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 | Protein arginine N-methyltransferase |
Enzyme Information
| 2.1.1.321 |
Type III protein arginine methyltransferase.
based on mapping to UniProt Q922X9
S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L- homocysteine + [protein]-N(omega)-methyl-L-arginine.
-!- Type III protein arginine methyltransferases catalyze the single methylation of one of the terminal nitrogen atoms of the guanidino group in an L-arginine residue within a protein. -!- Unlike type I and type II protein arginine methyltransferases, which also catalyze this reaction, type III enzymes do not methylate the substrate any further. -!- Cf. EC 2.1.1.319, EC 2.1.1.320 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)
| Q922X9 |
ANM7_MOUSE
Mus musculus
Protein arginine N-methyltransferase 7
|
PDB Structure
| PDB | 4C4A |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Insight Into Arginine Methylation by the Mouse Protein Arginine Methyltransferase 7: A Zinc Finger Freezes the Mimic of the Dimeric State Into a Single Active Site.
Acta Crystallogr.,Sect.D
|
