ID   SYLC_DICDI              Reviewed;        1058 AA.
AC   Q54N83;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=Leucine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
GN   Name=leuS; ORFNames=DDB_G0285451;
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: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000079; EAL64563.1; -; Genomic_DNA.
DR   RefSeq; XP_638060.1; XM_632968.1.
DR   AlphaFoldDB; Q54N83; -.
DR   SMR; Q54N83; -.
DR   STRING; 44689.Q54N83; -.
DR   PaxDb; 44689-DDB0231253; -.
DR   EnsemblProtists; EAL64563; EAL64563; DDB_G0285451.
DR   GeneID; 8625106; -.
DR   KEGG; ddi:DDB_G0285451; -.
DR   dictyBase; DDB_G0285451; leuS.
DR   eggNOG; KOG0437; Eukaryota.
DR   HOGENOM; CLU_004174_1_1_1; -.
DR   InParanoid; Q54N83; -.
DR   OMA; KFIEWQF; -.
DR   PhylomeDB; Q54N83; -.
DR   PRO; PR:Q54N83; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; 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:0006429; P:leucyl-tRNA aminoacylation; ISS:dictyBase.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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; TIGR00395; leuS_arch; 1.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
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; Reference proteome.
FT   CHAIN           1..1058
FT                   /note="Leucine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000328291"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           711..715
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         714
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1058 AA;  119529 MW;  62D8D2139322198E CRC64;
     MSTAKLDFVR AYEKEVQNKW ESDKQFEIDA LDAPDAEHPK YLATFPYPYM NGRLHVGHVF
     TITKAEFMCQ FQRLMGKRVL FPFAFHCTGM PIKACADKLK KEIEQFGCPP VFPVIEEKPI
     QEVTTAVKED PLSFKSKKTK AVAKSGGAVY QWKIMQSLGI SDEEIPMFAD SAYWLNYFPP
     HCESDLKLLG VGVDWRRSFI TTDVNGYYDS FVRWQFESLK ALGKVKYGKR YSIWSTIDDQ
     QCADHERAQG EGVGPQNYTL IKLEVVEPIP ECLKEIHSQG KKIYLVPGTL RPETMYGQTN
     CWILPTGKYG AFEMANGDIF VCTERSARNM SYQQMTTGKG EYKCLAKFEG SDILGAALKA
     PLAINPIVYV LPMLTIDENK GTGVVTSVPS DSPDDYASLQ DLKAKAPLRA KFSIKDEWVL
     PFEVVPIIDI PGYSNESAVR AYKDLGIKSQ NDRALLDQAK DLCYQKGFND GVMSVGPYAG
     RKVSEVKKII KDEMVASGQA VDYSEPTSKV VSRSGDECVV ALSDQWYINY GDDDIEWKNQ
     TIKQLESMEF YSAETKKKFE IALGWMNQWA CSRSFGLGTH LPWDEKFLIE SLSDSTIYMA
     FYTVAHLLQG DVNGSKPGSA GITPKQMTSA CWDYVLMGKP YPEGCEVSEE KLKELKKEFT
     YWYPVDIRVS GADLIQNHLT FFLYTHAAIF EKKFQPKSIR ANGFVNLNGE KMSKSTGNFL
     TLVDSVAKFS ADGTRVALAD AGDSIEDANF VDQTAVTSLL KLHTQIQWVQ ETLDSIDKFR
     SGPLDRIQDT IFESEINNII VESEKAYQKT NFRDALHLVF FDLQNARDHY KVTTLDQMHK
     DLVLRFIEVQ ALLIYPIAPH FAQKLFNMLG KGNILSAGWP KAGAIDYEAL KKNNYVQQTI
     YNFRMKLQVY QKAKLKGKPA GTKAIPDQST IIVSKSYPKW QQDVLEYLAT IYNEDSKSFT
     KDNNAIAEEL LSREEMKPHK KNLMGFVASA IQNVKESGKD ALQTSLSFDE TSTLTDNIDY
     ICKTLELTSF DVKDFNEIPQ ASQSKIQPIP GKPQFQFV
//