ID   SYLM_SACPA              Reviewed;         894 AA.
AC   P13503;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Leucine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
DE   Flags: Precursor;
GN   Name=NAM2;
OS   Saccharomyces paradoxus (Yeast) (Saccharomyces douglasii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=27291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HM300;
RX   PubMed=3054483; DOI=10.1007/bf00339595;
RA   Herbert C.J., Dujardin G., Labouesse M., Slonimski P.P.;
RT   "Divergence of the mitochondrial leucyl tRNA synthetase genes in two
RT   closely related yeasts Saccharomyces cerevisiae and Saccharomyces
RT   douglasii: a paradigm of incipient evolution.";
RL   Mol. Gen. Genet. 213:297-309(1988).
RN   [2]
RP   FUNCTION.
RX   PubMed=3284745; DOI=10.1002/j.1460-2075.1988.tb02835.x;
RA   Herbert C.J., Labouesse M., Dujardin G., Slonimski P.P.;
RT   "The NAM2 proteins from S. cerevisiae and S. douglasii are mitochondrial
RT   leucyl-tRNA synthetases, and are involved in mRNA splicing.";
RL   EMBO J. 7:473-483(1988).
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X12864; CAA31343.1; -; Genomic_DNA.
DR   AlphaFoldDB; P13503; -.
DR   SMR; P13503; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 2.
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; 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; 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; 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; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Transit peptide.
FT   TRANSIT         1..9
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           10..894
FT                   /note="Leucine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000035809"
FT   MOTIF           56..66
FT                   /note="'HIGH' region"
FT   MOTIF           646..650
FT                   /note="'KMSKS' region"
FT   BINDING         649
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   894 AA;  102194 MW;  AE42C20193DDF107 CRC64;
     MLPRPSSRFL STQRGPGRAV KKLIAIGEKW KQKTTRGPPK QGTLNNRSKY ILCQFPYPSG
     VLHIGHLRVY VISDSLNRFY KQRGYNVIHP MGWDAFGLPA ENAAIERGIN PAIWTRDNIA
     KMKQQMESML ANFDWDREVT TCDPEYYKFT QWIFLKLFEN GLAYRKEAEI NWDPVDKTVL
     ANEQVDAQGR SWRSGAIVEK KQLKQWFLGI TKFAPKLRKH LNQLKDWPSN VKQMQKNWIG
     ESIGAELVFK VADSKFENLI VFTTRPETLF AVQYVALALD HPIVQKYSEV IPDLKEFLQK
     SDQLPSDTKE GFRLPDIKAV NPLTKEELPI FAAPYVISSY GTAPSAVMGC PGHDSRDFEF
     WQQNCPGEHI KTCIAPFFDD ASKTSEKERQ KIIDTVPFTS ADGILTKESG EYSGVFTAVA
     RKSIMGKLHS KGLSKNIIRY RIRDWLISRQ RYWGTPIPII HCDNCGPVPV PESDLPVKLP
     ELKGLDTKGN PLSTIDEFVN VACPSCGSPA KRETDTMDTF IDSSWYYFRF LDPKNTSKPF
     DREIASEHMP VDIYIGGVEH AILHLLYSRF IAKFLGSINA WDDPTGIFEP FRKLVTQGMV
     QGKTYVDPDS GKFLTPDELT FVKDPSDGNT TIIKSNGKIP MVSYEKMSKS KHNGADPNEC
     ILRHGADATR AHILFQSPIA DALNWDESKI VGIERWLQKV LCLTKNILGL EKNLAISKDY
     KTPTDLNDAE VKFHNDFQRF LKSITESFEV HLSLNTVISD YMKLTNLLES ALKKSEVRKE
     MMVQNLQKLV TIIYPAVPSI SEEAAELISS QMEWNQYRWP EVERTTESKF KKFQIVVNGR
     VKFMYTADKD FLKSGRDAVI ETLLKLPEGR MYLMNKKIKK FVMKYNVISF LFHK