ID   BRLA_ASPPU              Reviewed;         421 AA.
AC   A0A0F0I5G4; Q8NJN7;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=C2H2 type master regulator of conidiophore development brlA {ECO:0000305};
GN   Name=brlA {ECO:0000303|Ref.1};
GN   ORFNames=P875_00034167 {ECO:0000312|EMBL:KJK62960.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA   Chang P.-K.;
RT   "Characterization of Aspergillus parasiticus brlA gene.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INDUCTION.
RX   PubMed=17660441; DOI=10.1099/mic.0.2006/005629-0;
RA   Yoshinari T., Akiyama T., Nakamura K., Kondo T., Takahashi Y., Muraoka Y.,
RA   Nonomura Y., Nagasawa H., Sakuda S.;
RT   "Dioctatin A is a strong inhibitor of aflatoxin production by Aspergillus
RT   parasiticus.";
RL   Microbiology 153:2774-2780(2007).
CC   -!- FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore
CC       development and conidium maturation (By similarity). They act
CC       individually and together to regulate their own expression and that of
CC       numerous other sporulation-specific genes (By similarity). Binds
CC       promoters of target genes at brlA response elements (BREs) containing
CC       the conserved sequence 5'-(C/A)(A/G)AGGG(G/A)-3' (By similarity).
CC       {ECO:0000250|UniProtKB:P22022}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10069}.
CC   -!- INDUCTION: Expression is down-regulated by dioctatin A (DotA), a
CC       metabolite of Streptomyces (PubMed:17660441).
CC       {ECO:0000269|PubMed:17660441}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF533070; AAM95989.1; -; Genomic_DNA.
DR   EMBL; JZEE01000588; KJK62960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I5G4; -.
DR   SMR; A0A0F0I5G4; -.
DR   STRING; 1403190.A0A0F0I5G4; -.
DR   EnsemblFungi; KJK62960; KJK62960; P875_00034167.
DR   Proteomes; UP000033540; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   2: Evidence at transcript level;
KW   Activator; Conidiation; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Sporulation; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..421
FT                   /note="C2H2 type master regulator of conidiophore
FT                   development brlA"
FT                   /id="PRO_0000435942"
FT   ZN_FING         309..333
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         339..364
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          228..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  46925 MW;  0BFF363B98E1650D CRC64;
     MRAQNNLTVE VDCHSLGSNE CPSMTSSFSP MDSPTPTPTS IYSQGSLASP GWQDAGSYPG
     HAYERHTGTT PMRSAFRLAG MTSNENMAMS YGAMEAQERM PMPDFLSAYD DNVEHFWLPS
     DAPKTYETGT HSLPYPHTLP QCPPMVRSNY RPHAAYLPEA ATNPCLSRSI FHHAERVPQS
     MSMGNMMPWI PQASESIAPQ TIAPSQVGPV TPPPSYSEFP TSIQTFKTHS PTTPLRSCSI
     GTASGPDTPI SRMSGGAADY LEDFQQSPPF RDGLNRLQRH PSRKMIRKQS SRQNMSLENL
     PSIIKQVQFK CKEPGCKGRF KRQEHLKRHM KSHSKEKPHV CWVPGCERAF SRSDNLNAHY
     TKTHSKRGGR NRYVATLDES SPDYDPDFRG QLTPDGRPIR GSTLDDPMPD TREYSVDGLD
     D