2.1.1.171	dimer	based on a comprehensive bioinformatic analysis of m2G methyltransferases it is inferred that the prokaryotic RsmC and RsmD methyltransferases are pseudodimers. The C-terminal catalytic domain is closely related to the structurally characterized Mj0882 protein, while the N-terminal domain lacks the cofactor-binding and catalytic side-chains	702877	
2.1.1.171	additional information	protein Rv2966c shows a two-domain structure with a short hairpin domain at the N-terminus and a C-terminal domain with the S-adenosylmethionine-methyltransferase-fold. The N-terminal hairpin is a minimalist functional domain that helps Rv2966c in target recognition. In contrast to the variable substrate binding domain, the C-terminal domain is a highly conserved structure consisting of the classical S-adenosyl-L-methionine-methyltransferase-fold found in several S-adenosyl-L-methionine-dependent methyltransferases. It consists of a central eight-stranded beta-sheet flanked by alpha-helices on both sides, the first five strands of the beta-sheet are parallel to each other and encompass the S-adenosyl-L-methionine binding site toward their C terminus end, whereas the remaining strands of the beta-sheet are antiparallel. The N-terminus of Rv2966c is the target recognition region that helps in binding to nucleic acids	719931