ID A0A2B7X096_9EURO Unreviewed; 663 AA.
AC A0A2B7X096;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN ORFNames=AJ79_07686 {ECO:0000313|EMBL:PGH02237.1};
OS Helicocarpus griseus UAMH5409.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH02237.1, ECO:0000313|Proteomes:UP000223968};
RN [1] {ECO:0000313|EMBL:PGH02237.1, ECO:0000313|Proteomes:UP000223968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH02237.1,
RC ECO:0000313|Proteomes:UP000223968};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC 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:PGH02237.1}.
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DR EMBL; PDNB01000161; PGH02237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7X096; -.
DR STRING; 1447875.A0A2B7X096; -.
DR OrthoDB; 1363150at2759; -.
DR Proteomes; UP000223968; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 InterPro; IPR013910; TF_PAP1.
DR InterPro; IPR023167; Yap1_redox_dom_sf.
DR PANTHER; PTHR40621:SF6; AP-1-LIKE TRANSCRIPTION FACTOR YAP1-RELATED; 1.
DR PANTHER; PTHR40621; TRANSCRIPTION FACTOR KAPC-RELATED; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF08601; PAP1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR SUPFAM; SSF111430; YAP1 redox domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000223968}.
FT DOMAIN 165..228
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 33..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 71931 MW; E4D9F9F488D0E5F5 CRC64;
MSDFDSLYQR SLYLSPEQQD LLLAALSSAD KSTKVSKNNF RGSPRVNYNM TDSLPKSTSP
QVINETDTSP HGFLESPSEQ ALGPNQLDFD GSPFLDFDFD VDFDANGAGE MIGDLAGTSS
AGDEGETGEK RKSIDGKDDE EESGKRRRET DDKTAKKPGR KPLTSEPTTK RKAQNRAAQR
AFRERKEKHL KDLETKVEEL EKASKSTSNE NKLLRAQVER LQVELKEYRK RLSWANTGNS
VSSMTGLGLR GSESRNNPRY SGNDFSFEFP KFGDLPGVHM FNNSAKASTN QPRTSEQPKS
NGALYRTSNI GNGNSFKGTA AGTQPSQYGL GKTSPAAPTP SSITSNDTVG SNGRNNNSDT
IDSPTAYYDN PVGLPSRNNT GLSYSGSGSG SISNYGSVHT GQQQTYQARH YGSSNVSNSN
SPSASSESQP CHISSNGTSP EPSLNSPPTG KLNEPGLNTT NGQKSGDGIE GEKTFYEKLG
RACGCAENPV PAALSDSNPS LQLPGRNHNS LAGDGILGFD WLAQQNGGQF DPVLFGDYRD
PQDAVLAQDF GTFFNDAFPL PDLGSPLQSL NDLNNNTAPK NDLMKQIDNN LEADDEEVVP
GEDRSQMLSC TKIWDRLQSM EKFRNGELDM DNLCSELRNK ARCSEGGVVV KEEDVEAIMK
RSK
//