ID   SYK1_METAC              Reviewed;         533 AA.
AC   Q8TTA3;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Lysine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00177};
DE            Short=LysRS 1 {ECO:0000255|HAMAP-Rule:MF_00177};
GN   Name=lysS1 {ECO:0000255|HAMAP-Rule:MF_00177}; Synonyms=lysK;
GN   OrderedLocusNames=MA_0534;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM03978.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TTA3; -.
DR   SMR; Q8TTA3; -.
DR   STRING; 188937.MA_0534; -.
DR   EnsemblBacteria; AAM03978; AAM03978; MA_0534.
DR   KEGG; mac:MA_0534; -.
DR   HOGENOM; CLU_025562_1_0_2; -.
DR   InParanoid; Q8TTA3; -.
DR   OMA; DWPMRWA; -.
DR   PhylomeDB; Q8TTA3; -.
DR   Proteomes; UP000002487; 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   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; Reference proteome.
FT   CHAIN           1..533
FT                   /note="Lysine--tRNA ligase 1"
FT                   /id="PRO_0000152751"
FT   MOTIF           26..34
FT                   /note="'HIGH' region"
FT   MOTIF           272..276
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   533 AA;  59593 MW;  718C638082F601B6 CRC64;
     MHWADVIAED VLNKSGKHLV ATGITPSGHI HIGNMREVVT ADAAYRALLD MGADARLIYI
     ADNYDPLRKV YPFLPESYAE HVGKPISEVP CPCGDCANYA EHFLKPFIEA LRRLGINPEV
     LRADEMYRAG LYTEAIKTAL AKRDEIAKIL EEVSGKTVAE DWSPFNPRCN ECGKITTTKV
     AGFDLEAETV DYVCACGHSG TVPMAGGGKL TWRVDWPARW AVLGVTVEPF GKDHASKGGS
     YDTGKRIVRE IYGHEPPFPI VYEWIMLGKR GAMSSSTGVV VSISDMLEVV PPEVLRYLII
     RTKPEKHIQF DPGQPLLNLV DEYERLRDKF RENDPSLGDF EKRIYELSRA TGICHPEIPF
     KQMVTIYQVA RGDFEQVLKI VKRSGFSTEN EKCIRELADN VSRWLELYAP PFAKFSVKEK
     VPVQTATLSE LQKAFLGAFA DLIETKGKIS GEEYHMLVYS AKDEGSELNR LIAQKVNVPV
     PQVDPKDLFK AIYTSILGQS SGPKAGWFLS SFEKGFLITR FREASTYNPE KSS