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 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
Plos One
|