ID   SYL_GEODF               Reviewed;         824 AA.
AC   B9M9F3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=Geob_2171;
OS   Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS   daltonii).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=316067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) 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; CP001390; ACM20525.1; -; Genomic_DNA.
DR   RefSeq; WP_012647254.1; NC_011979.1.
DR   AlphaFoldDB; B9M9F3; -.
DR   SMR; B9M9F3; -.
DR   STRING; 316067.Geob_2171; -.
DR   KEGG; geo:Geob_2171; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000007721; 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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; Reference proteome.
FT   CHAIN           1..824
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199208"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           581..585
FT                   /note="'KMSKS' region"
FT   BINDING         584
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   824 AA;  93327 MW;  03B7E84C731369F9 CRC64;
     MEEKYVPARV EEKWQKLWDS NKSFKAEKVE GKSKYYLLEM FPYPSGRIHM GHVRNYSIGD
     VIARFKRMKG FNVLHPMGWD AFGMPAENAA IQHKSHPAKW TYENIDYMRG QLKKMGFSYD
     WDRELATCNV EYYKWEQLIF LQMLEKGLAY KKKSSVNWCP RCETVLANEQ VEDGSCWRCD
     SLVEQKELEQ WSFRITDYAE ELLEDTYKLP GWPERVLTMQ RNWIGRSTGC EIDFSIEGRK
     DAIKVFTTRQ DTLFGATFMS LAPEHPLALQ LTTAENMIVV NAFLDKVKKT DKIKRTAEDF
     EKEGVFTGSY CINPVTNRRM PIYLANFVLT DYGTGAVMAV PTHDQRDFEF ARKYAIAMEV
     VIQPEGGSLD VATMTEAYTA EGIMVNSGRF DGLNSAVAKE QIADFLEQEG LGKKTVNFRL
     RDWGISRQRY WGNPIPVIYC DDCGAVPVPA KDLPVVLPMD ATFTGEGGNP LSKIDSFIKT
     TCPLCGKDAR RETDTMDTFV ESSWYFLRYC CPDFACGPLD KGKTEYWMSV DQYIGGIEHA
     VMHLLYARFF TKVLRDLGYC DINEPFTNLL TQGMVIKDGS KMSKSKGNVV DPNALIEKYG
     ADTARLFSLF AAPPEKDLDW SDQGVDGSYR FLNRVWKLVY ECLPLISATG PLDAAALTDE
     GKTLRRLVHK TIRKVSDDIE DRFHFNTAIA AIMEMVNAIQ AFEPKNQPRN VPVLKEAVES
     VVLLLAPFVP HFAEELWESL GHEDNLNEAA WPAFDAAAAV DEELLVVVQV NGKLRGKVTV
     AASATDEDIK GAVLADEKIR QLIDGMNIKK IVYVPGKLVN IVVG
//