ID   CHER_CHAGB              Reviewed;         536 AA.
AC   Q2HEW7;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Transcription factor cheR {ECO:0000303|PubMed:33622536};
DE   AltName: Full=Chaetoglobosin A biosynthesis cluster protein R {ECO:0000303|PubMed:33622536};
GN   Name=cheR {ECO:0000303|PubMed:33622536}; ORFNames=CHGG_01237;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
RN   [2]
RP   FUNCTION.
RX   PubMed=23611317; DOI=10.1021/ja402828w;
RA   Ishiuchi K., Nakazawa T., Yagishita F., Mino T., Noguchi H., Hotta K.,
RA   Watanabe K.;
RT   "Combinatorial generation of complexity by redox enzymes in the
RT   chaetoglobosin A biosynthesis.";
RL   J. Am. Chem. Soc. 135:7371-7377(2013).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RX   PubMed=33622536; DOI=10.1016/j.funbio.2020.10.010;
RA   Cheng M., Zhao S., Liu H., Liu Y., Lin C., Song J., Thawai C.,
RA   Charoensettasilp S., Yang Q.;
RT   "Functional analysis of a chaetoglobosin A biosynthetic regulator in
RT   Chaetomium globosum.";
RL   Fungal Biol. 125:201-210(2021).
CC   -!- FUNCTION: Transcription factor; part of the gene cluster that mediates
CC       the biosynthesis of chaetoglobosin A which has a unique inhibitory
CC       activity against actin polymerization in mammalian cells
CC       (PubMed:23611317, PubMed:33622536). Chaetoglobosin A and its
CC       intermediates are involved in the morphological differentiation of
CC       C.globosum (PubMed:33622536). Binds directly to asymmetric direct
CC       repeats present in the promoters of the chaetoglobosin A cluster genes
CC       (PubMed:33622536). {ECO:0000269|PubMed:23611317,
CC       ECO:0000269|PubMed:33622536}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Drastically reduces the transcription of
CC       chaetoglobosin A biosynthetic genes and completely abolishes
CC       chaetoglobosin A production (PubMed:33622536). Abolishes sporuration
CC       (PubMed:33622536). {ECO:0000269|PubMed:33622536}.
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DR   EMBL; CH408029; EAQ93002.1; -; Genomic_DNA.
DR   RefSeq; XP_001220458.1; XM_001220457.1.
DR   AlphaFoldDB; Q2HEW7; -.
DR   EnsemblFungi; EAQ93002; EAQ93002; CHGG_01237.
DR   GeneID; 4388309; -.
DR   eggNOG; ENOG502R9RH; Eukaryota.
DR   HOGENOM; CLU_508053_0_0_1; -.
DR   InParanoid; Q2HEW7; -.
DR   OMA; RHKLRCE; -.
DR   OrthoDB; 1558353at2759; -.
DR   Proteomes; UP000001056; 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   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   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..536
FT                   /note="Transcription factor cheR"
FT                   /id="PRO_0000438204"
FT   DNA_BIND        19..57
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          70..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  57676 MW;  5A88325833527DF3 CRC64;
     MASAEETFFS AARSRRLACD RCHRHKLRCE RSSVIVNGGV AVPLGPCKRC LKACIPCQTV
     QTISGAFTAA KTGDTPVPRR SAREADQAAS PAKRAPSPAR RPTASTPRNV PGLIHDDTLS
     GTDTAPFEIS VADAAMLDVS NFDFSGSEFI DLGSNGVLSS PTPIQSPPDH GSLIRDSEIR
     DRTPIPPHNQ PPPRYDDFAN DLSCFGTMAP KDDTISTLPA LTDVEKASTG SSKSAPERGP
     REECSQRLLE IHGLLLNELQ CITPADVTDA LMFPENGSFS GRTRTGQGPG NTVVHRVLFT
     SERLIELLSI IRAADTAING DKREAGIGPR NTSSFVDLPI VISILTCYVG LLSVYHAIFS
     HIYEALRVYE PLRAAKIRQR AWTRRGSVPG PKPGPGLVQP RAIYGADEAG GRPALNVLGI
     RIQLEIMTHM LEQIDSALFG PRVAHGADGD EGRTDTINRG GEVMFGHPAT KALLATMLSH
     EGYDSGVPVG PFADGDGDDD DDDGYMEGMR GCRMGFRTLM GLQKNIRRLL RTNSFG