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Protein Domain : Gcn5-related N-acetyltransferase (GNAT) domain, ATAT-type

Primary Identifier  IPR007965 Type  Domain
Short Name  GNAT_ATAT
description  The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetylcoenzyme A (CoA) to transfer an acetyl group to a substrate, a reactionimplicated in various functions from bacterial antibiotic resistance tomammalian circadian rhythm and chromatin remodeling. The Gcn5-relatedN-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoAdonor to a primary amine of the acceptor. The GNAT proteins share a domaincomposed of four conserved sequence motifs A-D [, ]. 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 []. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes [, , , , ].The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to7 beta strands (B) and 4 helices (H) in the topologyB1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may befrom the same monomer or contributed by another [, ]. MotifsD (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core[, , ], while the N-terminal motif C (B1-H1) is less conserved.This entry represents the ATAT-type of the GNAT domain []. Proteins containing this domain include alpha-tubulin N-acetyltransferase, originally known as mechanosensory abnormality protein 17 (Mec-17), as it is the protein product of one of the 18 genes required for the development and function of the touch receptor neuron for gentle touch []. Mec-17 specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules []. It is inefficient, and its activity is enhanced when tubulin is incorporated in microtubules []. It may affect microtubule stability and regulate microtubule dynamics.

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10 Protein Domain Regions