ID   ACTTR_ALTAL             Reviewed;         435 AA.
AC   Q589W9;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Transcription activator ACTTR {ECO:0000303|Ref.1};
DE   AltName: Full=ACT-toxin biosynthesis regulator {ECO:0000303|Ref.1};
GN   Name=ACTTR {ECO:0000303|Ref.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SH20;
RA   Masunaka A., Ishikura K., Asada K., Ohtsuki R., Tanaka A., Tsuge T.,
RA   Peever T.L., Timmer L.W., Yamamoto M., Yamamoto H., Akimitsu K.;
RT   "The pathway-specific regulatory protein ACTTR in the tangerine pathotype
RT   of Alternaria alternata activates ACTT3 required for ACT-toxin
RT   biosynthesis.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SH20;
RX   PubMed=19271978; DOI=10.1094/phyto-99-4-0369;
RA   Miyamoto M., Ishii Y., Honda A., Masunaka A., Tsuge T., Yamamoto M.,
RA   Ohtani K., Fukumoto T., Gomi K., Peever T.L., Akimitsu K.;
RT   "Function of genes encoding acyl-CoA synthetase and enoyl-CoA hydratase for
RT   host-selective act-toxin biosynthesis in the tangerine pathotype of
RT   Alternaria alternata.";
RL   Phytopathology 99:369-377(2009).
RN   [3]
RP   REVIEW ON HOST-SELECTIVE TOXINS.
RX   PubMed=22846083; DOI=10.1111/j.1574-6976.2012.00350.x;
RA   Tsuge T., Harimoto Y., Akimitsu K., Ohtani K., Kodama M., Akagi Y.,
RA   Egusa M., Yamamoto M., Otani H.;
RT   "Host-selective toxins produced by the plant pathogenic fungus Alternaria
RT   alternata.";
RL   FEMS Microbiol. Rev. 37:44-66(2013).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       gene clusters that mediate the biosynthesis of the host-selective
CC       toxins (HSTs) ACT-toxins responsible for brown spot of tangerine
CC       disease by the tangerine pathotype which affects tangerines and
CC       mandarins (Probable). ACT-toxins consist of three moieties, 9,10-epoxy-
CC       8-hydroxy-9-methyl-decatrienoic acid (EDA), valine and a polyketide
CC       (PubMed:22846083). ACT-toxin I is toxic to both citrus and pear; toxin
CC       II the 5''-deoxy derivative of ACT-toxin I, is highly toxic to pear and
CC       slightly toxic to citrus (PubMed:22846083). On cellular level, ACT-
CC       toxins affect plasma membrane of susceptible cells and cause a sudden
CC       increase in loss of K(+) after a few minutes of toxin treatment
CC       (PubMed:22846083). {ECO:0000303|PubMed:22846083, ECO:0000305|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- MISCELLANEOUS: Gene clusters encoding host-selective toxins (HSTs) are
CC       localized on conditionally dispensable chromosomes (CDCs), also called
CC       supernumerary chromosomes, where they are present in multiple copies
CC       (PubMed:22846083). The CDCs are not essential for saprophytic growth
CC       but controls host-selective pathogenicity (PubMed:22846083).
CC       {ECO:0000303|PubMed:22846083}.
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DR   EMBL; AB176851; BAD93200.1; -; Genomic_DNA.
DR   EMBL; AB176941; BAD93202.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q589W9; -.
DR   SMR; Q589W9; -.
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; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..435
FT                   /note="Transcription activator ACTTR"
FT                   /id="PRO_0000444840"
FT   DNA_BIND        16..43
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          48..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  47745 MW;  1D76E5AEF9C2FB76 CRC64;
     MLQCAPKKNE RLRGSCDFCT QSKLRCNKNK PSCRRCTIQQ QPCVYSVARR TGRPPKRPRK
     ANDGQEANEQ HGDQDPVTST PGGSCQQQSN HLLDVEGDGA NFTLADASTT AQDRETAACT
     ALDNALLMGG TFGFSSLLDD PLIQSDDFLS FSLCMPPGEE EGHMASPCSP PILPSIDVPH
     LPARFGFLES SVESGLHGRN GPHLIEQPDK TVPSSFSEME KIYDEGLTFS GLDSAINAVT
     NNGKGEPSIP GTMAAHPHSK RQCFCSTSMS KLQMLVSHPT LCQKNSRARF DMTLFLEEVV
     FSIYRDVLQC LVCQSKSLHS LASLCICTDW VIEALRDVAQ DLSSGQDNLG GFRAGLCPPK
     DKFSICVGRF VLDDQLRESC TRSLVRYRLR KLIPIMDTMM KLNYRGAGGA LSQAIRTMVE
     DVRHKIESAL GMMEL