ID   SYL_THEAC               Reviewed;         910 AA.
AC   Q9HK31;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=Ta0777;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(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 {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; AL445065; CAC11908.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HK31; -.
DR   SMR; Q9HK31; -.
DR   STRING; 273075.gene:9571990; -.
DR   PaxDb; 273075-Ta0777; -.
DR   EnsemblBacteria; CAC11908; CAC11908; CAC11908.
DR   KEGG; tac:Ta0777; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; Q9HK31; -.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000001024; 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; 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; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..910
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152148"
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;  105028 MW;  17FA01BB946DF0BE CRC64;
     MDDRGRRCCT HSGVIALDIE AKWQNAWDRD GIFVPKMDGR KKFMITVPWP YTNGSLHVGH
     GRTYTLGDII ARYKRSRNYN VLFPMGFHQS GTPILAFSER IRAGDRSTID LYTSYLKEYG
     EKDIDALIES FKDPKNIADY FSNAIINDFK HLGYSIDWTR RFTSADEFYQ KFVQWQFRRL
     NEKGLVKQGR YPILYSLEDD NAVGEDDIKD GDTDKVTIEE YTAIFFRGKS FDLIAASLRP
     ETIYGITNIW VNPDVKYVKV KISGRMAVVS EECSTKLKFQ GNEIEVAGEA SVQEIQKQTY
     TTPAGKEVKV YQADFVDPDN GTGIVYSVPS HSVYDYVYYR KKRGKDFPVI IEAPMKMKDI
     ESKYDLETEE GREEATKDLY RNEFYYGKLV DSGPYTGMTV REAREAVKRD LISSGNAFTF
     YETSRHAVTR SGSKVIVAVL PDQWFLDYSQ PWLKDLGHTM INTMTMHPEV YRNVMNDAID
     WLKERPCARR RGLGTRLPFD DRWVIESLSD STIYPAVYTN SIPLRSLYET GKLDDDAITR
     IFMNGEPKNE DESEAKRQFE YWYPVDIRLT AIPHISNHLS FYVLNHAAIF PKEKWPAGLI
     ISGLVVSNGA KISKSKGNVV SLLEIAKKYS ADIYRLYVAV QADISSTMDW NETDLASITR
     RFNEFKDLMA GFKQDTSDLT FEEAWFVARF SVRLRQFMES MDRYQIRDAY INIFYGVLND
     LRYLSSRGGD VNRALTPVIA DWLRALMPVI PHHAEEYWHS YVSDTYVSVD PFDENFQDRY
     ERTVRRFGMT CDQMYSAMDY VEKVLQDVKN IMQVTGIEPK SVEITVANAD VVRAAQEFLN
     NSVSGQSKKY MQYLAKRRKD IMIYGFDEYD VLQRNQVYLS KQIGCPVRIE RGDVINGKIA
     LPGKPVIYIS
//