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 ...
31-146
3.10e-14
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: 69.30 E-value: 3.10e-14
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
575-676
2.33e-40
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: 143.13 E-value: 2.33e-40
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ...
31-146
3.10e-14
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: 69.30 E-value: 3.10e-14
Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational ...
13-669
1.78e-56
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: 203.97 E-value: 1.78e-56
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
575-676
2.33e-40
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: 143.13 E-value: 2.33e-40
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ...
31-146
3.10e-14
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: 69.30 E-value: 3.10e-14
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
583-662
8.37e-05
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.
Pssm-ID: 239296 [Multi-domain] Cd Length: 105 Bit Score: 42.24 E-value: 8.37e-05
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
569-644
4.03e-03
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.
Pssm-ID: 239309 [Multi-domain] Cd Length: 123 Bit Score: 37.66 E-value: 4.03e-03
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
578-602
4.21e-03
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.
Pssm-ID: 239245 [Multi-domain] Cd Length: 93 Bit Score: 37.15 E-value: 4.21e-03
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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