CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.30 | Roll |
|
2.30.29 | PH-domain like |
|
2.30.29.30 | Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) |
Domain Context
CATH Clusters
| Superfamily | Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) |
| Functional Family | Coactivator-associated arginine methyltransferase 1 |
Enzyme Information
| 2.1.1.319 |
Type I protein arginine methyltransferase.
based on mapping to UniProt Q4AE70
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)
| Q4AE70 |
CARM1_RAT
Rattus norvegicus
Histone-arginine methyltransferase CARM1
|
PDB Structure
| PDB | 2OQB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains.
Embo J.
|