ID   SYK1_MYCPU              Reviewed;         491 AA.
AC   Q98QH1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Lysine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00252};
DE            Short=LysRS 1 {ECO:0000255|HAMAP-Rule:MF_00252};
GN   Name=lysS1 {ECO:0000255|HAMAP-Rule:MF_00252}; OrderedLocusNames=MYPU_3900;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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_00252};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00252};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00252};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00252}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC13563.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL445564; CAC13563.1; ALT_INIT; Genomic_DNA.
DR   PIR; F90560; F90560.
DR   RefSeq; WP_041364058.1; NC_002771.1.
DR   AlphaFoldDB; Q98QH1; -.
DR   SMR; Q98QH1; -.
DR   STRING; 272635.MYPU_3900; -.
DR   EnsemblBacteria; CAC13563; CAC13563; CAC13563.
DR   KEGG; mpu:MYPU_3900; -.
DR   eggNOG; COG1190; Bacteria.
DR   HOGENOM; CLU_008255_6_0_14; -.
DR   OrthoDB; 63621at2; -.
DR   BioCyc; MPUL272635:G1GT6-397-MON; -.
DR   Proteomes; UP000000528; 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..491
FT                   /note="Lysine--tRNA ligase 1"
FT                   /id="PRO_0000152652"
FT   BINDING         400
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT   BINDING         407
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT   BINDING         407
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
SQ   SEQUENCE   491 AA;  56912 MW;  E4672F765B1909BB CRC64;
     MNDNIKLTEQ EIIRREKLKK YESLGIKTFK KFDHEKINIY SNEIVEKYNH FSKDELLEKQ
     IKLIIAGRIL TQRGPFIVIQ DTNGKIQLYV DKKELEEQKE TLALLDIGDI IYVKGTLMKT
     MKGELTIKVN FFDLLTKGLT PLAEKYHGLV DVEERYRKRY LDLISNPNIK EIFWTRTKVI
     SKIRKFFDEQ NFMEVETPML HSILGGANAR PFKTYHNSLS SSFNLRIATE LPLKKLLVGG
     IDRVYEIGRI FRNEGIDTTH NPEFTSIEFY QAYSNLEIMM EQTENLIKFI AKELGLSKIK
     NHDVEIDLLA DFKKINMVDA VSEATKVDFR NIDLDKAIEV AGRYKVKVEK YFKVGHIINE
     LFELLIEKTL IQPTFVTGHP IEISPLAATS EDERFTERAE LFINTKEYAN MFTELNDPLD
     QRRRFEAQLE EKESGNEEAS EIDESFLSAL EYGLPPAGGC GIGIDRLVML LTEKESIREV
     ILFPTLKKKQ V