ID   A0A078B9F5_STYLE        Unreviewed;      1081 AA.
AC   A0A078B9F5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-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   Name=Contig17209.g18328 {ECO:0000313|EMBL:CDW91034.1};
GN   ORFNames=STYLEM_20183 {ECO:0000313|EMBL:CDW91034.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW91034.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW91034.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW91034.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; CCKQ01019027; CDW91034.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078B9F5; -.
DR   EnsemblProtists; CDW91034; CDW91034; STYLEM_20183.
DR   InParanoid; A0A078B9F5; -.
DR   OMA; KFIEWQF; -.
DR   OrthoDB; 5472610at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
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; 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; 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   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 {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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT   DOMAIN          48..115
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          176..742
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          786..921
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1081 AA;  123346 MW;  743AD90DDA22B822 CRC64;
     MESSKQAQQS EEKQQSRKRY DHLRAIEKQM NEVHLTTKVA EASPLEGYEN MSFEEKNQGK
     YFTTFPYPYM NGFMHLGHAF SLSKCEFSVR YQKQLGKNVL FPFAFHCTGM PIQAAAYRLK
     REIRTGNITS PGALPGQPKH STQYEILQQL GISEEDIPKF QDPLHWLHFF PPHGMQDLKD
     FGLYTDWRRS FITTEVNPFY DSFVQWQFNT LKAKDKIRFG NRPAIFSETD NQPCADHDRS
     KGEGVGPQEY TLIKIRCLEL PASMQEKFAD KTVFLVAATL RPETMYGQTN CYVLPEGEYG
     VFEMINNEYY VCSERSARNM SFQNMTKEHK QYPCLQKVSG QELIGLKLKA PLTKYEYVYA
     LPMTTISMFK GTGIVTSVPS DAPDDWAALR DLQTKKGLRE KYNVLEEWCN PFEPIPIIEI
     PGFGNMAAVK LVEEMKIQSQ KDKDKLTEAK DKVYLKGFYE GVMLLGPCAN MKVQDAKPIV
     RKQLIDNNEA AVYYEPENEV TSRSGDNCVV ALCDQWFLTY GEEQWKETVK AHVKSENFNA
     YTPKTQQEFE ETLEWLREWA CSRSVGLGTK LPWDTQFLIE SLSDSTIYMA YYTVAHLLQA
     GSFDGSVEGP LGIKASDLND AVWEYIFKQG AYPEGCAIPE ESLKKLRGEF EYWYPLDMRA
     SGKDLIRNHL TMSLYNHAAV WEDPKYMPRS IFCNGWILVN GLKMSKSTGN FLTIRECIEK
     YGVDATRMAL ADAGDSLDDA NFDENVANSA ILRLFVLEKW ISEEVKKHVP AEGLDFANQP
     QHDLWDQILD NELNYAIELT TKSYNDMRFK QALKHGFFEL QALKEDYLIA KHGNVNPFLL
     LKYVETQLIL INPIVPHFAD YCYQTHVLPI LEKSVNLQKP AQKLLINQGW PKASKAVDSG
     KTKRVYDYMK SVKSNVRMAL EKAKHGGKKG AKAAKGKGKE AAPVEEKGLE SCVLFVALEY
     PEWQKNTLET LQQFEFIDNK IQGNYIQAVK SSITGPKQGL ALKFAAFIAK EAETVGKEAA
     LEIATPFNEV DIIDQNRQYL FENMPGIKNI SVYPATTDVE IENSKNSREA ALPGKPSCFF
     F
//