InterPro domain: IPR032672

This entry includes bacterial tRNA(Met) cytidine acetyltransferase TmcA, budding yeast Kre33, fission yeast and mammalian N-acetyltransferase 10 (NAT10). They consist of an RNA helicase domain and a GCN5-related N-acetyltransferase (GNAT) domain.

TmcA catalyses the formation of N(4)-acetylcytidine (ac4C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and either ATP or GTP [ 1 ]. This modification is thought to ensure precise recognition of the AUG codon by strengthening C-G base-pair interaction and also prevent misrecognition of the near cognate AUA codon [ 2 ].

Kre33 and NAT10 are RNA cytidine acetyltransferases with specificity toward both 18S rRNA and tRNAs [ 3 , 4 , 5 ].

1. The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon. EMBO J. 27, 2194-203
2. RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon. EMBO J. 28, 1362-73
3. A single acetylation of 18 S rRNA is essential for biogenesis of the small ribosomal subunit in Saccharomyces cerevisiae. J. Biol. Chem. 289, 26201-12
4. Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1. Nucleic Acids Res. 43, 2242-58
5. RNA cytidine acetyltransferase of small-subunit ribosomal RNA: identification of acetylation sites and the responsible acetyltransferase in fission yeast, Schizosaccharomyces pombe. PLoS ONE 9, e112156