SYK_PROM9
ID SYK_PROM9 Reviewed; 512 AA.
AC Q318C3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00252};
DE EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00252};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00252};
DE Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00252};
GN Name=lysS {ECO:0000255|HAMAP-Rule:MF_00252};
GN OrderedLocusNames=PMT9312_1711;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000111; ABB50772.1; -; Genomic_DNA.
DR RefSeq; WP_011377253.1; NC_007577.1.
DR AlphaFoldDB; Q318C3; -.
DR SMR; Q318C3; -.
DR STRING; 74546.PMT9312_1711; -.
DR EnsemblBacteria; ABB50772; ABB50772; PMT9312_1711.
DR KEGG; pmi:PMT9312_1711; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_0_3; -.
DR OMA; EIFGEKC; -.
DR OrthoDB; 63621at2; -.
DR Proteomes; UP000002715; 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; IPR034762; Lys-tRNA-ligase_II_bac/euk.
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 PIRSF; PIRSF039101; LysRS2; 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.
FT CHAIN 1..512
FT /note="Lysine--tRNA ligase"
FT /id="PRO_1000012905"
FT BINDING 408
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT BINDING 415
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT BINDING 415
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
SQ SEQUENCE 512 AA; 58925 MW; 0F63322C160B31A9 CRC64;
MSEIREARLQ KANSLVSKGF ASYAESFSVS HTTKFLIQKF DYLENGQEED FSVSLAGRVM
AKRVMGKIAF FTISDQEGQI QLYLDKRMIN CNLENQKLLS FEDIKEIVDI GDWIGVYGTI
KKTNKGELSI KVEKWEMLSK SLQPLPDKWH GLTDIEKRYR QRYLDLIVNP HSKNVFKTRA
KCISFIRQWL DNRNFLEIET PILQSEAGGA EARPFITHHN TLDIPLYLRI ATELHLKRMV
VGGFEKVYEL GRIFRNEGIS TKHNPEFTSV EIYQAFSNYV DMMNLTEELI KDIVFNVCGS
LVINYQNKEI DFSKPWSRIS MKDIVKKYTG IDFDSFSGDF QSAKQAVKSI NVEFSNKVNS
MGRLLNEVFE QKVESELIEP TFVIDYPVEI SPLARPHLDN KEMVQRFELF IVGRELANAF
SELIDPVDQR ERMQLQQSLR DEGDHEAHCI DEDFLNALEI GMPPTGGLGI GIDRLIMLIT
NSPSIRDVIP FPLLKPEITS NKNEKLPLNE VK
