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_003082887 177 aa linear BCT 02-MAR-2025 ACCESSION WP_003082887 VERSION WP_003082887.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 177) AUTHORS Chinenov,Y. TITLE A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity? JOURNAL Trends Biochem Sci 27 (3), 115-117 (2002) PUBMED 11893502 REFERENCE 2 (residues 1 to 177) AUTHORS Neuwald,A.F. and Landsman,D. TITLE GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein JOURNAL Trends Biochem Sci 22 (5), 154-155 (1997) PUBMED 9175471 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 :: NF012792.6 Evidence Source :: EMBL-EBI Source Identifier :: PF00583.31 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..177 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..177 /product="GNAT family N-acetyltransferase" /EC_number="2.3.1.-" /GO_function="GO:0016747 - acyltransferase activity, transferring groups other than amino-acyl groups [Evidence IEA]" /calculated_mol_wt=19937 Region 12..169 /region_name="N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of an acyl group to a substrate" /note="NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, from bacterial antibiotic resistance to circadian rhythms in mammals. Members...; cl17182" /db_xref="CDD:473072" Site order(91..93,103..104) /site_type="other" /note="Coenzyme A binding pocket [chemical binding]" /db_xref="CDD:173926" ORIGIN 1 mtaesptirl eryserhveg ltalyndpav arqvlqmpyq sveqrrkrlh dsadddrlli 61 lvalhqgdvi gsasleqhpr irrshsgsig mgvavawqgk gvgsrllgel ldiadnwmnl 121 rrveltvytd napalalyrk fgfetegemr dyavrdgrfv dvysmarlrr vegrvge