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Database: UniProt
Entry: A0A0W8BV24_PHYNI
LinkDB: A0A0W8BV24_PHYNI
Original site: A0A0W8BV24_PHYNI 
ID   A0A0W8BV24_PHYNI        Unreviewed;       652 AA.
AC   A0A0W8BV24;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU003748};
DE            EC=6.1.1.6 {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU003748};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563, ECO:0000256|RuleBase:RU003748};
GN   ORFNames=AM587_10016222 {ECO:0000313|EMBL:KUF75683.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF75683.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUF75683.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) 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:RU003748};
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:KUF75683.1}.
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DR   EMBL; LNFO01005996; KUF75683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8BV24; -.
DR   STRING; 4790.A0A0W8BV24; -.
DR   EnsemblProtists; KUF75683; KUF75683; AM587_10016222.
DR   OMA; DFRNEGM; -.
DR   Proteomes; UP000052943; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00775; LysRS_core; 1.
DR   CDD; cd04322; LysRS_N; 1.
DR   Gene3D; 1.20.1050.10; -; 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; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR034762; Lys-tRNA-ligase_II_bac/euk.
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   PIRSF; PIRSF039101; LysRS2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 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:KUF75683.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943}.
FT   DOMAIN          236..566
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  72771 MW;  1D825AB652D8ECAB CRC64;
     MSTPSDAAPP TGNATAPISK NELKRRLKAE KAAKAKAEKA AKKAAEAASK PKKAAATDDE
     ELDPTAYFAN REKTLVELEK QGINPYPHKF HVSTSLPEFH AQFGDAEAGS HLSDVVVSVA
     GRLHSKRASG SKLVFYDLRA DGKKLQIMSD VGTYESAEAF AQIHSILRRG DIVGVKGHPG
     KSKKGELSIF PQQLVLLSPC MHMLPKSHAG LTLQQDTRYR QRYLDLIMND DSRGVFQTRA
     KIINFIRRFL DDKNFLEVET PMMNMIVGGA TAKPFVTYHN DLHMNLFMRV APELYLKQLV
     IGGLDRVYEI GRQFRNEGID LTHNPEFTSC EFYMAYADYN DLMTLTEKLF SEMVKEITGG
     YTITIQKEPG EEPVTIDFTP PFKRVSMVSA VEEATGVKIP IDEPEKCLVI LEELVTKYEL
     ECAPPRSIAR LLDKLVGHFI EDNKAYWTKP FFIMDQPVYN SPLAKYHREK AALTERFELF
     LAGAEICNAY TELNNPKVQR ERFIEQMEQA AAGDDEAQPH DESFCTAMEY GLPPTAGWGC
     GVDRLTMFLS NRFNIKEVLL FPAMKPDEQA APAPSASGSA SLISSTGSVA LDVLEKRLAG
     STFVNGSSPS KDDTAVFERV KVVGKDILKK YPNVEKWLDF VTAFPNELRA KW
//
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