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Database: UniProt
Entry: A0A2V5I2G3_9EURO
LinkDB: A0A2V5I2G3_9EURO
Original site: A0A2V5I2G3_9EURO 
ID   A0A2V5I2G3_9EURO        Unreviewed;       362 AA.
AC   A0A2V5I2G3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN   ORFNames=BP00DRAFT_271941 {ECO:0000313|EMBL:PYI28143.1};
OS   Aspergillus indologenus CBS 114.80.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI28143.1, ECO:0000313|Proteomes:UP000248817};
RN   [1] {ECO:0000313|EMBL:PYI28143.1, ECO:0000313|Proteomes:UP000248817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI28143.1,
RC   ECO:0000313|Proteomes:UP000248817};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ825554; PYI28143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5I2G3; -.
DR   Proteomes; UP000248817; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd14687; bZIP_ATF2; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR002112; Leuzip_Jun.
DR   PANTHER; PTHR19304:SF5; ACTIVATING TRANSCRIPTION FACTOR-2; 1.
DR   PANTHER; PTHR19304; CYCLIC-AMP RESPONSE ELEMENT BINDING PROTEIN; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00043; LEUZIPPRJUN.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   4: Predicted;
FT   DOMAIN          203..266
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          50..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..362
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  39772 MW;  8E6B7F7843762A6E CRC64;
     MSVNLDHASM PGAPSKSEIT WTGPMPFFLD STISSEFLTM PLFDGMQEWS MSGSSPGAAA
     AAASGRFDGF QQPPQQQQKP AHPSPLSQQQ QSFMNAYLEP NLFSPDQPMP PHVHQHPHPH
     PHLAPKEPLL DPIMHPFAAS TTSSYPVPMH EITSRGSISD QSHRSSYGSI SSSDSSSSRA
     TGYTAARRPS EAVFSPTHDA VEQQKRERFL ERNRVAANKC RRKKKEHTRQ LESRCMEVTH
     ANSRLESEVS QLRSQILELK NELLRHSGCD DPAIKAHLAR MVAHLSQRSA SVSGASEASA
     KEDGAPPGRS SRSTPLSPAH QSDAEPEVEP EAAFGFDDML HLGDSKADEQ EEEEEVRMQE
     SP
//
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