ID   ERT1_YEAS1              Reviewed;         529 AA.
AC   B3LMS3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Transcription activator of gluconeogenesis;
DE   AltName: Full=Ethanol regulator of translation 1;
GN   Name=ERT1; ORFNames=SCRG_02731;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor which regulates nonfermentable carbon
CC       utilization. Activator of gluconeogenetic genes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- SIMILARITY: Belongs to the ERT1/acuK family. {ECO:0000305}.
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DR   EMBL; CH408048; EDV11876.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LMS3; -.
DR   PRIDE; B3LMS3; -.
DR   EnsemblFungi; EDV11876; EDV11876; SCRG_02731.
DR   HOGENOM; CLU_010748_2_3_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   CDD; cd00067; GAL4; 1.
DR   CDD; cd00130; PAS; 1.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Gluconeogenesis; Metal-binding; Nucleus;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..529
FT                   /note="Transcription activator of gluconeogenesis"
FT                   /id="PRO_0000406473"
FT   DOMAIN          408..480
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DNA_BIND        40..68
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  60302 MW;  A096903DD1A53E43 CRC64;
     MCTPDENDYK TSTDPDTSAN TNHTLEKKKR KKRKNTNVAC VNCSRLHVSC EAKRPCLRCI
     SKGLTATCVD APRKKSKYLA GIPNRELPMS IQPDLPPRKI MIPIYNNSSN SSLNVNNMGE
     QQKFTSPQHI VHKAKFLSNA ADSEYSILSN IIYQDTLSNK IPIDILYSNT NSTSNSTIGN
     SSNNSPMVTN TSPEETEMEK IRQLYSEQRA NMPPHPYPSS NQNVYSILLG PNSAKIVASQ
     VNLFANHFPL VPVDSADNSL NFKRLLPRDP SEKSSQINWD SSINQYYLNS ETVTFPELAI
     PLKRRKNHLV SVSLESCSPD AANIKSNVGW EHSLRYSTPM EIYTSINAPF SHTPGFHHLL
     VYLKHRFNQQ DLVKMCRSIA EFRPIFIACS VTLTEEDMIF MEQCYQRTLL EYVKFIAQIG
     TPTCIWRRNG QISYVNEEFE ILCGWTREEL LNKMTFIVEI MDDESVRDYF KTLSKVAYRD
     FRGSEKMKVC RLLSPIKGKI IHCCCMWTLK RDVSGLPLMI LGNFMPILN