Entry
Name
type III protein arginine methyltransferase;
PRMT7 (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega-methyl-L-arginine-forming)
Reaction(IUBMB)
S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine [RN:
R11216 ]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:
C00019 ];
protein-L-arginine [CPD:
C00613 ]
Product
S-adenosyl-L-homocysteine [CPD:
C00021 ];
[protein]-Nomega-methyl-L-arginine
Comment
Type III protein arginine methyltransferases catalyse 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 catalyse this reaction, type III enzymes do not methylate the substrate any further. cf. EC
2.1.1.319 , type I protein arginine methyltransferase, EC
2.1.1.320 , type II protein arginine methyltransferase, and EC
2.1.1.322 , type IV protein arginine methyltransferase.
History
EC 2.1.1.321 created 2015
Orthology
K11438 type III protein arginine methyltransferase
Genes
PROB : 127214032 127234609(Prmt7)
SRX : 107707497(prmt7) 107739801
SGH : 107573013 107589198(prmt7)
CCAR : 109050591 109079422
CAUA : 113043703 113066814 113078202 113096605
CGIB : 127947235 128014723
MASI : 127435998 127437784
PFOR : 103142440(prmt7) 103142516
PLAI : 106936539(prmt7) 106946767
PMEI : 106904998(prmt7) 106933755
ARUT : 117424600 117425627
DSI : Dsimw501_GD25084(Dsim_GD25084)
AGA : AgaP_AGAP006938(ANM7_ANOGA)
AALB : 109412526 115254000
PPYR : 116174777 116174885
CFEL : 113367485 113374707
CEL : CELE_W06D4.4(prmt-7)
CBR : CBG_12433(Cbr-prmt-7)
BMY : BM_BM11397(Bma-prmt-7)
CSAT : 104718710 104723449 104731948
LJA : Lj4g3v1260350.3(Lj4g3v1260350.3)
MSYL : 126617593 126618787
EGT : 105962275 105963234 105963237
DOSA : Os06t0105500-01(Os06g0105500)
TAES : 123088560 123150848 123166842
PVIR : 120697247 120702336
PHAI : 112889501 112892764 112893952
ZOF : 121982395 121982400 121986290 121986293
SMO : SELMODRAFT_185054 SELMODRAFT_425255 SELMODRAFT_425258 SELMODRAFT_425264 SELMODRAFT_427394 SELMODRAFT_427398 SELMODRAFT_430728 SELMODRAFT_447442
SRE : PTSG_03146 PTSG_05080 PTSG_09839 PTSG_11677
SMIN : v1.2.018977.t1(symbB.v1.2.018977.t1) v1.2.026170.t3(symbB.v1.2.026170.t3)
AAF : AURANDRAFT_11485(PRMT2) AURANDRAFT_61429
EHX : EMIHUDRAFT_210815 EMIHUDRAFT_211926 EMIHUDRAFT_42351 EMIHUDRAFT_76098
» show all
Taxonomy
Reference
Authors
Miranda TB, Miranda M, Frankel A, Clarke S
Title
PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity.
Journal
Sequence
Reference
Authors
Gonsalvez GB, Tian L, Ospina JK, Boisvert FM, Lamond AI, Matera AG
Title
Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins.
Journal
Sequence
Reference
Authors
Feng Y, Hadjikyriacou A, Clarke SG
Title
Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 2.1.1.321