ID A0A316ZF22_9BASI Unreviewed; 458 AA.
AC A0A316ZF22;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN ORFNames=FA09DRAFT_325229 {ECO:0000313|EMBL:PWN98945.1};
OS Tilletiopsis washingtonensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC Tilletiopsis.
OX NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN98945.1, ECO:0000313|Proteomes:UP000245946};
RN [1] {ECO:0000313|EMBL:PWN98945.1, ECO:0000313|Proteomes:UP000245946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN98945.1,
RC ECO:0000313|Proteomes:UP000245946};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the bZIP family.
CC {ECO:0000256|ARBA:ARBA00007163}.
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DR EMBL; KZ819290; PWN98945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316ZF22; -.
DR STRING; 58919.A0A316ZF22; -.
DR OrthoDB; 1475660at2759; -.
DR Proteomes; UP000245946; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd14810; bZIP_u1; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR47416:SF8; BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTOR E-RELATED; 1.
DR PANTHER; PTHR47416; BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTOR F-RELATED; 1.
DR Pfam; PF07716; bZIP_2; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245946};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 297..360
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 34..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 336..363
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 226..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 47132 MW; C1902E057670E034 CRC64;
MASVDVAVPA APSSPAPWAA LSFDDFLTFP APSPAPTPAA LPSAPPAAAA AAAAAPAPAP
SPRRSAAVAP SSAATVQVAG TPPGATGPPP PPGSAPEVLF RYYLAAELRR IGSSADDHII
EKYVAQHYSS ISKKAAAPVA SSSSTASAAH APVAQPTLNY EPYRRAPSPP APSFAHAQAF
RDATPPSPEA FLDPHSLVLP PPALATLPQQ SSTVGVHEPF TVTRAPIVPS SNASGSYSKS
RRAADAMSED SSDGGQSEDD DEDDKASFAH LGSNTGGRGT LSAAAMLRPS PEEYRKLSSK
EKRQLRNKIS ARNFRTRRKE HITALESELS DRDSIIAGLR AQLSQLSVAN ASLTEEVRTL
KRTQLSATDV SRILEALQKS TGVALPAGAA PASDDQAMFA SSSNPASRPS TPTSPRPGLR
RNESSLLNTR KDVGPAAASK SFWGGRSAAQ GSALVAAS
//
