ID   M1KK81_ENCCN            Unreviewed;       874 AA.
AC   M1KK81;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN   ORFNames=ECU06_0280 {ECO:0000313|EMBL:AGE95646.1};
OS   Encephalitozoon cuniculi (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=6035 {ECO:0000313|EMBL:AGE95646.1};
RN   [1] {ECO:0000313|EMBL:AGE95646.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23376943; DOI=10.1128/EC.00307-12;
RA   Selman M., Sak B., Kvac M., Farinelli L., Weiss L.M., Corradi N.;
RT   "Extremely Reduced Levels of Heterozygosity in the Vertebrate Pathogen
RT   Encephalitozoon cuniculi.";
RL   Eukaryot. Cell 12:496-502(2013).
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         Evidence={ECO:0000256|ARBA:ARBA00001372};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; KC513609; AGE95646.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1KK81; -.
DR   VEuPathDB; MicrosporidiaDB:AEWD_060220; -.
DR   VEuPathDB; MicrosporidiaDB:AEWQ_060210; -.
DR   VEuPathDB; MicrosporidiaDB:AEWR_060220; -.
DR   VEuPathDB; MicrosporidiaDB:ECU06_0280; -.
DR   VEuPathDB; MicrosporidiaDB:M970_060220; -.
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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035}.
FT   DOMAIN          24..582
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
SQ   SEQUENCE   874 AA;  101100 MW;  92004BEDFA798B06 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 EKDVFENMDA QASGICVRES VKGDFFGGRR FSGFGKEVVC DAIEKDVPCV
     VKGTQDKKDP SLAEYIKNEI ELISKVESTE TQLAETKDLL KFYEPEEEVI SRSGGKCIVA
     LTDQWYINYC DPEWKKNVKR 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
//