SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
4-93
4.85e-05
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.
The actual alignment was detected with superfamily member pfam13623:
Pssm-ID: 463938 Cd Length: 145 Bit Score: 42.56 E-value: 4.85e-05
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
175-310
8.61e-11
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: 59.53 E-value: 8.61e-11
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
4-93
4.85e-05
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.
Pssm-ID: 463938 Cd Length: 145 Bit Score: 42.56 E-value: 4.85e-05
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
175-310
8.61e-11
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: 59.53 E-value: 8.61e-11
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
231-324
2.22e-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: 50.50 E-value: 2.22e-07
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
188-314
1.25e-06
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: 48.05 E-value: 1.25e-06
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
4-93
4.85e-05
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.
Pssm-ID: 463938 Cd Length: 145 Bit Score: 42.56 E-value: 4.85e-05
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
4-91
1.61e-04
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.
Pssm-ID: 433358 [Multi-domain] Cd Length: 162 Bit Score: 41.40 E-value: 1.61e-04
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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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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