ID A0A0S8DPQ3_9BACT Unreviewed; 424 AA.
AC A0A0S8DPQ3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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};
DE Flags: Fragment;
GN ORFNames=AMJ78_10350 {ECO:0000313|EMBL:KPK38206.1};
OS Omnitrophica WOR_2 bacterium SM23_29.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1703776 {ECO:0000313|EMBL:KPK38206.1, ECO:0000313|Proteomes:UP000050824};
RN [1] {ECO:0000313|EMBL:KPK38206.1, ECO:0000313|Proteomes:UP000050824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_29 {ECO:0000313|EMBL:KPK38206.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPK38206.1}.
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DR EMBL; LJUB01000157; KPK38206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DPQ3; -.
DR PATRIC; fig|1703776.3.peg.1789; -.
DR Proteomes; UP000050824; 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 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: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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:KPK38206.1};
KW Ligase {ECO:0000313|EMBL:KPK38206.1};
KW Magnesium {ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|RuleBase:RU000336}.
FT DOMAIN 164..424
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 424
FT /evidence="ECO:0000313|EMBL:KPK38206.1"
SQ SEQUENCE 424 AA; 48650 MW; 4271F2337F3346FA CRC64;
MEEVNEIIKQ RIKKLEALKE RGIVPYGGKY SKSSAIKELV QNFEEGKEVS VAGRIMAIRS
HGKSSFIDIK DSTGKIQGYI KSDVVGNDGY WVFENLDIGD IVGLKGKTFK TKTQEPTINV
SEITVLSKSI RPLPEKWHGL KDIELRYRQR YLDLLVNKEV REIFELRSRL ISRIRTFLDG
KGFLEVETPM MQPLPGGATA RPFKTHHEAL GVDLYLRIAP ELYLKRLLVG GFEKVYEINR
NFRNEGISPR HNPEFTMLEV YAAYANYQDM MELACELILD AAKHIFGKYK VNYKDGDIDL
SPPWANLTFH EAVTKYAGID YKAEKDIRHV AKGLGLEIEE TKLEEEVVNK IFEKFVEPKL
IKPTFVIDYP ARLCPLSKRK PDAPDLAERF ELFIGGQELA NAYSELNDPL EQRARFEEQV
EQDV
//
