ID   DAL81_YEAST             Reviewed;         970 AA.
AC   P21657; D6VVV4;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 3.
DT   08-NOV-2023, entry version 186.
DE   RecName: Full=Transcriptional activator protein DAL81;
DE   AltName: Full=Regulatory protein UGA35;
GN   Name=DAL81; Synonyms=DURL, UGA35; OrderedLocusNames=YIR023W;
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 [GENOMIC DNA].
RX   PubMed=1999281; DOI=10.1016/0378-1119(91)90048-g;
RA   Coornaert D., Vissers S., Andre B.;
RT   "The pleiotropic UGA35(DURL) regulatory gene of Saccharomyces cerevisiae:
RT   cloning, sequence and identity with the DAL81 gene.";
RL   Gene 97:163-171(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1990272; DOI=10.1128/mcb.11.2.1161-1166.1991;
RA   Bricmont P.A., Daugherty J.R., Cooper T.G.;
RT   "The DAL81 gene product is required for induced expression of two
RT   differently regulated nitrogen catabolic genes in Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 11:1161-1166(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [4]
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   [5]
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).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Positive regulation of genes required for catabolism of GABA
CC       (UGA4, UGA1, and UGA2), urea (DUR1 and DUR2), arginine and allantoin.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; M63498; AAA35192.1; -; Genomic_DNA.
DR   EMBL; M60415; AAA34557.1; -; Genomic_DNA.
DR   EMBL; Z38061; CAA86183.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08570.1; -; Genomic_DNA.
DR   PIR; S48485; S48485.
DR   RefSeq; NP_012289.3; NM_001179545.3.
DR   AlphaFoldDB; P21657; -.
DR   BioGRID; 35014; 582.
DR   DIP; DIP-5733N; -.
DR   IntAct; P21657; 5.
DR   MINT; P21657; -.
DR   STRING; 4932.YIR023W; -.
DR   iPTMnet; P21657; -.
DR   MaxQB; P21657; -.
DR   PaxDb; 4932-YIR023W; -.
DR   PeptideAtlas; P21657; -.
DR   EnsemblFungi; YIR023W_mRNA; YIR023W; YIR023W.
DR   GeneID; 854841; -.
DR   KEGG; sce:YIR023W; -.
DR   AGR; SGD:S000001462; -.
DR   SGD; S000001462; DAL81.
DR   VEuPathDB; FungiDB:YIR023W; -.
DR   eggNOG; ENOG502QQXX; Eukaryota.
DR   HOGENOM; CLU_006632_0_0_1; -.
DR   InParanoid; P21657; -.
DR   OMA; PSHIFAF; -.
DR   OrthoDB; 1360938at2759; -.
DR   BioCyc; YEAST:G3O-31442-MONOMER; -.
DR   BioGRID-ORCS; 854841; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P21657; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P21657; Protein.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR   GO; GO:1901717; P:positive regulation of gamma-aminobutyric acid catabolic process; IMP:SGD.
DR   GO; GO:1901714; P:positive regulation of urea catabolic process; IMP:SGD.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:SGD.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR31668; GLUCOSE TRANSPORT TRANSCRIPTION REGULATOR RGT1-RELATED-RELATED; 1.
DR   PANTHER; PTHR31668:SF4; TRANSCRIPTIONAL ACTIVATOR PROTEIN DAL81; 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..970
FT                   /note="Transcriptional activator protein DAL81"
FT                   /id="PRO_0000114947"
FT   DNA_BIND        150..179
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..970
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..935
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..970
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         833
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        77..82
FT                   /note="Missing (in Ref. 1; AAA35192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        465
FT                   /note="K -> R (in Ref. 1; AAA35192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="S -> L (in Ref. 1; AAA35192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        507
FT                   /note="D -> G (in Ref. 1; AAA35192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        760
FT                   /note="N -> S (in Ref. 1; AAA35192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        785
FT                   /note="T -> A (in Ref. 2; AAA34557)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   970 AA;  109174 MW;  9FEBD271A18AFC38 CRC64;
     MDPHQSPADN AASPTKSVKA TTKNSSTNNN VNSNNSNNNS NHDILNFNDN YTTILQHLAN
     DHPNILREKG GSQQQQHQQQ QQQQQQQQQQ QQQQSLDTLL HHYQSLLSKS DNAIAFDDNV
     SNSADHNGSN SNNNNNNNDI SSPGNLMGSC NQCRLKKTKC NYFPDLGNCL ECETSRTKCT
     FSIAPNYLKR TSSGANNNMP TSSNSKRMKN FEDYSNRLPS SMLYRHQQQQ QQQQQQQRIQ
     YPRSSFFVGP ASVFDLNLTK HVRLDNVDQI QLSKTLSLRK VSPTAQFILQ DDFDTTLHSK
     QEYEVDLVEN LVHPHGHLLV EIFFKLIHPF LPILHERVFL EKYSRSYREL TAPLLASIYS
     LALQYWDFHP ALLGFPKPDV TAQLNNIALE TFYARVGRPK LSIIQTGLLI LQCRSECHNN
     WVLCSSVVAL AEELGLGVEC NDWKLPKWEK DLRKRLAWAV WLMDKWCALN EGRQSHLILG
     RNWMIKLLNF DDFPLNSPTI LNSLQNDQSG SSPSSSNDVK NHQIAFGNLP IFNINPTLED
     FKNGTLMFQQ MVSLSIILGE IMDTFYTQGS MTINKSIEQV LKLAKPLQLK LREWYHSLPK
     NLSMSYATPQ KLNSNSTLTL AYFATEITLH RKIICALNPQ TPKELVQVCR TAARTRLVAA
     IEFIRDLKNE HINAFWYNCS TGNLMLIGTF AALLYVTSAT KEEAMIFRDY VRNYTWVLKI
     GSKYFDKLSN ALNNMHLLFA QIPGLLTDEP VVVSPNSNIN SVNPQRSGVQ SQIPIQFNVG
     SPAMTEQGSP LNQWKNLPQE ILQQLNSFPN GTTSTTTPVN PTSRQTQLES QGSPAINSAN
     NNSNNTPLPF APNKSSKKTS QSSPNVTPSH MSRHPPSNTS SPRVNSSTNV NSNTQMNASP
     LTSINETRQE SGDAADEKTA GRERTANEES STELKDDNPN SNQETSATGN QTIKMNDDKN
     VTINTRETPL
//