ID   SYK_METMI               Reviewed;         533 AA.
AC   P0CW66; O30522;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Lysine--tRNA ligase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   Name=lysS;
OS   Methanococcus maripaludis (Methanococcus deltae).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=39152;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-22.
RC   STRAIN=ATCC 43000 / DSM 2067 / JCM 10722 / JJ;
RX   PubMed=9353192; DOI=10.1126/science.278.5340.1119;
RA   Ibba M., Morgan S., Curnow A.W., Pridmore D.R., Vothknecht U.C.,
RA   Gardner W., Lin W., Woese C.R., Soell D.;
RT   "A euryarchaeal lysyl-tRNA synthetase: resemblance to class I
RT   synthetases.";
RL   Science 278:1119-1122(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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AF009824; AAB87410.1; -; Genomic_DNA.
DR   PIR; T46975; T46975.
DR   AlphaFoldDB; P0CW66; -.
DR   SMR; P0CW66; -.
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; IPR045462; aa-tRNA-synth_I_cd-bd.
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; PF19269; Anticodon_2; 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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..533
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152756"
FT   MOTIF           28..36
FT                   /note="'HIGH' region"
FT   MOTIF           278..282
FT                   /note="'KMSKS' region"
FT   CONFLICT        11
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  61273 MW;  007FA868A57A0AC2 CRC64;
     MHWADATSEK IMKKRNAEEY VVSSGITPSG HIHIGNARET LTADAVYKGM LKKGAEAKLI
     FIADDYDPLR KLYPFLPKEF EKYIGMPLSE IPCPQGCCKS YADHFLMPFL NSLEDLGVEI
     TTHRANECYK AGMYNEAIIT ALENRLKIKE LLDSYRKEPL ADNWYPLNVV CEKCGKMHET
     KVTSYNSEDK TITYVCKCGF ENTVQPFNGI GKLPWRVDWP ARWNIFGVTA EPMGKDHAAS
     GGSYDTGIKI ARQIFNYQAP EKMVYEWIQL KIGDKAMPMS SSSGVVFAVK DWTEICHPEV
     LRFLILKGKP TKHIDFDLKA ISNLVDDYDE LERKYFELIE KQKTEELNDN ENEKISLYEL
     VTPKIPERLP LQVAYRFCSI IAQIALDKET QKIDMERVFD ILGRNGYNPA EFSEYDKSRL
     EKRLYMSKKW ASDYGENLEI NDFEQAKEQY ETLSEEQKAW LKAFSKEVEN IEIDANTIHE
     LMYETATKLN LAPKEAFVAS YKILLGKNYG PKLGSFLASL KKEFVIGRFN LTE