ID A0A319APD8_ASPLB Unreviewed; 616 AA.
AC A0A319APD8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE SubName: Full=BZIP transcription factor {ECO:0000313|EMBL:PYH62076.1};
GN ORFNames=BO96DRAFT_323449 {ECO:0000313|EMBL:PYH62076.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH62076.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH62076.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH62076.1,
RC ECO:0000313|Proteomes:UP000247441};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ821338; PYH62076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319APD8; -.
DR OrthoDB; 1363150at2759; -.
DR Proteomes; UP000247441; 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 Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 180..239
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 24..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..242
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 24..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 66820 MW; 146C0C0E60F6D208 CRC64;
MADYNPLYQH GLYLSPDQQD LLLAALSSNN PPAKQQNNSH PPASKSDPES TPGTTGSYNM
SPAFDPSNPH SGGLGYGDDE SPFLDFNPEL DFDFQGSENL IGDIPDSLPQ SEEPEPGEKR
KDIDGDADEN EASGKKRRES DEKAAKKPGR KPLTSEPTSV RILGYRDVGA EGIVVLTNLQ
KRKAQNRAAQ RAFRERKEKH LKDLETKVDE LQKASDNANQ ENGLLRAQID RLQVELREYR
KRLSWLTTGT GVSAMNAIPG AYPNSKGSYG LQNNDFMFDF PKFGDLPGSH IFNNGQLSKT
QQSAKGEPST ATPRNDSRVP GVVSRNSLSS SQSNGVPAGR TPNSVSQQGS TPASTRKSTP
KVSIYNGTAH STSTHDSSTT DSPSSSSDSH QSQSLSSNGT SPEPTINSPA TKAHHNHGAH
DGCTYTTIDG EESFCAQLGM ACGNINNPIP AVRHNSQSAS NTPSQEAPHE DVAGLDMLAQ
QNGGQFDPVL FGDWREPQDA ILSQDFGTFF DDAFPLPDLG SPSHNLTEAA TQQPPKKDLI
AEIDSKLDEE VVPGEDKSQM LSCTKIWDRL QSMERFRNGE LDVDHLCSEL RMKARCSEGG
VVVNQQDVDD IMGRAK
//
