ID   ACLZ_ASPOR              Reviewed;         474 AA.
AC   Q2UPC3;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=C6 finger domain transcription factor aclZ {ECO:0000303|PubMed:25302411};
DE   AltName: Full=Aspirochlorine biosynthesis protein Z {ECO:0000303|PubMed:25302411};
GN   Name=aclZ {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000029;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=25302411; DOI=10.1002/anie.201407624;
RA   Chankhamjon P., Boettger-Schmidt D., Scherlach K., Urbansky B., Lackner G.,
RA   Kalb D., Dahse H.M., Hoffmeister D., Hertweck C.;
RT   "Biosynthesis of the halogenated mycotoxin aspirochlorine in koji mold
RT   involves a cryptic amino acid conversion.";
RL   Angew. Chem. Int. Ed. 53:13409-13413(2014).
CC   -!- FUNCTION: Transcription factor that specifically regulates the gene
CC       cluster that mediates the biosynthesis of aspirochlorine (or antibiotic
CC       A30641), an unusual halogenated spiro compound with distinctive
CC       antifungal properties due to selective inhibition of protein
CC       biosynthesis, and which is also active against bacteria, viruses, and
CC       murine tumor cells (PubMed:25302411). {ECO:0000305|PubMed:25302411}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; AP007154; BAE56592.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UPC3; -.
DR   EnsemblFungi; BAE56592; BAE56592; AO090001000029.
DR   HOGENOM; CLU_050742_0_0_1; -.
DR   Proteomes; UP000006564; Chromosome 2.
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..474
FT                   /note="C6 finger domain transcription factor aclZ"
FT                   /id="PRO_0000441211"
FT   DNA_BIND        42..69
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          85..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  51594 MW;  480F8655A08DF438 CRC64;
     MSFIPVEHIA CSTAKLPSSR CPLLLLQPNG SSTKPVRWRS ACNQCHAAKV RCSGERTGCD
     RCNNLQYQCV YAISRVGKVP GVRARGNKAV RTTTEALQRP ATASTLPDAD STGEFQTDQR
     SENDPLSRSD FGEQDAAHDA LSPKSHSALF PDWTEASDKS LNAYETADLF ILPSQLMSSD
     QDPSRSRGHS LQAPSHSGHS IADSHTAAMP DGGLFCPFNK PTTPIPALPD LDLHIQDFHP
     MDVPVSPLDN GPPVKRRPYS DASCGHSGHS SKGYMSSTFP YSELLSQIGC QTDCGRQPHH
     YNYRSWTVLI CNRIVEFLEH RIQGGVVALD VVMQTNKVTL GEISRILSKG AHKEGSNCAM
     LLLIAIDQIV TLFECGVKQG SPGDSDRASI GGRDLSALGD DLTGGNVLPN LRFGLFQINQ
     DEQLALRSYL LQRELQRCLQ VLTNLRDAIP LEPNPCTALE ARVKKLCSAI ADSH