ID A0A428QYN8_9HYPO Unreviewed; 581 AA.
AC A0A428QYN8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN ORFNames=CEP54_001869 {ECO:0000313|EMBL:RSL70328.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL70328.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL70328.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL70328.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-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:RSL70328.1}.
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DR EMBL; NKCI01000010; RSL70328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428QYN8; -.
DR STRING; 1325734.A0A428QYN8; -.
DR Proteomes; UP000288168; 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; 2.
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:UP000288168}.
FT DOMAIN 157..220
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 46..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 62843 MW; BAEFE7467BB214A5 CRC64;
MASAGTGGSL PPNFLLTPQQ QNLLFAALNS NKQQVSATPA NNALSLSPTS FHNSAAQPKG
TTNSAYQESP FLDNYDYDFG DSSFDFSFAT DDQPSMIGDI PSAAAATSKS DSTENEGTEK
RSHPDDEDEE ASPGKDPKRR ESTEKVPKKP GRKPLTSEPS SKRKAQNRAA QRAFRERKEK
HLKDLETKVE ELEKASQAAN HENGLLRAQV ERMTSELNQY KQKVSLMTNS KALPREKVPF
GNAAVSNLGD VNFQFEFPKF GMLPGPPVNK PQRSGSSPTS PLQKTYPSPS NFSNDSRSPQ
SQFKDDLAKF SGVFSPSMSS SATNPSRASV DSAGYSANGA TSSPSASSHS NTGPSSSCGT
SPEPFTQSPM GFKPVDTMTT IGEEQSSHAT TDHFSNVDLS STNFDWLAQQ NGGQFDPQLF
GDYREPQDNV LSNPGFDDFF NDALDTDFFV PYNMAPTSPA AKINAQPKKA PNLIDQIDAQ
QNSIDDEPLK KQNMNCNQLW EKLQACPKAQ NGEFDLDGLC SELTKKAKCS GTGPVVAETD
FDTILKKYMG KDVSSSCVAH TLGVEIEADK TKADKHLGLS A
//
