CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.70 | Distorted Sandwich |
|
2.70.160 | Hnrnp arginine n-methyltransferase1 |
|
2.70.160.11 | Hnrnp arginine n-methyltransferase1 |
Domain Context
CATH Clusters
| Superfamily | Hnrnp arginine n-methyltransferase1 |
| Functional Family | Probable histone-arginine methyltransferase CARM1 |
Enzyme Information
| 2.1.1.319 |
Type I protein arginine methyltransferase.
based on mapping to UniProt Q9WVG6
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.
-!- This eukaryotic enzyme catalyzes the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. -!- Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. -!- The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues. -!- PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells. -!- Cf. EC 2.1.1.320, 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)
| Q9WVG6 |
CARM1_MOUSE
Mus musculus
Histone-arginine methyltransferase CARM1
|
PDB Structure
| PDB | 5K8V |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
FEBS J.
|
