ID   ATE1_YEAST              Reviewed;         503 AA.
AC   P16639; D6VUC0;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Arginyl-tRNA--protein transferase 1;
DE            Short=Arginyltransferase 1;
DE            Short=R-transferase 1;
DE            EC=2.3.2.8 {ECO:0000269|PubMed:2185248};
DE   AltName: Full=Arginine-tRNA--protein transferase 1;
GN   Name=ATE1; OrderedLocusNames=YGL017W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=2185248; DOI=10.1016/s0021-9258(19)39136-7;
RA   Balzi E., Choder M., Chen W., Varshavsky A., Goffeau A.;
RT   "Cloning and functional analysis of the arginyl-tRNA-protein transferase
RT   gene ATE1 of Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 265:7464-7471(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 46191 / IL125-2B;
RX   PubMed=1882553; DOI=10.1002/yea.320070311;
RA   Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.;
RT   "The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and
RT   ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6
RT   gene, a new member of the genetic network controlling pleiotropic drug
RT   resistance.";
RL   Yeast 7:287-299(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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       (PubMed:2185248). Does not arginylate cysteine residues (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:2185248}.
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:0000269|PubMed:2185248};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10209;
CC         Evidence={ECO:0000305|PubMed:2185248};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 2030 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the R-transferase family. {ECO:0000305}.
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DR   EMBL; J05404; AAA34439.1; -; Genomic_DNA.
DR   EMBL; S58126; AAD13904.1; -; Genomic_DNA.
DR   EMBL; Z72539; CAA96717.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08081.1; -; Genomic_DNA.
DR   PIR; S64019; S64019.
DR   RefSeq; NP_011498.1; NM_001180882.1.
DR   PDB; 7TIF; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J/K/L=1-503.
DR   PDB; 8E3S; EM; 3.10 A; A=1-503.
DR   PDB; 8FZR; EM; 3.60 A; A=1-503.
DR   PDBsum; 7TIF; -.
DR   PDBsum; 8E3S; -.
DR   PDBsum; 8FZR; -.
DR   AlphaFoldDB; P16639; -.
DR   SASBDB; P16639; -.
DR   SMR; P16639; -.
DR   BioGRID; 33229; 34.
DR   DIP; DIP-6572N; -.
DR   IntAct; P16639; 3.
DR   MINT; P16639; -.
DR   STRING; 4932.YGL017W; -.
DR   MaxQB; P16639; -.
DR   PaxDb; 4932-YGL017W; -.
DR   PeptideAtlas; P16639; -.
DR   EnsemblFungi; YGL017W_mRNA; YGL017W; YGL017W.
DR   GeneID; 852867; -.
DR   KEGG; sce:YGL017W; -.
DR   AGR; SGD:S000002985; -.
DR   SGD; S000002985; ATE1.
DR   VEuPathDB; FungiDB:YGL017W; -.
DR   eggNOG; KOG1193; Eukaryota.
DR   GeneTree; ENSGT00500000044926; -.
DR   HOGENOM; CLU_020349_2_2_1; -.
DR   InParanoid; P16639; -.
DR   OMA; RNCCRLY; -.
DR   OrthoDB; 38036at2759; -.
DR   BioCyc; YEAST:YGL017W-MONOMER; -.
DR   BioGRID-ORCS; 852867; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P16639; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P16639; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004057; F:arginyl-tRNA--protein transferase activity; IDA:SGD.
DR   GO; GO:0016598; P:protein arginylation; IDA:SGD.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
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   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..503
FT                   /note="Arginyl-tRNA--protein transferase 1"
FT                   /id="PRO_0000195092"
FT   CONFLICT        122
FT                   /note="T -> S (in Ref. 1; AAA34439 and 2; AAD13904)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="Y -> I (in Ref. 1; AAA34439)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          11..14
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           38..42
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           67..74
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           111..124
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           139..148
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          150..158
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           164..178
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           185..192
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           199..203
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           206..212
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           213..217
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          228..236
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          239..249
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          252..260
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           262..267
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           269..283
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          288..290
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          310..313
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   TURN            314..317
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          318..322
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           323..325
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           326..329
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   TURN            330..332
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   TURN            352..356
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           373..377
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           383..398
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           434..443
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           445..449
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   TURN            450..452
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          454..457
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          460..462
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           469..471
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           474..487
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   HELIX           489..492
FT                   /evidence="ECO:0007829|PDB:7TIF"
FT   STRAND          495..499
FT                   /evidence="ECO:0007829|PDB:7TIF"
SQ   SEQUENCE   503 AA;  57930 MW;  4A4A8F1099C0825F CRC64;
     MSDRFVIWAP SMHNEPAAKC GYCHGNKGGN MDQLFALDSW AHRYMNKMDV VKIENCTIGS
     FVEHMDVATY DRMCNMGFRR SGKFLYKVDP LRNCCRLYTI RTAPQELNMT KELKKCISRF
     ATRITSEDYC PAAVASSDFV GKIVNAEMNS KTFYTRFEPA LYSEEKYHLF VKYQEKVHQD
     YNNSPKSFKR FLCDTPFGPE AVLGTQESWE QLNNWQRMKP GEKLKHMGPV HECYYYEGKL
     IAITVSDILP SGISSVYFIW DPDYSKWSLG KLSALRDLAI IQRTNLQYYY LGYYIEDCPK
     MNYKANYGAE VLDVCHSKYI PLKPIQDMIS RGKLFVIGEE ETKVTKELYL VDSETGRGEG
     FPTDNVVKYK NIAEEIYGVG GCAFKSANES ALELKELYGI PYEEEDLDTI YHLKEHNGHA
     PNGIPNVVPG LLPLWELLDI MQSGKITDLE GRLFLFEIET EGIRPLINFY SEPPNVKKRI
     CDVIRLFGFE TCMKAVILYS EQM
//