PYNR_ASPNC
ID PYNR_ASPNC Reviewed; 868 AA.
AC A5ABG4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Transcription factor pynR {ECO:0000303|PubMed:24106156};
DE AltName: Full=Pyranonigrins biosynthesis cluster protein R {ECO:0000303|PubMed:24106156};
GN Name=pynRA {ECO:0000303|PubMed:24106156}; ORFNames=An11g00290;
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.
RX PubMed=24106156; DOI=10.1002/cbic.201300430;
RA Awakawa T., Yang X.L., Wakimoto T., Abe I.;
RT "Pyranonigrin E: a PKS-NRPS hybrid metabolite from Aspergillus niger
RT identified by genome mining.";
RL ChemBioChem 14:2095-2099(2013).
RN [3]
RP FUNCTION.
RX PubMed=26414728; DOI=10.1021/acs.orglett.5b02435;
RA Yamamoto T., Tsunematsu Y., Noguchi H., Hotta K., Watanabe K.;
RT "Elucidation of pyranonigrin biosynthetic pathway reveals a mode of
RT tetramic acid, fused gamma-pyrone, and exo-methylene formation.";
RL Org. Lett. 17:4992-4995(2015).
CC -!- FUNCTION: Transcription factor that regulates th eexpression of the
CC gene cluster that mediates the biosynthesis of pyranonigrins, a family
CC of antioxidative compounds. {ECO:0000269|PubMed:24106156,
CC ECO:0000269|PubMed:26414728}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR EMBL; AM270218; CAK48262.1; -; Genomic_DNA.
DR RefSeq; XP_001394033.1; XM_001393996.1.
DR AlphaFoldDB; A5ABG4; -.
DR PaxDb; A5ABG4; -.
DR EnsemblFungi; CAK48262; CAK48262; An11g00290.
DR GeneID; 4984240; -.
DR KEGG; ang:ANI_1_1536094; -.
DR VEuPathDB; FungiDB:An11g00290; -.
DR HOGENOM; CLU_340661_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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:0019748; P:secondary metabolic process; IGC:AspGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 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 3: Inferred from homology;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..868
FT /note="Transcription factor pynR"
FT /id="PRO_0000450062"
FT DNA_BIND 11..37
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 94789 MW; 5C15C14C3618EE20 CRC64;
MAKKAELRRS CTFCRTRKIA CSGERICNAC RSRSIECVYD LEIAKGRPRL NKTTSTRASI
SAGPAGPSPI TLEDGEPGDG GHSITSAVNP SITPLTGVMA ELEVMFRENF GEDPMAAPSN
QFQDRVARFN RNLAAGRASQ GPSTPAGSLT YPGFLALLMQ DLAETVTGKF GDLGCHPFFG
PGERFYRACM LQDTTKTMFD TACLPSPSTS TPSGGEADIL ADYNSHLITQ HLEVWMSNHP
LSIIISKSLL LRDLRSQTAN RVLLAVMLAD AHHFADNSAK GDRLLQWAVS QLSNIPAGQE
DLTTAQITLL LGWFHVCRGH SRRALCYVGY AGRITTKLAS QLHESPLTGQ THINGIDRGA
VEAEMIHHMY WVMLALTVWS FIQMDMPLAD LLPAQLLQVL PARTTPDSTL LQLDRATDNL
STLKPQLSSL QSVWLLSHVT VLSAHLYALY PQHLRSPPEP QPWQDLMLHR LNRLLRQGRS
LTQICSDSRN ALLDIIVVLQ KESAHGRGEP TLLALYLAVS IHLLFPRDET GHHVHNSQTF
VLSDTLFQQL IASIQDLKQL FPAISSVARH DSSQPASTGS AGLHFYLLAL DALGRALMYV
LTVWDRVTAV EQRVWQDRLR GLLDGGLAMH DLFEYDALLQ DHRWRSVKKH LKTACKGIKG
VLSGSRDQGS RSSSSSVSSL DLSFALPSRP TPAMGIPTSE EGRSEMMFPT MPSASGIPSS
ISSSISHTSR EVGLSWPGDG QILPTQEQGP RESSHPAASD LSDFDLAPFV SLGSIDSMQN
GDERSRIMQQ FSPNPMSLPS FWHDPQFSPA HHLVGTMPPP SLISLADLGM GERGQKRSSE
KLGGLSEGDT PGTSADGGTK RRMKGMSN
