SMART: Pfam domain Acetyltransf

The domain within your query sequence starts at position 46 and ends at position 129; the E-value for the Acetyltransf_1 domain shown below is 7.1e-18.

EDENGKIVGYVLAKMEEDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAK
YVSLHVRKSNRAALHLYSNTLNFQ

Acetyltransf_1

PFAM accession number:	PF00583
Interpro abstract (IPR000182):	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 N-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. Some proteins known to contain a GNAT domain: Yeast GCN5 and Hat1, which are histone acetyltransferases (EC 2.3.1.48). Human PCAF, a histone acetyltransferase. Mammalian serotonin N-acetyltransferase (SNAT) or arylalkylamine NAT (AANAT), which acetylates serotonin into a circadian neurohormone that may participate in light-dark rhythms, and human mood and behavior. Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC 2.3.1.4). Escherichia coli rimI and rimJ, which acetylate the N-terminal alanine of ribosomal proteins S18 and S5, respectively (EC 2.3.1.128). Mycobacterium tuberculosis aminoglycoside 2'-N-acetyltransferase (aac), which acetylates the 2' hydroxyl or amino group of a broad spectrum of aminoglycoside antibiotics. Bacillus subtilis bltD and paiA, which acetylate spermine and spermidine. This entry represents the entire GNAT domain.
GO function:	N-acetyltransferase activity (GO:0008080)

PFAM accession number:

PF00583

Interpro abstract (IPR000182):

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 N-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.

Some proteins known to contain a GNAT domain:

Yeast GCN5 and Hat1, which are histone acetyltransferases (EC 2.3.1.48).
Human PCAF, a histone acetyltransferase.
Mammalian serotonin N-acetyltransferase (SNAT) or arylalkylamine NAT (AANAT), which acetylates serotonin into a circadian neurohormone that may participate in light-dark rhythms, and human mood and behavior.
Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC 2.3.1.4).
Escherichia coli rimI and rimJ, which acetylate the N-terminal alanine of ribosomal proteins S18 and S5, respectively (EC 2.3.1.128).
Mycobacterium tuberculosis aminoglycoside 2'-N-acetyltransferase (aac), which acetylates the 2' hydroxyl or amino group of a broad spectrum of aminoglycoside antibiotics.
Bacillus subtilis bltD and paiA, which acetylate spermine and spermidine.

This entry represents the entire GNAT domain.

GO function:

N-acetyltransferase activity (GO:0008080)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Acetyltransf_1