KEGG   ENZYME: 2.3.2.8Help
Entry
EC 2.3.2.8                  Enzyme                                 

Name
arginyltransferase;
arginine transferase;
arginyl-transfer ribonucleate-protein aminoacyltransferase;
arginyl-transfer ribonucleate-protein transferase;
arginyl-tRNA protein transferase;
L-arginyl-tRNA:protein arginyltransferase
Class
Transferases;
Acyltransferases;
Aminoacyltransferases
BRITE hierarchy
Sysname
L-arginyl-tRNAArg:protein arginyltransferase
Reaction(IUBMB)
L-arginyl-tRNAArg + protein = tRNAArg + L-arginyl-[protein] [RN:R03862]
Reaction(KEGG)
Substrate
L-arginyl-tRNA(Arg) [CPD:C02163];
protein [CPD:C00017]
Product
tRNA(Arg) [CPD:C01636];
L-arginyl-protein [CPD:C16739]
Comment
Requires mercaptoethanol and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
History
EC 2.3.2.8 created 1972, modified 1976, modified 2013
Orthology
K00685  arginyl-tRNA---protein transferase
K21419  arginyl-tRNA---protein transferase
Genes
HSA: 11101(ATE1)
PTR: 450786(ATE1)
PPS: 100982152(ATE1)
GGO: 101128164(ATE1)
PON: 100172501(ATE1)
NLE: 100599400(ATE1)
MCC: 705248(ATE1)
MCF: 102144999(ATE1)
CSAB: 103216824(ATE1)
RRO: 104666760 104675845(ATE1)
CJC: 100396459(ATE1)
SBQ: 101031620(ATE1)
MMU: 11907(Ate1)
RNO: 293526(Ate1)
CGE: 100774144(Ate1)
NGI: 103729271(Ate1)
HGL: 101706919(Ate1)
CCAN: 109691635(Ate1)
OCU: 100338175(ATE1)
TUP: 102482899(ATE1)
CFA: 486919(ATE1)
AML: 100468013(ATE1)
UMR: 103657811(ATE1)
ORO: 101380402(ATE1)
FCA: 101090722(ATE1)
PTG: 102948834(ATE1)
AJU: 106969381(ATE1)
BTA: 534601(ATE1)
BOM: 102269329(ATE1)
BIU: 109579031(ATE1)
PHD: 102330669(ATE1)
CHX: 102172865(ATE1)
OAS: 101110286(ATE1)
SSC: 100512816(ATE1)
CFR: 102510677(ATE1) 102524494
CDK: 105104041(ATE1)
BACU: 103015086(ATE1)
LVE: 103090015(ATE1)
OOR: 101271482(ATE1)
ECB: 100064881(ATE1)
EPZ: 103547116(ATE1)
EAI: 106839065(ATE1)
MYB: 102251663(ATE1)
MYD: 102760709(ATE1)
HAI: 109382995(ATE1)
RSS: 109458906(ATE1)
PALE: 102882310(ATE1)
LAV: 100663659(ATE1)
TMU: 101357460
MDO: 100025687(ATE1)
GGA: 423936(ATE1)
MGP: 100541056(ATE1)
CJO: 107316239(ATE1)
APLA: 101795405(ATE1)
ACYG: 106038938(ATE1)
TGU: 100230111(ATE1)
GFR: 102039014(ATE1)
FAB: 101813627(ATE1)
PHI: 102105295(ATE1)
PMAJ: 107206849(ATE1)
CCW: 104694657(ATE1)
FPG: 101920672(ATE1)
FCH: 102059182(ATE1)
CLV: 102096074(ATE1)
EGZ: 104123670(ATE1)
AAM: 106499020(ATE1)
ASN: 102387689(ATE1)
AMJ: 102574359(ATE1)
PSS: 102444012(ATE1)
CMY: 102938335(ATE1)
CPIC: 101934367(ATE1)
ACS: 100562215(ate1)
PVT: 110075325(ATE1)
PBI: 103054892(ATE1) 103057216
GJA: 107122328(ATE1)
XLA: 100101312(ate1.L) 432192(ate1.S)
XTR: 100495601(ate1)
NPR: 108793048(ATE1)
DRE: 100037311(ate1)
SRX: 107724575 107733354(ate1)
CCAR: 109094551
IPU: 108263492(ate1)
AMEX: 103027203(ate1)
TRU: 101073436(ate1)
LCO: 104925641(ate1)
NCC: 104948543(ate1)
MZE: 101465574(ate1)
OLA: 101172758(ate1)
XMA: 102235617(ate1)
PRET: 103477292(ate1)
NFU: 107375399(ate1)
CSEM: 103387588(ate1)
LCF: 108885765(ate1)
HCQ: 109523117(ate1)
BPEC: 110168150(ate1)
SASA: 106576889(ate1)
ELS: 105010631(ate1)
SFM: 108925826(ate1)
LCM: 102350731(ATE1)
CMK: 103180266 103185427(ate1)
CIN: 100182995
SPU: 584881
APLC: 110978852
SKO: 100377714
