METTL3 and METTL14 (methyltransferase-like) form a methyltransferase complex that methylates adenosine residues at the N6 position of some RNAs, forming N6-methyladenosine (m6A). METTL3, also known as MT-A70, is the catalytic subunit of this complex, and accepts S-adenosyl methionine, a donor for methylation. m6A, which is present at internal sites of some mRNAs, affects different aspects of mRNA metabolism such as half-life, splicing, and translation.Methyltransferases (EC 2.1.1.-) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.