ID   SYL_DESAP               Reviewed;         826 AA.
AC   B1I5R7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=Daud_1865;
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforudis.
OX   NCBI_TaxID=477974;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA   Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-2007) 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; CP000860; ACA60358.1; -; Genomic_DNA.
DR   RefSeq; WP_012302934.1; NC_010424.1.
DR   AlphaFoldDB; B1I5R7; -.
DR   SMR; B1I5R7; -.
DR   STRING; 477974.Daud_1865; -.
DR   KEGG; dau:Daud_1865; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000008544; 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..826
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091313"
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   826 AA;  93865 MW;  6363D3EDDC6C95AA CRC64;
     MEEKYVFAEI EEKLRRRWET EGIYHVPDFS NRPKYYCLEM FPYPSGNLHM GHVRNYAIGD
     VVARFKTMRG YDVLHPMGWD AFGLPAENAA IQHGVPPARW TWDNINVMRT QLKLLGVSYD
     WRRELATCHP GYYRWTQWLF LQFYHRGLAY KAKAPVNWCP SCATVLANEQ VVAGGCERCK
     TAVERRELEQ WFFRITAYAD RLLKDLAKLP GWPEKVKVMQ ENWIGRSTGA EIAFPLAGTD
     EAIRVFTTRP DTLGGVTYMT IAPEHPLVSR VTTPEHRAAV EAFTERARSL SELDRTAGEH
     EKEGLFTGAY CVNPLTGEQV PVFVANYVLM EYGTGCVMGV PAHDQRDFEF ARKYGLPVRV
     VIQPEGDLLD GDTMSQAYTG PGRLVNTPGF DRMANAEAIP AITRYLEARG AARFQVQYRL
     RDWLISRQRY WGAPIPIVYC EGCGVVPVPE EGLPVLLPED VAFKPTGRSP LTESPDFVNT
     TCPTCGGPAR RETDTMDTFM CSSWYYFRFT SPREENGPWG LERVDRWLPV DQYIGGVEHA
     ILHLMYSRFF TKVLYDMGLV KVQEPFTNLL TQGMVLKDGA KMSKSKGNVV SPEDILNRYG
     ADTTRLFVLF AAPPERDLEW SDQGVEGCYR FLQRVWRLVN SVADEIRGAA PVPSANLVGV
     NRSMRRLTHQ TIKKVTEDIE TRFNFNTAIS AAMELVNGMY HFRDRVAPVN RDPAVMREAV
     ERLLLLLAPF APFLADELWA RTGHPESIHR EPWPEYDPEL LVEDQVEIVV QINGRVRDRL
     MVAADIAPEA MRDTVLEQPR VQALVAGKEI VKVVPVPGKL VNIVVR
//