CATH Domain 5tbjD02

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.70	Distorted Sandwich
	2.70.160	Hnrnp arginine n-methyltransferase1
	2.70.160.11	Hnrnp arginine n-methyltransferase1

Domain Context

CATH Clusters

Superfamily	Hnrnp arginine n-methyltransferase1
Functional Family	Probable histone-arginine methyltransferase CARM1

Enzyme Information

2.1.1.319

Type I protein arginine methyltransferase.

based on mapping to UniProt Q9WVG6

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.

-!- This eukaryotic enzyme catalyzes the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. -!- Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. -!- The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues. -!- PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells. -!- Cf. EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322. -!- Formerly EC 2.1.1.23, EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126.

UniProtKB Entries (1)

Q9WVG6

CARM1_MOUSE

Mus musculus

Histone-arginine methyltransferase CARM1

PDB Structure

PDB	5TBJ
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Hijacking DNA methyltransferase transition state analogues to produce chemical scaffolds for PRMT inhibitors. Halby, L., Marechal, N., Pechalrieu, D., Cura, V., Franchini, D.M., Faux, C., Alby, F., Troffer-Charlier, N., Kudithipudi, S., Jeltsch, A., Aouadi, W., Decroly, E., Guillemot, J.C., Page, P., Ferroud, C., Bonnefond, L., Guianvarc'h, D., Cavarelli, J., Arimondo, P.B. Philos.Trans.R.Soc.Lond.B Biol.Sci.