SYK_THEKO
ID SYK_THEKO Reviewed; 526 AA.
AC Q5JHQ3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=lysS; OrderedLocusNames=TK2240;
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 [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-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AP006878; BAD86429.1; -; Genomic_DNA.
DR RefSeq; WP_011251190.1; NC_006624.1.
DR AlphaFoldDB; Q5JHQ3; -.
DR SMR; Q5JHQ3; -.
DR STRING; 69014.TK2240; -.
DR PRIDE; Q5JHQ3; -.
DR EnsemblBacteria; BAD86429; BAD86429; TK2240.
DR GeneID; 3235513; -.
DR KEGG; tko:TK2240; -.
DR PATRIC; fig|69014.16.peg.2195; -.
DR eggNOG; arCOG00485; Archaea.
DR HOGENOM; CLU_025562_1_0_2; -.
DR InParanoid; Q5JHQ3; -.
DR OMA; DWPMRWA; -.
DR OrthoDB; 9880at2157; -.
DR PhylomeDB; Q5JHQ3; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 6.10.20.10; -; 1.
DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR002904; Lys-tRNA-ligase.
DR InterPro; IPR042078; Lys-tRNA-ligase_SC_fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR37940; PTHR37940; 1.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00467; lysS_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..526
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152761"
FT MOTIF 30..38
FT /note="'HIGH' region"
FT MOTIF 280..284
FT /note="'KMSKS' region"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 526 AA; 61812 MW; 6B4043DD9E6B18E3 CRC64;
MVHWADYMAE KIIRERGDKE EYVVESGITP SGYVHIGNFR EFFTAYIVGH ALRDRGKRVR
HIHMWDDYDR FRKVPKNVPP EWKEHLTKPV REVPDPWGCH ESYADHFMSL FEEEISKLGI
EADFLHASEL YKSGEYAKEI RLALEKRDEI KAILDKYRER AKQPPLEDSW QPVMIYCPHC
RKEAEFVSWD GEWKVSYKCP HCGAEGETDI REGNVKLRWR VDWPMRWAHF KVDFEPAGKD
HLAAGSSYDT GKEIVEKVFG WKAPLTLMYE FVGIKGQKGK MSGSKGNVIL LSDLYEVLEP
GIIRFIYAKA RPNKELRIDL GLGLLNLYDE FDRVERIYFG LEHAKNPEEE EELKRTYELS
MPKLPERLVA QAPFRFLVTL VQMPHLDEDG IIRILQEQGH VPENLTDDDI ERIKLRIRLA
KNWVEKYAPD DVKFSLLERP PEIELRPEIR EAMLEVAEWL EEHERFSVDE LNNVIFDAAK
KRGIPSKEWF KALYNIFIGK DRGPRLAPFL ASLNREFVIK RLRLEG
