KEGG   ENZYME: 2.1.1.322
Entry
EC 2.1.1.322                Enzyme                                 

Name
type IV protein arginine methyltransferase;
RMT2 (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-N5-methyl-L-arginine-forming)
Reaction(IUBMB)
S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N5-methyl-L-arginine [RN:R11221]
Reaction(KEGG)
R11221
Substrate
S-adenosyl-L-methionine [CPD:C00019];
[protein]-L-arginine [CPD:C00613]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
[protein]-N5-methyl-L-arginine [CPD:C21190]
Comment
This enzyme, characterized from the yeast Saccharomyces cerevisiae, methylates the the delta-nitrogen atom of arginine residues within proteins. Among its substrates are Arg67 of the ribosomal protein L12. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, and EC 2.1.1.321, type III protein arginine methyltransferase.
History
EC 2.1.1.322 created 2015
Orthology
K18477  type IV protein arginine methyltransferase
Genes
SMM: Smp_024380
SHX: MS3_02768
OVI: T265_13792
EGL: EGR_07793
ATH: AT5G65860
ALY: 9301058
CRB: 17875279
CSAT: 104727248 104744337 104762774
EUS: EUTSA_v10005718mg
BRP: 103874022
BOE: 106328863
THJ: 104807092
CPAP: 110818793
CIT: 102617746
TCC: 18592010
GRA: 105769321
GAB: 108450487
DZI: 111312562
EGR: 104447825
VRA: 106761118
VAR: 108331651
VUN: 114162111
CCAJ: 109796001
CAM: 101504178
LJA: Lj1g3v1720140.1(Lj1g3v1720140.1) Lj1g3v1720140.2(Lj1g3v1720140.2)
ADU: 107461180
AIP: 107606376
LANG: 109343866
FVE: 101307454
RCN: 112174110
PPER: 18791164
PMUM: 103320401
PAVI: 110744880
MDM: 103441063
PXB: 103945293
CSV: 101206863
CMO: 103487848
MCHA: 111004738
CMAX: 111495906
CMOS: 111454147
CPEP: 111798359
RCU: 8288515
JCU: 105630874
HBR: 110671978
MESC: 110605917
POP: 18104803
PEU: 105128808
JRE: 108981343
VVI: 100259168
SLY: 101264002
SPEN: 107016038
SOT: 102604578
CANN: 107867217
NSY: 104249239
NTO: 104107915
NAU: 109215478
INI: 109153010
SIND: 105155586
OEU: 111389319
HAN: 110885808
LSV: 111901692
CCAV: 112514525
DCR: 108192844
BVG: 104902325
SOE: 110786191
NNU: 104611655
OSA: 4334192
DOSA: Os03t0761200-01(Os03g0761200)
OBR: 102707569
BDI: 100840055
ATS: 109743493(LOC109743493)
SBI: 8062466
ZMA: 100286312
SITA: 101761593
PDA: 103700807
EGU: 105058565
MUS: 103997354
DCT: 110099348
PEQ: 110023864
AOF: 109834172
ATR: 18431821
PPP: 112294549
APRO: F751_6706
SCE: YDR465C(RMT2)
ERC: Ecym_2800
KMX: KLMA_20552(RMT2)
NCS: NCAS_0A08140(NCAS0A08140)
NDI: NDAI_0H01030(NDAI0H01030)
TPF: TPHA_0D02720(TPHA0D02720)
TBL: TBLA_0J00700(TBLA0J00700)
TDL: TDEL_0A04560(TDEL0A04560)
KAF: KAFR_0A06740(KAFR0A06740)
PIC: PICST_66076(RMT2)
CAL: CAALFM_C500680WA(RMT2)
SLB: AWJ20_2397(RMT2)
NCR: NCU08111
NTE: NEUTE1DRAFT125124(NEUTE1DRAFT_125124)
MGR: MGG_09290
SSCK: SPSK_10638
MAW: MAC_02976
MAJ: MAA_04208
CMT: CCM_06279
BFU: BCIN_11g05680(Bcrmt2)
MBE: MBM_09897
ANI: AN6072.2
ANG: ANI_1_1792104(An12g04740)
ABE: ARB_05048
TVE: TRV_01451
CNE: CNA04170
CNB: CNBA4000
TASA: A1Q1_00168
ABP: AGABI1DRAFT71703(AGABI1DRAFT_71703)
ABV: AGABI2DRAFT204671(AGABI2DRAFT_204671)
MGL: MGL_2081
MRT: MRET_1613
SMIN: v1.2.008584.t1(symbB.v1.2.008584.t1)
 » show all
Reference
1  [PMID:9873020]
  Authors
Niewmierzycka A, Clarke S
  Title
S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase.
  Journal
J Biol Chem 274:814-24 (1999)
DOI:10.1074/jbc.274.2.814
  Sequence
[sce:YDR465C]
Reference
2  [PMID:11856739]
  Authors
Chern MK, Chang KN, Liu LF, Tam TC, Liu YC, Liang YL, Tam MF
  Title
Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase  2.
  Journal
J Biol Chem 277:15345-53 (2002)
DOI:10.1074/jbc.M111379200
  Sequence
[sce:YDR465C]
Reference
3  [PMID:17448464]
  Authors
Olsson I, Berrez JM, Leipus A, Ostlund C, Mutvei A
  Title
The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100.
  Journal
Exp Cell Res 313:1778-89 (2007)
DOI:10.1016/j.yexcr.2007.03.007
  Sequence
[sce:YDR465C]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.322
IUBMB Enzyme Nomenclature: 2.1.1.322
ExPASy - ENZYME nomenclature database: 2.1.1.322
BRENDA, the Enzyme Database: 2.1.1.322
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