InterPro domain: IPR044431

In pea (Pisum sativum), the protein-lysine methyltransferase (PsLSMT, also known as RBCMT) catalyses the trimethylation of Lys-14 in the large subunit (LS) of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) [ 1 ]. Arabidopsis homologue of RBCMT, LSMT, is a protein-lysine methyltransferase methylating chloroplastic fructose 1,6-bisphosphate aldolases [ 2 ]. The sequence conservation pattern and structure analysis of the SET domain provides clues regarding the possible active site residues of the domain. There are three conserved sequence motifs in most of the SET domain. The N-terminal motif (I) has characteristic glycines. The central motif (II) has a distinct pattern of polar and charged residues (Asn, His). The C-terminal conserved motif (III) has a characteristic dyad of polar residues and the hydrophobic residue tyrosine.

This entry represents the SET domain found in a group of ribulose-bisphosphate carboxylase]-lysine N-methyltransferases (RBCMTs) and related proteins from plants.

1. RUBISCO: structure and mechanism. J Biol Chem 21, 119-43
2. Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants. null 287, 21034-44