CATH Classification

Domain Context

CATH Clusters

Superfamily Divalent-metal-dependent TIM barrel enzymes
Functional Family Protein arginine N-methyltransferase 5

Enzyme Information

2.1.1.320
Type II protein arginine methyltransferase.
based on mapping to UniProt Q6NUA1
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega')-dimethyl-L-arginine.
-!- The enzyme catalyzes the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. -!- The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. -!- Cf. EC 2.1.1.319, 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)

Q6NUA1
ANM5_XENLA
Xenopus laevis
Protein arginine N-methyltransferase 5

PDB Structure

PDB 4G56
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity
Ho, M.C., Wilczek, C., Bonanno, J.B., Xing, L., Seznec, J., Matsui, T., Carter, L.G., Onikubo, T., Kumar, P.R., Chan, M.K., Brenowitz, M., Cheng, R.H., Reimer, U., Almo, S.C., Shechter, D.
Plos One