InterPro domain: IPR004557

These proteins exhibit homology to the Saccharomyces cerevisiae Mtq2 (also know as PrmC [ 1 ]). Mtq2 methylates eRF1 on 'Gln-182' using S-adenosyl L-methionine as methyl donor. eRF1 needs to be complexed to eRF3 in its GTP-bound form to be efficiently methylated [ 2 , 3 , 4 ]. In bacteria, the methylation of RF1/RF2 by PrmC is important for normal growth, to increase the affinity of RF1/RF2 for ribosomes and to enhance translation termination [ 5 , 6 ].Human homologue of Mtq2 is called hemK methyltransferase family member 2 (HEMK2, also known as N6AMT1), which is an N6-adenine-specific DNA methyltransferase [ 7 ].

1. Evolutionary insights into Trm112-methyltransferase holoenzymes involved in translation between archaea and eukaryotes. Nucleic Acids Res. 71, 306-318.e7
2. The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene. J. Biol. Chem. 280, 2439-45
3. The yeast translation release factors Mrf1p and Sup45p (eRF1) are methylated, respectively, by the methyltransferases Mtq1p and Mtq2p. J. Biol. Chem. 281, 2562-71
4. The zinc finger protein Ynr046w is plurifunctional and a component of the eRF1 methyltransferase in yeast. J. Biol. Chem. 281, 36140-8
5. A direct estimation of the context effect on the efficiency of termination. J. Mol. Biol. 282, 35638-45
6. Methylation of bacterial release factors RF1 and RF2 is required for normal translation termination in vivo. J. Biol. Chem.
7. N6-Methyladenine DNA Modification in the Human Genome. Mol. Cell 284, 579-90