ID   SYNC_NOSCE              Reviewed;         447 AA.
AC   C4V847;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Probable asparagine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
GN   ORFNames=NCER_100652;
OS   Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRL01;
RX   PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA   Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA   Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT   "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT   pathogen of honey bees.";
RL   PLoS Pathog. 5:E1000466-E1000466(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; ACOL01000040; EEQ82596.1; -; Genomic_DNA.
DR   RefSeq; XP_002996267.1; XM_002996221.1.
DR   AlphaFoldDB; C4V847; -.
DR   SMR; C4V847; -.
DR   STRING; 578460.C4V847; -.
DR   PRIDE; C4V847; -.
DR   EnsemblFungi; EEQ82596; EEQ82596; NCER_100652.
DR   KEGG; nce:NCER_100652; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_100652; -.
DR   HOGENOM; CLU_004553_2_0_1; -.
DR   InParanoid; C4V847; -.
DR   OMA; CKQHTVR; -.
DR   Proteomes; UP000009082; Unassembled WGS sequence.
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..447
FT                   /note="Probable asparagine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388390"
SQ   SEQUENCE   447 AA;  51927 MW;  96D0163975BEE422 CRC64;
     MVYEEVSLKN LKIKNDYKSI ELSEISKSDM HKRIKTFGWV DCCRTGKSIT FFDLTCQFKS
     IKCVYEKKID LTKCTSLTIY GTIQENKSKK ENAEFEVLVE KLEIFNDAIA PSFPLNKESS
     FDTMMKYGHL ALRNKQRGFF LKARSSLLKI IRDIFYEGNF IEITPPTIVQ TQVEGGSTLF
     KLKYYDKDAY LTQSSQLYLE TVAPVAYRAY CIASSYRAEK SNTTRHLSEY THVEAELANI
     EFEDLINNIE HLVTESIKRF YDLLGDEIKD LYPEIKLQNV PKRPFKRIRY VDAIKFLNDE
     GVKKDDDTDF VVGDDIPDSR EKIICERFGK GEPVLMTHFL VEHKPFYMKL DSSNETCTES
     FDLLYPGIGE IVGGSMRLDN YNKLIDGFKR EGLNPEDYDW YLDMARFGPC SHGGYGLGFE
     RLLMALMRYT NIEFATLYPR NTRRCHP