ID   ASAA_ASPFN              Reviewed;         338 AA.
AC   B8N0E6;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Ankyrin-repeat domain containing transcription coregulator asaA {ECO:0000303|PubMed:29674152};
DE   AltName: Full=Aspergillic acid biosynthesis cluster protein A {ECO:0000303|PubMed:29674152};
GN   Name=asaA {ECO:0000303|PubMed:29674152}; ORFNames=AFLA_023000;
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   IDENTIFICATION WITHIN THE CLUSTER, AND INDUCTION.
RX   PubMed=23834374; DOI=10.1111/mpp.12056;
RA   Dolezal A.L., Obrian G.R., Nielsen D.M., Woloshuk C.P., Boston R.S.,
RA   Payne G.A.;
RT   "Localization, morphology and transcriptional profile of Aspergillus flavus
RT   during seed colonization.";
RL   Mol. Plant Pathol. 14:898-909(2013).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=29674152; DOI=10.1016/j.fgb.2018.04.009;
RA   Lebar M.D., Cary J.W., Majumdar R., Carter-Wientjes C.H., Mack B.M.,
RA   Wei Q., Uka V., De Saeger S., Diana Di Mavungu J.;
RT   "Identification and functional analysis of the aspergillic acid gene
RT   cluster in Aspergillus flavus.";
RL   Fungal Genet. Biol. 116:14-23(2018).
CC   -!- FUNCTION: Transcription coregulator involved in regulation of gene
CC       cluster that mediates the biosynthesis of aspergillic acid, a
CC       hydroxamic acid-containing pyrazinone with aliphatic side chains that
CC       originates from leucine (Leu) and isoleucine (Ile) (PubMed:29674152).
CC       Aspergillic acid has antibiotic properties and was shown to be lethal
CC       to mice (PubMed:29674152). {ECO:0000269|PubMed:29674152}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:29674152}.
CC   -!- INDUCTION: Expressed during the earliest stages of maize kernel
CC       infection (PubMed:23834374). {ECO:0000269|PubMed:23834374}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the down-regulation of expression of
CC       asaB, asaC, asaD, and asaR; and completely abolishes ferriaspergillin
CC       production (PubMed:29674152). {ECO:0000269|PubMed:29674152}.
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DR   EMBL; EQ963473; EED55029.1; -; Genomic_DNA.
DR   RefSeq; XP_002373811.1; XM_002373770.1.
DR   AlphaFoldDB; B8N0E6; -.
DR   SMR; B8N0E6; -.
DR   EnsemblFungi; EED55029; EED55029; AFLA_023000.
DR   VEuPathDB; FungiDB:AFLA_023000; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   HOGENOM; CLU_070837_0_0_1; -.
DR   OMA; NDTEMMQ; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF12796; Ank_2; 1.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..338
FT                   /note="Ankyrin-repeat domain containing transcription
FT                   coregulator asaA"
FT                   /id="PRO_0000444454"
FT   REPEAT          235..264
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          268..297
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          301..330
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  36688 MW;  1896024F1E07C465 CRC64;
     MGAPHEEIQA LKRRREQNRL AQRRRRDNVR RRLRDLGLDT GSPASASQTS LCSSTDSRVT
     LNPHQSLRST DFLSFETSNS DTEMSPYDPP LQSKLRLDSQ IPLAEISFPS YASSVSPSSS
     AGPLSSSPSP SQRPFIDSTD LTSLQSVYNP TSLAVHLDES SMPCGEAEIP TRQDSNFPRT
     PNLKSLMSGC NDPSAYQPWI LTSSTVGEQM SSQALPHSPG PQHCSTPLPA ETRPRWTTAL
     HMAVSQGNFS VMRLLLSYGA DPNAVNSEGA TALHVGVMNG NYTMVAELLQ RGADPTLTNA
     AGWLPLHQAV HAGDEGCVRV LLEADQPVDY PISDLDYT