ID   SYK_METBA               Reviewed;         537 AA.
AC   Q9C4B7;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; Synonyms=lysK;
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Srinivasan G., Paul L., Lienard T., Gottschalk G., Krzycki J.A.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00177}.
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DR   EMBL; AF337056; AAK29405.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9C4B7; -.
DR   SMR; Q9C4B7; -.
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.
FT   CHAIN           1..537
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152752"
FT   MOTIF           30..38
FT                   /note="'HIGH' region"
FT   MOTIF           276..280
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   537 AA;  60199 MW;  A5920EA1C810E99A CRC64;
     MADTIHWADV IAEDVLKKNG KHLVATGITP SGNIHIGNMR EVVTADAVYR ALVDKGANAD
     FIYIADNYDP LRKVYPFLPE SYVEHVGKPI SEIPCPCGNC ANYAEHFLKP FLEALRRLGI
     NPKVYRADEM YKTGKYTEAI KTALVKRDAI AKILEEVSGK TVASDWSPFN PRCDQCGRIT
     TTKVTGFDLE AETVDYVCAC EHSGTVPMAG GGKLTWRVDW PARWSVLGVT VEPFGKDHAS
     RGGSYDTGKR IVKEIFGHEP PYPIVYEWIM LGKQGAMSSS TGVVVSISDM LKIVPPEVLR
     YLIIRTKPEK HIQFDPGQPL LSLVDEYERL RTQFRENDPS LGTFQGRVYE LSRATGVCQS
     EIPFKQMVTI YQVARGDFDQ VLKIVKRSGF STEDKKCIKE LADNVSKWLK LYAPPFAKFK
     VKEKVPVQAA TLSELQRAFL SAFAALIESR DEISGEEYHM LVYSAKDEGS ELNRRIAEKL
     NAHAPQVDPR ELFKAIYISL LGQSSGPKAG WFLSSFEKEF LVERFEEASN YSPEINV