ID   PSIR_PSICY              Reviewed;         370 AA.
AC   A0A286LEZ9;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Psilocybin cluster transcription regulator {ECO:0000303|PubMed:28763571};
GN   Name=psiR {ECO:0000303|PubMed:28763571};
OS   Psilocybe cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Strophariaceae; Psilocybe.
OX   NCBI_TaxID=93625;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, AND FUNCTION.
RC   STRAIN=FSU 12416;
RX   PubMed=28763571; DOI=10.1002/anie.201705489;
RA   Fricke J., Blei F., Hoffmeister D.;
RT   "Enzymatic synthesis of psilocybin.";
RL   Angew. Chem. Int. Ed. 56:12352-12355(2017).
CC   -!- FUNCTION: Transcription factor that may regulate the expression of the
CC       gene cluster that mediates the biosynthesis of psilocybin, a
CC       psychotropic tryptamine-derived natural product.
CC       {ECO:0000305|PubMed:28763571}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR   EMBL; MF000994; ASU62247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286LEZ9; -.
DR   SMR; A0A286LEZ9; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN           1..370
FT                   /note="Psilocybin cluster transcription regulator"
FT                   /id="PRO_0000445830"
FT   DOMAIN          208..258
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..221
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          222..258
FT                   /note="Helix-loop-helix motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          317..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  39103 MW;  1FCCF87F5674A4AD CRC64;
     MAPTTPATHD PALSHGAPPT QGSQAPANAA PNLTPADISG MQLNGLDQSQ IMNLLRSLPG
     MFTGAKIPDQ GQGNPKEDAA QTLSNLAQAS SPFGGQHLPI HYQTGAAGGL PGINDPGPST
     HPRGPPNLGQ LSAVAMQAAP ATIQHQDQQQ SGRQEDGEQA GNTSIDSPSA KDGENGTGEF
     NQTSTSTPSG GRRGGRSATM GSDEWSRQRK DNHKEVERRR RGNINEGINE LGRIVPSGSG
     EKAKGAILSR AVQYIHHLKE NEARNIEKWT LEKLLMDQAM GDLQAQLEEI KRLWEEERMA
     RTRLEAELEV LRNMNGVSTA GAGSGAAKDE SAAGTKRRST DGADAAGTNV EGGNNDNAEG
     ERDGKRQRTE