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Conserved domains on  [gi|446764062|ref|WP_000841318|]
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MULTISPECIES: thioredoxin domain-containing protein [Bacillus]

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, ...
 54-214 4.99e-42

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


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 139.36  E-value: 4.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  54 PVKVVEFGDFKCPACRTWDvTVLPRLKEEYIDkGKVQLYFINFPFIGKDSDLGAAAGEAIYKQDKdsFWIFYDEIYQNQK 133
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFH-PELPELLKKYVD-GKVRVVYRPFPLLHPDSLRAARAALCAADQGK--FWAFHDALFANQP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062 134 KdteewITEDLLLSIVKEklPKVDVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNL--ANPDFDSMKKAID 211
Cdd:COG1651   77 A-----LTDDDLREIAKE--AGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLvsGAVPYEELEAALD 149


                 ...
gi 446764062 212 KEL 214
Cdd:COG1651  150 AAL 152
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 54-214 4.99e-42

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 139.36  E-value: 4.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  54 PVKVVEFGDFKCPACRTWDvTVLPRLKEEYIDkGKVQLYFINFPFIGKDSDLGAAAGEAIYKQDKdsFWIFYDEIYQNQK 133
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFH-PELPELLKKYVD-GKVRVVYRPFPLLHPDSLRAARAALCAADQGK--FWAFHDALFANQP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062 134 KdteewITEDLLLSIVKEklPKVDVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNL--ANPDFDSMKKAID 211
Cdd:COG1651   77 A-----LTDDDLREIAKE--AGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLvsGAVPYEELEAALD 149


                 ...
gi 446764062 212 KEL 214
Cdd:COG1651  150 AAL 152
Thioredoxin_4 pfam13462
Thioredoxin;
44-212 2.05e-36

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 125.53  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062   44 TQQSLGKDDAPVKVVEFGDFKCPACRTWDVTVLPrLKEEYIDKGKVQLYFINFPFIG-KDSDLGAAAGEAIYKQDKDSFW 122
Cdd:pfam13462   3 TDPVIGNPDAPVTVVEYADLRCPHCAKFHEEVLK-LLEEYIDTGKVRFIIRDFPLDGeGESLLAAMAARCAGDQSPEYFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  123 IFYDEIYQNQkkdteEWITEDLLLSivkeKLPKVDVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNL--AN 200
Cdd:pfam13462  82 VIDKLLYSQQ-----EEWAQDLELA----ALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKvdGP 152

                         170
                  ....*....|..
gi 446764062  201 PDFDSMKKAIDK 212
Cdd:pfam13462 153 LTYEELKKLIDD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 49-211 3.72e-21

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: 85.72  E-value: 3.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  49 GKDDAPVKVVEFGDFKCPACRTwdvtVLPRLKEEYIDKGKVQLYFINFPFIGKDSDLGAAAGEAIYKQDKDSFWIFYDEI 128
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKK----LAPELEKLLKEDPDVRVVFKEFPILGESSVLAARVALAVWKNGPGKYLEFHNAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062 129 YQNQKKdteewITEDLLLSIVKEKlpKVDVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNLAN--PDFDSM 206
Cdd:cd03023   77 MATRGR-----LNEESLLRIAKKA--GLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPgaVPADTL 149


                 ....*
gi 446764062 207 KKAID 211
Cdd:cd03023  150 KEAID 154
dsbG PRK11657
disulfide isomerase/thiol-disulfide oxidase; Provisional
 49-109 8.43e-05

disulfide isomerase/thiol-disulfide oxidase; Provisional


Pssm-ID: 183262 [Multi-domain]  Cd Length: 251  Bit Score: 42.26  E-value: 8.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446764062  49 GKDDAPVKVVEFGDFKCPACRT-WDvTVLPrlkeeYIDKGKVQLYFINFPFIGKDSDLGAAA 109
Cdd:PRK11657 113 GKADAPRIVYVFADPNCPYCKQfWQ-QARP-----WVDSGKVQLRHILVGIIKPDSPGKAAA 168
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 54-214 4.99e-42

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 139.36  E-value: 4.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  54 PVKVVEFGDFKCPACRTWDvTVLPRLKEEYIDkGKVQLYFINFPFIGKDSDLGAAAGEAIYKQDKdsFWIFYDEIYQNQK 133
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFH-PELPELLKKYVD-GKVRVVYRPFPLLHPDSLRAARAALCAADQGK--FWAFHDALFANQP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062 134 KdteewITEDLLLSIVKEklPKVDVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNL--ANPDFDSMKKAID 211
Cdd:COG1651   77 A-----LTDDDLREIAKE--AGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLvsGAVPYEELEAALD 149


                 ...
gi 446764062 212 KEL 214
Cdd:COG1651  150 AAL 152
Thioredoxin_4 pfam13462
Thioredoxin;
44-212 2.05e-36

