ID   SYL_RUBXD               Reviewed;         817 AA.
AC   Q1AR71;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=Rxyl_3202;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
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., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-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; CP000386; ABG06107.1; -; Genomic_DNA.
DR   RefSeq; WP_011566112.1; NC_008148.1.
DR   AlphaFoldDB; Q1AR71; -.
DR   SMR; Q1AR71; -.
DR   STRING; 266117.Rxyl_3202; -.
DR   PRIDE; Q1AR71; -.
DR   EnsemblBacteria; ABG06107; ABG06107; Rxyl_3202.
DR   KEGG; rxy:Rxyl_3202; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   PhylomeDB; Q1AR71; -.
DR   Proteomes; UP000006637; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..817
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334808"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           588..592
FT                   /note="'KMSKS' region"
FT   BINDING         591
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   817 AA;  93833 MW;  FDE42442A52BC7CD CRC64;
     MSETFAKRAS RRGYDPRAIE ERWQRRWAET GLYKTDEDPS KPKHYALTML PYPSGDLHVG
     HWYAMTPSDT RARFMRMRGY RVFFPIGFDA FGLPAENAAI KRGIHPRDWT YSNIERMRGQ
     LRQMGTMFDF DAEVVTCDPE YYRWNQWFFL KFYEKGLAYR EKAPVDWCPS CNTTLAREQV
     VGPDRRCERC DTPVIKRNLA QWLFKITDYA EELLDFSEIE WPERVKALQR NWIGRSEGAE
     IEFEIEGYGG VTVFTTRPDT LFGATFFVVA PEHPAVESIT TPERGEEVRA YVERAARMSE
     IDRADVTREK TGVFTGAYAV NPANGERIPV YVADYVLMGY GTGAIMAVPA HDERDFEFAK
     KHGIEIRTVI APPDWDGSPL ERAYVGEGQM VNSGPFDGTP SAEGREKVTG WLRERGVGRP
     AVNYRLRDWL ISRQRYWGTP IPIVYCERCG TVPVPEEDLP VLLPEDAEFM PTGESPLKFN
     DEFRKTECPR CGGPAERETD TMDTFVDSSW YQYRYLSPHY EEGPFDPERG SRWLPVDQYT
     GGIEHATMHL LYTRFFTKVM RDLGLVDFDE PMLRLFNQGV ILGPDGNRMS KSRGNVVNPQ
     EYVDRYGSDV LRCYLMFIGP WDEGGPWDPG GIEGVARWLR RAFTLVAGGD VSEAEADPGE
     LSRRTHRLVK RVTEYLEGFR FNTAIAALME HTNYLLAVKG EVGEEEWREA MRSFLLVLAP
     FAPHHAEEMW EILGEEYSVH EQGWPSWDEE LVREETVTLV VQVNGKLRDR VEAPAGVDEG
     RARELALSSE RVRAHVEGRE LRKTVYVPGR LINLVVS