BRLA_ASPFU
ID BRLA_ASPFU Reviewed; 426 AA.
AC Q4WRE4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=C2H2 type master regulator of conidiophore development brlA {ECO:0000305};
GN Name=brlA {ECO:0000303|PubMed:17030990}; ORFNames=AFUA_1G16590;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=17030990; DOI=10.1128/ec.00192-06;
RA Mah J.H., Yu J.H.;
RT "Upstream and downstream regulation of asexual development in Aspergillus
RT fumigatus.";
RL Eukaryot. Cell 5:1585-1595(2006).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18333504; DOI=10.3852/mycologia.99.6.804;
RA Coyle C.M., Kenaley S.C., Rittenour W.R., Panaccione D.G.;
RT "Association of ergot alkaloids with conidiation in Aspergillus
RT fumigatus.";
RL Mycologia 99:804-811(2007).
RN [4]
RP INDUCTION.
RX PubMed=18849468; DOI=10.1128/ec.00224-08;
RA Palmer J.M., Perrin R.M., Dagenais T.R., Keller N.P.;
RT "H3K9 methylation regulates growth and development in Aspergillus
RT fumigatus.";
RL Eukaryot. Cell 7:2052-2060(2008).
RN [5]
RP INDUCTION.
RX PubMed=18298443; DOI=10.1111/j.1365-2958.2008.06122.x;
RA Soriani F.M., Malavazi I., da Silva Ferreira M.E., Savoldi M.,
RA Von Zeska Kress M.R., de Souza Goldman M.H., Loss O., Bignell E.,
RA Goldman G.H.;
RT "Functional characterization of the Aspergillus fumigatus CRZ1 homologue,
RT CrzA.";
RL Mol. Microbiol. 67:1274-1291(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19028996; DOI=10.1128/ec.00265-08;
RA Twumasi-Boateng K., Yu Y., Chen D., Gravelat F.N., Nierman W.C.,
RA Sheppard D.C.;
RT "Transcriptional profiling identifies a role for BrlA in the response to
RT nitrogen depletion and for StuA in the regulation of secondary metabolite
RT clusters in Aspergillus fumigatus.";
RL Eukaryot. Cell 8:104-115(2009).
RN [7]
RP INDUCTION.
RX PubMed=22822234; DOI=10.1128/ec.00032-12;
RA Lamoth F., Juvvadi P.R., Fortwendel J.R., Steinbach W.J.;
RT "Heat shock protein 90 is required for conidiation and cell wall integrity
RT in Aspergillus fumigatus.";
RL Eukaryot. Cell 11:1324-1332(2012).
RN [8]
RP FUNCTION.
RX PubMed=24123270; DOI=10.1128/ec.00217-13;
RA Upadhyay S., Torres G., Lin X.;
RT "Laccases involved in 1,8-dihydroxynaphthalene melanin biosynthesis in
RT Aspergillus fumigatus are regulated by developmental factors and copper
RT homeostasis.";
RL Eukaryot. Cell 12:1641-1652(2013).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24612080; DOI=10.1111/cmi.12284;
RA Lim F.Y., Ames B., Walsh C.T., Keller N.P.;
RT "Co-ordination between BrlA regulation and secretion of the oxidoreductase
RT FmqD directs selective accumulation of fumiquinazoline C to conidial
RT tissues in Aspergillus fumigatus.";
RL Cell. Microbiol. 16:1267-1283(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26032501; DOI=10.1016/j.bbrc.2015.05.090;
RA Shin K.S., Kim Y.H., Yu J.H.;
RT "Proteomic analyses reveal the key roles of BrlA and AbaA in biogenesis of
RT gliotoxin in Aspergillus fumigatus.";
RL Biochem. Biophys. Res. Commun. 463:428-433(2015).
RN [11]
RP INDUCTION.
RX PubMed=26190922; DOI=10.5941/myco.2015.43.2.150;
RA Seo Y.H., Kim S.S., Shin K.S.;
RT "In vitro antifungal activity and mode of action of 2',4'-dihydroxychalcone
RT against Aspergillus fumigatus.";
RL Mycobiology 43:150-156(2015).
