ID   CPC1_CRYPA              Reviewed;         247 AA.
AC   P87090;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Cross-pathway control protein 1;
GN   Name=CPC-1;
OS   Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC   Cryphonectria-Endothia species complex; Cryphonectria.
OX   NCBI_TaxID=5116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 38755 / EP155;
RX   PubMed=9501479; DOI=10.1006/fgbi.1997.1023;
RA   Wang P., Larson T.G., Chen C.H., Pawlyk D.M., Clark J.A., Nuss D.L.;
RT   "Cloning and characterization of a general amino acid control
RT   transcriptional activator from the chestnut blight fungus Cryphonectria
RT   parasitica.";
RL   Fungal Genet. Biol. 23:81-94(1998).
CC   -!- FUNCTION: General amino acid control transactivator. Binds to the AP-1
CC       consensus DNA binding element 5'-[AG]TGACTCAT-3'.
CC   -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily. {ECO:0000305}.
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DR   EMBL; U96134; AAC16255.1; -; Genomic_DNA.
DR   AlphaFoldDB; P87090; -.
DR   SMR; P87090; -.
DR   PHI-base; PHI:467; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   Activator; Amino-acid biosynthesis; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..247
FT                   /note="Cross-pathway control protein 1"
FT                   /id="PRO_0000076487"
FT   DOMAIN          186..247
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          107..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..210
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          214..228
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        148..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  26156 MW;  87D74040A31F5697 CRC64;
     MELDIDLPDF GPFEGGAPVS EFSSPDNPVF GLDLSGSLHS SVMSVSPTEL LLTENLMSAP
     GSTALTHLTT PSGYDTSPAF TEDWNASPLF AQNDFETAQE WPSLFPDAET SAAPAPALAA
     PAPVPAAQAE DSPSVDSEDF EPARRPSQAR KSSASSSPSG RHSSVSGVSA RRRGKPLPPI
     TIDDPSDTVG MKRAKNTLAA RKSRARKAER MDELERQVRE LEAEKEKLAA ELAHWKSLAS
     SQGAAGQ