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Entry: A0A0G0HRG5_9BACT
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Original site: A0A0G0HRG5_9BACT 
ID   A0A0G0HRG5_9BACT        Unreviewed;       487 AA.
AC   A0A0G0HRG5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   ORFNames=US58_C0004G0032 {ECO:0000313|EMBL:KKQ41195.1};
OS   Candidatus Magasanikbacteria bacterium GW2011_GWA2_37_8.
OC   Bacteria; Candidatus Magasanikbacteria.
OX   NCBI_TaxID=1619036 {ECO:0000313|EMBL:KKQ41195.1, ECO:0000313|Proteomes:UP000034333};
RN   [1] {ECO:0000313|EMBL:KKQ41195.1, ECO:0000313|Proteomes:UP000034333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP-
CC         Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00252,
CC         ECO:0000256|RuleBase:RU000336};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|RuleBase:RU000336};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKQ41195.1}.
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DR   EMBL; LBTN01000004; KKQ41195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0HRG5; -.
DR   STRING; 1619036.US58_C0004G0032; -.
DR   PATRIC; fig|1619036.3.peg.126; -.
DR   Proteomes; UP000034333; Unassembled WGS sequence.
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; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00499; lysS_bact; 1.
DR   PANTHER; PTHR42918:SF15; LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00252};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00252};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252}.
FT   DOMAIN          165..484
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   BINDING         403
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT   BINDING         403
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ   SEQUENCE   487 AA;  55748 MW;  4ECE289C412365C1 CRC64;
     MEKAKNEEDI RLEHLANLRQ AGLDPYPPRV ERSHTLLEAK KEPLDSKVTV LGRIVGMRVM
     GRLCFCHLKD ESGRLQVAIS EKELGKDLFK LFTKNLEMGD FIEVTGIIFN THAGETSVLV
     QSFKVLCKAL LPLPEKFHGL NDVEIRYRKR YLDLLANEES MRIAKIRSVL VKEIRNYFDA
     LGFYEVETPI LQTLYGGALA RPFVTHHNAL DIPLYLRIAP ELYLKRLIVG GFEKVYEIAR
     CFRNEGIDNN HNPEFTQIEF YWAYVDYNKL MDVIEDLLPK LITAVGLPLK FQTADGEADF
     TPPYPRKTMR QLVLDYAKID MEDYPDQISM YDVAKKLKVD GIEKNDGRGK LIDEIYKAYA
     RPHIKNPIFM TDHPIELSPL AKSKPGDPRY VERFQLLCVG GNELCNSFSE LNDPIDQEAR
     LREQVRLGES GDDESMPYDE DFVEALKHGM PPTGGLGMGI DRLVKLLVNA DNLKEVILFP
     TLKPEQK
//
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