BRLA_PENO1
ID BRLA_PENO1 Reviewed; 431 AA.
AC S7Z906;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=C2H2 type master regulator of conidiophore development brlA {ECO:0000305};
GN Name=brlA {ECO:0000303|PubMed:24113825}; ORFNames=PDE_00087;
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302;
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24113825; DOI=10.1007/s00253-013-5273-3;
RA Qin Y., Bao L., Gao M., Chen M., Lei Y., Liu G., Qu Y.;
RT "Penicillium decumbens BrlA extensively regulates secondary metabolism and
RT functionally associates with the expression of cellulase genes.";
RL Appl. Microbiol. Biotechnol. 97:10453-10467(2013).
RN [3]
RP INDUCTION.
RX PubMed=24613994; DOI=10.1016/j.fgb.2014.02.007;
RA Lei Y., Liu G., Li Z., Gao L., Qin Y., Qu Y.;
RT "Functional characterization of protein kinase CK2 regulatory subunits
RT regulating Penicillium oxalicum asexual development and hydrolytic enzyme
RT production.";
RL Fungal Genet. Biol. 66:44-53(2014).
CC -!- FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore
CC development and conidium maturation (PubMed:24113825). 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 Regulates the expression levels of seven secondary metabolism gene
CC clusters including a down-regulated cluster putatively involved in the
CC biosynthesis of the mycotoxins roquefortine C and meleagrin
CC (PubMed:24113825). Negatively regulates the expression of cellulase
CC genes (PubMed:24113825). {ECO:0000250|UniProtKB:P22022,
CC ECO:0000269|PubMed:24113825}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10069}.
CC -!- INDUCTION: Expression is controlled by the casein kinase CK2
CC (PubMed:24613994). {ECO:0000269|PubMed:24613994}.
CC -!- DISRUPTION PHENOTYPE: Blocks conidia formation and increases hyphal
CC branching (PubMed:24113825). Affects the expression of seven secondary
CC metabolism gene clusters including those in the biosynthesis of
CC roquefortine C and meleagrin, and up-regulates the expression levels of
CC most cellulase genes (PubMed:24113825). {ECO:0000269|PubMed:24113825}.
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DR EMBL; KB644408; EPS25156.1; -; Genomic_DNA.
DR AlphaFoldDB; S7Z906; -.
DR SMR; S7Z906; -.
DR STRING; 933388.S7Z906; -.
DR EnsemblFungi; EPS25156; EPS25156; PDE_00087.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_655506_0_0_1; -.
DR OrthoDB; 633411at2759; -.
DR PhylomeDB; S7Z906; -.
DR Proteomes; UP000019376; 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..431
FT /note="C2H2 type master regulator of conidiophore
FT development brlA"
FT /id="PRO_0000435947"
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 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 48585 MW; A545FF4A8EEB53F5 CRC64;
MRTQGQQISD RLTVEVDCHS LGPADCPSMT SSFSPLESPT PTPTSLYSHG SLTSPSWHEA
GHYHSLPMER RPSGTPLRNA FRVTDFPSAD PMGMQVGTME RPDQLPVSSE YLSGYDDIND
QLWIPHDSIP KTFEHPTFPY QAPMPQYHHT MGRNHYYRPQ AHTAYLPESA SNPCLSRPMF
SRHDGLSHSA SMSNMLPWMT APESLAPQTI TPQQAFPGAG PVTPPSSNYS DFPASLQTFK
PHTPSTPVRS LSLGTPRSDT PQSRMSGHYD YSEEYPVSPV YRDGHLIRTH RQPSRKPSKK
QLVRSNLSLE KLPPIIKQVQ FKCKEPGCKG RFKRQEHLKR HMKSHSKEKP HVCWVPGCHR
AFSRSDNLNA HYTKTHSKRG GRNRYVATLD ETSPDYDPEF RGQLTPDGRP IYGSKLEDLA
DCDLSVDGWE D
