ID I1HIX4_BRADI Unreviewed; 638 AA.
AC I1HIX4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Arginyl-tRNA--protein transferase {ECO:0000256|PIRNR:PIRNR037207};
DE EC=2.3.2.8 {ECO:0000256|PIRNR:PIRNR037207};
GN Name=100827158 {ECO:0000313|EnsemblPlants:KQK05989};
GN ORFNames=BRADI_2g23790v3 {ECO:0000313|EMBL:KQK05989.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQK05989};
RN [1] {ECO:0000313|EMBL:KQK05989.1, ECO:0000313|EnsemblPlants:KQK05989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK05989.1,
RC ECO:0000313|EnsemblPlants:KQK05989};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK05989.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK05989.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK05989}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK05989};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- FUNCTION: Involved in the post-translational conjugation of arginine to
CC the N-terminal aspartate or glutamate of a protein. This arginylation
CC is required for degradation of the protein via the ubiquitin pathway.
CC {ECO:0000256|PIRNR:PIRNR037207}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-
CC tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] +
CC tRNA(Arg); Xref=Rhea:RHEA:10208, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10638,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513,
CC ChEBI:CHEBI:78597, ChEBI:CHEBI:83562; EC=2.3.2.8;
CC Evidence={ECO:0000256|PIRNR:PIRNR037207};
CC -!- SIMILARITY: Belongs to the R-transferase family.
CC {ECO:0000256|ARBA:ARBA00009991, ECO:0000256|PIRNR:PIRNR037207}.
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DR EMBL; CM000881; KQK05989.1; -; Genomic_DNA.
DR EMBL; CM000881; KQK05990.1; -; Genomic_DNA.
DR RefSeq; XP_003568343.1; XM_003568295.3.
DR AlphaFoldDB; I1HIX4; -.
DR STRING; 15368.I1HIX4; -.
DR EnsemblPlants; KQK05989; KQK05989; BRADI_2g23790v3.
DR EnsemblPlants; KQK05990; KQK05990; BRADI_2g23790v3.
DR GeneID; 100827158; -.
DR Gramene; KQK05989; KQK05989; BRADI_2g23790v3.
DR Gramene; KQK05990; KQK05990; BRADI_2g23790v3.
DR KEGG; bdi:100827158; -.
DR eggNOG; KOG1193; Eukaryota.
DR HOGENOM; CLU_020349_1_0_1; -.
DR InParanoid; I1HIX4; -.
DR OMA; SDRMVYS; -.
DR OrthoDB; 38036at2759; -.
DR Proteomes; UP000008810; Chromosome 2.
DR ExpressionAtlas; I1HIX4; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004057; F:arginyl-tRNA--protein transferase activity; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR017137; Arg-tRNA-P_Trfase_1_euk.
DR InterPro; IPR030700; N-end_Aminoacyl_Trfase.
DR InterPro; IPR007472; N-end_Aminoacyl_Trfase_C.
DR InterPro; IPR007471; N-end_Aminoacyl_Trfase_N.
DR PANTHER; PTHR21367; ARGININE-TRNA-PROTEIN TRANSFERASE 1; 1.
DR PANTHER; PTHR21367:SF1; ARGINYL-TRNA--PROTEIN TRANSFERASE 1; 1.
DR Pfam; PF04377; ATE_C; 1.
DR Pfam; PF04376; ATE_N; 1.
DR PIRSF; PIRSF037207; ATE1_euk; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR037207};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037207};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR037207}.
FT DOMAIN 32..102
FT /note="N-end aminoacyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04376"
FT DOMAIN 345..486
FT /note="N-end rule aminoacyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04377"
FT REGION 118..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 71608 MW; CFDFF80B768EEE01 CRC64;
MADGASSSGA VAAGGGSGGE SVVIDYGRRR TTCGYCRSTS STSISHGLWA NSLKADDYQA
LLDRGWRRSG SFLYKPEMER TCCPSYTIRL KASDFICSKE QDRVLKRMQR FLDGELDPPV
GSPQCKTNPT KRSHDEPMNS PTSKVSRVLA YEYRTATCPS LVKEDEFICC LSSKINKAIE
MCFQSGILGS DVQLPKAVVK TVKPQVKKKV VEAAQKNKGG TVQDLVYTCN ISFQLAAAIR
RALPEEKHAV LGDLSPNYIA EKLVSTMEHD GAIAGFEVKA CNGHLNFYSA TIQAVQNHTS
IDAGAEASDK STSPKQSPKN RKNARHNQKA RKLEFSITRS HFDPEEFALY ERYQTKVHKE
KTVTESSYKR FLVDTPIVFV PPVSGDNTVP PCGFGSFHQQ YRIDGKLVAV GVVDILPKCL
SSKYLFWDPD LAFLSLGKYT ALKEIDWVKT TQRSCPSLQY YYLGYYIHSC NKMRYKAAYR
PSELLCPVRY EWVRYDVAKP LLDKNLYSVL SDFSTMQDEI PQTHTCGPYD ESSAKNDHCE
SPTDEDDEDS DYDESDMMVD EDMVRSESNA DTSEDCSDIS EIENVIMILN SSRVKYKELQ
SVVGPIERRH LSELERQLSR YVKVVGKELS DRMVYSLS
//
