cdd:cd03023    77 MATRGRLNEES-------LLRIAKKAGLDE------AKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIG------- 136
                         170       180
                  ....*....|....*....|
gi 1467773860 294 ktTTIMPGAPDFYRLQQAID 313
Cdd:cd03023   137 --DTVIPGAVPADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
139-316 4.69e-18

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 79.66  E-value: 4.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 139 DVAVIEFFDYMCHFCQQSSPVLEKAIAE--NKNVRTFFKDFTIFAdrtPISGMGAKIGLYIFNkygQEKYYEFHNKLMSe 216
Cdd:COG1651     1 KVTVVEFFDYQCPYCARFHPELPELLKKyvDGKVRVVYRPFPLLH---PDSLRAARAALCAAD---QGKFWAFHDALFA- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 217 agramkDRKDYTPSNLAALVNGLGykeiLDQQGnflLTVEMRDQ-LQNVLDANMMLADKLNYSGTPVFIVMNmknpqnkt 295
Cdd:COG1651    74 ------NQPALTDDDLREIAKEAG----LDAAK---FDACLNSGaVAAKVEADTALAQALGVTGTPTFVVNG-------- 132
                         170       180
                  ....*....|....*....|.
gi 1467773860 296 tTIMPGAPDFYRLQQAIDKAK 316
Cdd:COG1651   133 -KLVSGAVPYEELEAALDAAL 152
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
141-313 2.26e-07

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: 50.12  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 141 AVIEFFDYMCHFCQQSSPVLEKAIAENKNVRTFFKDFTIFADRtPISGMG------------------------------ 190
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLAGAK-KIGNVGpsnlpvklkymmadlerwaalygiplrfpa 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 191 --------AKIGLYIFNKYGQ--EKYYEFHNKLMSEaGRAMKDrkdytPSNLAALVNGLG-----YKEILDQQGNflltv 255
Cdd:pfam01323  80 nflgnstrANRLALAAGAEGLaeKVVRELFNALWGE-GAAITD-----DSVLREVAEKAGldaeeFDEFLDSPAV----- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1467773860 256 emrdqlQNVLDANMMLADKLNYSGTPVFIVmnmknpQNKTttiMPGAPDFYRLQQAID 313
Cdd:pfam01323 149 ------KEAVRENTAAAISLGVFGVPTFVV------GGKM---VFGADRLDTLADALA 191
 
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 ...
134-313 3.16e-40

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: 138.11  E-value: 3.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 134 GPDNADVAVIEFFDYMCHFCQQSSPVLEKAIAENKNVRTFFKDFTIFADRtpiSGMGAKIGLYIfNKYGQEKYYEFHNKL 213
Cdd:cd03023     1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGES---SVLAARVALAV-WKNGPGKYLEFHNAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 214 MSEAGRAMKDRkdytpsnLAALVNGLGYKEildqqgNFLLTVEMRDQLQNVLDANMMLADKLNYSGTPVFIVMnmknpqn 293
Cdd:cd03023    77 MATRGRLNEES-------LLRIAKKAGLDE------AKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIG------- 136
                         170       180
                  ....*....|....*....|
gi 1467773860 294 ktTTIMPGAPDFYRLQQAID 313
Cdd:cd03023   137 --DTVIPGAVPADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
139-316 4.69e-18

