ID   SYLC_CAEEL              Reviewed;        1186 AA.
AC   Q09996;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Leucine--tRNA ligase;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
GN   Name=lars-1 {ECO:0000312|WormBase:R74.1};
GN   Synonyms=lrs-1 {ECO:0000312|WormBase:R74.1};
GN   ORFNames=R74.1 {ECO:0000312|WormBase:R74.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23076791; DOI=10.1152/ajpcell.00294.2012;
RA   Lee E.C., Strange K.;
RT   "GCN-2 dependent inhibition of protein synthesis activates osmosensitive
RT   gene transcription via WNK and Ste20 kinase signaling.";
RL   Am. J. Physiol. 303:C1269-1277(2012).
CC   -!- FUNCTION: Involved in protein synthesis (PubMed:23076791). Catalyzes
CC       the specific attachment of an amino acid to its cognate tRNA in a 2
CC       step reaction: the amino acid (AA) is first activated by ATP to form
CC       AA-AMP and then transferred to the acceptor end of the tRNA.
CC       {ECO:0000269|PubMed:23076791, ECO:0000305}.
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   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an increase in
CC       the expression of gpdh-1 independent of hypertonic stress.
CC       {ECO:0000269|PubMed:23076791}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; Z36238; CAA85280.1; -; Genomic_DNA.
DR   EMBL; Z46787; CAA85280.1; JOINED; Genomic_DNA.
DR   PIR; T19334; T19334.
DR   RefSeq; NP_497837.1; NM_065436.5.
DR   AlphaFoldDB; Q09996; -.
DR   SMR; Q09996; -.
DR   BioGRID; 40775; 21.
DR   IntAct; Q09996; 1.
DR   STRING; 6239.R74.1.1; -.
DR   EPD; Q09996; -.
DR   PaxDb; 6239-R74-1-1; -.
DR   PeptideAtlas; Q09996; -.
DR   EnsemblMetazoa; R74.1.1; R74.1.1; WBGene00003073.
DR   GeneID; 175538; -.
DR   KEGG; cel:CELE_R74.1; -.
DR   UCSC; R74.1.1; c. elegans.
DR   AGR; WB:WBGene00003073; -.
DR   WormBase; R74.1; CE16317; WBGene00003073; lars-1.
DR   eggNOG; KOG0437; Eukaryota.
DR   GeneTree; ENSGT00390000012163; -.
DR   HOGENOM; CLU_004174_1_1_1; -.
DR   InParanoid; Q09996; -.
DR   OMA; KFIEWQF; -.
DR   OrthoDB; 5472610at2759; -.
DR   PhylomeDB; Q09996; -.
DR   PRO; PR:Q09996; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003073; Expressed in larva and 4 other cell types or tissues.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR   GO; GO:0006412; P:translation; IMP:UniProtKB.
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; IPR001412; aa-tRNA-synth_I_CS.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1186
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152152"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           718..722
FT                   /note="'KMSKS' region"
FT   BINDING         721
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1186 AA;  134520 MW;  7CC479B71AB53979 CRC64;
     MSKINKERKK VAQLQEIEKS IQELWESKKA FEADARDDGK PKYLVTFPFP YMNGRLHLGH
     TFSASKCEFA AGFQRLQGKE VLFPFGFHCT GMPIKACADK LKREMQDFGY PPNFPEDVVE
     EVKEEVSAVD EIIKDKSKGK KSKLVAKTGN AKYQWQIMKS LGLCDEEIKE FSDPNHWLYY
     FPPHCIADLK KMGLKADWRR SFITTDVNPY FDSFVRWQFN LLRAAKKIDF GKRYTIYSPK
     DGQPCMDHDR ASGEGVGPQE YTLIKLKVLD PKPQALSHIK EDIYLVAATL RPETMYGQTN
     CYLHPDIQYS VFYATENEKQ VFVATARSAR IMSYQGLTKE NGKVNYVLGL EKIAGSKILG
     APLSAPLAKY ERVYALPMLT IKDDKGTGVV TSVPSDSPDD FAALSDLKKK KPLREKYGLT
     DEMVLPFEPV PIIKIEGLGD LAAVEMCSRL KIESQNEKDK LEEAKKEVYL KGFYDGVMLV
     GKYAGKKTAD VKKVIQDDLT AEGLATKYVE PEKKVMSRSG DECVVALCDQ WYLNYGEAEW
     KAAAKKVLEP LRTFNDETRR GLETTVDWLH EYACSRSYGL GTKLPWDTQY LIESLSDSTI
     YNAYYTVAHL LQQGAFDGSV VGPAGIKADQ MTDASWSYVF LGEIYDSKTM PVEEEKLKSL
     RKEFMYWYPI DMRASGKDLI GNHLTYLLFN HAAIWPTDTS KWPKGIRANG HLLLNNEKMS
     KSTGNFMTLE EAIEKFSADG MRLSLADAGD GLEDANFVYA MADAAILRLF TMIEWIKEMI
     EQRDAGLLRK DAKKFADRVF ANEMNSLIAA TEQNYEATNF KDALKTGFFE YQAIRDTYRE
     LCAGIDEPMS ESLVFRFIET QMLILSPICP HIAEYIWQLL GKDGLIVNAP WPTVDPVDEK
     LAIGARFITE SLAEFRARLK TYMTPKKKAL KEIPEVPTEA VIYVAKEYPP WQKTILDILE
     KQAKANNGAL PDNKAISQLI GKEESLKKFA KKAMPFVQMI KERFEQKGVS ALASSSPVDQ
     TSILNENIDF IMNALDLDRV TIRHTDEEGI DANIVETTVP LVPMLNFTPN RPTIKLVARN
     VQICNAMFDV DVPIVNGDSV SMVIRKMRRI SKAIKPKFEV SLWRYKNAVW GDRQMISYRN
     PFEENIQLSD ADIFNFEADN KISVTSGSEK FDLGRTIVYK ANVPEN
//