This entry represents a structural domain found in several acyl-CoA acyltransferase enzymes. This domain has a 3-layer alpha/beta/alpha structure that contains mixed beta-sheets, and can be found in the following proteins: N-acetyl transferase (NAT) family members, including aminoglycoside N-acetyltransferases, the histone acetyltransferase domain of P300/CBP associating factor PCAF, the catalytic domain of GCN5 histone acetyltransferase, and diamine acetyltransferase 1. Autoinducer synthetases, such as protein LasI and acyl-homoserinelactone synthase EsaI.Leucyl/phenylalanyl-tRNA-protein transferase (LFTR), a close relative of the non-ribosomal peptidyltransferases; there is a deletion of the N-terminal half of the N-terminal NAT-like domain after the domain duplication/swapping events.Ornithine decarboxylase antizyme, which may have evolved a different function for this domain, although the putative active site maps to the same location in the common fold.Arginine N-succinyltransferase, alpha chain, AstA, which contains an extra C-terminal domain that is similar to the double psi beta-barrel fold domain (missing one strand and untangled psi-loops).Several proteins carry a duplication of this domain, which consists of two NAT-like domains swapped with the C-terminal strands, including: N-myristoyl transferase (NMT). FemXAB nonribosomal peptidyltransferases, including methicillin-resistance protein FemA (transfer glycyl residue from tRNA-Gly) and peptidyltransferase FemX. Hypothetical protein cg14615-pa from Drosophila melanogaster (Fruit fly).