EC number:2.1.1.322

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.322
Description:Type IV protein arginine methyltransferase.
Cath: 3.20.20.150; 2.30.29.30; 3.40.50.150; 2.70.160.11;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.322
BRENDA Enzyme Link: BRENDA 2.1.1.322
KEGG Enzyme Link: KEGG2.1.1.322
BioCyc Enzyme Link: BioCyc 2.1.1.322
ExPASy Enzyme Link: ExPASy2.1.1.322
EC2PDB Enzyme Link: EC2PDB 2.1.1.322
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.322
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.322
IntEnz Enzyme Link: IntEnz 2.1.1.322
MEDLINE Enzyme Link: MEDLINE 2.1.1.322

EC number:2.1.1.322

MSA:

2.1.1.322;
Phylogenetic Tree:

2.1.1.322;
Uniprot:
M-CSA:
RHEA:48116 L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[NH;+0:2]-[*:3].[*:4]-[S+;H0:5](-[*:6])-[CH3;+0:7]>>[*:1]-[N;H0;+0:2](-[*:3])-[CH3;+0:7].[*:4]-[S;H0;+0:5]-[*:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase.Niewmierzycka A, Clarke S1999 Jan 89873020
The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100.Olsson I, Berrez JM, Leipus A, Ostlund C, Mutvei A2007 May 1517448464
Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2.Chern MK, Chang KN, Liu LF, Tam TC, Liu YC, Liang YL, Tam MF2002 May 311856739