ATE1_YEAST
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 03-AUG-2022, entry version 167.
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 AlphaFoldDB; P16639; -.
DR BioGRID; 33229; 29.
DR DIP; DIP-6572N; -.
DR IntAct; P16639; 3.
DR MINT; P16639; -.
DR STRING; 4932.YGL017W; -.
DR MaxQB; P16639; -.
DR PaxDb; P16639; -.
DR PRIDE; P16639; -.
DR EnsemblFungi; YGL017W_mRNA; YGL017W; YGL017W.
DR GeneID; 852867; -.
DR KEGG; sce:YGL017W; -.
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; WEQLNNW; -.
DR BioCyc; YEAST:YGL017W-MON; -.
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:arginyltransferase 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; PTHR21367; 2.
DR Pfam; PF04377; ATE_C; 1.
DR Pfam; PF04376; ATE_N; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW 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"
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
