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Information on EC 2.1.1.320 - type II protein arginine methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38274

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IUBMB Comments
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
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Saccharomyces cerevisiae
UNIPROT: P38274
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
prmt5, prmt7, protein arginine methyltransferase 5, prmt9, type ii protein arginine methyltransferase, prmt-5, prmt-9, janus kinase-binding protein 1, jak-binding protein 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PRMT5
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PRMT9
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega,Nomega'-dimethyl-L-arginine-forming)
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
show the reaction diagram
histone H2A from calf thymus
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-
?
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
symmetric dimethylation is only observed when enzyme and the methyl-accepting substrate are incubated for extended times
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?
additional information
?
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sayegh, J.; Clarke, S.G.
Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast
Biochem. Biophys. Res. Commun.
372
811-815
2008
Saccharomyces cerevisiae (P38274), Saccharomyces cerevisiae
Manually annotated by BRENDA team