ID   SYK_STRCO               Reviewed;         580 AA.
AC   Q9X895;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 2.
DT   25-MAY-2022, entry version 125.
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=SCO3303; ORFNames=SCE15.20c, SCE68.01c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL939116; CAD55312.1; -; Genomic_DNA.
DR   RefSeq; NP_733599.1; NC_003888.3.
DR   RefSeq; WP_003975532.1; NZ_VNID01000025.1.
DR   AlphaFoldDB; Q9X895; -.
DR   SMR; Q9X895; -.
DR   STRING; 100226.SCO3303; -.
DR   PRIDE; Q9X895; -.
DR   GeneID; 1098737; -.
DR   KEGG; sco:SCO3303; -.
DR   PATRIC; fig|100226.15.peg.3364; -.
DR   eggNOG; COG1384; Bacteria.
DR   HOGENOM; CLU_025562_0_0_11; -.
DR   InParanoid; Q9X895; -.
DR   OMA; DWPMRWA; -.
DR   PhylomeDB; Q9X895; -.
DR   Proteomes; UP000001973; 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: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; 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; 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;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..580
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152744"
FT   REGION          178..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           43..51
FT                   /note="'HIGH' region"
FT   MOTIF           325..329
FT                   /note="'KMSKS' region"
FT   COMPBIAS        178..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  63552 MW;  2B1CDCD7A744D06D CRC64;
     MPIVAQSTET TDWVSRFADE VIAESERRAP GKPGVVVASG LSPSGPIHLG NLREVMTPHL
     VADEVRRRGH EVRHLISWDD YDRYRKVPAG VPGVDESWAE HIGKPLTSVP APKGSPHPNW
     AEHFKAAMVD SLAEMGVEFD GISQTAQYTS GVYREQILHA MKHRRDIDAI LDQYRTKKAP
     AKKSQKPLDE AELEAAEGSG AAAEDDGSSG SAGYFPYKPY CGNCEKDLTT VTAYDDDSTE
     LTYACTACGF SETVRLSEFN RGKLVWKVDW PMRWAYEGVV FEPSGVDHSS PGSSFQVGGQ
     IVGIFGGEQP IGPMYAFVGI SGMAKMSSSK GGVPTPADAL KIMEPQLLRW LYARRRPNQS
     FKIAFDQEIQ RLYDEWDRLD AKVADGSALP ADAAAHARAV GTAAGELPRT PRPLPYRTLA
     SVADITAGHE DQALRILGEL DPANPIASLD EARPRYDKAE AWINTHVPAD QRTIVRQEPD
     AELLKSLDEP SRQSLRLLLD GLADHWSLDG LTHHVYGVPK VQAGFPADAT PKELPPEIKT
     AQRTFFALLY HLLVGRDTGP RLPTLLLAVG QDRVRTLLGE