ID   SYNC_DEBHA              Reviewed;         552 AA.
AC   Q6BU46;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Asparagine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
GN   Name=DED81; OrderedLocusNames=DEHA2C13684g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382135; CAG86350.1; -; Genomic_DNA.
DR   RefSeq; XP_458273.1; XM_458273.1.
DR   AlphaFoldDB; Q6BU46; -.
DR   SMR; Q6BU46; -.
DR   STRING; 4959.XP_458273.1; -.
DR   EnsemblFungi; CAG86350; CAG86350; DEHA2C13684g.
DR   GeneID; 2900062; -.
DR   KEGG; dha:DEHA2C13684g; -.
DR   eggNOG; KOG0555; Eukaryota.
DR   HOGENOM; CLU_004553_2_10_1; -.
DR   InParanoid; Q6BU46; -.
DR   OMA; CKQHTVR; -.
DR   OrthoDB; 1056670at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
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:0003676; F:nucleic acid binding; IEA:InterPro.
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   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 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..552
FT                   /note="Asparagine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000176498"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  62236 MW;  926B1E81A92DCFD9 CRC64;
     MSQVYVNEKT GADSTDVSGS EQQPFQTPAF ALFKNEDAKI LVYKQLEDSE EFGYGEISAS
     ALKKAKKGAE GLKKKQEKQA KLQEEQRKHQ DDAAKKFAEM DLISIKEDES LPQAKKIKLR
     TVQDNIGTRV VVQGWIHRLR LQKGLGFITL RDGTGFIQCI LTGDLAKCKT THELTLESTV
     TIKGVINKLP EGKSAPGGVE LKVDYYEVVG LAPSGEEAFS NKVQENADPS LLLDQRHLAL
     RGESLSAVMK VRSTLLQAIR RFFAEEGLLE VTPPCMVQTQ VEGGSTLFKM DYYGEEAYLT
     QSSQLYLETC LPALGDVFCV QESFRAEKSH TRRHLSEYTH IESELGFIEF DDLLTHLERL
     ITYVVKYVVE DPVAGPLIKQ LNPNFVPPQM PFKRMEYIHA LDWLNEHGIP NEDGEKFKFG
     DDIAEAAERK MTDTIGVPIL LIRFPVEIKS FYMQKCADDP RVTESVDVLM PTVGEITGGS
     MRTYDNDELV AAIKREGLDL DSYYWFTDQR KYGTCPHGGY GLGTERILAW LCDRFTVRDC
     SLYPRFTGRC KP