The domain within your query sequence starts at position 349 and ends at position 514; the E-value for the NAT domain shown below is 3.5e-50.



PFAM accession number:PF04768
Interpro abstract (IPR006855):

The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetyl coenzyme A (CoA) to transfer an acetyl group to a substrate, a reaction implicated in various functions from bacterial antibiotic resistance to mammalian circadian rhythm and chromatin remodeling. The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoA donor to a primary amine of the acceptor. The GNAT proteins share a domain composed of four conserved sequence motifs A-D [ (PUBMED:9175471) (PUBMED:10940244) ]. This GNAT domain is named after yeast GCN5 (from General Control Nonrepressed) and related histone acetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residues of amino terminal histone tails, resulting in transcription activation. Another category of GNAT, the aminoglycoside N-acetyltransferases, confer antibiotic resistance by catalyzing the acetylation of amino groups in aminoglycoside antibiotics [ (PUBMED:12592013) ]. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes [ (PUBMED:9175471) (PUBMED:10940244) (PUBMED:12592013) (PUBMED:12527305) (PUBMED:15581578) ].

The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to 7 beta strands (B) and 4 helices (H) in the topology B1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may be from the same monomer or contributed by another [ (PUBMED:10940244) (PUBMED:15581578) ]. Motifs D (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core [ (PUBMED:10940244) (PUBMED:12527305) (PUBMED:15581578) ], while the N-terminal motif C (B1-H1) is less conserved.

This entry represents the vertebrate-like NAGS-type GNAT domain [ (PUBMED:23894642) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry NAT