ID   SYK_SACS2               Reviewed;         494 AA.
AC   P95970;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 137.
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=SSO0090; ORFNames=C04_032;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA   Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA   Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA   Ragan M.A., Charlebois R.L.;
RT   "Organizational characteristics and information content of an archaeal
RT   genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL   Mol. Microbiol. 22:175-191(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; Y08257; CAA69561.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40448.1; -; Genomic_DNA.
DR   PIR; S75398; S75398.
DR   AlphaFoldDB; P95970; -.
DR   SMR; P95970; -.
DR   STRING; 273057.SSO0090; -.
DR   PRIDE; P95970; -.
DR   EnsemblBacteria; AAK40448; AAK40448; SSO0090.
DR   KEGG; sso:SSO0090; -.
DR   PATRIC; fig|273057.12.peg.87; -.
DR   eggNOG; arCOG00408; Archaea.
DR   HOGENOM; CLU_008255_6_0_2; -.
DR   InParanoid; P95970; -.
DR   OMA; EIFGEKC; -.
DR   PhylomeDB; P95970; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00775; LysRS_core; 1.
DR   CDD; cd04322; LysRS_N; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..494
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152714"
FT   BINDING         399
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  57801 MW;  AF19750B74CE2443 CRC64;
     MLMNWDERRV KIVEELRKNG IEPYPHKYEV THLIKDIKLI AKSQGNKSHE PFMFNISTAG
     RVANIRRHGK ASFVDIFDEG EKLQLYMRVD ELKEKYDKFF IYVGRGDIIG VKGDLFYTMK
     GELSLLVKDY QLLSKALIEP PDWSKLSPEF RYAHRYVDFL YNDNARKAME IRYTIIREIR
     EFLYSKGFIE VETPIVQPVY GGALAKPFKT HVNYLNEDWY LRIALELYLK RYIIGGFNKV
     FEIGKVFRNE DIDVTHNPEF TLLELYWAYA DYNDIMNLTE DLLKSVVKKV TNSTKIVYGK
     YEIDFEGPFK RISMYDSLSE ILGKDVESMS DNELKELMKK YNLTPRGNQY VRGLMIEKLF
     DKLVTPTLTN PTFITDYPIE TTPLCKPHRN KPGLVERFEM FIAGMEVANA YTELNDPILQ
     DKLFREEQEM FRRGDEEAHP YDKDFVRALS YGMPPTGGLG IGIDRIVMLV TNNYSIKEVI
     PFPMISSKVI LEDD