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LOCUS WP_016962163 84 aa linear BCT 22-OCT-2024 ACCESSION WP_016962163 VERSION WP_016962163.1 KEYWORDS RefSeq. SOURCE Enterovibrio ORGANISM Enterovibrio Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae. REFERENCE 1 (residues 1 to 84) AUTHORS Fernandes,A.P. and Holmgren,A. TITLE Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system JOURNAL Antioxid Redox Signal 6 (1), 63-74 (2004) PUBMED 14713336 REFERENCE 2 (residues 1 to 84) AUTHORS Powis,G. and Montfort,W.R. TITLE Properties and biological activities of thioredoxins JOURNAL Annu Rev Biophys Biomol Struct 30, 421-455 (2001) PUBMED 11441809 REFERENCE 3 (residues 1 to 84) AUTHORS Arner,E.S. and Holmgren,A. TITLE Physiological functions of thioredoxin and thioredoxin reductase JOURNAL Eur J Biochem 267 (20), 6102-6109 (2000) PUBMED 11012661 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10530477 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..84 /organism="Enterovibrio" /db_xref="taxon:188143" Protein 1..84 /product="glutaredoxin family protein" /calculated_mol_wt=9135 Region 3..78 /region_name="Glrx-like" /note="Glutaredoxin-like domain (DUF836); pfam05768" /db_xref="CDD:399055" ORIGIN 1 malilysteg chlceeamal yqaadnsaal nvidiafndt lfsrygvtip vishqtqdgs 61 videlswpfd sfalttwlvk hgid