ID   SYL_THEFY               Reviewed;         830 AA.
AC   Q47MY0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 141.
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=Tfu_2156;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000088; AAZ56189.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47MY0; -.
DR   SMR; Q47MY0; -.
DR   STRING; 269800.Tfu_2156; -.
DR   KEGG; tfu:Tfu_2156; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OrthoDB; 9810365at2; -.
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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
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; 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..830
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334834"
FT   REGION          379..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           593..597
FT                   /note="'KMSKS' region"
FT   BINDING         596
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   830 AA;  92640 MW;  1A44B3A2BAE1EACE CRC64;
     MTAVSGDQTT SGSYDVRALQ EKWQARWAKE NPFTASEDPA DPRPRRYVLD MFPYPSGDLH
     MGHAEAFAIG DVIARYHFAR GENVLHPIGW DSFGLPAENA AIKHNFHPAE WTYTNIETQA
     ESFRRYAISL DWSRRLHTSD PEYYRWNQWF FLRFFERGLA YRKDGLVNWC PKDQTVLANE
     QVIQGKCERC GTEVERRALN QWYFKITDYA QRLLDDMEQL EGKWPERVLT MQRNWIGRSE
     GADVQFTIEG REEPVTVFTT RPDTLYGATF FVVAPDSPLA DELCAPEQRE AFEAYRTQVS
     KLSDIERQST EREKTGVFLG RYAINPVNGE RIPVWAADYV LADYGHGAIM AVPAHDQRDL
     DFARKFNLPV RVVVDTGEPD PAETGIATPG EGTLINSGPL NGLSKSEAIP RIIEILTERG
     TGKAAVNYRL RDWLVSRQRF WGTPIPIIHC PECGEVPVPD EELPVRLPDL RGAALAPKGV
     SPLAAATDWV NVSCPRCGGP AKRDTDTMDT FVDSSWYFLR YCSPNLDTAP FDQEKVAKWG
     PIDQYVGGVE HAILHLLYSR FFTKVLYDMG MVPFTEPFVR LLNQGQVINQ GKAMSKSLGN
     GVDLGQEIDR YGVDAVRLTM VFAGPPEEDI DWADVSPGAS VKFLNRAYRV MAEAAAASAP
     GVDPATGDLA LRRMTHQTLA KVTEAVEAQR FNVAIARIME LVTAARRAID SGPGAADPAV
     REAAEVIAIT LGLFAPYVAE EGWEMLGHTG SVSVGTWREP DPALLVQESV TCVVQVASKV
     RDKLQVSPDI SAEELERLAL ASEKVQNHIA GREIRRIVVR EPKLVNIVVA
//