ID   SYK_METST               Reviewed;         529 AA.
AC   Q2NHG8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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}; OrderedLocusNames=Msp_0249;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC56665.1; -; Genomic_DNA.
DR   RefSeq; WP_011405864.1; NC_007681.1.
DR   AlphaFoldDB; Q2NHG8; -.
DR   SMR; Q2NHG8; -.
DR   STRING; 339860.Msp_0249; -.
DR   EnsemblBacteria; ABC56665; ABC56665; Msp_0249.
DR   GeneID; 41324822; -.
DR   KEGG; mst:Msp_0249; -.
DR   eggNOG; arCOG00485; Archaea.
DR   HOGENOM; CLU_025562_1_0_2; -.
DR   OMA; DWPMRWA; -.
DR   OrthoDB; 9880at2157; -.
DR   Proteomes; UP000001931; 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   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; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR002904; Lys-tRNA-ligase.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..529
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_1000199267"
FT   MOTIF           29..37
FT                   /note="'HIGH' region"
FT   MOTIF           274..278
FT                   /note="'KMSKS' region"
FT   BINDING         277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   529 AA;  61587 MW;  A3A116FF992CC8C2 CRC64;
     MSKHWTERIA EELSQQKKDE YIIGSGTSIS GSVHIGNSCD IFIANAVSKE LRKIGENAKT
     VWIADDYDPL RKVPYPLPEN YSKYLGQPYY EIPCPEGCCE NFVEHFQKPF VNSLKPFDIE
     NLEIKSGAQM YKNGVYTEAT KVALENTERI REIFNEYREH PLSEDWLPYN AICSECGRVN
     TTHAYDFEGT NIKYKCDCGH EGEVDYTTGM GKLTWRVEWA ARWKILNITC EPFGKDHAAS
     GGSYDVSKII SDEIFNYPAP YPVPYEWITL DGDAMSKSKG VFFSPEAWLK IGKPETLNYY
     IFRNKPLKPK DFTPKMGFLD LMDQYDRVER IAYGQEEASN EKEKEKLTKI YEVSQINDMP
     DEMPFQPSYR FLTVAYQIAN GNANKIYTIL KNNNQLPERL ENVTFEDLSE FDRDTFLQRI
     EYVHNWLETY GPKFVKFQVM NKMPRIEITD EQKEFLKQIA NILESETFEN DVQFHDRMYE
     VLESLGMKPQ KAFQAIYKTI IGKKQGPRAA SFVLSLDKDF VIKRFRLEE