EC number:2.1.1.320

Enzyme

Download
EC Tree
     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.320
Description:Type II protein arginine methyltransferase.
Cath: 3.20.20.150; 2.30.29.30; 3.40.50.150; 2.70.160.11;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.320
BRENDA Enzyme Link: BRENDA 2.1.1.320
KEGG Enzyme Link: KEGG2.1.1.320
BioCyc Enzyme Link: BioCyc 2.1.1.320
ExPASy Enzyme Link: ExPASy2.1.1.320
EC2PDB Enzyme Link: EC2PDB 2.1.1.320
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.320
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.320
IntEnz Enzyme Link: IntEnz 2.1.1.320
MEDLINE Enzyme Link: MEDLINE 2.1.1.320

EC number:2.1.1.320

MSA:

2.1.1.320;
Phylogenetic Tree:

2.1.1.320;
Uniprot:
M-CSA:
RHEA:48108 L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]-[S+;H0:6](-[*:7])-[CH3;+0:8].[NH2;+0:9]-[*:10]=[NH;+0:11]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]-[S;H0;+0:6]-[*:7].[CH3;+0:8]-[NH;+0:9]-[*:10]=[N;H0;+0:11]-[CH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Unique Features of Human Protein Arginine Methyltransferase 9 (PRMT9) and Its Substrate RNA Splicing Factor SF3B2.Hadjikyriacou A, Yang Y, Espejo A, Bedford MT, Clarke SG2015 Jul 325979344
NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of human complex I.Rhein VF, Carroll J, Ding S, Fearnley IM, Walker JE2013 Nov 1524089531
Substrate specificity, processivity, and kinetic mechanism of protein arginine methyltransferase 5.Wang M, Xu RM, Thompson PR2013 Aug 1323866019
Crystal structure of the human PRMT5:MEP50 complex.Antonysamy S, Bonday Z, Campbell RM, Doyle B, Druzina Z, Gheyi T, Han B, Jungheim LN, Qian Y, Rauch C, Russell M, Sauder JM, Wasserman SR, Weichert K, Willard FS, Zhang A, Emtage S2012 Oct 3023071334
Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs.Wilczek C, Chitta R, Woo E, Shabanowitz J, Chait BT, Hunt DF, Shechter D2011 Dec 922009756
An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs.Chari A, Golas MM, Klingenhäger M, Neuenkirchen N, Sander B, Englbrecht C, Sickmann A, Stark H, Fischer U2008 Oct 3118984161
Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast.Sayegh J, Clarke SG2008 Aug 818515076
The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5.Lacroix M, El Messaoudi S, Rodier G, Le Cam A, Sardet C, Fabbrizio E2008 May18404153
SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis.Wang X, Zhang Y, Ma Q, Zhang Z, Xue Y, Bao S, Chong K2007 Apr 417363895
Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A.Miranda TB, Sayegh J, Frankel A, Katz JE, Miranda M, Clarke S2006 May 116426232
PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins.Branscombe TL, Frankel A, Lee JH, Cook JR, Yang Z, Pestka S, Clarke S2001 Aug 3111413150
Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase.Lee JH, Cook JR, Pollack BP, Kinzy TG, Norris D, Pestka S2000 Jul 2110903903