BRLA_ASPNC
ID BRLA_ASPNC Reviewed; 425 AA.
AC A2QA83;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=C2H2 type master regulator of conidiophore development brlA {ECO:0000305};
GN Name=brlA {ECO:0000303|PubMed:25629352}; ORFNames=An01g10540;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25629352; DOI=10.1371/journal.pone.0116269;
RA van Munster J.M., Nitsche B.M., Akeroyd M., Dijkhuizen L.,
RA van der Maarel M.J., Ram A.F.;
RT "Systems approaches to predict the functions of glycoside hydrolases during
RT the life cycle of Aspergillus niger using developmental mutants delta-brlA
RT and delta-flbA.";
RL PLoS ONE 10:E0116269-E0116269(2015).
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 (PubMed:25629352). 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 Coordinates also the expression of carbohydrate-active enzymes and of
CC the key effectors of cell wall remodeling during autolysis
CC (PubMed:25629352). {ECO:0000250|UniProtKB:P22022,
CC ECO:0000269|PubMed:25629352}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10069}.
CC -!- DISRUPTION PHENOTYPE: Forms aconidial fluffy colonies
CC (PubMed:25629352). {ECO:0000269|PubMed:25629352}.
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DR EMBL; AM269980; CAK37235.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QA83; -.
DR SMR; A2QA83; -.
DR PaxDb; A2QA83; -.
DR EnsemblFungi; CAK37235; CAK37235; An01g10540.
DR HOGENOM; CLU_655506_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
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 3: Inferred from homology;
KW Activator; Conidiation; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Sporulation; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..425
FT /note="C2H2 type master regulator of conidiophore
FT development brlA"
FT /id="PRO_0000435944"
FT ZN_FING 321..345
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..376
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 28..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47419 MW; FB7FE0D132B8238A CRC64;
MRSQGNMSDR LTIEVDCTSL GSNECPSMAS SFSPMESPTP TPTSVYSQGS LASPTWHEGG
SYPGQGYERH TGTTPMRSAF RLASMTSNDS MGMSYGQMEA QERMPMTDFL SGYDENVEHF
WIPQEAQKAY EHGVPGLPYP QAMPQYSTMG RSSYRQHAAP YLPDSATNPC LSRSIFHQPE
RVPNSMSMGN VIPWMAPQPD SIAPQTIAPS QVAPVTPPPS YSEFSGSINT FKTHSPTTPV
RSCSLGTTSG TDTPMSRLSG GMDYLDDFNQ SPVYRDNLAR VQRQPSRKVA RKQSSKQSLS
LENLPSIIKQ VQFKCKEPGC KGRFKRQEHL KRHMKSHSKE KPHVCWVPGC ERAFSRSDNL
NAHYTKTHSK RGGRNRYVAT LDENSPDYNP EYRGQLTADG RPVYNSKSQD LMPDARETSE
EAWLE
