ID   SYK_CENSM               Reviewed;         524 AA.
AC   P0CW89; A0RWR7; O74059;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 39.
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   Cenarchaeum symbiosum.
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=46770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B;
RX   PubMed=9748430; DOI=10.1128/jb.180.19.5003-5009.1998;
RA   Schleper C., Delong E.F., Preston C.M., Feldman R.A., Wu K.-Y.,
RA   Swanson R.V.;
RT   "Genomic analysis reveals chromosomal variation in natural populations of
RT   the uncultured psychrophilic archaeon Cenarchaeum symbiosum.";
RL   J. Bacteriol. 180:5003-5009(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF083072; AAC62702.1; -; Genomic_DNA.
DR   PIR; T31311; T31311.
DR   AlphaFoldDB; P0CW89; -.
DR   SMR; P0CW89; -.
DR   PRIDE; P0CW89; -.
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; 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; 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.
FT   CHAIN           1..524
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000409229"
FT   MOTIF           39..47
FT                   /note="'HIGH' region"
FT   MOTIF           294..298
FT                   /note="'KMSKS' region"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   524 AA;  57799 MW;  12D077116E34B03F CRC64;
     METIGRGTWI DKLAHELVER EEALGRDTEM INVESGLGAS GIPHMGSLGD AVRAYGVGLA
     VGDMGHSFRL IAYFDDLDGL RKVPEGMPSS LEEHIARPVS AIPDPYGCHD SYGMHMSGLL
     LEGLDALGIE YDFRRARDTY RDGLLAEQIH RILSNSSVIG EKIAEMVGQE KFRSSLPYFA
     VCEQCGKMYT AESVEYLADS RKVRYRCGDA EVGGRKIAGC GHEGEADTGG AGGKLAWKVE
     FAARWQAFDV RFEAYGKDIM DSVRINDWVS DEILSSPHPH HTRYEMFLDK GGKKISKSSG
     NVVTPQKWLR YGTPQSILLL MYKRITGARE LGLEDVPSLM DEYGDLQREY FAGGGRGGKA
     REAKNRGLFE YTNLLEAQEG PRPHAGYRLL VELSRLFREN RTERVTKKLV EYGVIDGPSP
     GIERLIALAG NYADDMYSAE RTEVELDGAT RGALSELAEM LGSAPEGGLQ DVIYGVAKSH
     GVPPRDFFKA LYRIILDASS GPRIGPFIED IGREKVAGMI RGRL