ID   SYNC_SACPA              Reviewed;          87 AA.
AC   P41908;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Asparagine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
DE   Flags: Fragment;
GN   Name=DED81;
OS   Saccharomyces paradoxus (Yeast) (Saccharomyces douglasii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=27291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8017101; DOI=10.1002/yea.320100304;
RA   Adjiri A., Chanet R., Mezard C., Fabre F.;
RT   "Sequence comparison of the ARG4 chromosomal regions from the two related
RT   yeasts, Saccharomyces cerevisiae and Saccharomyces douglasii.";
RL   Yeast 10:309-317(1994).
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.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X73886; CAA52090.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41908; -.
DR   SMR; P41908; -.
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:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; SSF55681; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           <1..87
FT                   /note="Asparagine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000176500"
FT   NON_TER         1
SQ   SEQUENCE   87 AA;  9934 MW;  98174AB082C64E78 CRC64;
     VDVLMPNVGE ITGGSMRIDD MNELMAGFKR EGIDTDAYYW FIDQRKYGTC PHGGYGIGTE
     RILAWLCDRF TVRDCSLYPR FSGRCKP