ID   ATNE_ARTSZ              Reviewed;         493 AA.
AC   A0A455M2Z1;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Transcription factor atnE {ECO:0000303|PubMed:29797385};
DE   AltName: Full=Arthripenoid biosynthesis cluster protein E {ECO:0000303|PubMed:29797385};
GN   Name=atnE {ECO:0000303|PubMed:29797385};
OS   Arthrinium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Apiosporaceae; Arthrinium;
OC   unclassified Arthrinium.
OX   NCBI_TaxID=1756131;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PATHWAY.
RC   STRAIN=NF2194;
RX   PubMed=29797385; DOI=10.1002/anie.201804317;
RA   Zhang X., Wang T.T., Xu Q.L., Xiong Y., Zhang L., Han H., Xu K., Guo W.J.,
RA   Xu Q., Tan R.X., Ge H.M.;
RT   "Genome mining and comparative biosynthesis of meroterpenoids from two
RT   phylogenetically distinct fungi.";
RL   Angew. Chem. Int. Ed. 57:8184-8188(2018).
CC   -!- FUNCTION: Transcription factor; part of the gene cluster that mediates
CC       the biosynthesis of the meroterpenoids arthripenoids.
CC       {ECO:0000269|PubMed:29797385}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; MH183011; AYO60878.1; -; mRNA.
DR   AlphaFoldDB; A0A455M2Z1; -.
DR   SMR; A0A455M2Z1; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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   2: Evidence at transcript level;
KW   DNA-binding; Membrane; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..493
FT                   /note="Transcription factor atnE"
FT                   /id="PRO_0000452565"
FT   TRANSMEM        445..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        12..39
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          94..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  54278 MW;  40FABEA11C83B756 CRC64;
     MGKEQFRART GCLTCRDRHI KCDEALPRCK NCCKSNRQCE RGIRLNFIET QTSNAQPQAE
     LPPGTKLKFH DESQAIASGY AVGAQEVKLV QISNTEPKPQ TELPQAGASK DGSIPQAKTV
     SSTEQTTLVS AQRSPLPALR LITDHDESLL MEIFLGKVAP WMDCLVANKP FTNTAPFCAL
     RHPALYNAIM ACGEKYLMPT EESLYYGKAC QGLQLETAKP NTDHGLCVAT STLLNAYETM
     GDGVNECRSD RTRALMGKAN LDGGSSDSLV RDSKLSCDTD RMKAALNVDH GAEVAQGTYN
     DSPQRLSQDC EQYKGWCDEW ASNVPRSMMP LCYIPPPDQD ASSATATHFP QVMFVGSSST
     VARLLYHVSC LLLARIQAAE RSAESQEAQS RQTRHAMDIC GIASQGEDKY ETLSLDEQTH
     ELLLHSSSPF RGTGTLITIF PETETLATWL SAVFPLLFGI LTNLKSRKKH FKFWIELLKT
     HLGGRASFNP KSV