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 79.66  E-value: 4.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 139 DVAVIEFFDYMCHFCQQSSPVLEKAIAE--NKNVRTFFKDFTIFAdrtPISGMGAKIGLYIFNkygQEKYYEFHNKLMSe 216
Cdd:COG1651     1 KVTVVEFFDYQCPYCARFHPELPELLKKyvDGKVRVVYRPFPLLH---PDSLRAARAALCAAD---QGKFWAFHDALFA- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 217 agramkDRKDYTPSNLAALVNGLGykeiLDQQGnflLTVEMRDQ-LQNVLDANMMLADKLNYSGTPVFIVMNmknpqnkt 295
Cdd:COG1651    74 ------NQPALTDDDLREIAKEAG----LDAAK---FDACLNSGaVAAKVEADTALAQALGVTGTPTFVVNG-------- 132
                         170       180
                  ....*....|....*....|.
gi 1467773860 296 tTIMPGAPDFYRLQQAIDKAK 316
Cdd:COG1651   133 -KLVSGAVPYEELEAALDAAL 152
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
142-241 9.73e-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: 54.72  E-value: 9.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 142 VIEFFDYMCHFCQQSSPVLEKAIAEN-KNVRTFFKDFTIFADRTPISGMGAKIGLYIfnkYGQEKYYEFHNKLMSEAgRA 220
Cdd:cd02972     1 IVEFFDPLCPYCYLFEPELEKLLYADdGGVRVVYRPFPLLGGMPPNSLAAARAALAA---AAQGKFEALHEALADTA-LA 76
                          90       100
                  ....*....|....*....|.
gi 1467773860 221 MKDRKDYTPsnlAALVNGLGY 241
Cdd:cd02972    77 RALGVTGTP---TFVVNGEKY 94
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
141-313 2.26e-07

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: 50.12  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 141 AVIEFFDYMCHFCQQSSPVLEKAIAENKNVRTFFKDFTIFADRtPISGMG------------------------------ 190
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLAGAK-KIGNVGpsnlpvklkymmadlerwaalygiplrfpa 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 191 --------AKIGLYIFNKYGQ--EKYYEFHNKLMSEaGRAMKDrkdytPSNLAALVNGLG-----YKEILDQQGNflltv 255
Cdd:pfam01323  80 nflgnstrANRLALAAGAEGLaeKVVRELFNALWGE-GAAITD-----DSVLREVAEKAGldaeeFDEFLDSPAV----- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1467773860 256 emrdqlQNVLDANMMLADKLNYSGTPVFIVmnmknpQNKTttiMPGAPDFYRLQQAID 313
Cdd:pfam01323 149 ------KEAVRENTAAAISLGVFGVPTFVV------GGKM---VFGADRLDTLADALA 191
Thioredoxin_4 pfam13462
Thioredoxin;
130-314 5.63e-07

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 48.49  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 130 TPNYGPDNADVAVIEFFDYMCHFC----QQSSPVLEKAIAENKnVRTFFKDFtifadrtpisgmgakiglyIFNKYGQEK 205
Cdd:pfam13462   4 DPVIGNPDAPVTVVEYADLRCPHCakfhEEVLKLLEEYIDTGK-VRFIIRDF-------------------PLDGEGESL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 206 --------YYEFHNKLMSEAGRAMKDRKD--YTPSNLAALVNGlgykeiLDQQGNFLLTvemRDQLQNVLDANMMLADKL 275
Cdd:pfam13462  64 laamaarcAGDQSPEYFLVIDKLLYSQQEewAQDLELAALAGL------KDEEFEACLE---EEDFLALVMADVKEARAA 134
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1467773860 276 NYSGTPVFIVmnmkNPQNKTttimpGAPDFYRLQQAIDK 314
Cdd:pfam13462 135 GINFTPTFII----NGKKVD-----GPLTYEELKKLIDD 164
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
137-285 3.88e-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: 37.65  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 137 NADVAVIEFFDYMCHFCQQSSPVLEKAIAEN-KNVR------TFFKDFTIFADRT----PISGMGAKIGLYIFNKYGQEK 205
Cdd:cd03019    14 SGKPEVIEFFSYGCPHCYNFEPILEAWVKKLpKDVKfekvpvVFGGGEGEPLARAfyaaEALGLEDKLHAALFEAIHEKR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1467773860 206 YYEFHNKLMSEAGR-AMKDRKDYTpsnlaALVNGLGYKEILDQQgnflltvemrdqlqnvldanMMLADKLNYSGTPVFI 284
Cdd:cd03019    94 KRLLDPDDIRKIFLsQGVDKKKFD-----AAYNSFSVKALVAKA--------------------EKLAKKYKITGVPAFV 148

                  .
gi 1467773860 285 V 285
Cdd:cd03019   149 V 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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