CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.150 | Vaccinia Virus protein VP39 |
Domain Context
CATH Clusters
| Superfamily | Vaccinia Virus protein VP39 |
| 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)
| O14744 |
ANM5_HUMAN
Homo sapiens
Protein arginine N-methyltransferase 5
|
PDB Structure
| PDB | 4GQB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of the human PRMT5:MEP50 complex.
Proc.Natl.Acad.Sci.USA
|