ID   ATE1_MACFA              Reviewed;         518 AA.
AC   Q2PFX0;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Arginyl-tRNA--protein transferase 1;
DE            Short=Arginyltransferase 1;
DE            Short=R-transferase 1;
DE            EC=2.3.2.8;
DE   AltName: Full=Arginine-tRNA--protein transferase 1;
GN   Name=ATE1; ORFNames=QflA-16011;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RA   Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT   oligo-chips.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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       Does not arginylate cysteine residues (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Monomer. Interacts with LIAT1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Z2A5, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Z2A5}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9Z2A5}.
CC   -!- SIMILARITY: Belongs to the R-transferase family. {ECO:0000305}.
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DR   EMBL; AB220467; BAE73000.1; -; mRNA.
DR   RefSeq; NP_001306295.1; NM_001319366.1.
DR   AlphaFoldDB; Q2PFX0; -.
DR   GeneID; 102144999; -.
DR   CTD; 11101; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004057; F:arginyltransferase activity; IEA:UniProtKB-EC.
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; PTHR21367; 1.
DR   Pfam; PF04377; ATE_C; 1.
DR   Pfam; PF04376; ATE_N; 1.
DR   PIRSF; PIRSF037207; ATE1_euk; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..518
FT                   /note="Arginyl-tRNA--protein transferase 1"
FT                   /id="PRO_0000351081"
FT   REGION          149..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95260"
SQ   SEQUENCE   518 AA;  59014 MW;  7CAA62C5CB5F3264 CRC64;
     MAFWAGGSPS VVDYFPSEDF YRCGYCKNES GSRSNGMWAH SMTVQDYQDL IDRGWRRSGK
     YVYKPVMNQT CCPQYTIRCR PLQFQPSKSH KKVLKKMLKF LAKGEVPKGS CEDEPMDSTM
     DDAVAGDFAL INKLDIQCDL KTLSDDVKES LQSEGKNSKK EEPHELLQSQ DSVGEKLGSG
     EPSHSVKVHT VPKPGKGADL SKPPCRKAKE IRKERKRLKL MQQNPAGELE GFQAQGHPPS
     LFPPKAKSNQ PKSLEDLIFE SLPENASHKL EVRLVPASFE DPEFKSSFSQ SFSLYVKYQV
     AIHQDLPDEC GKTEFTRFLC SSPLEAETPP NGPDCGYGSF HQQYWLDGKI IAVGVIDILP
     NYVSSVYLYY DPDYSFLSLG VYSALREIAF TRQLHEKTSQ LSYYYMGFYI HSCPKMKYKG
     QYRPSDLLCP ETYVWVPIEQ CLPSLENSKY CRFNQDPEAV DEDRSTEPDR LQVFHKRAIM
     PYGVYKKQQK DPSEEAAVLQ YASLVGQKCS ERMLLFRN