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   16-JUN-2009, entry version 62.
DE   RecName: Full=Leucyl-tRNA synthetase;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucine--tRNA ligase;
DE            Short=LeuRS;
GN   Name=lrs-1; ORFNames=R74.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP +
CC       diphosphate + L-leucyl-tRNA(Leu).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; Z36238; CAA85280.1; -; Genomic_DNA.
DR   EMBL; Z46787; CAA85280.1; JOINED; Genomic_DNA.
DR   EMBL; Z46787; CAA86751.1; -; Genomic_DNA.
DR   EMBL; Z36238; CAA86751.1; JOINED; Genomic_DNA.
DR   PIR; T19334; T19334.
DR   RefSeq; NP_497837.1; -.
DR   UniGene; Cel.34027; -.
DR   IntAct; Q09996; 5.
DR   Ensembl; R74.1; Caenorhabditis elegans.
DR   GeneID; 175538; -.
DR   KEGG; cel:R74.1; -.
DR   WormBase; WBGene00003073; lrs-1.
DR   WormPep; R74.1; CE16317.
DR   OMA; Q09996; HVTGTPI.
DR   BRENDA; 6.1.1.4; 672.
DR   NextBio; 888576; -.
DR   ArrayExpress; Q09996; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0040007; P:growth; IMP:WormBase.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
DR   GO; GO:0000003; P:reproduction; IMP:WormBase.
DR   InterPro; IPR015413; aa-tRNA-synt_I.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   TIGRFAMs; TIGR00395; leuS_arch; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1   1186       Leucyl-tRNA synthetase.
FT                                /FTId=PRO_0000152152.
FT   MOTIF        50     60       "HIGH" region.
FT   MOTIF       718    722       "KMSKS" region.
FT   BINDING     721    721       ATP (By similarity).
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
//