ID C7GYY2_9FIRM Unreviewed; 507 AA.
AC C7GYY2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252};
DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252};
GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252,
GN ECO:0000313|EMBL:EEU03877.1};
GN ORFNames=GCWU000322_00182 {ECO:0000313|EMBL:EEU03877.1};
OS Eubacterium saphenum ATCC 49989.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=592031 {ECO:0000313|EMBL:EEU03877.1, ECO:0000313|Proteomes:UP000018436};
RN [1] {ECO:0000313|EMBL:EEU03877.1, ECO:0000313|Proteomes:UP000018436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49989 {ECO:0000313|EMBL:EEU03877.1,
RC ECO:0000313|Proteomes:UP000018436};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-
CC Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00252,
CC ECO:0000256|RuleBase:RU000336};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00252,
CC ECO:0000256|RuleBase:RU000336};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00252}.
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:EEU03877.1}.
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DR EMBL; ACON01000001; EEU03877.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GYY2; -.
DR STRING; 592031.GCWU000322_00182; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_0_9; -.
DR OrthoDB; 9801152at2; -.
DR Proteomes; UP000018436; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00775; LysRS_core; 1.
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:0000256|HAMAP-Rule:MF_00252};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00252};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00252};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000313|EMBL:EEU03877.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW ECO:0000256|RuleBase:RU000336};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00252};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252};
KW Reference proteome {ECO:0000313|Proteomes:UP000018436}.
FT DOMAIN 182..501
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 413
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ SEQUENCE 507 AA; 58275 MW; EB94077E64751650 CRC64;
MSNIEKEPQE IYEETAENIS EQRQIRREKL LKLQNEGRNP FLTEKWDVDA YSKEIKDGFD
DFDGKEVSCA GRIMANRHMG KASFIDIKDK LGRIQCYIRQ DEITPEEYEV FKTYDIGDIV
GVKGSVFKTR HGEISIRVSD IALLSKSLQV LPDKFKGLKD QDLRYRQRYV DLIVNDDVAD
TFRKRAAIIK EIRRYLEDDR GFLDVDTPVL TTIAGGANAR PFNTHHNTLD LDMKLRISNE
LYLKRLIVGG LDRVYEMGKM FRNEGMDRNH NPEFTSMELY QAYGDMDTVM DITENLIAKV
SEKVNGSMKI TYQGKEFDLT PPWDRITMVD AVKKWANEDF DKIQTDEEAI EVAKKHKIEN
ADKMSRGTII AELFEMYCED HLEGPIFVTG HPVEISPLSK RDSSDPRITR RFEAYINCWE
VANGFSELND PIDQLKRFKS QQEQLDAGDD EAHPMDEDFV NALEVGLPPT GGLGIGIDRV
IMLITNAASI RDVILFPTMK PLDKEDK
//
