ID   SYKC_ENTBH              Reviewed;         518 AA.
AC   A9CS74;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Probable lysine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   ORFNames=EBI_25548;
OS   Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC   Enterocytozoon.
OX   NCBI_TaxID=481877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA   Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA   Keeling P.J.;
RT   "Patterns of genome evolution among the microsporidian parasites
RT   Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT   bieneusi.";
RL   PLoS ONE 2:E1277-E1277(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA   Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA   Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT   "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT   Enterocytozoon bieneusi.";
RL   PLoS Pathog. 5:E1000261-E1000261(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; ABGB01000002; EDQ31218.1; -; Genomic_DNA.
DR   RefSeq; XP_001828066.1; XM_001828014.1.
DR   AlphaFoldDB; A9CS74; -.
DR   SMR; A9CS74; -.
DR   STRING; 481877.A9CS74; -.
DR   EnsemblFungi; EDQ31218; EDQ31218; EBI_25548.
DR   VEuPathDB; MicrosporidiaDB:EBI_25548; -.
DR   HOGENOM; CLU_008255_6_0_1; -.
DR   InParanoid; A9CS74; -.
DR   Proteomes; UP000001742; Unassembled WGS sequence.
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..518
FT                   /note="Probable lysine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388395"
SQ   SEQUENCE   518 AA;  59508 MW;  5C7E270F6D80B097 CRC64;
     MSKSHNDKEE SPDNYYFQRR EQMQELQSLG INVYPHKFYF NNTFQDVFTA AETCSSNEKT
     NISVELVGRV IRARIHSMTN FYDVKKDNDE LQIVYNKNLQ GKENPIAIKI VDCIRRGDII
     GFKGIVGRTK TGEISVFAHE IQILSPCLRA FPSEKNLITN PELIYRHRHI DLLVNQDSRN
     RFITRSKIIQ HIREYFNKIG FLEVETPIMN NKVGGASARP FLTHHNELKI DLYLRVAPEL
     FLKQLVVGGL ERVFEIGKNF RNEGIDLTHN PEFTAIEFYM AYADYNDLMC IVEELLSGLV
     KLIKGSSKFI YQPCKRETID EIKVPLDFST PFKRIDILEE LNKSLNIELT GENIEKPETL
     ELLIKKAEEL NIIVNNPKTL NRMLDAFIGE YIEPQCINPT FVTGFPICMS PLAKDHRSKA
     GITERFEMFC NGKELVNAYT ELNIPDLQRK RFLMQDADAN AGDDEAMPND EDFCQVLEYG
     LPPTGGCGIG IDRLVMYLTD AANIRDVILF PTLKPEQK