ID   AKTR1_ALTAL             Reviewed;         444 AA.
AC   Q9P4V0;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Transcription activator AKTR-1 {ECO:0000303|PubMed:10975654};
DE   AltName: Full=AK-toxin biosynthesis regulator 1 {ECO:0000303|PubMed:10975654};
GN   Name=AKTR-1 {ECO:0000303|PubMed:10975654};
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=15A;
RX   PubMed=10975654; DOI=10.1094/mpmi.2000.13.9.975;
RA   Tanaka A., Tsuge T.;
RT   "Structural and functional complexity of the genomic region controlling AK-
RT   toxin biosynthesis and pathogenicity in the Japanese pear pathotype of
RT   Alternaria alternata.";
RL   Mol. Plant Microbe Interact. 13:975-986(2000).
RN   [2]
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) AK-toxins responsible for Japanese pear black spot
CC       disease by the Japanese pear pathotype (Probable). AK-toxins are esters
CC       of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA)
CC       (PubMed:22846083). On cellular level, AK-toxins affect plasma membrane
CC       of susceptible cells and cause a sudden increase in loss of K(+) after
CC       a few minutes of toxin treatment (PubMed:22846083).
CC       {ECO:0000303|PubMed:22846083, ECO:0000305|PubMed:10975654}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of AF-toxins and their
CC       precuror 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid; and impairs
CC       the pathogenicity. {ECO:0000269|PubMed:10975654}.
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:10975654). The CDCs are not essential for saprophytic growth
CC       but controls host-selective pathogenicity (PubMed:10975654).
CC       {ECO:0000269|PubMed:10975654}.
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DR   EMBL; AB035491; BAB07810.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P4V0; -.
DR   SMR; Q9P4V0; -.
DR   PHI-base; PHI:2831; -.
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   4: Predicted;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..444
FT                   /note="Transcription activator AKTR-1"
FT                   /id="PRO_0000444841"
FT   DNA_BIND        16..43
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          49..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  48406 MW;  FF080D7F10250032 CRC64;
     MLQCAPKKNE RLRGSCDFCT QSKLRCNKNK PSCRRCTIQQ QPCVYSVARR TGRPPKHPRK
     ANDCQEANGQ HGEQDPVTST PGGSCQQQSN HLLDVEGDGA NFTLADASTT AQGRETAASS
     ALDNALLVGE TFGFSSLLDD PLIQSDDFLS FSLCMPPGEE EGHMASPRAL NGSTGPCSPT
     VLSSIDVPHL PARFGFLESS VESGLHGRTG PHLVEQPDKI VPSSFSEMEK IYDEGLTFSG
     LDSAINAVTN NGKGEPSASG TMAAHPHSKR QCFCSTSMSK LQMLISHPTL CQKNSRARFD
     MTLFLEEVVF NIHRDVLQCL VCQSKSLHSL ASLCICTDWV IEALRDVAQD LSSGQDNLGG
     FRAGLCPPKD KFSICVGRFV LDDQLRESCT RSLVKYRLRK LVPIMDTMMK LNYRGAGGAL
     SQAIRTMVED VRHKIESALG MMEL