SYK_METMP
ID SYK_METMP Reviewed; 533 AA.
AC P0CW67; O30522;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=MMP1318;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP CHARACTERIZATION.
RX PubMed=11121028; DOI=10.1073/pnas.97.26.14224;
RA Soell D., Becker H.D., Plateau P., Blanquet S., Ibba M.;
RT "Context-dependent anticodon recognition by class I lysyl-tRNA
RT synthetases.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14224-14228(2000).
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.
CC -!- MISCELLANEOUS: Able to charge E.coli tRNA(Lys) in vitro.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF30874.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX950229; CAF30874.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048064106.1; NC_005791.1.
DR AlphaFoldDB; P0CW67; -.
DR SMR; P0CW67; -.
DR STRING; 267377.MMP1318; -.
DR EnsemblBacteria; CAF30874; CAF30874; MMP1318.
DR GeneID; 2761127; -.
DR KEGG; mmp:MMP1318; -.
DR PATRIC; fig|267377.15.peg.1353; -.
DR eggNOG; arCOG00485; Archaea.
DR HOGENOM; CLU_025562_0_0_2; -.
DR OMA; DWPMRWA; -.
DR OrthoDB; 9880at2157; -.
DR BioCyc; MMAR267377:MMP_RS06790-MON; -.
DR Proteomes; UP000000590; 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; 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; 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..533
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000408228"
FT MOTIF 28..36
FT /note="'HIGH' region"
FT MOTIF 278..282
FT /note="'KMSKS' region"
SQ SEQUENCE 533 AA; 61237 MW; 590032CCF31E5B31 CRC64;
MHWADATSEK IMKKRNAEEY VVSSGITPSG HIHIGNARET LTADAVYKGM LKKGAEAKLI
FIADDYDPLR KLYPFLPKEF EKYIGMPLSE IPCPQGCCKS YADHFLMPFL NSLEDLGVEI
TTHRANECYK AGMYNDAIIT ALENRLKIKE LLDSYRKEPL ADDWYPLNVV CEKCGKMHET
KVINYNSEDK TITYVCKCGF ENTVKPFNGI GKLPWRVDWP ARWNIFGVTA EPMGKDHAAS
GGSYDTGIKI ARQIFNYQAP EKMVYEWIQL KVGDKAMPMS SSSGVVFAVK DWTEICHPEV
LRFLILKGKP TKHIDFDLKA ISNLVDDYDE LERKYFELIE KQKTEELNDN ENEKISLYEL
VTPKIPERLP LQVAYRFCSI IAQIALDKET QKIDMERVFD ILGRNGYNPA EFSEYDKSRL
EKRLYMSKKW ASDYGENLEI NDLDQAKEQY ETLSEEQKAW LKAFSKEVEN IEIDANTIHE
LMYETATKLN LAPKEAFVAS YKILLGKNYG PKLGSFLASL KKEFVIGRFN LTE