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
//
