SYLC_CAEEL
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 03-AUG-2022, entry version 147.
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; 19.
DR IntAct; Q09996; 1.
DR STRING; 6239.R74.1.1; -.
DR EPD; Q09996; -.
DR PaxDb; Q09996; -.
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 CTD; 175538; -.
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; AWNMAFQ; -.
DR OrthoDB; 75155at2759; -.
DR PhylomeDB; Q09996; -.
DR PRO; PR:Q09996; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003073; Expressed in larva and 4 other 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 Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 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; 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 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
