InterPro: IPR013216 Methyltransferase type 11

Methyl transfer from the ubiquitous S-adenosyl-L-methionine (SAM) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalyzed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such as catechol for regulatory purposes. The various aspects of the role of DNA methylation in prokaryotic restriction-modification systems and in a number of cellular processes in eukaryotes including gene regulation and differentiation is well documented.

This entry represents a methyltransferase domain found in a large variety of SAM-dependent methyltransferases including, but not limited to:

• Arsenite methyltransferase (EC:2.1.1.137) which converts arsenical compounds to their methylated forms [1]
• Biotin synthesis protein bioC, which is involved in the early stages of biotin biosyntheis [2]
• Arginine N-methyltransferase 1, an arginine-methylating enzyme which acts on residues present in a glycine and argine-rich domain and can methylate histones [3]
• Hexaprenyldihydroxybenzoate methyltransferase (EC:2.1.1.114), a mitochodrial enzyme involved in ubiquinone biosynthesis [4]
• A probable cobalt-precorrin-6Y C(15)-methyltransferase thought to be involved in adenosylcobalamin biosynthesis [5]
• Sterol 24-C-methyltransferase (EC:2.1.1.41), shown to participate in ergosterol biosynthesis [6]
• 3-demethylubiquinone-9 3-methyltransferase (EC:2.1.1.64) involved in ubiquinone biosynthesis [7]