ID   F0LM71_THEBM            Unreviewed;       526 AA.
AC   F0LM71;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   04-NOV-2026, entry version 73.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN   OrderedLocusNames=TERMP_00942 {ECO:0000313|EMBL:ADT83918.1};
OS   Thermococcus barophilus (strain DSM 11836 / MP).
OC   Archaea; Methanobacteriati; Methanobacteriota; Thermococci; Thermococcales;
OC   Thermococcaceae; Thermococcus.
OX   NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT83918.1, ECO:0000313|Proteomes:UP000007478};
RN   [1] {ECO:0000313|EMBL:ADT83918.1, ECO:0000313|Proteomes:UP000007478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX   PubMed=21217005; DOI=10.1128/JB.01490-10;
RA   Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT   "Complete genome sequence of the hyperthermophilic, piezophilic,
RT   heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL   J. Bacteriol. 193:1481-1482(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Lys) + L-lysine + ATP = L-lysyl-tRNA(Lys) + AMP +
CC         diphosphate; 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:0000256|ARBA:ARBA00048573, ECO:0000256|HAMAP-
CC         Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00177}.
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DR   EMBL; CP002372; ADT83918.1; -; Genomic_DNA.
DR   RefSeq; WP_013467216.1; NC_014804.1.
DR   GeneID; 10041259; -.
DR   KEGG; tba:TERMP_00942; -.
DR   PATRIC; fig|391623.17.peg.945; -.
DR   eggNOG; arCOG00485; Archaea.
DR   HOGENOM; CLU_025562_1_0_2; -.
DR   OMA; AACAWNW; -.
DR   OrthoDB; 6838at2157; -.
DR   CDD; cd00674; LysRS_core_class_I; 1.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 1.10.10.770; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 6.10.20.10; Lysine tRNA ligase, stem contact fold domain; 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; LYSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   NCBIfam; TIGR00467; lysS_arch; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
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   Proteomes; UP000007478; Chromosome.
DR   AlphaFoldDB; F0LM71; -.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00177};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00177};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00177};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00177};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00177}; Reference proteome {ECO:0000313|Proteomes:UP000007478}.
FT   DOMAIN          445..523
FT                   /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19269"
FT   MOTIF           30..38
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   MOTIF           280..284
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   526 AA;  61498 MW;  ABB29ACD099E81AD CRC64;
     MVHWADYMAE KIIRERGDKE EYVVESGITP SGYVHIGNFR ELFTAYIVGH ALKDKGKKVR
     HIHMWDDYDR FRKVPKNVPG EWKEYLTMPV SEVPDPWGCH NSYAEHFMEL FESEVEKLGI
     EVDFLRASRL YKTGEYAKDI RKALENREKI VAILNKFRDM AKQPHLEESW QPVQIYCPKC
     RKEADFIQWD GGWKVEYKCP HCGSEGKTDI REGNVKLRWR VDWPMRWAHF GVDFEPAGKD
     HLAAGSSFDT GREIIKTVYG KEPPLTLMYE FVGIKGQKGK MSGSKGNVIL LSDLYEVLEP
     GVIRFLYARH RPNKEIKIDL GLGLLNLYDE FDKVERIYFG LENAKNKEEE IELKRTYELS
     MPKIPERLVA QAPFRFLVVL VQMPHLDEGK IIEILKKQGH IPQDLAEEDT ERIKLRIMLA
     KNWVSKYAPD TVKFSLLQEP PRIEISEEIK EALNEVANWL ESREEFSVDE LNNIIFDAAK
     KRNIPSKQWF KILYQLFIGK DRGPRLASFL ASLDKDFVTR RLRLKA
//