ID   MFM5_PHOSM              Reviewed;         126 AA.
AC   A0A3G1DJG8;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=C2H2-type zinc-finger transcription factor M5 {ECO:0000303|PubMed:27056201};
DE   AltName: Full=Squalestatin S1 biosynthesis cluster protein M5 {ECO:0000303|PubMed:27056201};
GN   Name=M5 {ECO:0000303|PubMed:27056201};
OS   Phoma sp. (strain ATCC 20986 / MF5453).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Phoma.
OX   NCBI_TaxID=1828523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=27056201; DOI=10.1039/c6cc02130a;
RA   Bonsch B., Belt V., Bartel C., Duensing N., Koziol M., Lazarus C.M.,
RA   Bailey A.M., Simpson T.J., Cox R.J.;
RT   "Identification of genes encoding squalestatin S1 biosynthesis and in vitro
RT   production of new squalestatin analogues.";
RL   Chem. Commun. (Camb.) 52:6777-6780(2016).
CC   -!- FUNCTION: Transcription factor that probably regulates the expression
CC       of the gene cluster that mediates the biosynthesis of squalestatin S1
CC       (SQS1, also known as zaragozic acid A), a heavily oxidized fungal
CC       polyketide that offers potent cholesterol lowering activity by
CC       targeting squalene synthase (SS). {ECO:0000305|PubMed:27056201}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KU946987; AMY15062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G1DJG8; -.
DR   SMR; A0A3G1DJG8; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   SUPFAM; SSF57667; SSF57667; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Nucleus; Repeat; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..126
FT                   /note="C2H2-type zinc-finger transcription factor M5"
FT                   /id="PRO_0000447835"
FT   ZN_FING         51..76
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         83..115
FT                   /note="C2H2-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          17..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   126 AA;  14473 MW;  DEA5D0997854414E CRC64;
     MDIENWDTID QLMADSAQPD FEDWGDLGDL MPDVLPESNG SSSGTATDND NRCWDHGCNG
     KKFLNHSNLV RHRRENGSAR PRFTCPMCGA YFSRSTARNQ HLEKKSCNRV RRYSNGRERP
     RPRVKD