CATH Domain 5fa5A01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.20	Alpha-Beta Barrel
	3.20.20	TIM Barrel
	3.20.20.150	Divalent-metal-dependent TIM barrel enzymes

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 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	PDBSum Proteopedia
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