ID   SYLC_ENCCU              Reviewed;         874 AA.
AC   Q8SRS8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable leucine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
GN   OrderedLocusNames=ECU06_0280;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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; AL590446; CAD25388.1; -; Genomic_DNA.
DR   RefSeq; NP_585784.1; NM_001041406.1.
DR   AlphaFoldDB; Q8SRS8; -.
DR   SMR; Q8SRS8; -.
DR   STRING; 284813.Q8SRS8; -.
DR   GeneID; 859207; -.
DR   KEGG; ecu:ECU06_0280; -.
DR   VEuPathDB; MicrosporidiaDB:ECU06_0280; -.
DR   HOGENOM; CLU_004174_0_0_1; -.
DR   InParanoid; Q8SRS8; -.
DR   OMA; MLIGEFV; -.
DR   OrthoDB; 75155at2759; -.
DR   Proteomes; UP000000819; Chromosome VI.
DR   GO; GO:0005737; C:cytoplasm; 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   Gene3D; 3.90.740.10; -; 2.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR45794; PTHR45794; 3.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   SUPFAM; SSF47323; SSF47323; 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..874
FT                   /note="Probable leucine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388413"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           544..548
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         547
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   874 AA;  101082 MW;  2021A5BAFA798E90 CRC64;
     MEERSKLRYL SMLEVERDTI SDVSEKRKFF VTFTYPYMNG RLHLGHLFSI SKADFFSYYK
     ELQGYNVLFP FSFHCTGMPI SASAKKLAEE LSGEKVDLSV KKIIEDLGFD DVKPFTDPVH
     WVRTFPGLCE RSLKRFHGNI DWRRSFITTD INKYYDSFIK WQFNRLNELG HLSFGKRHSI
     FCPVDKQPCL DHDRRKGENV KPVGVVLCKL RFSEGILLAR IKQGCVPSKA VVGSRCDFIG
     FEYCNEKYFA EKDVFENVDA QASGICVRES VKGDFFGGRR FSGFGKEVVC DAIEKDVPCV
     VKGTQDKKDP SLAEYIKNEI ELISKVESTE TQLAETKDLL KFYEPEEEVI SRSGGKCIVA
     LTDQWYINYC DPEWKKKVKR CIENLVCTDD TRAILEDGLE WIGKWGFSRS FGLGTRIPWD
     SEYLIDSLSD STIYMAMYTF KHFLYRDLEG KDELFPSNRL SDDVWNYIFL NRSITEDLAP
     YEEILSNCRE SFNYFYPIDL RVGGKDLLKN HLIFFLFNHV ALFEEKHWPK RMFTNGHLML
     NSEKMSKSSG NYMTVDESLD KFGVSSTRMC LAVCGDGNED ANFVESNANA FVLKLYSYVK
     MIEELCTGRS LNPCILDLMK GYGEMGFADR FLMQTISMNV AHATRAHEDM TYRDVVKYGF
     YEMVHAKEMY HILGGTNNEI LFLLCKAMTQ LLYPIIPSLA RYLIETYFYS NFSLPVPFLS
     DTAEIDGVSY LKNTLKRLVA QKRRKKRCEV VEILVGVEYS EWKRKCMSII DQIACECKVL
     NINVSEEMKT GESQFVPKII DAVREVLKEF GIPEKKGILF SMDYLNHPEN YSVKFNEYEV
     LKAHKYYIEN NTGLEVIVCV SPRADPGTPL FEFK