ID   ADAR_ASPNG              Reviewed;         777 AA.
AC   G3KLH2;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=C6 finger domain transcription factor adaR {ECO:0000303|PubMed:21866960};
DE   AltName: Full=2-acetyl-2-decarboxamidoanthrotainin biosynthesis cluster protein R {ECO:0000303|PubMed:21866960};
GN   Name=adaR {ECO:0000303|PubMed:21866960}; ORFNames=ATCC64974_92740;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND FUNCTION.
RC   STRAIN=ATCC 1015 / NV DSM 2061;
RX   PubMed=21866960; DOI=10.1021/ja206906d;
RA   Li Y., Chooi Y.H., Sheng Y., Valentine J.S., Tang Y.;
RT   "Comparative characterization of fungal anthracenone and naphthacenedione
RT   biosynthetic pathways reveals an alpha-hydroxylation-dependent Claisen-like
RT   cyclization catalyzed by a dimanganese thioesterase.";
RL   J. Am. Chem. Soc. 133:15773-15785(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64974 / FGSC A733 / N402;
RX   PubMed=30319579; DOI=10.3389/fmicb.2018.02269;
RA   Laothanachareon T., Tamayo-Ramos J.A., Nijsse B., Schaap P.J.;
RT   "Forward genetics by genome sequencing uncovers the central role of the
RT   Aspergillus niger goxB locus in hydrogen peroxide induced glucose oxidase
RT   expression.";
RL   Front. Microbiol. 9:2269-2269(2018).
CC   -!- FUNCTION: Transcription factor that specifically regulates the
CC       expression of the ada gene cluster involved in the biosynthesis of the
CC       linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist.
CC       {ECO:0000269|PubMed:21866960}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; JN257714; AEN83885.1; -; Genomic_DNA.
DR   EMBL; OGUI01000016; SPB51664.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3KLH2; -.
DR   VEuPathDB; FungiDB:An11g07350; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1187773; -.
DR   VEuPathDB; FungiDB:ATCC64974_92740; -.
DR   VEuPathDB; FungiDB:M747DRAFT_298767; -.
DR   OrthoDB; 402788at2759; -.
DR   Proteomes; UP000236662; 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   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..777
FT                   /note="C6 finger domain transcription factor adaR"
FT                   /id="PRO_0000446343"
FT   DNA_BIND        24..50
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  85148 MW;  EB31D93F1AD507BD CRC64;
     MEQRSSPARS LPPRKTTTTP QLSCELCRKR KVKCDKLTPC TNCAASGTVC VPIYRTRLPR
     GRHATRPRRV SSPPPTSAPG ETDRIIQPSV PVNEDLQERI YRLEALIQGM NSHSHTRTPS
     ATSREQSVQL SDTSTFQTAP NPNTSPILNS SIVSKRLMLQ RPDQFWADLV DEIHGLREVV
     ESSLAGGQEG PIPSSDSAKS EPPNDDGIQV LGLGASNPSA ALRSMSPLHN PVVARQLCEV
     YLQQVDPVIK ILHRPSLNRW MVQGEPYLSY ADGHPAVEAL GSAVCYSAIS SMTDNQCSVM
     FHANKADLLA EARVACETAI GRAGLLTTRD ITVLQAFVLY LVARRSEDRT PAVWTLIALA
     VRIGKGLGLY LDPETETFFD QQIRRRLWFT ICLMDLQASF GQASEPLISV DESASTALPQ
     HINDSDFDPT TAAHSDPNRE GLTDTTFALV TYHAQRTGRL LNFVQHDRKV DGGIPTPTSS
     TSGTSTSRSR TCDPSWPQQQ ARHFEQEALR LLHFCDPGTS AYAWFTWHGT QSLIATVRLA
     AARPLQWHGQ APPPRREGNT ELLRLCLPVL EKAQLMHTDP RAEGFRWYVT IPWYALAMAL
     AECYVSSDTA LVRYAWPLVE SSYLQYEATL GQSLGGPFGQ LMRRMKEKLA APAALPPSSL
     PSTNWSPATP PTFPGVPRPQ SSHDDRHAPG CSWPVPTGST PPADLGVPSL LPVSTWEALS
     PPSLDNPSLF GVPPTTTAVA DGMDPGADIM WEELFSGIPF NEIAGPDTFF FDMNWGS