ID   SYL_MYCVP               Reviewed;         968 AA.
AC   A1TI06;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 111.
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=Mvan_6054;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
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   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
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; CP000511; ABM16806.1; -; Genomic_DNA.
DR   RefSeq; WP_011783150.1; NZ_JACKSD010000348.1.
DR   AlphaFoldDB; A1TI06; -.
DR   SMR; A1TI06; -.
DR   STRING; 350058.Mvan_6054; -.
DR   KEGG; mva:Mvan_6054; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   Proteomes; UP000009159; 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; 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..968
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334779"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           75..86
FT                   /note="'HIGH' region"
FT   MOTIF           741..745
FT                   /note="'KMSKS' region"
FT   BINDING         744
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   968 AA;  107296 MW;  332228120EF1A332 CRC64;
     MTETPTGTQS SRETAADDTP RHRYTAGLAG EIERAWQQRW TQDGTFDVAN PVGSLAPADG
     SAVPADKMFV QDMFPYPSGE GLHVGHPLGY IATDVYARYY RMTGRNVLHA LGFDAFGLPA
     EQYAIQTGTH PRTRTEANIV NFRRQLGRLG LGHDSRRSFS TTDVDFYKWT QWIFLQIYNA
     WFDTAQNKAR PVAELIAEFE AGTREVGDGR RWADLDAGER ADVVDSRRLV YLADSVVNWC
     PGLGTVLANE EVTSDGRSER GNFPVFRKRL RQWMMRITAY SDRLLEDLDV LDWPDKVKTM
     QRNWIGRSTG ASVEFGTDAG DIEVFTTRPD TLFGATYMVL APEHDLVDRL VADQWPADVD
     ARWTFGAATP REAVAAYRAS IAAKSDLERQ ENKAKTGVFI GAYATNPANA KQVPVFIADY
     VLAGYGTGAI MAVPGGDQRD WDFATEFGLP IIEVVRPVAD RPGEDTGAGG DVSQAAYTGD
     GVMVNSGFLD GMDVSAAKEA MTERLSADGR GRERVEYKLR DWLFARQRYW GEPFPIVYDA
     DDRAHGLPEE LLPVELPDVP DYSPVLFDPD DADSEPSPPL AKATEWVNVE LDLGDGRKRY
     TRDTNVMPQW AGSSWYELRY ADPHNTEALC AKENEAYWMG PRPAEHGPDD PGGVDLYVGG
     VEHAVLHLLY SRFWHKVLYD LGHVSSREPY RRLVNQGYIQ AFAYTDARGS YVPAAEVVER
     DGKFFWPGPD GEIEVNQEFG KIGKSLKNSV SPDEICDDYG ADTLRVYEMS MGPLEASRPW
     ATKDVVGAHR FLQRVWRLVV SEETGETVVT DDALDEDTLR LLHRTIAGTA DDYAALRNNT
     AAAKLIEYTN HLTKQSVTAR AALEPLVLMV APLAPHLAEE LWRRLGHDAS LAHGPFPVAD
     ERYLVEDTVE YPVQVNGKVR GRVTVAADAP ADAVEAAALA DDKVVAFLDG KTPKKVIVVA
     GRLVNVVL
//