ID   SYNC_ENCCU              Reviewed;         451 AA.
AC   Q8SQK8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Probable asparagine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
GN   OrderedLocusNames=ECU09_1680;
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-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC         asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC         Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
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; AL590451; CAD27140.2; -; Genomic_DNA.
DR   RefSeq; XP_955721.1; XM_950628.1.
DR   AlphaFoldDB; Q8SQK8; -.
DR   SMR; Q8SQK8; -.
DR   STRING; 284813.Q8SQK8; -.
DR   GeneID; 860507; -.
DR   KEGG; ecu:ECU09_1680; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_1680; -.
DR   HOGENOM; CLU_004553_2_10_1; -.
DR   InParanoid; Q8SQK8; -.
DR   OrthoDB; 1056670at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 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; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00457; asnS; 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..451
FT                   /note="Probable asparagine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388388"
SQ   SEQUENCE   451 AA;  52045 MW;  08591ABE16CC1503 CRC64;
     MSEKVEKEIG EQITKLDLSE YRSIELSKLS KENIGQKIRT FGWVANVRSQ STITFIELYA
     HYRTVKCVYQ KKMHLTMCTS MTVYGTVSKN FGKKDAHEFE IQVEGVEIYN GAIAPSFPLN
     EDSSVNAILT NGHLGLRTKK RQLFLKARGH LLKIIRDFYF EGEYTEVTPP TMVQTQVEGG
     STLFKLDYYG EDAYLTQSSQ LYLETVVPAS HRAYCIMPSY RAEKSRTRRH LSEYTHVEAE
     MADIDLDGLI SSIEALVSYS MRRFYEEMKS DILSVFPEFE FHKVPRTPFK RIKYSEAIEL
     LKSKGYKKED NTDFELGDDI PDAAERYLVE VVGDGCPVFL THFLVGHKPF YMRKDENDKG
     LTESTDLLFP GIGEILGGSM RQDTYEDLIE GFRRENINID PYYWYLDMAR FGPCKHGGYG
     LGFERFLMGL MRYESVDEAT LYPRKVSRCQ P