CATH Classification

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 Q86X55
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)

Q86X55
CARM1_HUMAN
Homo sapiens
Histone-arginine methyltransferase CARM1

PDB Structure

PDB 5DX1
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
Boriack-Sjodin, P.A., Jin, L., Jacques, S.L., Drew, A., Sneeringer, C., Scott, M.P., Moyer, M.P., Ribich, S., Moradei, O., Copeland, R.A.
Acs Chem.Biol.