ID   SYL_RHOJR               Reviewed;         945 AA.
AC   Q0SAL1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=RHA1_ro03622;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG95425.1; -; Genomic_DNA.
DR   RefSeq; WP_011596228.1; NC_008268.1.
DR   AlphaFoldDB; Q0SAL1; -.
DR   SMR; Q0SAL1; -.
DR   STRING; 101510.RHA1_ro03622; -.
DR   EnsemblBacteria; ABG95425; ABG95425; RHA1_ro03622.
DR   KEGG; rha:RHA1_ro03622; -.
DR   PATRIC; fig|101510.16.peg.3650; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000008710; 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; -; 3.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; 1.
DR   Pfam; PF08264; Anticodon_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..945
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334804"
FT   MOTIF           66..77
FT                   /note="'HIGH' region"
FT   MOTIF           716..720
FT                   /note="'KMSKS' region"
FT   BINDING         719
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   945 AA;  105846 MW;  F7F47175CDDBCE1C CRC64;
     MTEHVQPANP SDATPQHRYT AELAGQIEQR WQDRWSEEGT FNAPNPVGPL AGDVPADKLF
     VQDMFPYPSG TGLHVGHPLG YIATDVFARY HRMQGHNVLH TLGYDAFGLP AEQYAVQTGT
     HPRTTTEANI VNMKRQLRRL GLGHDERRTF ATTDTDFYHW TQWIFLQIHD AWFDKEAGKA
     RRISELEAEF VSGARSLEDG REWASLSVSE KEAVLDSYRL VYHSDSMVNW CPGLGTVLAN
     EEVTADGRSD RGNFPVFRKH LQQWMMRITA YSDRLVDDLE YLDWPEKVKT MQRNWIGRSH
     GAQVKFQADG HEIEVFTTRP DTLFGATYVT LAPEHELVDD IVAAEWPRGV DSRWTGGAAT
     PAEAVAAYRK SIAAKSDLER QEYKEKTGVF LGTYAVNPVN GHKLPVFIAD YVLTGYGTGA
     IMAVPGHDHR DYEFATEFGL DIVEVISGGD LTKDAYTGDG TIVNSDFLNG MSVADAKKAI
     TERLEADGTG KGTIQYKLRD WLFARQRYWG EPFPIVYDAE GNAHALPESS LPVELPEVED
     YAPVSFDPDD ASSEPSPPLA KAVDWVNVEL DLGDGLQTYR RDTNVMPQWA GSSWYQLRYI
     DPTNPDVFCD KENERYWTGP RPEIHGPNDP GGVDLYVGGV EHAVLHLLYS RFWHKVLFDL
     GYVSSSEPYR RLYNQGYIQA YAYTDARGVY VPADEVEEKD GKFFHQGVEV NREYGKMGKS
     LKNSVSPDEI CEEYGADTLR VYEMSMGPLD TSRPWATKDV VGAQRFLQRA WRVVVDEESG
     ALRVTDDAPA EDTLRALNKA IAGVSEDYTA LRDNTAAAKL IEYTNHLTKA YPGGAPRSVV
     EPLVLMLAPL APHLAEELWS RLGHEKSLAH GPFPVAEEKW LVEDTVEYPI QVNGKVRSRV
     TVAADAPREE IEKIALADDK IVALLDGQDP RKVIVVPGKM VNIVR