ID   SYL_MYCSS               Reviewed;         950 AA.
AC   Q1B0U5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   27-MAR-2024, entry version 119.
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=Mmcs_5389;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
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   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG11489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000384; ABG11489.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q1B0U5; -.
DR   SMR; Q1B0U5; -.
DR   KEGG; mmc:Mmcs_5389; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   BioCyc; MSP164756:G1G6O-5501-MONOMER; -.
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; 2.
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.
FT   CHAIN           1..950
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334778"
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;  105595 MW;  F3C2F0E3A9616CC6 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 AYWMGPQPAE 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
//