ID   SYL_MYCSJ               Reviewed;         950 AA.
AC   A3Q8Q1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 98.
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=Mjls_5765;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABO01529.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000580; ABO01529.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A3Q8Q1; -.
DR   SMR; A3Q8Q1; -.
DR   STRING; 164757.Mjls_5765; -.
DR   KEGG; mjl:Mjls_5765; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   BioCyc; MSP164757:G1G8C-5827-MON; -.
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; -; 3.
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   PANTHER; PTHR43740; PTHR43740; 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; 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.
FT   CHAIN           1..950
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334776"
FT   MOTIF           72..83
FT                   /note="'HIGH' region"
FT   MOTIF           722..726
FT                   /note="'KMSKS' region"
FT   BINDING         725
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   950 AA;  105623 MW;  DCC3614026DCFC7A CRC64;
     MTETPTAQPD RAADADTPQH RYTAELAGQI EGAWQQTWAV EGTFNVPNPV GELAPPDGTV
     PADKMFVQDM FPYPSGEGLH VGHPLGYIAT DVYARYYRMT GRNVLHALGF DAFGLPAEQY
     AVQTGTHPRT RTEANIVNFR RQLGRLGLGH DTRRSFSTTD VDFYTWTQWI FLQIYNAWFD
     RDANRARPIA ELIGEFESGV RTLDDGRPWS ELSAGERADV VDSYRLVYRA DSMVNWCPGL
     GTVLANEEVT ADGRSDRGNF PVFRKRLRQW MMRITAYSDR LLEDLEVLDW PDKVKTMQRN
     WIGRSTGASV QFGTDAGDIE VFTTRPDTLF GATYLVLAPE HPLVEQLAAE QWPDDVDGRW
     TFGATTPREA VAAYRASIAA KSDLERQENK TKTGAFLGAY ATNPANGQQV PIFIADYVLI
     GYGTGAIMAV PGHDQRDWEF AHEFGLPVVE VISGGDISEA AYAGDGLLVN SDYLDGLDVA
     AAKAAITDRL VADGRGRARV EYKLRDWLFA RQRYWGEPFP IVYDSDGRPH PLPESALPVE
     LPDVPDYSPV LFDPDDADSE PNPPLNKATD WVHVELDLGD GLQTYTRDTN VMPQWAGSSW
     YELRYTDPLN KEALCAKENE AYWMGPRPAE HGPDDPGGVD LYVGGVEHAV LHLLYSRFWH
     KVLYDLGHVS SREPYRRLVN QGYIQAFAYT DSRGSYVPAA EVVERDGKFW FEGAEVFQEF
     GKIGKSLKNS VSPDEICDNY GADTLRVYEM SMGPLEASRP WATKDVVGAH RFLQRVWRLV
     VDEQSGAVRV ANHEALDTDT LRALHRTVAG VSEDYAALRN NTAAAKLIEY TNHLTKEGVT
     ARAAIEPLVL MVAPLAPHLA EELWRRLGHD TSLAHGPFPV ADPQYLVTDT VEYPVQVNGK
     VRSRITVDAD AGKDTLEAAA LADEKVQAFL NGATPKKVIV VPGRLVNLVV