ID A0A0G1EPW5_9BACT Unreviewed; 495 AA.
AC A0A0G1EPW5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=UV50_C0018G0008 {ECO:0000313|EMBL:KKS76608.1};
OS Parcubacteria group bacterium GW2011_GWB1_42_9.
OC Bacteria.
OX NCBI_TaxID=1618871 {ECO:0000313|EMBL:KKS76608.1, ECO:0000313|Proteomes:UP000034249};
RN [1] {ECO:0000313|EMBL:KKS76608.1, ECO:0000313|Proteomes:UP000034249}
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:KKS76608.1}.
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DR EMBL; LCES01000018; KKS76608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1EPW5; -.
DR PATRIC; fig|1618871.3.peg.642; -.
DR Proteomes; UP000034249; 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:KKS76608.1};
KW Ligase {ECO:0000313|EMBL:KKS76608.1};
KW Magnesium {ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|RuleBase:RU000336}.
FT DOMAIN 183..488
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 495 AA; 56972 MW; 5FEEE1099BDA59F3 CRC64;
MEDSLKSNLI GQRKIRLEKL EKIKSLGVNP YPAKSERDIQ IGEIKRDFDN YEGKIHTVAG
RITGWRTHGK LTFADIKDQT GSIQIIVKSD WLENDKESLS WENLELLDLA DFIEVRGEIG
KSKSGEISIL AKGVKLLTKS LRPIPRKLKN KEQKFRRRYI DLVINPESIK LFERKARFWE
VQREYLKKEG FMEVEVPVLE TVTGGADAKP FITHHNALDL DVYLRISTGE LWQKKLMVAG
LPKTFEIGRV FRNEGMDAEH LQDYTALEFY SAYSDYREGM ELVRELYRFV AEKTFGTQKF
TIRGFEVDLS KDWETYDFVA IIKEQTDIDI LSADLGVMEN KLRELGIVYD QKGFNLTRAI
DNLWKYCRKQ IAGPGFLINV PVTMEPLAKR QAENPALVER FQVIIAGSEN GKGFSELNDP
LDQAGRFADQ AKLREAGDEE AQRYDYEFVE ALEYGMPPTF GFGVSERLFS FLCDKPARET
QIFPLMRPKG NENLS
//
