CATH Classification

Domain Context

CATH Clusters

Superfamily Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Functional Family Coactivator-associated arginine methyltransferase 1

Enzyme Information

2.1.1.319
Type I protein arginine methyltransferase.
based on mapping to UniProt Q4AE70
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)

Q4AE70
CARM1_RAT
Rattus norvegicus
Histone-arginine methyltransferase CARM1

PDB Structure

PDB 2OQB
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains.
Troffer-Charlier, N., Cura, V., Hassenboehler, P., Moras, D., Cavarelli, J.
Embo J.