SYLM_DICDI
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 03-AUG-2022, entry version 129.
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 (Slime mold).
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}.
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DR EMBL; AAFI02000177; EAL61657.1; -; Genomic_DNA.
DR RefSeq; XP_635155.1; XM_630063.1.
DR AlphaFoldDB; Q54ET5; -.
DR SMR; Q54ET5; -.
DR STRING; 44689.DDB0231251; -.
DR PaxDb; Q54ET5; -.
DR PRIDE; Q54ET5; -.
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 Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR43740; PTHR43740; 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; 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; 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
