ID A0A364KSK3_9EURO Unreviewed; 595 AA.
AC A0A364KSK3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN ORFNames=BHQ10_002537 {ECO:0000313|EMBL:RAO66525.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO66525.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO66525.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO66525.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO66525.1}.
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DR EMBL; MIKG01000003; RAO66525.1; -; Genomic_DNA.
DR STRING; 1196081.A0A364KSK3; -.
DR OrthoDB; 1363150at2759; -.
DR Proteomes; UP000249363; 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:UP000249363}.
FT DOMAIN 163..226
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 24..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 64878 MW; C570FB50DD4AFBC8 CRC64;
MSDFNSLYQQ GLYLSPEQQV LLMAALNSNN PSQNQVENKK DAQNRSRTQS SSNDTSPSNS
NAFDPASSSY FESPLLQDAP GSGQLGFGTD ESPFLDFDPD VDFDFQGTDQ LIGDLPEFEN
HESGDKRKSF DGDEDDSSSG KKRRESDDKD KSAKKPGRKP LTSEPTTKRK AQNRAAQRAF
RERKEKHLKD LETKVDELEK ASQTANQENG LLRAQVERLQ VELKEYRKRI SWLSGGNGLS
TMAAMSNMNS RNLSNLNNND FYFDFPKFGD LPGKHMFSNG GQNKQKSSTP STTAVSPTAQ
VPENGRNSLN SKNLSKAAKA NGMTNGQTYQ SRASASSAAS NTDSPSASSD SQHGQSSSIG
TSPEPSLNSP NVGKMGDNSF EFYGNEAATN YGTIDGEKSF CEKLGMACGN INNPMPAALN
KNNDNPQLLG QLQPAAADQS LSFDWLAQQN GGSFXPVLFN DXREPQDAIL SQDFGAFFND
AFPLPDLDSP FGDANDVTTS PKDSVAAKKG PAQAGRKQDD EEEVVPGEDK AQIMSCTNIW
DRLQSMEKFR NGEIDIDSLC TELRTKARCS EGGVVVFRKD VDDIVGRAGN EMQSH
//
