ID   SYL_METKA               Reviewed;         943 AA.
AC   Q8TVM4;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=MK1364;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC   Methanopyraceae; Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02577.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TVM4; -.
DR   SMR; Q8TVM4; -.
DR   STRING; 190192.MK1364; -.
DR   PaxDb; 190192-MK1364; -.
DR   EnsemblBacteria; AAM02577; AAM02577; MK1364.
DR   KEGG; mka:MK1364; -.
DR   PATRIC; fig|190192.8.peg.1516; -.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; Q8TVM4; -.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000001826; 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; 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; 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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..943
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152132"
FT   REGION          910..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT   MOTIF           623..627
FT                   /note="'KMSKS' region"
FT   COMPBIAS        919..933
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   943 AA;  108672 MW;  9B5D4567D2588094 CRC64;
     MAERPEERQW KEWEEAGLFE ADPDDRESVY ITVAYPYPSG SMHVGHARTY LVPDIYARFK
     RMQGYNVLFP MAFHVTGTPV VGIAERIKEG DEDTIRLYRD LYGVPEEELE KFTEPEAIVE
     YFAREYEENM KRMGYSIDWR RKFTTVDPEY RSFITWQYLR LREKGLVDKG EHPVRYCPHC
     ENPVGDHDLL EGEDATIEEL TLVKFPVEGD DLILVAATFR PETLYGATNV WVKPDEEYLV
     VEVDGERWVV SEEAYRNLRH QKDGVEKVDT VRGEELIGES VVNPVTGEAL PVLPAEFIDP
     KFGTGVVYSV PAHAPADAAA LEDLKKDPSV LEEYGVDPSV VEELEPVQVI EVEGYGEFPA
     YDALEEHGIE SQTDPELEKA TQEVYRAELH KGVMVVDEFE GTPVREAREE IKSRLIESGD
     ADVMYDFSEK PVICRCGTEC VVRILKDQWF LRYSDGEWKE RAEELLGRME IVPEEVRANF
     EDTIEWLDDW ACARRVGLGT PLPWDPDWIV EPLSDSTVYM AYYTIAHRLK GKGELPPEVF
     DYVFLGEGDP EEIAEKAGLD VEELEAMREE FEYWYPLNWR LSAKDLVTNH LTFFIFHHAA
     LFPEDKWPKG IVVFGMGLLE GQKMSSSKGN VVLLSEALDE YGPDVVRLFL ATSAEPWQDF
     DWRDEYVRGV QRHLERFETL IRDHADESVE DKDAVDRWFL HEFREVVEET TEALEGFQIR
     RAYNRAFYGV MKLLREYEAM KGHVKILGEI AEDWLKLLHP VIPFATDRLW REVLGEDSFL
     LEEEWPDPSE YPEEPELSVA KEVLDRLIED VRDVEKVIGA EPGYTLHVYL APEWQWRALE
     LILKDKEFGE VMSELMKDEG LREKGDEVAK IVQELTKEDL PEDVDVDALR EALTEFLEAA
     GRALTDKTGA SEVVIHTDPE EAPGPEDRKA GARPLRPGIW LEE
//