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Database: UniProt
Entry: R4XJT2_TAPDE
LinkDB: R4XJT2_TAPDE
Original site: R4XJT2_TAPDE 
ID   R4XJT2_TAPDE            Unreviewed;       603 AA.
AC   R4XJT2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=TAPDE_005204 {ECO:0000313|EMBL:CCG84693.1};
OS   Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS   / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Taphrinaceae; Taphrina.
OX   NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG84693.1, ECO:0000313|Proteomes:UP000013776};
RN   [1] {ECO:0000313|EMBL:CCG84693.1, ECO:0000313|Proteomes:UP000013776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC   NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX   PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA   Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA   Overmyer K., Hauser P.M., Pagni M.;
RT   "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT   agent of peach leaf curl.";
RL   MBio 4:e00055-e00013(2013).
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:CCG84693.1}.
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DR   EMBL; CAHR02000288; CCG84693.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4XJT2; -.
DR   STRING; 1097556.R4XJT2; -.
DR   VEuPathDB; FungiDB:TAPDE_005204; -.
DR   eggNOG; KOG1885; Eukaryota.
DR   Proteomes; UP000013776; 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; 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; 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; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000013776}.
FT   DOMAIN          260..591
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          22..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  68537 MW;  797306A1A624C5FC CRC64;
     MAEAIKDSLA EVTEKVSNLT TENDGLHLDD VTGERVSKTE LKKRQKQRIN DAKKAAKPPR
     AAVKAKVEGA DANVQELNPN EFHKIRSAAI NDMRSKVATG GRNPYPHKFH VSTRLPEFIK
     KYSHLKRGDL LQDDMITVAG RVHNKREAGN KLRFYDIQAE GVQIQIMCQI QDCKEGEDFG
     EMHDLIKRGD IVGVTGYPGV TSPRGREESG ELSVFCKQIT LLSPSLHMLP KAQPGLKSQE
     TRYRQRYLDL IMNNSTRDKF IMRSRIVQYV RRFLDARDFL EVETPMMNMI AGGATAKPFI
     THHNDLNMDL FMRVAPELYL KMLVVGGLDR VYEIGRQFRN EGIDLTHNPE FTTCEFYWAY
     ADVYDVMDLT EVMISELVKE VTGSYEIKYH PEGPEGPELN LNFARPWRRI DMLPYLSEKL
     GVQFPAAKDL QTPEANQFLK DLCKQNKIEC SPPHTSARLL DKLVGEYIES EGINPTFITG
     HPQMMSPLAK SHRDTPGICE RFEVFVATKE ICNAYTELND PFDQRLRFEE QAAQKDQGDD
     EAQLVDENFC TALEYGLPPT GGWGMGIDRM VMFLTDSNNI KEVLLFPAMK PSEQEVKSAS
     NTQ
//
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