ID A0A1F6DG20_9BACT Unreviewed; 486 AA.
AC A0A1F6DG20;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=A2765_02990 {ECO:0000313|EMBL:OGG60389.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_01_FULL_56_24.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798487 {ECO:0000313|EMBL:OGG60389.1, ECO:0000313|Proteomes:UP000176377};
RN [1] {ECO:0000313|EMBL:OGG60389.1, ECO:0000313|Proteomes:UP000176377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG60389.1}.
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DR EMBL; MFLA01000010; OGG60389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6DG20; -.
DR Proteomes; UP000176377; 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:OGG60389.1};
KW Magnesium {ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|RuleBase:RU000336}.
FT DOMAIN 177..483
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 486 AA; 55341 MW; DC9E95FC5435C5CC CRC64;
MASGDDIRAD RLKKLELLKL AGMGPYPAHT DKDADITEFL ADFDARLDAG TKSTLAGRVM
SKRGQGGIVF IDLFDGTEKA QIVFQKEEID EALFQLFSDT VDVGDFIEVT GVAYKTQRGH
NSLKASVWKM LAKSLLPIPD QWFGLKDEEA ILRQRYLDIL LDEEVRAMFA RRTRFWQAAR
EFLLARSFME VETPILETTP GGADARPFST HHNALDIDLH LRISLELWLK RLLVAGYPKV
FEIGRIFRNE GQSREHLQDY TQLETYEAYS DMRKGMQFTQ DLYRHIVNEV YGKYTFSISD
HTVDFAEEWP LIDFGEALEK AYGVNPITCS EKEAIQAARD AKVELGDSPN KARAIDNLWK
QLRKKIAGPA FLIGVPVYLE PLAKRSEANS DVVERFQVIL AGSEMGKGFS ELNDPQDQRA
RFEDQQKMRD AGDDEAQRLD EDYVKAMEYG MPPAFGFGVS ERLFSFLENR PAHEAQLFPL
LRPKND
//
