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. Author manuscript; available in PMC: 2019 May 1.
Published in final edited form as: Trends Cell Biol. 2018 Feb 21;28(5):346–355. doi: 10.1016/j.tcb.2018.01.007

Figure 2. The Prokaryotic Xenobiotic Acetyltransferase (XAT) Architecture of GCN5L1 is Highly Conserved in Human Lysine Acetyltransferases.

Figure 2

A. Alignment of the streptogramin acetyltransferase from Burkholderiathailandensis (BtXAT) and the short isoform of GCN5L1. The XAT-containing region of GCN5L1 (grey highlight), BtXAT substrate-binding (grey line), BtXAT acetyl-CoA-binding (black line) and XAT repeats (open box) are marked. B. Sequence alignment of GCN5L1 proteins from Homo sapiens, Mus musculus, Bos taurus, Xenopus laevis, Danio rerio, Drosophila melanogaster and Arabidopsis thaliana. The XAT-hexapeptide repeat regions are highlighted by horizontal bars. C. The human HAT1 acetyltransferase core domain contains two XAT repeats (grey highlight) which bracket the conserved motif A. The three motifs of the HAT1 core domain are identified by boxes.