ID   SYL_METJA               Reviewed;         942 AA.
AC   Q58050;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 129.
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}; OrderedLocusNames=MJ0633;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB98628.1; -; Genomic_DNA.
DR   PIR; A64379; A64379.
DR   AlphaFoldDB; Q58050; -.
DR   SMR; Q58050; -.
DR   STRING; 243232.MJ_0633; -.
DR   PRIDE; Q58050; -.
DR   EnsemblBacteria; AAB98628; AAB98628; MJ_0633.
DR   KEGG; mja:MJ_0633; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; Q58050; -.
DR   OMA; AWNMAFQ; -.
DR   PhylomeDB; Q58050; -.
DR   Proteomes; UP000000805; 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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR45794; PTHR45794; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..942
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152131"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           633..637
FT                   /note="'KMSKS' region"
FT   BINDING         636
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   942 AA;  110184 MW;  25A551461566A399 CRC64;
     MMVMIDFKEI EKKWQKRWEE AKIFEANPDD REKFFITAAF PYLNGVLHAG HLRTFTIPEV
     VARFQRMKNK NVLWTFGYHV TGTPILGLAE LIKNRDEKTI WAYTELHGIP KEELLELTTP
     EKIVEYFSKK AEEAFKRMGF SLDWRRNFKT DDKVFNKFIE WQFHKLKEKG LIVKGSHPVR
     YCPRCDNPVE DHDILVGENA TLVEYILIKF TTEDGCIMPM ATLRPETVFG VTNVWVNPEA
     TYVKAKVYLE KETENGIELI ENGIWIMAKE CAEKLKHQDR KIEIIEEFKG EQLINKKVKN
     PVTGKEVPIL PAKFVKTNIG TGCVMSVPAH APYDYIALRD LGLVDEIGLI PLINVPGYGK
     YPAKEIVEKM GIKSQEEEDK LEEATKKIYK DEFHKGVLNE NCLDYEGIPV REIKDKLTKD
     LIDKGLAEIM YEFSEEKVIC RCGTPCIVKM VKGQWFIKYS DEKWKELAHK CIDKMRFIPE
     NLRQVFHEKI DWMKDKACVR RRGLGTKFPF EEGWVIESLS DSTIYPAYYT VAKYINQHNI
     KPEQLTLELF DYVFLGKGDV DKIAKETGIP KDIIEGMRKE FIYYYPVDWR CSAKDLIPNH
     LTFYIFNHVA IFPEEFWPRG IVVNGYVTIE GKKLSKSKGP VLPVLEVAEK FGADVGRFYI
     TTCAELPQDA DIKFKEMENT KKVLERLYLF AKEIAERRGE TGEEFSYIDK WLLSRLYKAV
     KQYDEYMENF ELRKAGILLY QLLDDLKWYR RRGGNNIRVL EEFLEVIIKL MMPFTPHLCE
     EMWEILGKEG FVSLAKFPEV KEEFINDEIE KGEEYLKAVM EDIKEIINVA KVQPKRIYLY
     TADDWKYEIL KIIKENEGKT IKELMPIIMK NPEFRKYGKE IPKLVNQLIK LNAEIINEVE
     VLENAKEFLK KEVGVEDIII NGEDKANKKR VAIPFKPAIY LE