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Database: UniProt
Entry: R5PYX0_9BURK
LinkDB: R5PYX0_9BURK
Original site: R5PYX0_9BURK 
ID   R5PYX0_9BURK            Unreviewed;       419 AA.
AC   R5PYX0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
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};
GN   ORFNames=BN489_00411 {ECO:0000313|EMBL:CCZ19284.1};
OS   Sutterella wadsworthensis CAG:135.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=1263111 {ECO:0000313|EMBL:CCZ19284.1, ECO:0000313|Proteomes:UP000018089};
RN   [1] {ECO:0000313|EMBL:CCZ19284.1, ECO:0000313|Proteomes:UP000018089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:135 {ECO:0000313|Proteomes:UP000018089};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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,
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   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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:CCZ19284.1}.
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DR   EMBL; CAZN010000454; CCZ19284.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5PYX0; -.
DR   Proteomes; UP000018089; 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   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|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000313|EMBL:CCZ19284.1};
KW   Magnesium {ECO:0000256|RuleBase:RU000336};
KW   Metal-binding {ECO:0000256|RuleBase:RU000336};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}.
FT   DOMAIN          185..414
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   419 AA;  48051 MW;  D050A859291BC188 CRC64;
     MTNENISVTE VQNENSVIAE RRAKLLKLRE HGVAYPNDFV RKDLFGDLNE KYGNKTAEEL
     AALAPKVACA GRVMLKRVMG RLTFATVRDY TGTMQYFVQE STVGEAAYAD FKTLDLGDIV
     ACEGTLMRTQ AGDLAIKVTS FRLMAKSLRP MPDKHKGLQD QEFCYRRRYV DLMVNAESRE
     RFIKRSKAIA SIRNFMLAND FLEVETPMLH PIPGGANARP FITHHNALNT EMYLRIAPEL
     YLKRLVVGGF ERVFEINRNF RNEGIDARHN PEFTMMEFYA TYWTYKDQME FTEALLRHVA
     REVTGSAIVT YQGMTINFEE PFDKLTPKQA ILKYSPEYTE SQLVDEDFLK KELKRLGADE
     QIDPTLGSLQ MALFDETVEK KLIKPTFIID YPTEISPLAR ASDVNPDITE RFELYCGTL
//
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