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Database: UniProt
Entry: A0A177DFI3_ALTAL
LinkDB: A0A177DFI3_ALTAL
Original site: A0A177DFI3_ALTAL 
ID   A0A177DFI3_ALTAL        Unreviewed;       598 AA.
AC   A0A177DFI3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN   ORFNames=CC77DRAFT_193083 {ECO:0000313|EMBL:OAG18505.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG18505.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG18505.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG18505.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441483; OAG18505.1; -; Genomic_DNA.
DR   RefSeq; XP_018383926.1; XM_018530566.1.
DR   AlphaFoldDB; A0A177DFI3; -.
DR   GeneID; 29116160; -.
DR   KEGG; aalt:CC77DRAFT_193083; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_193083; -.
DR   OMA; PSHNYDM; -.
DR   OrthoDB; 1475660at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
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; PTHR40621:SF10; BZIP DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR40621; TRANSCRIPTION FACTOR KAPC-RELATED; 1.
DR   Pfam; PF00170; bZIP_1; 1.
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:UP000077248}.
FT   DOMAIN          292..355
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          33..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          317..344
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        33..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   598 AA;  66109 MW;  F14456BACF8BA169 CRC64;
     MATAVQPAMT MAPFNQHPNQ CVDPNEFFDF GQMPSPTQPA TLKRESSATS TMASPTSTNI
     DDDLQTPAKP SHEYERFKQQ TGLPTGSISG LNAGYNTGFP MFSSTGLDEM AMMGGDSMMD
     GAWNTGLPMD VGMNMGVDYR QNSFAFNDAS DDYVDPSAIT QEEVANVRVW PGMHQQQAAM
     AKAQAQAQQQ RAQQLAHQKQ QQAMQQQQQQ QQNRMPSTSS ASRKTSSPLS DAHTEEMITR
     VVAQIRADSQ NASASMQNDN QGLLPHIIRA KKDEEDMDED ERLLASEEGK KLSSKERRQL
     RNKVSARAFR SRRKEYIGQL EGEVAMKVNE ANELRAQNRL LMEENARSRA FIERLLRHQA
     FTPFLEELSR DESLQAKAPM TSMPSTSTPV ATAPAPAQFQ QQQQQFNGMS QAENTHVGMT
     MVPEPQLDFA MLNLNNNGNN GNNWGVNNGF SFQQPVAFAV TELPEGPSNP LDIKAMSGKG
     YSAILNAEDD SPVEEAKADY PVIERPVQSE PAAAIEETEE EEDAEYDLYY SSSTPSATAP
     IEDQEALFTN PEKAFARYSL IISDDANEAL LAERLERKIA AMSPVMQRIA DITSMLDS
//
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