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 125.53  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062   44 TQQSLGKDDAPVKVVEFGDFKCPACRTWDVTVLPrLKEEYIDKGKVQLYFINFPFIG-KDSDLGAAAGEAIYKQDKDSFW 122
Cdd:pfam13462   3 TDPVIGNPDAPVTVVEYADLRCPHCAKFHEEVLK-LLEEYIDTGKVRFIIRDFPLDGeGESLLAAMAARCAGDQSPEYFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  123 IFYDEIYQNQkkdteEWITEDLLLSivkeKLPKVDVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNL--AN 200
Cdd:pfam13462  82 VIDKLLYSQQ-----EEWAQDLELA----ALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKvdGP 152

                         170
                  ....*....|..
gi 446764062  201 PDFDSMKKAIDK 212
Cdd:pfam13462 153 LTYEELKKLIDD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 49-211 3.72e-21

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: 85.72  E-value: 3.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  49 GKDDAPVKVVEFGDFKCPACRTwdvtVLPRLKEEYIDKGKVQLYFINFPFIGKDSDLGAAAGEAIYKQDKDSFWIFYDEI 128
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKK----LAPELEKLLKEDPDVRVVFKEFPILGESSVLAARVALAVWKNGPGKYLEFHNAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062 129 YQNQKKdteewITEDLLLSIVKEKlpKVDVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNLAN--PDFDSM 206
Cdd:cd03023   77 MATRGR-----LNEESLLRIAKKA--GLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPgaVPADTL 149


                 ....*
gi 446764062 207 KKAID 211
Cdd:cd03023  150 KEAID 154
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 52-212 3.59e-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: 59.61  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  52 DAPVKVVEFGDFKCPACRTWDvTVLPRLKEEYIDKGKVQLYFINFPfiGKDSDLGA---AAGEAIYKQDKDSFWIFydEI 128
Cdd:cd03019   14 SGKPEVIEFFSYGCPHCYNFE-PILEAWVKKLPKDVKFEKVPVVFG--GGEGEPLArafYAAEALGLEDKLHAALF--EA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062 129 YQNQKKDteeWITEDLLLSIVKEKlpKVDVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNG----NLANPDFD 204
Cdd:cd03019   89 IHEKRKR---LLDPDDIRKIFLSQ--GVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGkyvvNPSAIGGD 163


                 ....*...
gi 446764062 205 SMKKAIDK 212
Cdd:cd03019  164 DTLQVLDE 171
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 57-196 2.09e-09

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: 52.79  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062  57 VVEFGDFKCPACRTWDvtvlPRLKE-EYIDKGKVQLYFINFPFIGKDSDLGAAAGEAIY-KQDKDSFWIFYDEIyqnqkk 134
Cdd:cd02972    1 IVEFFDPLCPYCYLFE----PELEKlLYADDGGVRVVYRPFPLLGGMPPNSLAAARAALaAAAQGKFEALHEAL------ 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446764062 135 dteewitedlllsivkeklpkvdvaqfkkdlhskeikekvrKDSDRAQKLKVQGAPSVYVNG 196
Cdd:cd02972   71 -----------------------------------------ADTALARALGVTGTPTFVVNG 91
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 90-211 5.93e-06

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: 45.11  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446764062   90 QLYFINFPFIG---KDSDLGAAAGEAIYKQDK--DSFWIFYDEIYQNQKKDTEEwiteDLLLSIVkEKLpKVDVAQFKKD 164
Cdd:pfam01323  69 ALYGIPLRFPAnflGNSTRANRLALAAGAEGLaeKVVRELFNALWGEGAAITDD----SVLREVA-EKA-GLDAEEFDEF 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 446764062  165 LHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNLA--NPDFDSMKKAID 211
Cdd:pfam01323 143 LDSPAVKEAVRENTAAAISLGVFGVPTFVVGGKMVfgADRLDTLADALA 191
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 142-215 4.02e-05

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: 42.95  E-value: 4.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446764062 142 EDLLLSIVKEklpkV--DVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSVYVNGNLANP---DFDSMKKAIDKELK 215
Cdd:COG2761  131 REVLLDLAAE----VglDAEEFRADLESDEAAAAVRADEAEARELGVTGVPTFVFDGKYAVSgaqPYEVFEQALRQALA 205
dsbG PRK11657
disulfide isomerase/thiol-disulfide oxidase; Provisional
 49-109 8.43e-05

disulfide isomerase/thiol-disulfide oxidase; Provisional


Pssm-ID: 183262 [Multi-domain]  Cd Length: 251  Bit Score: 42.26  E-value: 8.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446764062  49 GKDDAPVKVVEFGDFKCPACRT-WDvTVLPrlkeeYIDKGKVQLYFINFPFIGKDSDLGAAA 109
Cdd:PRK11657 113 GKADAPRIVYVFADPNCPYCKQfWQ-QARP-----WVDSGKVQLRHILVGIIKPDSPGKAAA 168
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 157-192 9.42e-04

DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239323 [Multi-domain]  Cd Length: 193  Bit Score: 38.84  E-value: 9.42e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446764062 157 DVAQFKKDLHSKEIKEKVRKDSDRAQKLKVQGAPSV 192
Cdd:cd03025  138 DVEEFLEDFQSDEAKQAIQEDQKLARELGINGFPTL 173
 
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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