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Database: UniProt
Entry: A0A0B7N5M0_9FUNG
LinkDB: A0A0B7N5M0_9FUNG
Original site: A0A0B7N5M0_9FUNG 
ID   A0A0B7N5M0_9FUNG        Unreviewed;       338 AA.
AC   A0A0B7N5M0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN   Name=PARPA_07743.1 scaffold 30360 {ECO:0000313|EMBL:CEP13628.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP13628.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP13628.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP13628.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LN730358; CEP13628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7N5M0; -.
DR   STRING; 35722.A0A0B7N5M0; -.
DR   OrthoDB; 1361169at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd14687; bZIP_ATF2; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR19304; CYCLIC-AMP RESPONSE ELEMENT BINDING PROTEIN; 1.
DR   PANTHER; PTHR19304:SF43; TRANSCRIPTION FACTOR ATF1-RELATED; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT   DOMAIN          219..282
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          244..278
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  37629 MW;  01D4E42CA99EC8EE CRC64;
     MISSNSVIAD TNSRPLQPGK DSMLPVYPMI SDRHSQDGSL IIGKASVPDL LAENSYSDNP
     SGPSSTEEAV FPPTYAALPT TKLEEEPNPF EQSFESLEKS KIQLRKHNKA QLMETSYASN
     QNEWDSKSES IILPPSMLSR PTKTNTMVYG STASTFNNAS ILINQMTYTG SQQKRMRQPS
     ATNSCCSEDS SFIISTPSKP TNKKSRKPKK SSMEQPEDEE KRKNFLERNR IAALKCRQRK
     KQWLQNLQTK VECLGADNEQ FQMQANALRD EVIRLKTLLM IHKDCPINPS DVQAALSRPI
     PGIFDPSNSP HSSLLRSTTA PSMSPPPFSS SNDRNTLV
//
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