ID   SYL_STRCO               Reviewed;         966 AA.
AC   Q9RDL5;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 131.
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=SCO2571; ORFNames=SCC123.09c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939113; CAB66249.1; -; Genomic_DNA.
DR   RefSeq; NP_626809.1; NC_003888.3.
DR   RefSeq; WP_003976232.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; Q9RDL5; -.
DR   SMR; Q9RDL5; -.
DR   STRING; 100226.gene:17760173; -.
DR   PaxDb; 100226-SCO2571; -.
DR   PATRIC; fig|100226.15.peg.2616; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   InParanoid; Q9RDL5; -.
DR   OrthoDB; 9810365at2; -.
DR   PhylomeDB; Q9RDL5; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 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; 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; 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; Reference proteome.
FT   CHAIN           1..966
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152093"
FT   REGION          561..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           71..82
FT                   /note="'HIGH' region"
FT   MOTIF           734..738
FT                   /note="'KMSKS' region"
FT   BINDING         737
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   966 AA;  107128 MW;  87C81658A6C12B87 CRC64;
     MSETNPAATA PVSADAAPHR YTAAMAAEIE ARWQDFWDAE GTYAAPNPKG DLAGDPELVA
     KPKKFIMDMF PYPSGAGLHV GHPLGYIATD VFARFQRMTG HNVLHTLGFD AFGLPAEQYA
     VQTGTHPRVS TEANMKNMQS QLRRLGLGHD RRRSFATIDP EYYKWTQWIF LQIFNSWYDD
     EAKKARPIAE LVAQFASGER EVPGHAGRAW SSLSEAERAD VLGEYRLAYA SDAPVNWCPG
     LGTVLANEEV TADGRSERGN FPVFKSKLRQ WNMRITAYAD RLLDDLDQLD WPEAIKLQQR
     NWIGRSEGAR VDFPVDGERI TVFTTRPDTL FGATYMVLAP EHPLVEKFTP AVWPEGTRDA
     WTGGHATPTE AVAAYRAQAA SKSDVERQAE AKDKTGVFIG AYATNPVNGE QVPVFVADYV
     LMGYGTGAIM AVPAHDSRDF EFARAFELPV RCVVEPTDGR GTDTSTWDEA FASYDAKIVN
     SSGTDVSLDG LGVVEAKERV TEWLERAGAG AGTVNFRLRD WLFSRQRYWG EPFPIVYDED
     GIAHPLPDSM LPLELPEVED YSPRTFDPDD ADTKPETPLS RNEDWVHVTL DLGDGRGPRK
     YRRETNTMPN WAGSCWYELR YLDPHNGERL VDPEIEQYWM GPREGLPHGG VDLYVGGAEH
     AVLHLLYARF WSKVLFDLGH VSSAEPFHKL FNQGMIQAYV YRDSRGIAVP AAEVEERDGA
     YYYQGEKVSR LLGKMGKSLK NAVTPDEICA EYGADTLRLY EMAMGPLDVS RPWDTRAVVG
     QFRLLQRLWR NVVDEDTGEL SVADVAESDI DAGTLRALHK AVDGVRQDLE GMRFNTAIAK
     VTELNNHLTK AGGPVPRSVA ERLVLLVAPL APHVAEELWR KLGHESSVVH EDFPVADPAY
     VVDETVTCVV QIKGKVKARL EVAPSISEDD LEKAALADEK VVAALGGAGI RKVIVRAPKL
     VNIVPA
//