Rubisco LSMT methyltransferase, plant (IPR011192)

Short name: Rubisco_LSMT_MeTrfase_plant

Overlapping homologous superfamilies


Family relationships



Members of this family are Rubisco methyltransferases (RMT) encoding protein methylase activity. The enzyme activity has been mapped to the SET domain. The SET domain was originally identified in Su(var)3-9, E(z) and Trithorax genes in Drosophila melanogaster [PMID: 12039029]. Homology between the SET domains of LSMTs and of the SUV39H1 family of position-effect variegation (PEV) modifiers provided the first hint that SUV39H1 proteins were histone methyltransferases [PMID: 10949293]. Methylation of Rubisco large subunits resembles histone methylation in many respects. Lys-14 is the site of methylation on the Rubisco large subunit, and is located in the flexible N terminus of the large subunit [PMID: 1525466]. The precise role of Rubisco tail methylation is unknown at this time, but is thought to involve targeting of other proteins to interact with the tail. LSMTs are highly expressed in leaves during daylight and may be involved in the regulation of Rubisco during photosynthesis [PMID: 7888616, PMID: 10593982]. 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.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0030785 [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity

Cellular Component

GO:0009507 chloroplast

Contributing signatures

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