ID   SYKC_ENCCU              Reviewed;         510 AA.
AC   Q8SS56;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Probable lysine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   OrderedLocusNames=ECU04_0580;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590444; CAD25246.2; -; Genomic_DNA.
DR   RefSeq; NP_584742.1; NM_001041092.1.
DR   AlphaFoldDB; Q8SS56; -.
DR   SMR; Q8SS56; -.
DR   STRING; 284813.Q8SS56; -.
DR   GeneID; 858889; -.
DR   KEGG; ecu:ECU04_0580; -.
DR   VEuPathDB; MicrosporidiaDB:ECU04_0580; -.
DR   HOGENOM; CLU_008255_6_0_1; -.
DR   InParanoid; Q8SS56; -.
DR   OrthoDB; 837479at2759; -.
DR   Proteomes; UP000000819; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 1.
DR   Gene3D; 3.30.930.10; -; 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   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PIRSF; PIRSF039101; LysRS2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..510
FT                   /note="Probable lysine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388394"
SQ   SEQUENCE   510 AA;  58603 MW;  74B7DAF89CD438A3 CRC64;
     MVKHDSEVEL SEEDFYMQRV SMVRKEMKEG ASMYPHKFQI SHSFQEILQE IEKTSTQFVG
     EDVVRSAGRI MSMRLHARFC FFVVTSNGES LQVVVDTKEA GREQMAKFLR RGDVVGFTGN
     PGRTRTLEAS VFATDIIVLT PCLRTIPTEH FGLKDPETIY RKRYMDLLIN RESRNRFQKR
     AQIIGYIRSF LDSRGFLEVE TPMMNLIPGG AAAKPFITHH NELKLDLYMR VSPELYLKKL
     VVGGLERVYE IGKQFRNEGI DLTHNPEFTS CEFYMAYADY NDLMEMTEEL ISGMVENMFG
     TDTIVYSPKK REERTESVEL SFKRPFRVIS ILEELNARLG LDLSGETLDR EETLEKLLSA
     CDKEGLSVEK PRTLSRVLDK LIGHVIEPQC VNPTFVKDHP IAMSPLAKNH RSKAGLTERF
     ELFINCKEIC NAYTELNNPF EQRERFLQQT QDLNAGDDEA MMNDEDFCTA LEYGLPPTGG
     WGIGIDRLVM YLTDAANIRD VIFFPTMKPE