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 | Blast:Protein arginine N-methyltransferase 1 |
Enzyme Information
| 2.1.1.319 |
Type I protein arginine methyltransferase.
based on mapping to UniProt Q9NR22
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.
|
| 2.1.1.321 |
Type III protein arginine methyltransferase.
based on mapping to UniProt Q9NR22
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)
| Q9NR22 |
ANM8_HUMAN
Homo sapiens
Protein arginine N-methyltransferase 8
|
PDB Structure
| PDB | 5DST |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Novel helical assembly in arginine methyltransferase 8
J.Mol.Biol.
|
