ID A0A0P1BQ95_9BASI Unreviewed; 528 AA.
AC A0A0P1BQ95;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=PROTEIN CRH-2, ISOFORM B {ECO:0000313|EMBL:CEH19067.1};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH19067.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH19067.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the bZIP family.
CC {ECO:0000256|ARBA:ARBA00007163}.
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DR EMBL; CCYA01000277; CEH19067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BQ95; -.
DR STRING; 401625.A0A0P1BQ95; -.
DR OrthoDB; 5628742at2759; -.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR044280; Hac1/HY5.
DR PANTHER; PTHR46714; TRANSCRIPTIONAL ACTIVATOR HAC1; 1.
DR PANTHER; PTHR46714:SF6; TRANSCRIPTIONAL ACTIVATOR HAC1; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT DOMAIN 67..124
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 54921 MW; DFEDDFB8E27F7F66 CRC64;
MASTSPDLRS PAMFSASTLE ASPSPSASIS IASASASASA SASATSSSST KRKADSQGPK
PMDPARRARL EARQARNRTS AQISRNRKKA HVEMLEVEVE ELRKRNAELE ERAKDAEDTK
QRLKVLEQLV QALFSNSPVN DALRSTRSII DAPLGRAQSS TAQPLPQTCV PDGLVAPSSI
QLDSSPPFLT PSLHAAAPSS SSSTSSILPS LLAASPSSPS TFNVLLPSNT SMTSNLPSTI
FASSTLSTSS PTSSSSPCHS RTGAAPISPS SPSHALTAPS GGVSPCGSPA ADVRKEFDEM
DEDRESGDAK SRREKGEVHG SSLESGLAKG GCFDDEQTEK SSIVRGCAKQ TGWPGKVCGG
VGHDTAVGLH ETLFGSSEAH RLGCDAEEDE KDHFEIQAEG AQQAPDSSEE RMSEASTWKC
RSMQGQEETD RLLALLGLSP GAACGVDTST KTSTSAFGVL DADGYVDFSM NLDVDADALH
GLFGDAAHES RDGAFQLGSA MDLSERAAMQ DVCSGNELGL TLGSLASL
//
