protein-disulfide reductase DsbD family protein, similar to DsbD that facilitates the formation of correct disulfide bonds in some periplasmic proteins and is required for the assembly of the periplasmic c-type cytochromes
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ...
47-147
6.69e-16
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a transmembrane electron transporter. DsbD binds to a DsbC dimer and selectively activates it using electrons from the cytoplasm. The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD.
:
Pssm-ID: 463273 [Multi-domain] Cd Length: 115 Bit Score: 74.31 E-value: 6.69e-16
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
578-679
1.00e-34
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.
Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 127.33 E-value: 1.00e-34
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ...
47-147
6.69e-16
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a transmembrane electron transporter. DsbD binds to a DsbC dimer and selectively activates it using electrons from the cytoplasm. The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD.
Pssm-ID: 463273 [Multi-domain] Cd Length: 115 Bit Score: 74.31 E-value: 6.69e-16
Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational ...
7-675
1.73e-60
Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational modification, protein turnover, chaperones, Energy production and conversion];
Pssm-ID: 443377 [Multi-domain] Cd Length: 681 Bit Score: 215.15 E-value: 1.73e-60
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
578-679
1.00e-34
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.
Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 127.33 E-value: 1.00e-34
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ...
47-147
6.69e-16
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a transmembrane electron transporter. DsbD binds to a DsbC dimer and selectively activates it using electrons from the cytoplasm. The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD.
Pssm-ID: 463273 [Multi-domain] Cd Length: 115 Bit Score: 74.31 E-value: 6.69e-16
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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