ID D5ETN2_PRER2 Unreviewed; 575 AA.
AC D5ETN2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
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:ADE83576.1};
GN OrderedLocusNames=PRU_1691 {ECO:0000313|EMBL:ADE83576.1};
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Xylanibacter.
OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE83576.1, ECO:0000313|Proteomes:UP000000927};
RN [1] {ECO:0000313|EMBL:ADE83576.1, ECO:0000313|Proteomes:UP000000927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG North American Consortium for Rumen Bacteria;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(2010).
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}.
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DR EMBL; CP002006; ADE83576.1; -; Genomic_DNA.
DR RefSeq; WP_013065558.1; NC_014033.1.
DR AlphaFoldDB; D5ETN2; -.
DR STRING; 264731.PRU_1691; -.
DR KEGG; pru:PRU_1691; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_0_10; -.
DR Proteomes; UP000000927; Chromosome.
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: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|HAMAP-Rule:MF_00252};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000313|EMBL:ADE83576.1};
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:UP000000927}.
FT DOMAIN 188..499
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
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 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ SEQUENCE 575 AA; 65384 MW; 26FBB2CE205F11FA CRC64;
MNILELSEQE IGRRQSLQEL RSMGIDPYPA AEFPTNAFST EIKESFKDDE DREVVIAGRM
MSRRVMGKAS FAELQDSKGR IQVYITRDDI CPGENKDLYN NVFKRLLDIG DFIGVKGKVF
RTQTGEISVH ASELTLLSKS LKPLPIVKYK DGVAYDKFDD PELRYRQRYV DLVVNEGVKD
TFLKRATIIR TMRSILDNAG YTEVDTPILQ SIAGGASARP FITHFNALNQ DMYMRIATEL
YLKRLIVGGF EGVYEMGKNF RNEGMDKTHN PEFTCMELYV SYKDLLWGMT FTEKMLEEIC
TAVNGKPEVE IDGKVISFKA PFRRLPILDA IKEKTGFDCD GKTEDEIRAF CLSKGMDVDE
TMGKGKLIDE LFGEFCESTF IQPTFITDYP VEMSPLTKMH RSKPGLTERF ELMVNGKELA
NAYSELNDPI DQEERFIEQM KLADKGDDEA MIIDHDFLRA LQYGMPPTFG IGIGIDRLVM
LMTGKFAIGE VMLFPQMKPE KKIPQSSVAE WAEIGVPEDI VPVLRKAGFN LITNIKDEKP
QGLQQKIGEI FKKYKLELQK PSVDEVAAWI EKANV
//
