ID   SYL_HALHL               Reviewed;         817 AA.
AC   A1WYZ7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Hhal_2145;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1;
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   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-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; CP000544; ABM62909.1; -; Genomic_DNA.
DR   RefSeq; WP_011814931.1; NC_008789.1.
DR   AlphaFoldDB; A1WYZ7; -.
DR   SMR; A1WYZ7; -.
DR   STRING; 349124.Hhal_2145; -.
DR   EnsemblBacteria; ABM62909; ABM62909; Hhal_2145.
DR   KEGG; hha:Hhal_2145; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000647; 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   Gene3D; 3.90.740.10; -; 1.
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; 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; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..817
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009352"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   817 AA;  91337 MW;  EE6BA3B245421A21 CRC64;
     MDNQYQPKEI EAEAQAYWEQ QQTFQAREDS ARPKYYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRYKRMQG YNVLQPMGWD AFGLPAENAA MERGVPPAAW TRENIGAMRE QLKGLGFGYD
     WSRELATCDP EYYRWEQWLF IRLYRKGLVY RDTAAVNWDP VDQTVLANEQ VIEGRGWRSG
     ALVERREIPQ WFLRITDYAD ELLEALDELD GWPEQVRNMQ RNWIGRSEGV ELSFDLAGRD
     EQLTVFTTRP DTLYGVTYMG LAPEHPISLE LAEHHPAIAE LVEEARSGGT AEADLATREK
     RGADTGLEAI HPLTGERIPV WVANFVLMEY GSGAVMAVPA HDQRDWEFAS TYGLPIRPVV
     HPADGTELDI AAGAFSDYGV LADSGPFSGM PSDRAFAAIA ERLEAEGRGQ RRVQYRLRDW
     GVSRQRYWGA PIPMIHCADC GPVPVPDDQL PVTLPEDVEI SGGGSPLKSM PAFYQTACPQ
     CGADAERETD TFDTFMESSW YFARFACADQ DGAMLDERAD HWTPVDQYIG GIEHAVLHLL
     YARFYHKVLR DEGLVSSDEP FTRLLTQGMV LKDGTKMSKS KGNTVDPQEL VDRFGADTVR
     LFTMFAAPPD QSLEWSDSGV EGAYRFLRRL HGLVRDHVAA GPAPALDPQA LSDTQRDLRR
     KVHETIAKAS DDVGKRLTFN TAIAAVMELC NALGKAQDDS AAGRAVMQEG LEAAVLILAP
     ITPHLCHHLW FQLGHTAPVV EAPWPEADKQ ALVRDEVELV VQVNGKLRGH VTLPADADQQ
     QAQEAALAEH NVQRFVADKE IKKVVFVPGK LINVVAK