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 27-MAR-2024, entry version 74.
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 STRING; 332952.B8N0E6; -.
DR EnsemblFungi; EED55029; EED55029; AFLA_023000.
DR VEuPathDB; FungiDB:AFLA_000136; -.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_070837_0_0_1; -.
DR OMA; NDTEMMQ; -.
DR OrthoDB; 1750615at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR PANTHER; PTHR24197:SF44; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 54; 1.
DR PANTHER; PTHR24197; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 61; 1.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 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
//
