ID   SYL_FRACC               Reviewed;        1064 AA.
AC   Q2J641;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=Francci3_3901;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / HFP020203 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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}.
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DR   EMBL; CP000249; ABD13251.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2J641; -.
DR   SMR; Q2J641; -.
DR   STRING; 106370.Francci3_3901; -.
DR   KEGG; fra:Francci3_3901; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OrthoDB; 9810365at2; -.
DR   PhylomeDB; Q2J641; -.
DR   Proteomes; UP000001937; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 3.40.50.620; HUPs; 3.
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; 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: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; 2.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1064
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334759"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           106..117
FT                   /note="'HIGH' region"
FT   MOTIF           831..835
FT                   /note="'KMSKS' region"
FT   BINDING         834
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   1064 AA;  116146 MW;  8AB4FEFDF66F6DF6 CRC64;
     MARAMSETAE PGARTGAADT TVAPTGASGG IIPAAAGTAG GAPAGTGSVE PSFRYDARLA
     ADIERRWQRR WADEGTFNSP NPVGPLSTGF EKVAGREPFY IMDMFPYPSG SGLHVGHPLG
     YIGTDVFARY LRMSGRHVLH PFGYDSFGLP AEQYAINTGQ HPRDTTNANI ANMRRQLSRL
     GLGHDTRREI ATTDVGYYRW TQWIFQQIFN SWYDPQAGRA RPIAELIEEF AAGTRAPVAG
     PAGGNTAVSV DAVRAANPAG LAWTELDEVS RRKVVNAHRL AYISEQLVNW CPGLGTVLAN
     EEVTADGRSD IGNYPVFRRP LKQWILRITA YAERLISDLD LVDWPDSIKQ MQRNWISPSE
     GASVEFTVVA PGEEAGASDP SGSSTARRIE VYTTRPDTLA GATFLVLAPE HPLADALIAD
     TWPADTPVSW RFPAGRPGGG TEPADTAGPE AGADPAWTPR AAVDAYREFA AHRSDRQRGE
     EVIDRTGVFT GSYVRNPVGG GVIPVFLADY VLLGYGTGAI MAVPAHDSRD FSFARAFDLP
     IPAVLEPDAD WYAAHGVVPA TPSAQWPEAF SGAGEYRPGP ASAPVLVGLS KSEAIKATVH
     WLEEIGAGRS ARSYRLRDWL FSRQRYWGEP FPIVFDVDGL PHAVPDELLP IELPEMTDFR
     PTAMAEDDAS DPVPPLARVA DWVTVTLDLG DGPKQYRRET NTMPQWAGSC WYYLRYLDPT
     NTERFVDPTV ERYWMARPGA VPGDGGVDLY VGGVEHAVLH LLYARFWHKV LYDLGHVSTK
     EPFKRLFNQG YIQADAFTDA RGMYVPAAEV TATPDGRFLF QGAPVNRRSG KMGKSLKNSV
     SPDEMYDRFG ADTLRVYEMA MGPLDADRPW HTDDIVGSHR FLQRLWRTVV DETTGAAAVV
     DEPLDDEALR VLHRTILTVT AEYAGLRFNT AVARLIELTN FVSKSYGKSP TPRALAEPLT
     LMAAPLAPHI AEELWSRLGH EESVSTVAFP IGDPALAAES VRTIPVQVNG KVRFTIEVPD
     GSAEQTVRDL LAAHPEFARQ TDGRTIKKII VVPGRIVNIA ISPA
//