Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_003114799 183 aa linear BCT 20-JUL-2024 ACCESSION WP_003114799 VERSION WP_003114799.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 183) AUTHORS Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A. TITLE Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT) JOURNAL Int J Mol Sci 17 (7), 1018 (2016) PUBMED 27367672 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 183) AUTHORS Favrot,L., Blanchard,J.S. and Vergnolle,O. TITLE Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation JOURNAL Biochemistry 55 (7), 989-1002 (2016) PUBMED 26818562 REFERENCE 3 (residues 1 to 183) AUTHORS Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S., Roderick,S.L. and Blanchard,J.S. TITLE Structure and functions of the GNAT superfamily of acetyltransferases JOURNAL Arch Biochem Biophys 433 (1), 212-226 (2005) PUBMED 15581578 REFERENCE 4 (residues 1 to 183) AUTHORS Dyda,F., Klein,D.C. and Hickman,A.B. TITLE GCN5-related N-acetyltransferases: a structural overview JOURNAL Annu Rev Biophys Biomol Struct 29, 81-103 (2000) PUBMED 10940244 REMARK Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi] 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 11447364 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..183 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..183 /product="GNAT family N-acetyltransferase" /EC_number="2.3.-.-" /GO_function="GO:0008080 - N-acetyltransferase activity [Evidence IEA]" /GO_function="GO:0016746 - acyltransferase activity [Evidence IEA]" /calculated_mol_wt=20629 Region 10..177 /region_name="RimL" /note="Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones]; COG1670" /db_xref="CDD:441276" ORIGIN 1 mfilpissdl hlelldqpra eelfrlvran sehlapwmpw vpltqsvddt rrfigegqrl 61 waerrscrcg ivesgclvgv idlhdfteds rsasigywla asaqgrglla ralgktielg 121 flgydrqrlv ircstenlrs qraaerqgfr rdgviranei iagrahdhai ytllrsewha 181 aha