The domain within your query sequence starts at position 26 and ends at position 106; the E-value for the Acetyltransf_CG domain shown below is 6e-25.



PFAM accession number:PF14542
Interpro abstract (IPR031165):

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.

The entry represents the NAGS-type GNAT domain [(PUBMED:23894642), (PUBMED:18709443)].

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