DME: Dmel_CG9204(Ate1)
DSE: Dsec_GM19800(Dsec_Ate1)
DSI: Dsimw501_GD25293(Dsim_Ate1)
MDE: 101901427
AAG: 5567137
AME: 412018
BIM: 100744130
BTER: 100645093
SOC: 105194979
AEC: 105154994
ACEP: 105626892
PBAR: 105426400
HST: 105189076
CFO: 105255984
LHU: 105669842
PGC: 109857882
NVI: 100123281
TCA: 656450
DPA: 109538352
NVL: 108564715
BMOR: 101740113
PMAC: 106712120
PRAP: 110998113
PXY: 105388162
DNX: 107167514
ZNE: 110829756
FCD: 110851412
TUT: 107365680
CEL: CELE_K07A1.9(ate-1)
CBR: CBG03713
BMY: Bm1_24425
TSP: Tsp_00010
CRG: 105348638
OBI: 106875152
LAK: 106168678
SHX: MS3_00912
EPA: 110235569
ADF: 107350479
HMG: 100203025
ATH: AT3G11240(ATE2) AT5G05700(ATE1)
THJ: 104816553
CIT: 102609591
TCC: 18585891
GRA: 105777212
GHI: 107931832
DZI: 111310127
VRA: 106757616
VAR: 108329024
CCAJ: 109798503
CAM: 101508561
LJA: Lj0g3v0139249.1(Lj0g3v0139249.1)
ADU: 107469507
AIP: 107622768
FVE: 101299816
PPER: 18785506
PMUM: 103332767
PAVI: 110749750
ZJU: 107413867
CSV: 101204837
CMO: 103485565
MCHA: 111006235
RCU: 8270472
JCU: 105646368
HBR: 110633288
JRE: 108980033
VVI: 100253633
SLY: 101255406
SPEN: 107023673
SOT: 102605228
CANN: 107873336
NSY: 104238551
NTO: 104108322
INI: 109186817
SIND: 105167058
OEU: 111404065
LSV: 111901294
DCR: 108199726
BVG: 104903479
SOE: 110802162
NNU: 104596942
OSA: 4338945
DOSA: Os05t0446800-01(Os05g0446800)
OBR: 102705074
BDI: 100827158
ATS: 109770159(LOC109770159)
ZMA: 100383012
SITA: 101778225
PDA: 103723669
EGU: 105032579
MUS: 103996874
DCT: 110108787
AOF: 109829757
ATR: 18437929
PPP: 112280162
MNG: MNEG_4156
APRO: F751_2528
SCE: YGL017W(ATE1)
ERC: Ecym_7226
KMX: KLMA_50148(ATE1)
NCS: NCAS_0A01680(NCAS0A01680)
NDI: NDAI_0D03600(NDAI0D03600)
TPF: TPHA_0F00570(TPHA0F00570)
TBL: TBLA_0C04130(TBLA0C04130)
TDL: TDEL_0F02430(TDEL0F02430)
KAF: KAFR_0F03220(KAFR0F03220)
PIC: PICST_82344(ATE1)
CAL: CAALFM_C200230WA(CaO19.2110)
CAUR: QG37_02686
SLB: AWJ20_3579(ATE1)
NCR: NCU01803
NTE: NEUTE1DRAFT83942(NEUTE1DRAFT_83942)
MGR: MGG_06681
SSCK: SPSK_01642
MAW: MAC_03538
MAJ: MAA_02649
BFU: BCIN_14g04690(Bcate1)
MBE: MBM_09092
ANI: AN6250.2
ANG: ANI_1_242024(An02g01770)
ABE: ARB_04832
TVE: TRV_04587
PTE: PTT_16465
ABP: AGABI1DRAFT73525(AGABI1DRAFT_73525)
ABV: AGABI2DRAFT202585(AGABI2DRAFT_202585)
MGL: MGL_0785
DDI: DDB_G0269024(ate1)
DFA: DFA_02655(ate1)
PYO: PY17X_0310300(PY02988)
PCB: PCHAS_031190(PC000219.02.0)
SPAR: SPRG_07547
 » show all
Taxonomy
Reference
1  [PMID:5416661]
  Authors
Soffer RL.
  Title
Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm.
  Journal
J Biol Chem 245:731-7 (1970)
Reference
2  [PMID:4572514]
  Authors
Soffer RL.
  Title
Peptide acceptors in the arginine transfer reaction.
  Journal
J Biol Chem 248:2918-21 (1973)
Reference
3  [PMID:5811819]
  Authors
Soffer RL, Horinishi H.
  Title
Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm.
  Journal
J Mol Biol 43:163-75 (1969)
DOI:10.1016/0022-2836(69)90086-2
Other DBs
ExplorEnz - The Enzyme Database: 2.3.2.8
IUBMB Enzyme Nomenclature: 2.3.2.8
ExPASy - ENZYME nomenclature database: 2.3.2.8
BRENDA, the Enzyme Database: 2.3.2.8
CAS: 37257-24-2

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