ID   ACRR_ASPA1              Reviewed;         631 AA.
AC   A0A1L9WQN2;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Acurin A biosynthesis cluster transcription regulator {ECO:0000303|PubMed:32234543};
DE   AltName: Full=Acurin A biosynthesis cluster protein R {ECO:0000303|PubMed:32234543};
GN   Name=acrR {ECO:0000303|PubMed:32234543}; ORFNames=ASPACDRAFT_122290;
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=32234543; DOI=10.1016/j.fgb.2020.103378;
RA   Wolff P.B., Nielsen M.L., Slot J.C., Andersen L.N., Petersen L.M.,
RA   Isbrandt T., Holm D.K., Mortensen U.H., Noedvig C.S., Larsen T.O.,
RA   Hoof J.B.;
RT   "Acurin A, a novel hybrid compound, biosynthesized by individually
RT   translated PKS- and NRPS-encoding genes in Aspergillus aculeatus.";
RL   Fungal Genet. Biol. 139:103378-103378(2020).
CC   -!- FUNCTION: Transcription factor that positively regulates the expression
CC       of the cluster that mediates the biosynthesis of acurin A, a highly
CC       reduced polyketide coupled to a serine via a peptide bond.
CC       {ECO:0000269|PubMed:32234543}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of acurin A.
CC       {ECO:0000269|PubMed:32234543}.
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DR   EMBL; KV878980; OJJ98493.1; -; Genomic_DNA.
DR   RefSeq; XP_020054833.1; XM_020196522.1.
DR   AlphaFoldDB; A0A1L9WQN2; -.
DR   SMR; A0A1L9WQN2; -.
DR   EnsemblFungi; OJJ98493; OJJ98493; ASPACDRAFT_122290.
DR   GeneID; 30970336; -.
DR   VEuPathDB; FungiDB:ASPACDRAFT_122290; -.
DR   OrthoDB; 1622631at2759; -.
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   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; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..631
FT                   /note="Acurin A biosynthesis cluster transcription
FT                   regulator"
FT                   /id="PRO_0000450427"
FT   DNA_BIND        30..62
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  68135 MW;  85C17D97382FAD81 CRC64;
     MSPNMSLTAS HPQQPQPTPQ SKAQLTRQAC NRCHASKLKC LRPPGVTTSK SCIRCIKADT
     ECVYDPPQRF GRPRQKSRPQ PESVPPRIEA REPEVTDPRR ARHGSTIGAR WESSERESNG
     SLAPSSAAES PYTAAESPDN RSSAAVAAAP LVGMDYASSH FPEPLESERT SELLDAFQSE
     SMQLDVDSYW GETDPVMPPA ATVPYSDLLT GPIDLDFTVS DQDDRAKIPK HALDPALSGA
     DTGSTADDYV LDLVQLQASV NQNNRELAAM IRKAQSALGM SDGRVGQALP IPDSQFKTHL
     QRNLKASEQT LDVLHRINSQ FAPVSRETRP PSRSYGLDPT LDRLYADCVS QDHAFGVGGD
     ELGVRATTPP GVSAADPQHS ILAFLVLTTY LRLLHNFDAL ISILQDRLRC SASLDPRRPL
     HLSEDISASD SSSNPLLDVS LGSFSFSSSS ARSLQAMLNV QMINTVLTKI KSSTQRMLLG
     PDYLPPSSCS SSASTSSTAS TTSCSTRAPP SSATGGAHHP ATAGSIFFHH AHSHSHSSSD
     HLFSQPEGRG YAPYNHAFHP PPPSRHTHNY PTPETITPPS SVLGGVSGTT PPPFVSGVDH
     VVRRALTEVQ ELELSLRNRA RAIQQWSEEG F