ID   SYL_THEM4               Reviewed;         823 AA.
AC   A6LJM9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=Tmel_0256;
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=391009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermosipho melanesiensis BI429.";
RL   Submitted (MAY-2007) 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; CP000716; ABR30130.1; -; Genomic_DNA.
DR   RefSeq; WP_012056491.1; NC_009616.1.
DR   AlphaFoldDB; A6LJM9; -.
DR   SMR; A6LJM9; -.
DR   STRING; 391009.Tmel_0256; -.
DR   EnsemblBacteria; ABR30130; ABR30130; Tmel_0256.
DR   KEGG; tme:Tmel_0256; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001110; 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; -; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
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; PTHR43740; PTHR43740; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..823
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000071115"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           580..584
FT                   /note="'KMSKS' region"
FT   BINDING         583
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   823 AA;  95319 MW;  3202B8451A516850 CRC64;
     MKEYIPGEIE PKWQKVWAES KVFETPQRSD KKKFYNLVMF PYPSGTLHVG HVKNYVIGDI
     VARYKRMKGY NVLHPFGYDA FGLPAENAAI KNKIHPEVWT FKNIDIIRNQ IKKIGISYDW
     SREVITCTEE YYKWTQWIFL KLYENGLAYK KKAAVNWCPS CQTVLANEQV VDGKCERCGT
     EVTMKHLEQW YFKITDYAEK LLNDIDKLRG WPENVKIMQK NWIGKSTGAE IDFPVDRLDM
     KIKVFTTRPD TIWGVTFMAI APESPLVEML VTDERKDELS QFLKKVSLED RFKRTSLEAE
     KEGFFLGRYA INPVTGEKIP IYVANYILYE YGTGAIMAVP AHDQRDFDFA KKYGISIRVV
     IDNPEESIDV EKMEKAYEEE GIMVNSGPFN GMRSTLALEK IIEYLEEKGI GKRSVQYKLR
     DWLISRQRYW GAPIPIVYCE KCGIVPVPEK DLPVKLPKDV EFLPTGQSPL SLDEQFLNTT
     CPKCGGPAKR EADTMDTFVD SSWYYLRYIN PKLEDKPFDT EDINYWMPVD QYIGGVEHAV
     LHLLYSRFIT KVLYDLGYLK FEEPFENLFT QGMIYKDGWK MSKSKGNVVS PDEMIEKYGA
     DTLRTYILFM APPEKDAEWS DAGIEGVNRF LKRLWNNIYS ILPRIKDVKV EKIELKNKQE
     KDLRRKLHQS IKKITEDIEG GFKFNTAIAG LMELNNNLSE YLNSAKDLNL PLLRELVEKL
     TLILSPFAPH MAEEIWHDLG NDTLVVNEEW PAYDENALKV DEVTVIIQIN GKVRGKIQTK
     VDVSEGEIKK LAFENAKIAS YVDGREIVKV IYVKNKLLNI VVK