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SYK_VIBCH
ID   SYK_VIBCH               Reviewed;         510 AA.
AC   Q9KU60;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 2.
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=VC_0664;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93829.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF93829.1; ALT_INIT; Genomic_DNA.
DR   PIR; A82296; A82296.
DR   RefSeq; NP_230313.1; NC_002505.1.
DR   RefSeq; WP_000128764.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KU60; -.
DR   SMR; Q9KU60; -.
DR   STRING; 243277.VC_0664; -.
DR   DNASU; 2615453; -.
DR   EnsemblBacteria; AAF93829; AAF93829; VC_0664.
DR   GeneID; 57739381; -.
DR   KEGG; vch:VC_0664; -.
DR   PATRIC; fig|243277.26.peg.636; -.
DR   eggNOG; COG1190; Bacteria.
DR   HOGENOM; CLU_008255_6_2_6; -.
DR   OMA; EIFGEKC; -.
DR   Proteomes; UP000000584; Chromosome 1.
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..510
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152700"
FT   BINDING         420
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   510 AA;  58077 MW;  D62F5C9111294C45 CRC64;
     MTDAVQNEIN QEQIAQEENK LIAERRSKLD HIRKNCKANG HPNSFRRDSL AGDLQKKFGE
     KSKEELEALN HVVSIAGRVM AKRGPFLVIQ ETSGRIQAYA SKEVQQELKD KYQGLDIGDI
     IGVQGALHKS GKGDLYVNME QFQLLTKALR PLPEKFHGLT DQEMRYRQRY VDLIVNENSR
     NAFIVRSKVM SAIRNFMISK QFMEVETPMM HVIPGGASAR PFITHHNALD MPMYLRIAPE
     LYLKRLVVGG FDRVFEINRN FRNEGLSPRH NPEFTMMEFY MAYADYKDLM DLTEELLSSV
     ALEVLGSTSM PYGEHTVEFG GKYARMSMFD AIKHYNPNHA QIQALTEEDI QNRDLMVSIA
     KSVHVDVEPF WTCGQLLEEI FGETAEPKLM QPTFITGYPA DISPLARRSD DNPFFTDRFE
     FFIGGREVAN GFSELNDAED QDARFKAQVE AKESGDDEAM FYDADYITAL EHGLPPTAGQ
     GIGIDRLVML LTNTHTIRDV ILFPAMRPQQ
 
 
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