CC -!- FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore
CC development and conidium maturation (PubMed:17030990). 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 Positively regulates expression of the gliotoxin biosynthetic gene
CC cluster in actively growing vegetative cells, and likely bridges
CC morphological and chemical development during the life-cycle
CC (PubMed:26032501). Regulates (directly or indirectly) the ergot cluster
CC genes (PubMed:18333504). Positively regulates expression of the
CC fumiquinazoline C biosynthetic gene cluster (PubMed:24612080).
CC Positively regulates expression of the melanin biosynthetic gene
CC cluster (PubMed:24123270). Mediates repression of ribosomal protein
CC gene expression in response to nitrogen depletion (PubMed:19028996).
CC {ECO:0000250|UniProtKB:P10069, ECO:0000269|PubMed:17030990,
CC ECO:0000269|PubMed:18333504, ECO:0000269|PubMed:19028996,
CC ECO:0000269|PubMed:24123270, ECO:0000269|PubMed:24612080,
CC ECO:0000269|PubMed:26032501}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10069}.
CC -!- INDUCTION: Expression increases dramatically during the synchronous
CC asexual development (PubMed:18298443). Expression is positively
CC regulated by hsp90 (PubMed:22822234). Expression is controlled by
CC upstream regulators fluG and flbA (PubMed:17030990). Expression is
CC controlled by the histone methyltransferase clrD (PubMed:18849468).
CC Expression is decreased by 2',4'-Dihydroxychalcone (2',4'-DHC)
CC (PubMed:26190922). {ECO:0000269|PubMed:17030990,
CC ECO:0000269|PubMed:18298443, ECO:0000269|PubMed:18849468,
CC ECO:0000269|PubMed:22822234, ECO:0000269|PubMed:26190922}.
CC -!- DISRUPTION PHENOTYPE: Abolishes completely conidiation
CC (PubMed:17030990). Results in production of bristle-like structures
CC instead of conidiophores and conidia and fails to produce ergot
CC alkaloids (PubMed:18333504). Reduces significantly expression of
CC gliotoxin biosynthetic gene cluster including gliM, gliP, gliT, and
CC gliZ (PubMed:26032501). Impairs down-regulation of genes encoding
CC ribosomal proteins under nitrogen-limiting, but not carbon-limiting,
CC conditions (PubMed:19028996). Abolishes the production of
CC fumiquinazoline C (PubMed:24612080). {ECO:0000269|PubMed:17030990,
CC ECO:0000269|PubMed:18333504, ECO:0000269|PubMed:19028996,
CC ECO:0000269|PubMed:24612080, ECO:0000269|PubMed:26032501}.
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DR EMBL; AAHF01000004; EAL90988.1; -; Genomic_DNA.
DR RefSeq; XP_753026.1; XM_747933.1.
DR AlphaFoldDB; Q4WRE4; -.
DR SMR; Q4WRE4; -.
DR STRING; 746128.CADAFUBP00001564; -.
DR EnsemblFungi; EAL90988; EAL90988; AFUA_1G16590.
DR GeneID; 3510052; -.
DR KEGG; afm:AFUA_1G16590; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_655506_0_0_1; -.
DR InParanoid; Q4WRE4; -.
DR OMA; NPCLSRP; -.
DR OrthoDB; 633411at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
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..426
FT /note="C2H2 type master regulator of conidiophore
FT development brlA"
FT /id="PRO_0000435941"
FT ZN_FING 316..340
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 346..371
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 25..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47477 MW; 9E206F2D536C3EEF CRC64;
MRSQGNMSDR LGVEVDCHSL GSNECPSMGS SFSPLESPTP TPTSIYSQGS LASPSWPENG
SYPGHAYDRG TGSTPIRGHF RLASMPSHEN MGLPPYSSLD GQDRMAVTDF LPSYDENADQ
FWLPSDVPKT YDHHVHGLPC PPSMHQYPPM LRSNYRHHPA PYFPESATNP CLSRPIFHHQ
PERLPPSLSM SHMMPWMGHT ESIAPETIAP SQVAPVTPPP SYTDFSNSIN TFKTHSPDTP
IRSCSLGTVS GADTPLSRLS GGAGEYMDEC HQSPIYRDAS GVRLQRQPSR KMARKQPSKQ
SLSLENLPSI IKQVQFKCKE PGCKGRFKRQ EHLKRHMKSH SKEKPHVCWV PGCHRAFSRS
DNLNAHYTKT HSKRGGRNRY VATLDETSPD YNPDYRGPLT ADGRPMPGGT LDESMPSREI
SMEWDE
