ID A0A0G0WP46_9BACT Unreviewed; 483 AA.
AC A0A0G0WP46;
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=UU32_C0019G0002 {ECO:0000313|EMBL:KKR86235.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_41_10.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618577 {ECO:0000313|EMBL:KKR86235.1, ECO:0000313|Proteomes:UP000033858};
RN [1] {ECO:0000313|EMBL:KKR86235.1, ECO:0000313|Proteomes:UP000033858}
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:KKR86235.1}.
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DR EMBL; LCAE01000019; KKR86235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0WP46; -.
DR PATRIC; fig|1618577.3.peg.301; -.
DR Proteomes; UP000033858; 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 Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:KKR86235.1};
KW Ligase {ECO:0000313|EMBL:KKR86235.1};
KW Magnesium {ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|RuleBase:RU000336}.
FT DOMAIN 178..482
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 483 AA; 55474 MW; 98E032821DC9B869 CRC64;
MALMDTVRAE RLAKIARLKE AGMDAYPARA SRTHTIEQFL ENHETLQGNS EQVILVGRVM
SIREHGGSVF VDIFDGTKGQ CYVQRNKLDE SSYELFTATV DTGDIVEFAG LAFMTKRGMP
SLDVTGWRML TKSLRPLPDE WFGIKDEDER FRKRYLDILL TKDLAERIRR RSKFWNVIRS
YFLDRDFVEV ETPVLETTTG GADARPFETH HNALDMDVYL RISAGELWQK RLIVAGLPKV
FEIGRIFRNE GMSAEHLQDY TQLEFYEAFK DYEAGMGMIT DLYRTVADKV YGRQTFSIKG
FDIDLSKEWE TYDFCALMQK EYDLDPLDEG ANWASVLIKK NISFEKGVGV ERLVDVAWKQ
VRKTLSGPGF LINVPVYMEP LAKKSAKNPR VVERFQVMIA GSEMGKGFSE LNDPVDQAER
FERQQQLREE GDEEAQMLDA EFVEALEYGM PPAFGFGVSE RLFSFLEGVS VREGQIFPLM
RPR
//
