CATH Classification
Level | CATH Code | Description |
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2 | Mainly Beta |
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2.70 | Distorted Sandwich |
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2.70.160 | Hnrnp arginine n-methyltransferase1 |
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2.70.160.11 | Hnrnp arginine n-methyltransferase1 |
Domain Context
CATH Clusters
Superfamily | Hnrnp arginine n-methyltransferase1 |
Functional Family | protein arginine N-methyltransferase 6 |
Enzyme Information
2.1.1.319 |
Type I protein arginine methyltransferase.
based on mapping to UniProt Q96LA8
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.
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UniProtKB Entries (1)
Q96LA8 |
ANM6_HUMAN
Homo sapiens
Protein arginine N-methyltransferase 6
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PDB Structure
PDB | 4HC4 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural basis of arginine asymmetrical dimethylation by PRMT6.
Biochem. J.
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