mRNA (2-O-methyladenosine-N(6)-)-methyltransferase (IPR025848)

Short name: MT-A70

Overlapping homologous superfamilies


Family relationships

  • MT-A70-like (IPR007757)
    • mRNA (2-O-methyladenosine-N(6)-)-methyltransferase (IPR025848)


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 [PMID: 27281194]. m6A, which is present at internal sites of some mRNAs, affects different aspects of mRNA metabolism such as half-life, splicing, and translation [PMID: 24284625, PMID: 26751643, PMID: 26593424, PMID: 26046440, PMID: 25799998].

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 [PMID: 16225687, PMID: 21858014, PMID: 12826405]. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM [PMID: 7897657]. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids [PMID: 16225687, PMID: 21858014, PMID: 7897657]. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [PMID: 16225687, PMID: 21858014, PMID: 12826405]. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.

GO terms

Biological Process

GO:0001510 RNA methylation

Molecular Function

GO:0016422 mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity

Cellular Component

GO:0005634 nucleus

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles