ID   SYL_METTP               Reviewed;         950 AA.
AC   A0B7B7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Mthe_0802;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK14591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B7B7; -.
DR   SMR; A0B7B7; -.
DR   STRING; 349307.Mthe_0802; -.
DR   EnsemblBacteria; ABK14591; ABK14591; Mthe_0802.
DR   KEGG; mtp:Mthe_0802; -.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   Proteomes; UP000000674; 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   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; 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   PANTHER; PTHR45794; PTHR45794; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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..950
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334847"
FT   REGION          928..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           629..633
FT                   /note="'KMSKS' region"
FT   BINDING         632
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   950 AA;  109145 MW;  DFCBC447C11687B6 CRC64;
     MLRNEYSAHE IEAKWQRIWE EEGVFHAEPD SRKKFFLTIP YPYLNGNLHA GHTRTFTIGD
     AIARYHRMLG ENVLFPMAFH ATGTPIVGLS ELIANRDPLI WDVYTRLHGI PEEELEKLTT
     PEAIVDYFRK QAKLAMRSIG YSIDWRREFT TTDPAYNRFI EWQFGILREK GYVTKGSHPV
     RWCPNDQNPV EDHDILRGED ATILDFTLIK FRLDDKVLPC ATLRPETVFG VTNLWVNPNV
     VHYIARVNDE VWIVSPQAYH KLTFTDRSVK KIGEIPGEEL IGKKARNPVT GDEIIILPAT
     FVDPDSGSGI VMSVPAHAPL DYLALRDLYD ADLSKYGITE DLRKIKFISL ISVPEYGEFP
     AVDAVNELGV KDQNDPKAEE ATKLVYRREF HNGVLKEITG RYAGTPVHRI KDILLQDLIN
     QGVAEIFYEF SETPVICRCG ARCVVKMVRD QWFLEYSDPV WKSRVLECLA GMQIIPEEMR
     AEFINKIDWL KDKACARRKG LGTRLPWDRE WLIESLADST IYMAFYILAK YVNAGMKIDR
     LVPQFFDYIF LGKGTPEEVS SLTGVDVDTV RRIREDFEYW YPVDLRTSGK DLVANHLLFF
     LYHHVAIFPE SLWPRAIAVN GFVSLEGQKM SKSRGPILTL KQAVAENGAD VTRLYILANA
     EYTQDADWRN DGAQATRGQV ERFYTLAREI IERNDIDESA ELTLIDRWML SRLQRRIIET
     TDALNNIQTR RALQSAFYHM LNDLRWYERR GGRNQLRRIL NVWVRLMAPF TPHICEEIWQ
     NIGEGYVSRA PWPVPDASLI DEQAERAEAY LEQTQKDIEE IIRVTKTKPR RIVLYTTPVW
     KREMLRLALE VSKGGRLDMG ALMKSAMGHP EIQSHKKDAP KYGGKLAKSV HALSGDVLAL
     DELGILSRER EYLSQAFGCP VEVYSADNPP YDPKGRAQNA EPGRPAIYIE