ID   SYL_THEVO               Reviewed;         910 AA.
AC   Q97AN8;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=TV0772;
GN   ORFNames=TVG0775903;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; BA000011; BAB59914.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q97AN8; -.
DR   SMR; Q97AN8; -.
DR   STRING; 273116.gene:9381562; -.
DR   PaxDb; 273116-14324988; -.
DR   KEGG; tvo:TVG0775903; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OrthoDB; 23906at2157; -.
DR   PhylomeDB; Q97AN8; -.
DR   Proteomes; UP000001017; Chromosome.
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-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR020791; Leu-tRNA-lgase_arc.
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; 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.
FT   CHAIN           1..910
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152149"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           611..615
FT                   /note="'KMSKS' region"
FT   BINDING         614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   910 AA;  104994 MW;  C21870CE07188ED3 CRC64;
     MDYSRCCGST NSRVIYMNID EKWQNAWERD HVFEPKIDER KKFMITVPWP YTNGSLHVGH
     GRTYTLGDII ARYKRSRNYN VLFPMGFHQS GTPILAFSER IRAGDASTIA LYRSYLSEYG
     EKDIDGWLEK FKDPRNIADY FSNAIINDFK HLGYSIDWTR KFTSADEFYQ NVVKWQFHKL
     NEKGLIKQDK YPILYSIDDD NAVGEDDIKD GDTDKVSVEE YTAVFFESNS YSLIAASLRP
     ETLFGVTNIW INPTGEYVKI KIGDKIAVVS KEAVDKLKYQ RNDVSVIGPI SAESIQRKKF
     TTPFGKEVPV YKADFVDTDN GTGVVYSVPS HSVYDFVYYR RKKSGQTPVV IEAPLKMPEV
     EIKFDLNSKE GLDEATKELY KSEFYYGKLV NSGEYTGLTV RDAREKIKKD LIGSGKAIIF
     YETSRKAVTR GGSKVIVAVL PDQWFIDYSA DWLKKLSHDM LNRMMIYPEM YRNVMNDAID
     WLKERPCARR RGLGTKLPFD DRWVIESLSD STIYPAVYTT SIQMRKLYEN GKLDENAIER
     IFDGGEVQND EERTARNEFS YWYPVDIRLT AVPHISNHLS FYVMNHAAIF PPEKWPSGLI
     ISGLVVSNGA KISKSKGNVV SLLEITKKYS ADIYRLYVAV QADVSSTMDW NENDLSNIVR
     RFNEFKTIMD SFKPDTSELN FEETWFVSRF AERLKQFMDQ MDGFQIRDAY INIFYGTLND
     LKYAVNRGAS QNRSLASIIA DWLRALMPVI SHHAEEYWHR YVSNTYVSIN PFDDNFAEKY
     ERLAKVYGLS TSEFYQVMDY VEHIIQDINN IISVTGIEPK SVEITVANED VIKASREFLS
     NSVSERSKRY LQYLAKRRKD IVVYPFNEID ILRRNSSYIS RQVKADVSIN TGDIINGKIA
     VPGKPVIHIT
//