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Database: UniProt
Entry: A0A395HE50_9EURO
LinkDB: A0A395HE50_9EURO
Original site: A0A395HE50_9EURO 
ID   A0A395HE50_9EURO        Unreviewed;       304 AA.
AC   A0A395HE50;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN   ORFNames=BO80DRAFT_370583 {ECO:0000313|EMBL:RAL06132.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL06132.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL06132.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL06132.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ824419; RAL06132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HE50; -.
DR   STRING; 1448316.A0A395HE50; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_370583; -.
DR   OrthoDB; 1947844at2759; -.
DR   Proteomes; UP000249402; Unassembled WGS sequence.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd14688; bZIP_YAP; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.10.238.100; YAP1 redox domain. Chain B; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR40621:SF8; AP-1-LIKE TRANSCRIPTION FACTOR YAP3; 1.
DR   PANTHER; PTHR40621; TRANSCRIPTION FACTOR KAPC-RELATED; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT   DOMAIN          121..184
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          12..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  33372 MW;  57CAE4182CE231DB CRC64;
     MDYSFYSNPH QQPYPLYGVH GLPTPDQSNP TPHAENLQGT FASLGAQHYQ SFDPNLRFQD
     PHAGASFVAP PHSPPESLTK HSVSSNDFAN QHLDQASLDG DDQLLDQNLG RSSSEEKDSL
     TPAQSKRKAQ NRAAQRAFRE RKERHVRELE EKVSNLENES TSLMADNERL KRELARFTTE
     NEILRATSTS LRHSNQHSAD PEPTTTGPMK YSPTDLSSDL GGGHAPAHRI TVCGKTGERL
     LDAGATWDLI QGHELFKRGL VNIGDVSGRL QGTAQCDGQG PAFRESQVLQ AIEESAASGN
     DDLL
//
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