ID   SYK_CENSY               Reviewed;         525 AA.
AC   P0CW90; A0RWR7; O74059;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Lysine--tRNA ligase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   Name=lysS; OrderedLocusNames=CENSYa_1157;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(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   -!- 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; DP000238; ABK77784.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CW90; -.
DR   SMR; P0CW90; -.
DR   STRING; 414004.CENSYa_1157; -.
DR   PRIDE; P0CW90; -.
DR   EnsemblBacteria; ABK77784; ABK77784; CENSYa_1157.
DR   KEGG; csy:CENSYa_1157; -.
DR   PATRIC; fig|414004.10.peg.1053; -.
DR   HOGENOM; CLU_025562_1_0_2; -.
DR   OMA; DWPMRWA; -.
DR   Proteomes; UP000000758; 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; 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; Reference proteome.
FT   CHAIN           1..525
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152748"
FT   MOTIF           40..48
FT                   /note="'HIGH' region"
FT   MOTIF           295..299
FT                   /note="'KMSKS' region"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   525 AA;  57652 MW;  1E415EA10835BF20 CRC64;
     MEETIGRGTW IDKLAHELIE REKALGRSTD MINVESGLGA SGIPHMGSLG DAVRAYGVGL
     ALGDMGHAFK LIAYSDDLDG LRKVPEGMPS SLEEHIARPV SAIPDPYGCH DSYGMHMSGL
     LLEGLDALNI EYDFRRARDT YRDGLLSEQI HGILSSSSKI GEKIAEMVGQ EKFRSSLPYF
     AVCGQCGKMY TAEAVEYVAD SRKVRYRCAD AKVGGKQVAG CGHEGEADIG GAGGKLAWKV
     EFAARWQAFD VRFEAYGKDI MDSVRINDWV SDEILSNPHP HHARYEMFLD KGGKKISKSS
     GNVVTPQKWL RYGTPQSILL LMYKRITGAR ELGLEDVPAL MDEYGDLQRE YFAGGGRGGK
     AREAKNRGLF EYANLLVKQA GPRPHAAYRL LVELSRLFKE DRAERVTKKL VEYGVVDGPS
     PEIERLIGLA GNYADDMYAA ERSDIELDEA TKGALSELVE LLGSAPGDGL QDAIYGIAKS
     HGVPPRDFFR ALYRIILDTP SGPRIGPFIE DIGREKVAGM IRGRL