ID   SYLC_YEAST              Reviewed;        1090 AA.
AC   P26637; D6W3K8;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Leucine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
GN   Name=CDC60; OrderedLocusNames=YPL160W; ORFNames=P2564;
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].
RX   PubMed=1398122; DOI=10.1016/0378-1119(92)90007-c;
RA   Hohmann S., Thevelein J.M.;
RT   "The cell division cycle gene CDC60 encodes cytosolic leucyl-tRNA
RT   synthetase in Saccharomyces cerevisiae.";
RL   Gene 120:43-49(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8948103;
RX   DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA   Purnelle B., Coster F., Goffeau A.;
RT   "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT   small nuclear RNA, a new putative protein kinase and two new putative
RT   regulators.";
RL   Yeast 12:1483-1492(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 158000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X62878; CAA44671.1; -; Genomic_DNA.
DR   EMBL; X96770; CAA65561.1; -; Genomic_DNA.
DR   EMBL; Z73516; CAA97865.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11274.1; -; Genomic_DNA.
DR   PIR; JC1421; JC1421.
DR   RefSeq; NP_015165.1; NM_001183974.1.
DR   AlphaFoldDB; P26637; -.
DR   SMR; P26637; -.
DR   BioGRID; 36023; 386.
DR   DIP; DIP-6365N; -.
DR   IntAct; P26637; 19.
DR   MINT; P26637; -.
DR   STRING; 4932.YPL160W; -.
DR   BindingDB; P26637; -.
DR   ChEMBL; CHEMBL1075253; -.
DR   DrugCentral; P26637; -.
DR   iPTMnet; P26637; -.
DR   MaxQB; P26637; -.
DR   PaxDb; 4932-YPL160W; -.
DR   PeptideAtlas; P26637; -.
DR   EnsemblFungi; YPL160W_mRNA; YPL160W; YPL160W.
DR   GeneID; 855943; -.
DR   KEGG; sce:YPL160W; -.
DR   AGR; SGD:S000006081; -.
DR   SGD; S000006081; CDC60.
DR   VEuPathDB; FungiDB:YPL160W; -.
DR   eggNOG; KOG0437; Eukaryota.
DR   GeneTree; ENSGT00390000012163; -.
DR   HOGENOM; CLU_004174_1_1_1; -.
DR   InParanoid; P26637; -.
DR   OMA; KFIEWQF; -.
DR   OrthoDB; 5472610at2759; -.
DR   BioCyc; YEAST:G3O-34056-MONOMER; -.
DR   BRENDA; 6.1.1.4; 984.
DR   BioGRID-ORCS; 855943; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P26637; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P26637; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IDA:SGD.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IDA:SGD.
DR   GO; GO:1903432; P:regulation of TORC1 signaling; IMP:SGD.
DR   CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   NCBIfam; TIGR00395; leuS_arch; 1.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1090
FT                   /note="Leucine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000152155"
FT   MOTIF           66..76
FT                   /note="'HIGH' region"
FT   MOTIF           729..733
FT                   /note="'KMSKS' region"
FT   BINDING         732
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         142
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   1090 AA;  124142 MW;  199B5A69089914C1 CRC64;
     MSSGLVLENT ARRDALIAIE KKYQKIWAEE HQFEIDAPSI EDEPITMDSE ELHRTYPKFM
     SSMAYPYMNG VMHAGHCFTL SKVEFSIGFE RMNGKRALFP LGFHCTGMPI LACADKLKRE
     AELFGKNFDN VPAEEEEIKE ETPAEKDHED VTKFKAKKSK AAAKKGRGKY QFEIMLQLGI
     PREEIIKFAD AKYWLTYFPP LCESDCTSLG ARIDWRRSFV TTDANPYYDA FIRWQMNKLK
     AAGKIKFGER YTIYSEKDGQ ACMDHDRQSG EGVTPQEYIG VKIEALEFAD DAAKIIDSSS
     DLDKSKKFYF VAATLRPETM YGQTCCFVSP TIEYGIFDAG DSYFITTERA FKNMSYQKLT
     PKRGFYKPIV TVPGKAFIGT KIHAPQSVYP ELRILPMETV IATKGTGVVT CVPSNSPDDY
     ITTKDLLHKP EYYGIKPEWI DHEIVPIMHT EKYGDLTAKA IVEEKKIQSP KDKNLLAEAK
     KIAYKEDYYT GTMIYGPYKG EKVEQAKNKV KADMIAAGEA FVYNEPESQV MSRSGDDCIV
     SLEDQWYVDY GEESWKKQAI ECLEGMQLFA PEVKNAFEGV LDWLKNWAVC RTYGLGTRLP
     WDEKYLVESL SDSTIYQSFY TIAHLLFKDY YGNEIGPLGI SADQMTDEVF DYIFQHQDDV
     KNTNIPLPAL QKLRREFEYF YPLDVSISGK DLIPNHLTFF IYTHVALFPK KFWPKGIRAN
     GHLMLNNSKM SKSTGNFMTL EQTVEKFGAD AARIAFADAG DTVEDANFDE SNANAAILRL
     FNLKEWAEEI TKESNLRTGE ITDFFDIAFE HEMNALIEKT YEQYALTNYK NALKYGLFDF
     QAARDYYREA SGVMHKDLIA RYIETQALLL APIAPHFAEY IYREVLGNQT SVQNAKFPRA
     SKPVDKGVLA ALDYLRNLQR SIREGEGQAL KKKKGKSAEI DASKPVKLTL LISESFPEWQ
     SQCVEIVRKL FSEQTLDDNK KVREHIEPKE MKRAMPFISL LKQRLANEKP EDVFERELQF
     SEIDTVKAAA RNVKKAAQAL KIAEFSAISF PYGAKTGKDI FTGEEVEIPP VTKIVENAVP
     GNPGVVFQNI
//