ID   AACUS_ASPA1             Reviewed;         429 AA.
AC   A0A1L9WLK0;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Transcriptional coactivator AacuS {ECO:0000303|PubMed:28196534};
DE   AltName: Full=Secalonic acid biosynthesis cluster protein S {ECO:0000303|PubMed:30996871};
GN   Name=AacuS {ECO:0000303|PubMed:30996871}; ORFNames=ASPACDRAFT_6036;
OS   Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=690307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 16872 / CBS 172.66 / WB 5094;
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=28253713; DOI=10.4149/neo_2017_304;
RA   Gao X., Sun H.L., Liu D.S., Zhang J.R., Zhang J., Yan M.M., Pan X.H.;
RT   "Secalonic acid- F inhibited cell growth more effectively than 5-
RT   fluorouracil on hepatocellular carcinoma in vitro and in vivo.";
RL   Neoplasma 64:344-350(2017).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=29248948; DOI=10.1007/s00284-017-1411-y;
RA   Yodsing N., Lekphrom R., Sangsopha W., Aimi T., Boonlue S.;
RT   "Secondary Metabolites and Their Biological Activity from Aspergillus
RT   aculeatus KKU-CT2.";
RL   Curr. Microbiol. 75:513-518(2018).
RN   [4]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=30996871; DOI=10.1039/c8sc05126g;
RA   Greco C., de Mattos-Shipley K., Bailey A.M., Mulholland N.P., Vincent J.L.,
RA   Willis C.L., Cox R.J., Simpson T.J.;
RT   "Structure revision of cryptosporioptides and determination of the genetic
RT   basis for dimeric xanthone biosynthesis in fungi.";
RL   Chem. Sci. 10:2930-2939(2019).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=30678274; DOI=10.3390/molecules24030393;
RA   Xie L., Li M., Liu D., Wang X., Wang P., Dai H., Yang W., Liu W., Hu X.,
RA   Zhao M.;
RT   "Secalonic Acid-F, a Novel Mycotoxin, Represses the Progression of
RT   Hepatocellular Carcinoma via MARCH1 Regulation of the PI3K/AKT/beta-catenin
RT   Signaling Pathway.";
RL   Molecules 24:0-0(2019).
RN   [6]
RP   BIOTECHNOLOGY.
RX   PubMed=33015446; DOI=10.1021/acsomega.0c02505;
RA   Farooq S., Qayum A., Nalli Y., Lauro G., Chini M.G., Bifulco G.,
RA   Chaubey A., Singh S.K., Riyaz-Ul-Hassan S., Ali A.;
RT   "Discovery of a Secalonic Acid Derivative from Aspergillus aculeatus, an
RT   Endophyte of Rosa damascena Mill., Triggers Apoptosis in MDA-MB-231 Triple
RT   Negative Breast Cancer Cells.";
RL   ACS Omega 5:24296-24310(2020).
RN   [7]
RP   FUNCTION.
RX   PubMed=33891392; DOI=10.1021/acs.jnatprod.1c00022;
RA   Wei X., Chen X., Chen L., Yan D., Wang W.G., Matsuda Y.;
RT   "Heterologous biosynthesis of tetrahydroxanthone dimers: determination of
RT   key factors for selective or divergent synthesis.";
RL   J. Nat. Prod. 84:1544-1549(2021).
CC   -!- FUNCTION: Transcriptional coactivator; part of the gene cluster that
CC       mediates the biosynthesis of the tetrahydroxanthone dimer secalonic
CC       acid D. {ECO:0000269|PubMed:30996871, ECO:0000269|PubMed:33891392}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- BIOTECHNOLOGY: Secalonic acids show unprecedented anticancer activities
CC       against various human cancer cells and might be interesting for further
CC       derivatization, targeting diseases such as cancer.
CC       {ECO:0000269|PubMed:28253713, ECO:0000269|PubMed:29248948,
CC       ECO:0000269|PubMed:30678274, ECO:0000269|PubMed:33015446}.
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DR   EMBL; KV878984; OJJ97036.1; -; Genomic_DNA.
DR   RefSeq; XP_020053376.1; XM_020203550.1.
DR   SMR; A0A1L9WLK0; -.
DR   STRING; 690307.A0A1L9WLK0; -.
DR   EnsemblFungi; OJJ97036; OJJ97036; ASPACDRAFT_6036.
DR   GeneID; 30977364; -.
DR   VEuPathDB; FungiDB:ASPACDRAFT_6036; -.
DR   OrthoDB; 817726at2759; -.
DR   Proteomes; UP000184546; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..429
FT                   /note="Transcriptional coactivator AacuS"
FT                   /id="PRO_0000453503"
FT   DOMAIN          80..144
FT                   /note="HTH iclR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   DNA_BIND        110..129
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
SQ   SEQUENCE   429 AA;  46554 MW;  599BBBAA00F11BC6 CRC64;
     MLNLAQLQSQ TRELLAALKQ LTEHCPSAVD GTTEGMIPGL SPWSTTGESG EATRARETVL
     KCLAKLQVSL AGPIDVLQHM ASQTQLLACL QWLGEFQVPA CIPLDGSASI KDVAELIGVP
     ENHICRIVRM AITAGFLQEP ELGHVAHSPL SAAFVTNPSY LDAAMFLARI TTPAALNMPS
     ITRQRTAGMC ERVNQVEQNN NIINMVTSST LDETALPRLE RQWYAYLRFG TGNLCDTATD
     IISCLNSFQG TSATVVEVGA RSLDRAMTLA NRYPTLRFII QIHLPSSASG SGKDEAKYDR
     TRAIRSHSQI TVQYRTPGTP QQIQDAAVYI INFPLPFPGV SSCSISAQLE TELRAHLQAL
     RLSPAATLVL TAPALPERGA RGTEVAVLTR IRDLSFLQLA NDREPEISEL INLLNGVGDS
     EGRFVVVKK