ID   SYLM_DICDI              Reviewed;         940 AA.
AC   Q54ET5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Leucine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.4;
DE   AltName: Full=LeuRM;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE   Flags: Precursor;
GN   Name=mleuS; ORFNames=DDB_G0291346;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {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; AAFI02000177; EAL61657.1; -; Genomic_DNA.
DR   RefSeq; XP_635155.1; XM_630063.1.
DR   AlphaFoldDB; Q54ET5; -.
DR   SMR; Q54ET5; -.
DR   STRING; 44689.Q54ET5; -.
DR   PaxDb; 44689-DDB0231251; -.
DR   EnsemblProtists; EAL61657; EAL61657; DDB_G0291346.
DR   GeneID; 8628101; -.
DR   KEGG; ddi:DDB_G0291346; -.
DR   dictyBase; DDB_G0291346; mleuS.
DR   eggNOG; KOG0435; Eukaryota.
DR   HOGENOM; CLU_004427_0_0_1; -.
DR   InParanoid; Q54ET5; -.
DR   OMA; TFMVLAP; -.
DR   PhylomeDB; Q54ET5; -.
DR   PRO; PR:Q54ET5; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
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; ISS:dictyBase.
DR   GO; GO:0000372; P:Group I intron splicing; ISS:dictyBase.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; ISS:dictyBase.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; 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; 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; 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; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..940
FT                   /note="Leucine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000328292"
FT   REGION          724..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           54..64
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        730..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   940 AA;  108734 MW;  275CCEC592792E38 CRC64;
     MFNLYRSSLK NLKLPNINNN IKSNLVIRSY TTNINGNIKN DDDNNKFYSL SQFPYPSGAL
     HMGHVRVYTI SDCIARLKRM QGYDVIHPMG WDAFGLPAEN AAIDKQVSPS EWTNLNISSM
     RDQLKLLNFQ FDWDRELSTC NKEYYRWTQE IFLRLLKSGL AYRKSATVNW DPIDQTVLAN
     EQVDAQGRSW RSNAIVEKKE MKQWFYKITS MADRLTDDLD QLPGWSDEIK NMQKEWIGRS
     YGHLIEFQSC AQKPLSNITV FTTRAETIYG VSFLAISPHH SEINQIRANL INDEKRLELD
     QYLKEIQEIK NKMGTQEDVE NLKTFNTGLT FYQPITKKYI PLILSNFVHA DYGTGAVMGV
     PSHNRSDYQV AKQQNLKLLP VLGIEREQQQ QQQQQQQQQQ LEIEEECYDY SNTGKLINSG
     QDTGIEFKEF IKRLEDQQLI KRQTNYRIHD WLISRQRYWG TPIPIIVCEK CGDVPVPSDQ
     LPVELPIDIQ FTGKGNLLNQ LDHWKNVKCP CCGSQATRET DTMDTFVDSS WYFLRFLDSK
     NSQSIFSSEL VNRFMPIDVY VGGIEHAILH LLYSRFITKF LKDQQLIDHS EPFKVLLAQG
     LVKSPTYRDS ITNKPIHPSN VEFKTIKSNE SGKSQQQTIN KLTGNQVSVT IEKMSKSKLN
     GIDPKEIIDK YGSDTLKTYI LFKAPPEKSL DWDTQGIEGC KKWLTRINVS IQSFLNQFDV
     IEGKEQHQHQ QQQHQQPLPS SEFNEQQSKE VKDILFETHL TMNKVTESID KHSFNTGIAA
     LMELSNTLQK SSPQIKLTKE YYQSLRALTL MLFPFSPIFS QIHWKSLIDD LPQSCKSFYS
     ENYSSFEQQS YGNSNDNDVF NQRWPKPTPS ALVRDFNSLV IQFDGKTKGV ESIPTSITDF
     SNFVQSNSKY LNRFKDKTID QIFIGTTKTG NSINFTFKKK
//