ID   OPS3_BEAB2              Reviewed;         741 AA.
AC   J4KLU1;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Oosporein cluster regulator OpS3 {ECO:0000303|PubMed:26305932};
DE   AltName: Full=Oosporein biosynthesis protein 3 {ECO:0000303|PubMed:26305932};
GN   Name=OpS3 {ECO:0000303|PubMed:26305932}; ORFNames=BBA_08181;
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860;
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA   St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26305932; DOI=10.1073/pnas.1503200112;
RA   Feng P., Shang Y., Cen K., Wang C.;
RT   "Fungal biosynthesis of the bibenzoquinone oosporein to evade insect
RT   immunity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:11365-11370(2015).
CC   -!- FUNCTION: Transcription factor involved in regulation of gene cluster
CC       that mediates the biosynthesis of oosporein, a metabolite required for
CC       fungal virulence that acts by evading host immunity to facilitate
CC       fungal multiplication in insects (PubMed:26305932). Binds oosporein
CC       cluster genes at a conserved 5'-CGGA-3' motif with the exception of
CC       OpS5 (PubMed:26305932). The presence of this motif in the OpS3 promoter
CC       would suggest the formation of a positive feedback loop for self-
CC       activation (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: With the exception of OpS5, disables the
CC       expression of other genes associated with oosporein biosynthesis
CC       (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
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DR   EMBL; JH725181; EJP62794.1; -; Genomic_DNA.
DR   RefSeq; XP_008601500.1; XM_008603278.1.
DR   AlphaFoldDB; J4KLU1; -.
DR   SMR; J4KLU1; -.
DR   EnsemblFungi; EJP62794; EJP62794; BBA_08181.
DR   GeneID; 19891193; -.
DR   HOGENOM; CLU_374668_0_0_1; -.
DR   InParanoid; J4KLU1; -.
DR   Proteomes; UP000002762; 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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
PE   3: Inferred from homology;
KW   Coiled coil; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Virulence; Zinc.
FT   CHAIN           1..741
FT                   /note="Oosporein cluster regulator OpS3"
FT                   /id="PRO_0000438574"
FT   DNA_BIND        44..69
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          16..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          473..500
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        17..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  81251 MW;  49EBD946BBEB37B2 CRC64;
     MFYTFNAVMT DVVSAGRPAR GQSTTTRSRN TQQSAPTSQN FRACRRCRQH RIKCSEKPCE
     PCRANNSKCV WTEEKPTAAV LTPISPANLA ANRPMMAPAA GSTITKPIAS HYASPTYTDG
     EDGGGEPWPL QHPCSCAQHP NTPNSCPSQS GDIRQQQIPC SQHASPASNA SKTFHQFLEG
     LGMAVTAEEG ELHQFPPLPS AEEGKTSTAA AGLLPSAPTA SETLNWDGQL YFVRLFWMSL
     APLFPIMPES EFEALYAADG PYLLGQRTIE GALINGMTAL GIQCAEATGS GARILSCSPT
     AASRSSIEYF RRCRDVLRDQ DTSTTTCVHT IRCYILLTLY HLQANQLEKA YYLAGLGVRR
     AHMGRFHLTP AAHSSARVAD DRIRVWWLLS WLDVYCSLQL GRPAAVQRSS NPCPPPSSPP
     MRFTPMHADV VSRKEASLDN YRFVLSKLTM IVVEALDDVP VFQSLEEMHG SSTAGQSMAR
     LSETIRQLET ALDELPEQLL TRHGSRTPTN NGQTHRSRPT CSTMPHTNRQ VTSSASSAAL
     TVGLPDWLQR QRLILELHYL DACLVLQRPF VLWKQICSSD ASITKHAESA FSRACSVLSM
     LHSIYSRSDI LDRLTMVLPF IWNAIITIAA YVFVGSADDD KKTQLLKAMN NALAILEPLA
     RINPDSLKVY QISQALAAEL REASGGTDVV AMPPPPSAAT STSTTFTDDL FKSTFTGSLD
     LDEFLNDEVT MTDDFSELYS F