SYLC_DICDI
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 03-AUG-2022, entry version 110.
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 (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: 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.DDB0231253; -.
DR PaxDb; Q54N83; -.
DR PRIDE; Q54N83; -.
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; AWNMAFQ; -.
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; -; 1.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR45794; PTHR45794; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00395; leuS_arch; 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
