ID   ATE1_DICDI              Reviewed;         629 AA.
AC   Q55EI0;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=DDB_G0269024;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- SIMILARITY: Belongs to the R-transferase family. {ECO:0000305}.
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DR   EMBL; AAFI02000004; EAL73101.1; -; Genomic_DNA.
DR   RefSeq; XP_647040.1; XM_641948.1.
DR   AlphaFoldDB; Q55EI0; -.
DR   STRING; 44689.DDB0238346; -.
DR   PaxDb; Q55EI0; -.
DR   PRIDE; Q55EI0; -.
DR   EnsemblProtists; EAL73101; EAL73101; DDB_G0269024.
DR   GeneID; 8616735; -.
DR   KEGG; ddi:DDB_G0269024; -.
DR   dictyBase; DDB_G0269024; ate1.
DR   eggNOG; KOG1193; Eukaryota.
DR   HOGENOM; CLU_020349_1_0_1; -.
DR   InParanoid; Q55EI0; -.
DR   OMA; SDRMVYS; -.
DR   PhylomeDB; Q55EI0; -.
DR   BRENDA; 2.3.2.8; 1939.
DR   PRO; PR:Q55EI0; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR   GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR   GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR   GO; GO:0004057; F:arginyltransferase activity; IDA:dictyBase.
DR   GO; GO:0016477; P:cell migration; IMP:dictyBase.
DR   GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR   GO; GO:0016598; P:protein arginylation; IMP:dictyBase.
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   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..629
FT                   /note="Arginyl-tRNA--protein transferase 1"
FT                   /id="PRO_0000351082"
FT   REGION          274..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..396
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  73820 MW;  9118972C8AA2F55F CRC64;
     MERFLMQSSL STSSLIYPHG SYDSSCNYCD AGEDKKGRIC YGMVADQLTC EDYQLLIDQG
     WRRSGTFLYK PNNSDKKTCC PQYTIRLDTS SFKPSKDNKS TIKKFNNYIL NNIIKEKDSS
     TTSTTKDIIN TTQIKSNTKN NNNKTNDENI IKLNNDIIEI ILNNEFINKF NEQDKKILKE
     NLKIKINSNK MIKETGSYSL SFGIFNKYRS ELNQHSITID QIINFTILEF NKTINNSDYQ
     FNLEKGQNNH INFKMINSSQ ILNDSTKTKT LNIQNNSNKN STTTATTATT TTTTTNEPKH
     KFEISIHKPK CTDEVFSLYC KYQKIIHKED DEKTKSGFKR FLVDSPLIPI IHPDESYDDY
     VYDGKDDDDD DDDKDEKEDD EDEDQEDDED EDDGNNEDEK KITKENKEKE IKNHIYKIGK
     KSKTLKTRKF GEIKTPKPGY GSFHQYYRLD GKLVGVGVID ILPECLSSVY FFYDPDFNFL
     SLGKYSALNE IEWVQKVSQS IPQLKYYYMG YYIHSCQKMK YKANYQPSQL LCLETFKWVE
     FKKAISFLQP DKKYSRFYFD ENENNNNEKL TYFEKEPELL ERVKFRQKNF TFHFSDVSVR
     FQNLLKDQVI DYINHVGPEL TKELIFYFK