SYK_METH1
ID SYK_METH1 Reviewed; 488 AA.
AC P46191; D1J8J2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=MHO_4040;
OS Metamycoplasma hominis (strain ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC
OS 10111 / PG21) (Mycoplasma hominis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=347256;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8181699; DOI=10.1111/j.1574-6968.1994.tb06715.x;
RA Ozkokmen D., Birkelund S., Christiansen G.;
RT "Characterization of a Mycoplasma hominis gene encoding lysyl-tRNA
RT synthetase (LysRS).";
RL FEMS Microbiol. Lett. 116:277-282(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC 10111 / PG21;
RX PubMed=19816563; DOI=10.1371/journal.pgen.1000677;
RA Pereyre S., Sirand-Pugnet P., Beven L., Charron A., Renaudin H., Barre A.,
RA Avenaud P., Jacob D., Couloux A., Barbe V., de Daruvar A., Blanchard A.,
RA Bebear C.;
RT "Life on arginine for Mycoplasma hominis: clues from its minimal genome and
RT comparison with other human urogenital mycoplasmas.";
RL PLoS Genet. 5:E1000677-E1000677(2009).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; X74912; CAA52877.1; -; Genomic_DNA.
DR EMBL; FP236530; CAX37539.1; -; Genomic_DNA.
DR PIR; S69892; S69892.
DR RefSeq; WP_012855678.1; NC_013511.1.
DR AlphaFoldDB; P46191; -.
DR SMR; P46191; -.
DR STRING; 347256.MHO_4040; -.
DR PRIDE; P46191; -.
DR EnsemblBacteria; CAX37539; CAX37539; MHO_4040.
DR GeneID; 57140094; -.
DR KEGG; mho:MHO_4040; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_0_14; -.
DR OMA; EIFGEKC; -.
DR OrthoDB; 63621at2; -.
DR Proteomes; UP000002631; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00775; LysRS_core; 1.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002313; Lys-tRNA-ligase_II.
DR InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00499; lysS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..488
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152648"
FT BINDING 398
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 5
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..131
FT /note="IVL -> MVT (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="I -> M (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="L -> T (in Ref. 1; CAA52877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 56790 MW; F55E569E50080B9F CRC64;
MERKLSEQEE IRRNKIAELE KNNLQAFHKT IKPTANSKEL NEKYKNLSRE DLDKQNLEFV
FNGRIMTIRG PFIVLQDNCG QMQIYANKKT LNESSAKTFS LMDFGDILSV RGTLSKTNTD
ALVIKAQDIV LLTKSLKPLP DKFHGLVDPE ERRRQRYVDL IMNEKTRNTF VMRTQIIKGI
REYFDSLNYI EVDTPILNPI LGGAAAKPFI TFYNALNRNF YLRIATELPL KKLIVGGLDR
VYEIGRIFRN EGVDTTHNPE FTSIEFYEAY SDLWGMMERT EGVFKHLINK FNIKEVKFNG
FDITFNFPFK RVNMIDAISE KINVDIRKLN EEQMFELAKK HGIKIEKFFR YGHIINELFE
KYVEETLIEP TFVYGHPIEI SPLAAIDPDD KRFTLRAELF IGTKEFANMF TELNDPIDQL
QRFENQLLEK ENGNEEANEI DWDFVNALEY GMPPTGGSGI GIDRLIMLLT QNDSIRDVVL
FPQLKDLK
