ID   CPCA_ASPNG              Reviewed;         245 AA.
AC   Q00096;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Cross-pathway control protein A {ECO:0000303|PubMed:14648200};
GN   Name=cpcA {ECO:0000303|PubMed:14648200};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9089 / N402;
RX   PubMed=9004217; DOI=10.1046/j.1365-2958.1997.1741549.x;
RA   Wanke C., Eckert S., Albrecht G., van Hartingsveldt W., Punt P.J.,
RA   van den Hondel C.A.M.J.J., Braus G.H.;
RT   "The Aspergillus niger GCN4 homologue, cpcA, is transcriptionally regulated
RT   and encodes an unusual leucine zipper.";
RL   Mol. Microbiol. 23:23-33(1997).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14648200; DOI=10.1007/s00438-003-0955-7;
RA   Pries R., Boemeke K., Draht O., Kuenzler M., Braus G.H.;
RT   "Nuclear import of yeast Gcn4p requires karyopherins Srp1p and Kap95p.";
RL   Mol. Genet. Genomics 271:257-266(2004).
CC   -!- FUNCTION: Master transcriptional regulator that mediates the response
CC       to amino acid starvation (By similarity). Binds variations of the DNA
CC       sequence 5'-ATGA[CG]TCAT-3' (By similarity).
CC       {ECO:0000250|UniProtKB:P03069}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P03069}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14648200}.
CC   -!- DOMAIN: The leucine-zipper is atypical but could still mediate protein-
CC       protein interaction. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily. {ECO:0000305}.
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DR   EMBL; X99215; CAA67605.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00096; -.
DR   SMR; Q00096; -.
DR   STRING; 5061.CADANGAP00000766; -.
DR   VEuPathDB; FungiDB:An01g07900; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1171387; -.
DR   VEuPathDB; FungiDB:ATCC64974_17040; -.
DR   VEuPathDB; FungiDB:M747DRAFT_307851; -.
DR   eggNOG; KOG0837; Eukaryota.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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   SUPFAM; SSF57959; SSF57959; 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..245
FT                   /note="Cross-pathway control protein A"
FT                   /id="PRO_0000076486"
FT   DOMAIN          187..245
FT                   /note="bZIP"
FT   REGION          19..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..211
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03069"
FT   REGION          222..243
FT                   /note="Leucine-zipper (atypical)"
FT                   /evidence="ECO:0000250|UniProtKB:P03069"
FT   MOTIF           193..211
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:14648200"
FT   COMPBIAS        20..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   245 AA;  26812 MW;  D8CBBB5C18E51323 CRC64;
     MSTPNIAQDF PELFDLQSNR FGDDLSSPES NMLSPQINTS FFSPMGEVAP PGTVSPKDLF
     FDASAPPSTT FTDLSTPPLD TPGFFSQNTS PMINTEMDLN AVPEEWESLF PQDGFSLDLD
     SAALELAASL QQPKATGPPP TPVIRASASP APSASPAPSR QGTKHSTVAG VNARQRKPLP
     PIKFDSADPA AMKRARNTEA ARKSRARKLE RQGEMERRIE ELERMLEESK QREEYWRSMA
     KTGTN