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LOCUS WP_003092626 242 aa linear BCT 20-NOV-2023 isomerase/oxidoreductase DsbC [Pseudomonas]. ACCESSION WP_003092626 VERSION WP_003092626.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 242) AUTHORS Fabianek,R.A., Hennecke,H. and Thony-Meyer,L. TITLE Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli JOURNAL FEMS Microbiol. Rev. 24 (3), 303-316 (2000) PUBMED 10841975 REFERENCE 2 (residues 1 to 242) AUTHORS Chen,J., Song,J.L., Zhang,S., Wang,Y., Cui,D.F. and Wang,C.C. TITLE Chaperone activity of DsbC JOURNAL J. Biol. Chem. 274 (28), 19601-19605 (1999) PUBMED 10391895 REFERENCE 3 (residues 1 to 242) AUTHORS Frishman,D. TITLE DSBC protein: a new member of the thioredoxin fold-containing family JOURNAL Biochem. Biophys. Res. Commun. 219 (3), 686-689 (1996) PUBMED 8645242 REFERENCE 4 (residues 1 to 242) AUTHORS Zapun,A., Missiakas,D., Raina,S. and Creighton,T.E. TITLE Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli JOURNAL Biochemistry 34 (15), 5075-5089 (1995) PUBMED 7536035 REFERENCE 5 (residues 1 to 242) AUTHORS Bardwell,J.C. TITLE Building bridges: disulphide bond formation in the cell JOURNAL Mol. Microbiol. 14 (2), 199-205 (1994) PUBMED 7830566 REFERENCE 6 (residues 1 to 242) AUTHORS Missiakas,D., Georgopoulos,C. and Raina,S. TITLE The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation JOURNAL EMBO J. 13 (8), 2013-2020 (1994) PUBMED 8168498 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: NF008129.0 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK10877 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..242 /organism="Pseudomonas" /db_xref="taxon:286" gene 1..242 /gene="dsbC" Protein 1..242 /product="bifunctional protein-disulfide isomerase/oxidoreductase DsbC" /EC_number="5.3.4.1" /GO_component="GO:0042597 - periplasmic space [Evidence IEA]" /calculated_mol_wt=25964 Region 1..237 /region_name="Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold" /note="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...; cl00388" /db_xref="CDD:469754" Site order(39..47,50..60,62..78) /site_type="other" /note="dimerization domain [polypeptide binding]" /db_xref="CDD:239318" Site 71..78 /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:239318" Site order(130,133) /site_type="active" /note="catalytic residues [active]" /db_xref="CDD:239318" ORIGIN 1 mrvtrflaaa alglmstlal adnadqnirk tlqalqpdlp idsiassplq glyqvqlkgg 61 rvlyasadgq fvmqgylyqv kdgkpvnlte kaesqaiaka ingvpasemv vypakgqaka 121 hitvftdttc pycqklhaev pdlteqgiev rymafprqgp qsagdkqlqa vwcakeptka 181 mdammngkei kssecknpvd kqfqmgqmvg vqgtpaivla ngqllpgyqp akqlaklale 241 ak