BRLA_ACRCH
ID BRLA_ACRCH Reviewed; 376 AA.
AC A0A0A7HJC7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=C2H2 type master regulator of conidiophore development brlA {ECO:0000305};
GN Name=brlA {ECO:0000303|PubMed:26283234};
OS Acremonium chrysogenum (Cephalosporium acremonium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX NCBI_TaxID=5044;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=GMCC 3.3795;
RX PubMed=26283234; DOI=10.1016/j.fgb.2015.08.003;
RA Hu P., Wang Y., Zhou J., Pan Y., Liu G.;
RT "AcstuA, which encodes an APSES transcription regulator, is involved in
RT conidiation, cephalosporin biosynthesis and cell wall integrity of
RT Acremonium chrysogenum.";
RL Fungal Genet. Biol. 83:26-40(2015).
CC -!- FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore
CC development and conidium maturation (PubMed:26283234). 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, ECO:0000269|PubMed:26283234}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10069}.
CC -!- INDUCTION: Expression is positively regulated by stuA through direct
CC binding of stuA to the abaA promoter region (PubMed:26283234).
CC {ECO:0000269|PubMed:26283234}.
CC -!- DISRUPTION PHENOTYPE: Abolishes conidiation (PubMed:26283234).
CC {ECO:0000269|PubMed:26283234}.
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DR EMBL; KM207846; AIZ05821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A7HJC7; -.
DR SMR; A0A0A7HJC7; -.
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 SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Conidiation; DNA-binding; Metal-binding; Nucleus; Repeat;
KW Sporulation; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..376
FT /note="C2H2 type master regulator of conidiophore
FT development brlA"
FT /id="PRO_0000435950"
FT ZN_FING 277..301
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..332
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 20..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 42535 MW; 1ECBB0A099766175 CRC64;
MEDGFGMYSH SMSCPSTAST SFSSASSSAY DPFTPSSRRS TPNELSLDLD GSCSYAAHQH
SLELTPPTTS MAKYFMGQTI KQEPEQMSFG SLPTTPMKKV DGGFAAEYDL IDMNMASHHS
MGTITPSNSF GLHTISPETA MGPTSYMMTP TQSLSGSEIA ESSSSWSVTN ESPINFFQQP
KDLSFHDMDS LDLDERHHHH HNHHQHHHAQ QSPMGQHFQL HSNTGASPNS MRVQRKMMLH
EAQRKTSELQ RAQIRESRKR AGKPESGAVD VVRRAMCKCD YPGCNKAFRR NEHLKRHKQT
FHGEGPNRFS CEFCGKDQFN RQDNLNNHRK LHARPNSRNR GVEFIPEAVP IIEHEERSRK
RRAPPKSKAE KRDYDF