ID   ATFB_ASPFN              Reviewed;         318 AA.
AC   B8NLU5;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Basic leucine zipper (bZIP) transcription factor atfB {ECO:0000303|PubMed:28830793};
GN   Name=atfB {ECO:0000303|PubMed:28830793}; ORFNames=AFLA_094010;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   INDUCTION, FUNCTION, AND DNA-BINDING.
RX   PubMed=24951443; DOI=10.1128/ec.00099-14;
RA   Baidya S., Duran R.M., Lohmar J.M., Harris-Coward P.Y., Cary J.W.,
RA   Hong S.Y., Roze L.V., Linz J.E., Calvo A.M.;
RT   "VeA is associated with the response to oxidative stress in the aflatoxin
RT   producer Aspergillus flavus.";
RL   Eukaryot. Cell 13:1095-1103(2014).
RN   [3]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=28830793; DOI=10.1016/j.fgb.2017.08.005;
RA   Caceres I., El Khoury R., Bailly S., Oswald I.P., Puel O., Bailly J.D.;
RT   "Piperine inhibits aflatoxin B1 production in Aspergillus flavus by
RT   modulating fungal oxidative stress response.";
RL   Fungal Genet. Biol. 107:77-85(2017).
CC   -!- FUNCTION: Transcription factor that acts as a key player in the
CC       regulatory circuit that integrates secondary metabolism and cellular
CC       response to oxidative stress (By similarity). Regulates the genes
CC       involved in development and stress response through direct binding to
CC       their promoters (PubMed:24951443, PubMed:28830793).
CC       {ECO:0000250|UniProtKB:A0A0F0IP79, ECO:0000269|PubMed:24951443,
CC       ECO:0000305|PubMed:28830793}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- INDUCTION: Expression is positively regulated by the developmental and
CC       secondary metabolism regulator veA (PubMed:24951443). Expression is
CC       highly increased following piperine exposure (PubMed:28830793).
CC       {ECO:0000269|PubMed:24951443, ECO:0000269|PubMed:28830793}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR   EMBL; EQ963480; EED49320.1; -; Genomic_DNA.
DR   RefSeq; XP_002381221.1; XM_002381180.1.
DR   AlphaFoldDB; B8NLU5; -.
DR   SMR; B8NLU5; -.
DR   STRING; 5059.CADAFLAP00009086; -.
DR   EnsemblFungi; EED49320; EED49320; AFLA_094010.
DR   VEuPathDB; FungiDB:AFLA_094010; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_888511_0_0_1; -.
DR   OMA; HAQCGDE; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Stress response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..318
FT                   /note="Basic leucine zipper (bZIP) transcription factor
FT                   atfB"
FT                   /id="PRO_0000444005"
FT   DOMAIN          160..223
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          114..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..199
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          202..216
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          275..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   318 AA;  35914 MW;  52A8A1AA8C7E7FDA CRC64;
     MSVDQTLYSR TPAAMADPTC AGPAAFTAAG AFSQPDLMAF SLREEEPIWG FDTIAPSMAS
     WQGKMEQQTF CNPNMERGLK NTHVRNGQPT PPPFDDKKLQ TPMGEMYPVA QYAFNSSPPE
     YAPPKHRSSL SEQSQTDGYG VSTRRRKASA IDQCEQQQER EKREKFLERN RLAASKCRQK
     KKEHTKLLET RFREVSNKKG ELESEIEHLR SEVLNLKNEM LRHAQCGDEA IKIHLAQMVR
     LITSKDTPNR DLVSPMRSPE QMAASTPHGL SFGFDGPMQL PSEMGSPLDQ RRDSEQSIMT
     ESSYTFSTDD SFEELINV