ID   ASCR_ACREG              Reviewed;         512 AA.
AC   A0A455R614;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Ascofuranone/ascochlorin biosynthesis clusters transcription regulator {ECO:0000303|PubMed:30952781};
GN   Name=ascR {ECO:0000303|PubMed:30952781};
OS   Acremonium egyptiacum (Oospora egyptiaca).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX   NCBI_TaxID=749675;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION,
RP   AND PATHWAY.
RC   STRAIN=F-1392;
RX   PubMed=30952781; DOI=10.1073/pnas.1819254116;
RA   Araki Y., Awakawa T., Matsuzaki M., Cho R., Matsuda Y., Hoshino S.,
RA   Shinohara Y., Yamamoto M., Kido Y., Inaoka D.K., Nagamune K., Ito K.,
RA   Abe I., Kita K.;
RT   "Complete biosynthetic pathways of ascofuranone and ascochlorin in
RT   Acremonium egyptiacum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:8269-8274(2019).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=12084465; DOI=10.1016/s0925-4439(02)00086-8;
RA   Nihei C., Fukai Y., Kita K.;
RT   "Trypanosome alternative oxidase as a target of chemotherapy.";
RL   Biochim. Biophys. Acta 1587:234-239(2002).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=12798927; DOI=10.1016/s1383-5769(03)00012-6;
RA   Yabu Y., Yoshida A., Suzuki T., Nihei C., Kawai K., Minagawa N.,
RA   Hosokawa T., Nagai K., Kita K., Ohta N.;
RT   "The efficacy of ascofuranone in a consecutive treatment on Trypanosoma
RT   brucei brucei in mice.";
RL   Parasitol. Int. 52:155-164(2003).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=20688188; DOI=10.1016/j.parint.2010.07.006;
RA   Nakamura K., Fujioka S., Fukumoto S., Inoue N., Sakamoto K., Hirata H.,
RA   Kido Y., Yabu Y., Suzuki T., Watanabe Y., Saimoto H., Akiyama H., Kita K.;
RT   "Trypanosome alternative oxidase, a potential therapeutic target for
RT   sleeping sickness, is conserved among Trypanosoma brucei subspecies.";
RL   Parasitol. Int. 59:560-564(2010).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       asc-1 and asc-2 gene clusters that mediate the biosynthesis of both
CC       ascochlorin and ascofuranone, a strong inhibitor of cyanide-insensitive
CC       alternative oxidases and a promising drug candidate against African
CC       trypanosomiasis (PubMed:30952781). Binds the 5'-CGGYGNNTTW-3' motif
CC       within promoters of the target genes (Probable).
CC       {ECO:0000269|PubMed:30952781, ECO:0000305|PubMed:30952781}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- INDUCTION: Expression is induced on AF medium.
CC       {ECO:0000269|PubMed:30952781}.
CC   -!- BIOTECHNOLOGY: Ascofuranone is a specific inhibitor of trypanosome
CC       alternative oxidase (TAO), and quickly kills African trypanosomes in
CC       vitro and cures infected mice. As an essential factor for trypanosome
CC       survival, TAO is a promising drug target due to the absence of
CC       alternative oxidases in the mammalian host.
CC       {ECO:0000269|PubMed:12084465, ECO:0000269|PubMed:12798927,
CC       ECO:0000269|PubMed:20688188}.
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; LC406756; BBF25312.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A455R614; -.
DR   SMR; A0A455R614; -.
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; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..512
FT                   /note="Ascofuranone/ascochlorin biosynthesis clusters
FT                   transcription regulator"
FT                   /id="PRO_0000448997"
FT   DNA_BIND        14..49
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          54..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  55269 MW;  F14D78E599CA23D7 CRC64;
     MGNSANEDKL RYACDRCHSQ KLRCPRSVEP EKANPEEPCS RCRKAGVPCV VSLRGKVGRP
     SKATKKKSAR SPRATSTPEA EFPPYDINSV LSGEVDGSIP WASPSGDRMM DMFDLASGSG
     SVTTSASPKT MAEDYQPEGQ RPFPDPLMGP GLIQVPYEPF LMEFDTDADY PTFCIPPSLT
     DMPAGVEFNQ PQDKTFNSSQ MDSFMDVKTD ASMMMPHADM DMTSPKGTGP TIDPVTVDPR
     MSFSAHAAQS PGDIFASDDF EAGAEFSSTA SYQKLSDLNL RILQCGSTAQ AGTAPQNSSQ
     LLKDVVGFSG ELIDIARQSM PHFVGCTRSS SRASTTSKGS SMESDEGDGS IDTAFSQSSW
     GSLKPGSASG PQATSQSVPE SAVIFLLLGC YTQILHLFEL TTNCLWAQHC EAGQPAPQND
     DTSGTIGSLL EASIAIHTVT YLLSRLHRAL AAPEMDASTD AADSHGWKKS FVGGKELEDG
     LLGRAFGEIR EREQWLMRRT KHLQQRINKC HI