ID   ASND1_YEAST             Reviewed;         525 AA.
AC   Q04489; D6W0I9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Asparagine synthetase domain-containing protein YML096W;
GN   OrderedLocusNames=YML096W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3750 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z46660; CAA86641.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09803.1; -; Genomic_DNA.
DR   PIR; S49630; S49630.
DR   RefSeq; NP_013613.1; NM_001182456.1.
DR   AlphaFoldDB; Q04489; -.
DR   SMR; Q04489; -.
DR   BioGRID; 35047; 65.
DR   STRING; 4932.YML096W; -.
DR   MaxQB; Q04489; -.
DR   PaxDb; Q04489; -.
DR   PRIDE; Q04489; -.
DR   EnsemblFungi; YML096W_mRNA; YML096W; YML096W.
DR   GeneID; 854877; -.
DR   KEGG; sce:YML096W; -.
DR   SGD; S000004562; YML096W.
DR   VEuPathDB; FungiDB:YML096W; -.
DR   eggNOG; KOG0573; Eukaryota.
DR   GeneTree; ENSGT00390000012446; -.
DR   HOGENOM; CLU_012368_2_0_1; -.
DR   InParanoid; Q04489; -.
DR   OMA; LEMDWQR; -.
DR   BioCyc; YEAST:G3O-32681-MON; -.
DR   PRO; PR:Q04489; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04489; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01991; Asn_Synthase_B_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Asparagine biosynthesis; Cytoplasm;
KW   Glutamine amidotransferase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..525
FT                   /note="Asparagine synthetase domain-containing protein
FT                   YML096W"
FT                   /id="PRO_0000056940"
FT   DOMAIN          2..209
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          210..523
FT                   /note="Asparagine synthetase"
FT   REGION          503..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   525 AA;  59469 MW;  862705A8C789AA6C CRC64;
     MCGILLHYCP NNNYLNDELI EFPEGTEFGD TTCTNESSIF NKIIPYIAAR GPNYSSLRAV
     KAYRISWFSS VLSLRQPFTK QSINVDDRYF LQFNGELYNK EISQGDNDSL YIASMLQNLK
     EGMGVIDVIK SLEGEYAYTI YDVNSSKLYF GRDPIGRRSL SYSVTPDNEL YVASVTGSAG
     SFQDCIGGVI YEYDTRTKLL NSNQRSHLPY EVTSEIDLNF TSLSEVSKNL YAVLRDSVKK
     RVESIHPRHI ENSPIAVLFS GGIDCSVIVA LICEVLQEND YKCGKPVIEL LNVSFENPRT
     GLFPSDTPDR KLSINSAKTL QNLYPNVDIK LVEVDVPYDE YLKWKPFVIN LMYPKQTEMD
     LSIAIAFFFA SRGRGFLTSL NGERTPYQRH GIVLFSGLGA DELYGGYHKF ANKPPHELVE
     ELTRQINNIY DRNLNRDDKV IAHNGVEVRY PFLDEYVIKL STAEIPINFK VNKLILRKVA
     SQYLKLDGIS SEPKRAIQFG AKSAKMTKDG NKHGTDLLKE NRNCS