1 keywords

CATH Domain 5fa5A03

CATH Classification

Level CATH Code Description
Class 2 Mainly Beta
Architecture 2.70 Distorted Sandwich
Topology 2.70.160 Hnrnp arginine n-methyltransferase1
Homologous Superfamily 2.70.160.11 Hnrnp arginine n-methyltransferase1

Domain Context

CATH Clusters

Superfamily Hnrnp arginine n-methyltransferase1
Functional Family Protein arginine N-methyltransferase 5

Enzyme Information

2.1.1.320
Type II protein arginine methyltransferase.
based on mapping to UniProt O14744
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)

P62805
H4_HUMAN
Homo sapiens
Histone H4

PDB Structure

PDB 5FA5
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Disordered methionine metabolism in MTAP/CDKN2A-deleted cancers leads to dependence on PRMT5.
Mavrakis, K.J., McDonald, E.R., Schlabach, M.R., Billy, E., Hoffman, G.R., deWeck, A., Ruddy, D.A., Venkatesan, K., Yu, J., McAllister, G., Stump, M., deBeaumont, R., Ho, S., Yue, Y., Liu, Y., Yan-Neale, Y., Yang, G., Lin, F., Yin, H., Gao, H., Kipp, D.R., Zhao, S., McNamara, J.T., Sprague, E.R., Zheng, B., Lin, Y., Cho, Y.S., Gu, J., Crawford, K., Ciccone, D., Vitari, A.C., Lai, A., Capka, V., Hurov, K., Porter, J.A., Tallarico, J., Mickanin, C., Lees, E., Pagliarini, R., Keen, N., Schmelzle, T., Hofmann, F., Stegmeier, F., Sellers, W.R.
Science