ID   SYK_SOLLC               Reviewed;         588 AA.
AC   Q43776;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Lysine--tRNA ligase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   Name=LYSRS;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bonner Beste; TISSUE=Root;
RX   PubMed=9118995; DOI=10.1111/j.1432-1033.1997.00310.x;
RA   Giritch A., Herbik A., Balzer H.-J., Ganal M., Stephan U.W., Baumlein H.;
RT   "A root-specific iron-regulated gene of tomato encodes a lysyl-tRNA-
RT   synthetase-like protein.";
RL   Eur. J. Biochem. 244:310-317(1997).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X94451; CAA64223.1; -; mRNA.
DR   PIR; T07085; T07085.
DR   RefSeq; NP_001234285.1; NM_001247356.1.
DR   AlphaFoldDB; Q43776; -.
DR   SMR; Q43776; -.
DR   STRING; 4081.Solyc10g076610.1.1; -.
DR   PaxDb; Q43776; -.
DR   PRIDE; Q43776; -.
DR   GeneID; 778357; -.
DR   KEGG; sly:778357; -.
DR   eggNOG; KOG1885; Eukaryota.
DR   InParanoid; Q43776; -.
DR   OrthoDB; 837479at2759; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q43776; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IBA:GO_Central.
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; IPR034762; Lys-tRNA-ligase_II_bac/euk.
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   PIRSF; PIRSF039101; LysRS2; 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   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..588
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152769"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  67116 MW;  66590227238C20CF CRC64;
     MDSSVSTEPL SKNALKREKK AKEKEQLEQE KKAAAVAKRQ MEQHNLPEND DLDPTQYLAN
     RLRNIESLRE SGINPYPHKF FITMSIPEFI SRYAHLNTGE FPEDIDMSLA GRVISKRASS
     SKLYFYELLG GGARVQVLAS ARDSDVDAVQ FSNYQSGVKR GDIIGVRGYP GKSKRGELSI
     FAKPFIVLAP CLHMLPRRLT SSIVDETRTQ NFQGITAYDT WTPGDLRNPE SYVLRDQETR
     YRQRYLDLMM NPEVRALFRT RARIISYIRS FLDNLEFLEV ETPSMNLTAG GASARPFITH
     HNELDTELLI RVSPELYLKK LVVGGFDRVY ELGKHFRNEG MDLTHSPEFT MCELYMAYAD
     YNDLMDLTEQ LLSGMVKDLT GSYKIRYHAN GLDNEPIEID FTPPFRKIDM LSELEKVANI
     SIPRDLSSES ANKHLVDVCE KFDVKCPPPH TTTRLLDKLV GHFIEVNCIN PTFIINHPEI
     MSPLAKSRRS EPGLTERFNL FVNRRELCDA YTELNDPTAQ RERFAEQLKD RQLGDDEAMD
     LDESFITALE YGLPPTGGLG MGIDRLTMLL TDSQNVKEVI LFPAMRLQ