ID   A0A1V6Z3U1_PENNA        Unreviewed;       266 AA.
AC   A0A1V6Z3U1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN   ORFNames=PENNAL_c0004G04647 {ECO:0000313|EMBL:OQE94164.1};
OS   Penicillium nalgiovense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE94164.1, ECO:0000313|Proteomes:UP000191691};
RN   [1] {ECO:0000313|Proteomes:UP000191691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQE94164.1}.
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DR   EMBL; MOOB01000004; OQE94164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6Z3U1; -.
DR   STRING; 60175.A0A1V6Z3U1; -.
DR   OMA; SALWAEP; -.
DR   OrthoDB; 1837724at2759; -.
DR   Proteomes; UP000191691; 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:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR13044; ACTIVATING TRANSCRIPTION FACTOR ATF 4/5; 1.
DR   PANTHER; PTHR13044:SF38; BZIP TRANSCRIPTION FACTOR JLBA_IDI-4; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191691};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          199..262
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          217..251
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  29236 MW;  2655AC8CFB2A16E5 CRC64;
     MSRGEQPIIN QSYETYSPRQ RSRPPPTGSN PPSTGTQERH QGPAEYSPWA SLHPYSDNDL
     FSSLAPPLEG FPSAVPVCQS FDTLTHESAL WAEPDLSLAG TDWNFISVNH STPYPPDYDG
     GDVSVMDPGY GSVSAFNSLS DSGSIEHQNY VSASLDPSSA NSLDGHSHPS PISPFPAPVS
     TSLSSPSTSQ GDDTLSRVDS SRVEKRKLNT LAARRCRQRR VDRMKELEAE LEKVRKERDD
     WRLRCSKLEG ETDALKGLLT RKSQDT
//