ID   AZPA6_ASPTN             Reviewed;         166 AA.
AC   Q0CRP6;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Transcriptional regulator ATEG_03638 {ECO:0000303|PubMed:31908094};
DE   AltName: Full=Azasperpyranone A biosynthesis cluster A protein ATEG_03638 {ECO:0000303|PubMed:31908094};
GN   ORFNames=ATEG_03638;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=24412543; DOI=10.1016/j.chembiol.2013.12.005;
RA   Wang M., Beissner M., Zhao H.;
RT   "Aryl-aldehyde formation in fungal polyketides: discovery and
RT   characterization of a distinct biosynthetic mechanism.";
RL   Chem. Biol. 21:257-263(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=23621425; DOI=10.1021/ja401945a;
RA   Chiang Y.M., Oakley C.E., Ahuja M., Entwistle R., Schultz A., Chang S.L.,
RA   Sung C.T., Wang C.C., Oakley B.R.;
RT   "An efficient system for heterologous expression of secondary metabolite
RT   genes in Aspergillus nidulans.";
RL   J. Am. Chem. Soc. 135:7720-7731(2013).
RN   [4]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RX   PubMed=31908094; DOI=10.1002/anie.201915514;
RA   Huang X., Zhang W., Tang S., Wei S., Lu X.;
RT   "Collaborative biosynthesis of a class of bioactive azaphilones by two
RT   separate gene clusters containing four PKS/NRPSs with transcriptional
RT   cosstalk in fungi.";
RL   Angew. Chem. Int. Ed. 59:4349-4353(2020).
CC   -!- FUNCTION: Specific transcriptional regulator for the azasperpyranone A
CC       biosynthesis cluster A. {ECO:0000269|PubMed:31908094}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC   -!- INDUCTION: Expression is induced by the azasperpyranone transcriptional
CC       regulator ATEG_07667. {ECO:0000269|PubMed:31908094}.
CC   -!- DISRUPTION PHENOTYPE: Results in the significant down-regulation of
CC       cluster A, whereas it exerts no influence on cluster B.
CC       {ECO:0000269|PubMed:31908094}.
CC   -!- BIOTECHNOLOGY: Azasperpyranones display potential anti-cancer
CC       activities (PubMed:31908094). Azasperpyranones A, C, D, and F exhibit
CC       potent growth-inhibitory activity against the A549, HepG2, HCT-116, and
CC       HL-60 cell lines, with IC(50) values of 2.39-14.42 mm, respectively
CC       (PubMed:31908094). Moreover, azasperpyranone D significantly inhibits
CC       HCT-116 xenograft tumor growth in BALB/c-nu mice (PubMed:31908094). In
CC       addition, azasperpyranones A and C can bind with four kinds of
CC       therapeutic targets for cancer, eEF2K, FGFR, survivin, and TNF-a
CC       (PubMed:31908094). {ECO:0000269|PubMed:31908094}.
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DR   EMBL; CH476598; EAU35440.1; -; Genomic_DNA.
DR   RefSeq; XP_001212816.1; XM_001212816.1.
DR   AlphaFoldDB; Q0CRP6; -.
DR   SMR; Q0CRP6; -.
DR   STRING; 341663.Q0CRP6; -.
DR   EnsemblFungi; EAU35440; EAU35440; ATEG_03638.
DR   GeneID; 4318498; -.
DR   VEuPathDB; FungiDB:ATEG_03638; -.
DR   eggNOG; KOG0048; Eukaryota.
DR   HOGENOM; CLU_1602357_0_0_1; -.
DR   OrthoDB; 219341at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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   CDD; cd00167; SANT; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   Pfam; PF00249; Myb_DNA-binding; 2.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51294; HTH_MYB; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Membrane; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..166
FT                   /note="Transcriptional regulator ATEG_03638"
FT                   /id="PRO_0000450089"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          56..83
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DOMAIN          84..138
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        111..134
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
SQ   SEQUENCE   166 AA;  18497 MW;  728CC781AC319C96 CRC64;
     MESAMTPYVV GFSLDGLVIC YLFGVPCMLQ EVASAAPFRL GPGTCETDRS TSQTQGSVSW
     HEIASFLPGR TNKDCRKRWY GTTATKVNKG PWTEEEDERL GKAVQHHGTK WAVVASVVGT
     RLPDQCSKRW MHALNPEIDH SPWTPEEVVF ACSFSPKDFV FLMHAC