ID   YANR_ASPNA              Reviewed;         817 AA.
AC   G3Y415;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Transcription factor yanR {ECO:0000303|PubMed:24684908};
DE   AltName: Full=Yanuthone D biosynthesis cluster protein R {ECO:0000303|PubMed:24684908};
GN   Name=yanR {ECO:0000303|PubMed:24684908}; ORFNames=ASPNIDRAFT_44961;
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7;
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=11031048; DOI=10.1021/jo0006831;
RA   Bugni T.S., Abbanat D., Bernan V.S., Maiese W.M., Greenstein M.,
RA   Van Wagoner R.M., Ireland C.M.;
RT   "Yanuthones: novel metabolites from a marine isolate of Aspergillus
RT   niger.";
RL   J. Org. Chem. 65:7195-7200(2000).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24684908; DOI=10.1016/j.chembiol.2014.01.013;
RA   Holm D.K., Petersen L.M., Klitgaard A., Knudsen P.B., Jarczynska Z.D.,
RA   Nielsen K.F., Gotfredsen C.H., Larsen T.O., Mortensen U.H.;
RT   "Molecular and chemical characterization of the biosynthesis of the 6-MSA-
RT   derived meroterpenoid yanuthone D in Aspergillus niger.";
RL   Chem. Biol. 21:519-529(2014).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       gene cluster that mediates the biosynthesis of yanuthone D, a fungal
CC       isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi
CC       and bacteria (PubMed:24684908). {ECO:0000269|PubMed:24684908}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Leads to significant down-regulation of the
CC       yanuthone D gene clister and losses the ability to produce yanuthones D
CC       and E (PubMed:24684908). {ECO:0000269|PubMed:24684908}.
CC   -!- BIOTECHNOLOGY: Yanuthone D is an antibiotic against Candida albicans,
CC       methicillin-resistant Staphylococcus aureus (MRSA), and vancomycin-
CC       resistant Enterococcus (PubMed:11031048).
CC       {ECO:0000269|PubMed:11031048}.
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DR   EMBL; ACJE01000012; EHA22192.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3Y415; -.
DR   EnsemblFungi; EHA22192; EHA22192; ASPNIDRAFT_44961.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1090334; -.
DR   HOGENOM; CLU_018877_0_0_1; -.
DR   Proteomes; UP000009038; 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   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..817
FT                   /note="Transcription factor yanR"
FT                   /id="PRO_0000436768"
FT   DNA_BIND        19..46
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          102..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   817 AA;  90121 MW;  A2CDE568812F9DF9 CRC64;
     MPPPPEPRQI KRPRLSLSCI VCRRRKVRCG REHPECANCV RMKENCVYKT MVHDEFTGRV
     RQVSPPPVPQ GDNPNGPEFC ANNSEERTGG FTWSHWMSQG SGNVLDLSDE APLPRPTISP
     ASAPPPQKRS TQAKCDASSV PHPHHSSTIL TPAPSSHPQV DLVYPTVPSW EEAIQLPDNH
     HASSRAGTSR TSSVSQDASP AVSESARAPS TSTSYSGLPS PDYLSVRRGA RVRYIGQAFW
     GLVAGKETLS DDFFDCNRDA SMEQSLTHIS SLGMFNLLRS LPTKPVSDAL LDAFFFAVWP
     LSPLVHGPTL RADYDNFWEW CRNSDRALPP EKVRDDPTFL CLLFAILYCG ASAAPPTSWA
     CTNLQSLRKE TTIKHLKSAY TTSLSLCQHL EHPTLNTLVS TLLTAPFLDR DVAPMRNMVS
     VSTTVRIAQS MGLHREGTWS SSLSPVDREI RRRAWWYIIG LDVQSSISTG LPPCYATEAL
     DIVSMIADTR DEDIGDLSNH RSPEPVPRPS EQSLAVILAI ARSETARLQS KIVSRLQNGR
     RLAQTELTEL VTSAKKLQQK LDTLIARVPS QGIPEKGFIP SRLAKASPLY QTPAFSPYVW
     FCYRHYGPLQ CVFLILVYLH TFPESGDIVL ARYCIDEIID HTVSHYQVPQ DSFGATRADN
     SESDEGATED QIPLAIQVLV DLHNRLQSHP RSDNQTTDRL DGNEYQFSPY SLELGIQGTE
     EDTIDKSIFS LPSLSSSSSR THIHRNQEAP STTTAPQMPS GTKHGPPSSV FVADSDGGSD
     LDILASLSDF ETWSSSLVVD PSDILAHPTS MAPHHPV