ID A0A1F8N3G3_9CHLR Unreviewed; 476 AA.
AC A0A1F8N3G3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=A2Y91_07695 {ECO:0000313|EMBL:OGO05370.1};
OS Chloroflexi bacterium RBG_13_54_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797630 {ECO:0000313|EMBL:OGO05370.1, ECO:0000313|Proteomes:UP000180313};
RN [1] {ECO:0000313|EMBL:OGO05370.1, ECO:0000313|Proteomes:UP000180313}
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:OGO05370.1}.
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DR EMBL; MGMX01000015; OGO05370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8N3G3; -.
DR Proteomes; UP000180313; 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 Ligase {ECO:0000313|EMBL:OGO05370.1};
KW Magnesium {ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|RuleBase:RU000336}.
FT DOMAIN 193..476
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 476
FT /evidence="ECO:0000313|EMBL:OGO05370.1"
SQ SEQUENCE 476 AA; 54717 MW; 3B5A4288150B929E CRC64;
MPEVKPSLQP AEVIPYNIAL YPEMSKRLDD ITQRRLDKLQ RLRSQGINPY PHRYRRTHTA
QGAKDSFEQG AITADSEVNL AGRIMAQRGM GKATFFDLRD GSGRIQVYLR RDELGEAKYE
LAQDLDIGDI IGVRGKLFRT KSGETTLRVS DFGMLAKSLE PLPEKWHGLV DVEKRYRQRY
LDLISNEVAR NTFLIRSRTI TALRRFLDSR GFVEVETPVL HSVPGGARAQ PFKTHHQALD
QDFYLRIATE LYLKRLIVGG FDKVYEIGRI FRNEGISTKH NPEFTMLESY EAYADYHDVM
IMTEEMVSQV SEEVLGTRKI QFSEETIDLT PPWRRVTLRE AILEKCGIDI EDCLRGGMQG
LRHAMQAAGM ELDETLSPAY LIDKLVSTYV EPGLIQPTFL MDYPAETTPL AKRKEGNELL
VERFEVFVAG IEIANAFTEL NDPEDQANRF RIQEQWRTDF GDEEAERYQE DFIMAL
//
