SYL_THEKO
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 03-AUG-2022, entry version 117.
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 PRIDE; Q8NKR7; -.
DR EnsemblBacteria; BAD85650; BAD85650; TK1461.
DR GeneID; 3234295; -.
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 OMA; AWNMAFQ; -.
DR OrthoDB; 4914at2157; -.
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 Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR45794; PTHR45794; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00395; leuS_arch; 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
