ID A0A0G0XRB4_9BACT Unreviewed; 471 AA.
AC A0A0G0XRB4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU000336};
DE EC=6.1.1.6 {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU000336};
GN ORFNames=UU84_C0007G0013 {ECO:0000313|EMBL:KKS27300.1};
OS Candidatus Yanofskybacteria bacterium GW2011_GWC2_41_9.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619029 {ECO:0000313|EMBL:KKS27300.1, ECO:0000313|Proteomes:UP000033859};
RN [1] {ECO:0000313|EMBL:KKS27300.1, ECO:0000313|Proteomes:UP000033859}
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,
CC ECO:0000256|RuleBase:RU000336};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU000336};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|RuleBase:RU000336};
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:KKS27300.1}.
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DR EMBL; LCCE01000007; KKS27300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0XRB4; -.
DR PATRIC; fig|1619029.3.peg.172; -.
DR Proteomes; UP000033859; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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:SF9; LYSINE--TRNA LIGASE; 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 4: Predicted;
KW Ligase {ECO:0000313|EMBL:KKS27300.1};
KW Magnesium {ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|RuleBase:RU000336}.
FT DOMAIN 176..442
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 471 AA; 54800 MW; 9AAE56B8D206EE80 CRC64;
MALEEILNIK KEKIKDLKRA GIDPYPAQSS RTHKISEVLK QFDKLSADKE TLILAGRVRA
LRGHGGVIFF DIDDGSAKIQ GLIKEDAAGK DFFKNFTKFI DIGDFVEIKG SLFKTKKEEK
TLEVQEYRLL TKTLLPLPEK WHGLQDIEER LRRRYLDLIM DSDEREIFVK KSHFWQSIRK
FLINEGGLEV ETPVLERIPG GADAEPFSTR MNALDMDLYL RISLELNLKR LIVGGYDKVF
EIGRIFRNEG IDREHLQDYT QMEMYWAYYD YEKLMVLLKN MYQAVITETI GSLAHEYQGR
QIDWSGDWLK IDYYDFFKKH TGLDLSSVSE AGLKAYGSEN NIDISQHLGR GRLIDVIFKK
KVRPNLIQPC FLVLPPVDIE PLAKRWPQDH GRVERFQIMA GGSELGKGFS ELNDPMDQRE
RFEEQSRLRE AGDKEAQRMD EDFVEALECF AFITDRSVRE TVFFPLMKPK E
//
