ID   SYL_MYCA1               Reviewed;         969 AA.
AC   A0Q8W7;
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=MAV_0055;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-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=ABK69297.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000479; ABK69297.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_031344725.1; NC_008595.1.
DR   AlphaFoldDB; A0Q8W7; -.
DR   SMR; A0Q8W7; -.
DR   PRIDE; A0Q8W7; -.
DR   EnsemblBacteria; ABK69297; ABK69297; MAV_0055.
DR   KEGG; mav:MAV_0055; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001574; 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; -; 3.
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; 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..969
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334773"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           78..89
FT                   /note="'HIGH' region"
FT   MOTIF           737..741
FT                   /note="'KMSKS' region"
FT   BINDING         740
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   969 AA;  106886 MW;  1EE8B551CF991D7D CRC64;
     MTESPTTSPA TGSGAAAPDS DAPPYRYTAA LAGRIEGSWQ DTWAKLGTFN VPNPVGSLAP
     TDGTPVPEDK LFVQDMFPYP SGEGLHVGHP LGYIATDVYA RYFRMTGRNV LHALGFDAFG
     LPAEQYAVQT GTHPRTRTEA NVVNFRRQLG RLGLGHDSRR SFSTTDVEFY KWTQWIFLQI
     YNAWFDPAAN KARPIAELVA EFDSGARSLD DGRNWSELSA GERADVIDSH RLVYRADSMV
     NWCPGLGTVL ANEEVTADGR SDRGNFPVFR KRLRQWMMRI TAYSDRLLDD LDLLDWPEPV
     KTMQRNWIGR STGAKALFAA TGADGAALDI EVFTTRPDTL FGATYMVLAP EHELVDELVA
     PAWPDGTDPR WTYGAATPGE AVAAYRRAIA SKSDLERQES KAKTGVFLGS YATNPTNGKP
     VPIFIADYVL AGYGTGAIMA VPGHDQRDWD FAHEFGLPIV EVIAGGDISE GAYAGDGLLV
     NSGYLDGLDV AAAKEAITAR LEAEGRGCAR VEFKLRDWLF ARQRYWGEPF PIVYDSDGRP
     HALDEAALPV ELPDVPDYSP VLFDPDDADS EPSPPLAKAT DWVHVELDLG DGLKPYSRDT
     NVMPQWAGSS WYELRYTDPH NSERFCAKEN EAYWMGPRPA EHGPQDPGGV DLYVGGAEHA
     VLHLLYARFW HKVLYDLGHV SSREPYRRLV NQGYIQAFAY TDSRGSYVPA EEVVERDGRF
     FYRGPDGEIE VFQEFGKIGK SLKNSISPDE ICDDYGADTL RVYEMSMGPL EASRPWATKD
     VVGAHRFLQR VWRLVVDEQT GETRVVDGAG RDLPTGTLRL LHRTIAGVSE DYAGLRNNTA
     VAKLIEYTNH LTKEHRDAVP RAAVEPLVLM LAPLAPHMAE ELWLRLGHTT SLAHGPFPVA
     DPAYLVEDTV EYPVQVNGKV RGRVTVAADA DRDTLEAAAL ADEKVLAFLA GAQPRKVIVV
     PGRLVNLVV