ID   SYL_THEON               Reviewed;         967 AA.
AC   B6YST9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=TON_0141;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; CP000855; ACJ15626.1; -; Genomic_DNA.
DR   RefSeq; WP_012571099.1; NC_011529.1.
DR   AlphaFoldDB; B6YST9; -.
DR   SMR; B6YST9; -.
DR   STRING; 523850.TON_0141; -.
DR   GeneID; 7017795; -.
DR   KEGG; ton:TON_0141; -.
DR   PATRIC; fig|523850.10.peg.141; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR020791; Leu-tRNA-lgase_arc.
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; 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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..967
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199235"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           650..654
FT                   /note="'KMSKS' region"
FT   BINDING         653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   967 AA;  113529 MW;  BC2818D12683C5ED CRC64;
     MAELNFKAIE EKWQKRWMED RVFEPDRNAK PKEKKFYITV AFPYLSGHLH VGHARTYTIP
     DVIARFKRMQ GYNVLFPMAW HITGAPIVGI AERIKNRDPK TIHIYRDVYK VPEEILWKFE
     DPKEIVKYFM KAARETFIRA GFSVDWSREF HTTSLFPPFS KFIEWQFWTL KDMGLVVKGA
     HRVRWDPVVG TPLGDHDIME GEDVQILEYV IIKFILEENG EEIYMPAATL RPETVYGVTN
     MWLNPEAIYV KAKVRRGDRE ETWIISKEAA YKLSFQDREI EVIEEFKGER LIGKYVKNPV
     TGDEVIILPA EFVDPDNATG VVMSVPAHAP FDHVALEDLK KETEILLKYD IDPRVVEEIS
     YISLIKLEGY GEFPAVEEVE KLGVKSQKDE EKLEEATKNI YKAEYHKGVF KIEPYAGKPV
     QEVKDLIAKE LQEKGIAEIM YEFAEKPVIS RFGNQAVIKI IHDQWFIDYG NPEWKEKARE
     ALANMTIYPE SRRTQFEAVI DWLDKKACAR KVGLGTPLPW DPEWVIESLS DSTIYMAYYT
     ISRHINKLRE EGRLDPEKLD REFFDYLFRE EFSEEREKEL AEKTGIPAEI IHEMKEEFEY
     WYPLDWRCSA KDLIPNHLTF FIFNHVAIFR KGHWPRGIAV NGFGTLEGQK MSKSKGNVLN
     FIDAIEENGA DVVRLYIMGL AEHDSDFDWR RKEVGKLRKQ VERFYELVSE FASYEAKEGV
     ELKDIDRWML HRLNKAIEGA TKGLEEFRTR TAVQWAFYSV LNDLRWYLRR TEGRDDEAKR
     YVLRTLADVW VRLMAPFTPH ISEELWEKLG GEGFVSLAKW PEPNPAWWNE TIELEEEYVK
     NLIEDIKEII RVAKIEDAKR AYIYTAPEWK WRVAEAVAEK RDFKAAMSEL MKDPEMRKHG
     KEISKMIQRL IKDRAFEIKR IDEEKALREA KDFIEKELGL EIIINPEEDK GGKKKAAMPM
     KPAVFVE
//