SYLC_YEAST
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 03-AUG-2022, entry version 189.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 359.
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; P26637; -.
DR PRIDE; P26637; -.
DR EnsemblFungi; YPL160W_mRNA; YPL160W; YPL160W.
DR GeneID; 855943; -.
DR KEGG; sce:YPL160W; -.
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; AWNMAFQ; -.
DR BioCyc; YEAST:G3O-34056-MON; -.
DR BRENDA; 6.1.1.4; 984.
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 Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR45794; PTHR45794; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00395; leuS_arch; 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
