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Database: UniProt
Entry: Q8NKR7
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Original site: Q8NKR7 
ID   SYL_THEKO               Reviewed;         967 AA.
AC   Q8NKR7; Q5JH65;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   27-MAR-2024, entry version 125.
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=TK1461;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RA   Sawaki T., Amano H., Shiraki K., Fukuzawa K., Fujiwara S., Sekiguchi T.,
RA   Takagi M.;
RT   "Thermococcus kodakaraensis KOD1 LeuRS gene for leucyl-tRNA synthetase.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AB090309; BAC10608.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85650.1; -; Genomic_DNA.
DR   RefSeq; WP_011250412.1; NC_006624.1.
DR   AlphaFoldDB; Q8NKR7; -.
DR   SMR; Q8NKR7; -.
DR   IntAct; Q8NKR7; 119.
DR   MINT; Q8NKR7; -.
DR   STRING; 69014.TK1461; -.
DR   EnsemblBacteria; BAD85650; BAD85650; TK1461.
DR   GeneID; 78447983; -.
DR   KEGG; tko:TK1461; -.
DR   PATRIC; fig|69014.16.peg.1423; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; Q8NKR7; -.
DR   OrthoDB; 23906at2157; -.
DR   PhylomeDB; Q8NKR7; -.
DR   Proteomes; UP000000536; 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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   CDD; cd00812; LeuRS_core; 1.
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; Reference proteome.
FT   CHAIN           1..967
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152141"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           650..654
FT                   /note="'KMSKS' region"
FT   BINDING         653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
FT   CONFLICT        321
FT                   /note="V -> C (in Ref. 1; BAC10608)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590
FT                   /note="T -> A (in Ref. 1; BAC10608)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        654..655
FT                   /note="SK -> RQ (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        657
FT                   /note="N -> Q (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        659
FT                   /note="L -> Q (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        663
FT                   /note="D -> Y (in Ref. 1; BAC10608)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        822
FT                   /note="E -> D (in Ref. 1; BAC10608)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   967 AA;  113135 MW;  13A9161049DC233C CRC64;
     MAELNFKAIE EKWQKRWMEA RVFEPDRKAK PKEKKFYITV AFPYLSGHLH VGHARTYTIP
     DVIARFKRMQ GYNVLFPMGW HITGAPIVGI AERIKNRDPK TIHIYRDVYK VPEEILWKFE
     DPKEIVKYFM KAAKETFIRA GFSVDWTREF HTTSLFPPFS KFIEWQFWTL KDMGLVVKGA
     HRVRWDPVVG TPLGDHDIME GEDVQILEYV IIKFILEENG ETIYLPAATL RPETVYGVTN
     MWLNPEATYV KAKVRKGDRE ELWIVSKEAA YKLSFQDREI EVIEEFKGEK LIGKYVKNPV
     TGDEVIILPA EFVDPDNATG VVMSVPAHAP FDHIALEDLK KETEILLKYD IDPRVVEEIS
     YISLISLEGY GEFPAVEEAE RLGVKSQKDK EKLEQATKNI YKAEYHKGIF KIEPYAGKPV
     QEVKELVAKE MMEKGIAEIM YEFADKPVIS RFGNQAVIKI IHDQWFIDYG NPEWKAKARE
     ALANMTIYPE SRRAQFEAVI DWLDKKACAR KVGLGTPLPW DPDWVIESLS DSTIYMAYYT
     ISRHINQLRK EGKLDAEKLD REFFDYIFRE PFSEEKERKL SEKTGIPAET IHEMKEEFEY
     WYPLDWRCSA KDLIPNHLTF FIFNHVAIFD KKHWPKGIAV NGFGTLEGQK MSKSKGNVLN
     FIDAIEENGA DVVRLYIMGL AEHDSDFDWR RKEVGKLRKQ VERFYELVSE FATYEAKEGV
     ELKDIDRWML HRLNKAIEGA TKALEEFRTR TAVQWAFYTV LNDLRWYLRR TEGRDDDAKR
     YVLRTLADVW VRLMAPFTPH ISEELWEKLG GEGFVSLAPW PEPVPEWWNE TVEAEEDFVK
     SLIEDIKEII TVAKIENPKR AYIYTAPEWK WRVVEVVAEK RDFKAAMAEL MKDPEMRKHG
     KEVSKLIQRL IKERAFEVKR IDEEKALREA KDFIEKELGI EIIINPEEDR GGKKKQAMPL
     KPAVFVE
//
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