ID G1VV11_9FIRM Unreviewed; 641 AA.
AC G1VV11;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
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 ORFNames=HMPREF9022_03842 {ECO:0000313|EMBL:EGX72651.1};
OS Erysipelotrichaceae bacterium 2_2_44A.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=457422 {ECO:0000313|EMBL:EGX72651.1, ECO:0000313|Proteomes:UP000003043};
RN [1] {ECO:0000313|EMBL:EGX72651.1, ECO:0000313|Proteomes:UP000003043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_2_44A {ECO:0000313|EMBL:EGX72651.1,
RC ECO:0000313|Proteomes:UP000003043};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium 2_2_44A.";
RL Submitted (JUN-2011) 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:EGX72651.1}.
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DR EMBL; ADCZ01000034; EGX72651.1; -; Genomic_DNA.
DR AlphaFoldDB; G1VV11; -.
DR PATRIC; fig|457422.3.peg.4039; -.
DR HOGENOM; CLU_008255_6_1_9; -.
DR OrthoDB; 9801152at2; -.
DR Proteomes; UP000003043; 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:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
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; 2.
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 InterPro; IPR002547; tRNA-bd_dom.
DR NCBIfam; TIGR00499; lysS_bact; 1.
DR PANTHER; PTHR42918:SF15; LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00252};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00252};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00252};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00252};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00252};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00252};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 178..492
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 536..641
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT BINDING 404
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 411
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 411
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ SEQUENCE 641 AA; 72877 MW; 5EFC3416C54271BC CRC64;
MEKLTEQEVI RRQKMEDLRA MGIEPFGHAY QRTHKSGEIR AAYEDCTKEE LEEKDLTVKI
AGRIMTKRRQ GKAGFMHIQD IDGQIQIYVR KDVIGEEAYE VFKKSDLGDI VGIEGKVMKT
NHGELSVKAE VYTHLTKALR PLPEKYHGLQ DVEERFRRRY VDLITNENSK RIALTRPRII
RAIQNYLDNE GLVEVETPVL QPILGGASAR PFVTHHNTLD MPFYLRIATE LPLKRLIVGG
LEGVYEIGRL FRNEGMDATH NPEFTTVEAY VAYSDLSGMM DLVEGLLNHV AEKVCGTTEI
EWQDKTISLK APFKRLHMVD GIKEACGVDF WQEMSFADAC AIAKEHDIEV EKKHNSVGHI
INLFFEKYVE ETLIQPTYVY GHPVEISPLA KKNAQDPRFA DRYELFIDGH EYANAFSELN
DPIDQRERFE NQLKLRDLGD DEANEMDTDY VEALEYGLPP TGGVGLGIDR LVMLLTNSQT
IREVLLFPTM KPLNDVNKGN DVKNQPVEEM KAEPEKIDFS KVKIEPLFEE TVDFDTFSKS
DFRAVKVKEC VAVPKSKKLL QFTLDDGTGT DRTILSGIHA YYEPEELVGK TLIAITNLPP
RAMMGIDSCG MLLSAIHEEE GEEKLHLLMV DDHIPAGAKL Y
//