SYK_AQUAE
ID SYK_AQUAE Reviewed; 597 AA.
AC O67258;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=aq_1202;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC07218.1; -; Genomic_DNA.
DR PIR; G70403; G70403.
DR RefSeq; NP_213822.1; NC_000918.1.
DR AlphaFoldDB; O67258; -.
DR SMR; O67258; -.
DR STRING; 224324.aq_1202; -.
DR EnsemblBacteria; AAC07218; AAC07218; aq_1202.
DR KEGG; aae:aq_1202; -.
DR PATRIC; fig|224324.8.peg.936; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_2_0; -.
DR InParanoid; O67258; -.
DR OMA; EIFGEKC; -.
DR OrthoDB; 63621at2; -.
DR Proteomes; UP000000798; 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; -; 2.
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; 2.
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..597
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152595"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 597 AA; 70024 MW; 66D6DAB0D588819B CRC64;
MLSLLSSEIF FSAIQYNLSL MEEVRLKKLQ ELREKGINPY PYRFEVTDFI GNIRKQYEEE
PPENYKVRVK GVAKRVSRTE NGYMVRLADE KGIEILVFTK EEGLKPKESY TFEGILKRVE
GKLSLVEAVL TEEEGEEVYK IKEQFDYDPN FRPVSLAGRL VSMRSMGKAI FGHIQDLTGK
IQIYLKKDVI GEEKLKFFND YIDVGDIVGV RGKLFRTNTG ELTVEVEEYQ LLAKSLHPLP
EKWHGLKDVE VRYRQRYLDL IANPEARRIF MLRTKLITEM RKFFEMHGFI EVETPILQPI
ASGANARPFV TYHNFLETEL YLRIAPELYL KRLIVGGFPR VYEIGKNFRN ESVDRTHNPE
FTMVEFYAAY WDYHDLIKFT EDMFVYLLEK TLGTLKVKYG EWELDFSPPF KKVRYFDLLK
EKTGKDKDFF LKDLEGLRKL AKELEIPDVE RMTHAKLLDK VFEKVAEEDL IQPTFVIDFP
KILSPLAKTH REDPDLVERF ELIIARYEVA NAYTELNDPF DQKERFLEQL KEKQMGDEEA
MDMDEDFIRA LEYGMPPTAG EGIGIDRLVM ILANTDSIRE VILFPQLKPE KKKKEAP
