ID AKTR2_ALTAL Reviewed; 435 AA. AC Q9P4U8; DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 22-FEB-2023, entry version 74. DE RecName: Full=Transcription activator AKTR-2 {ECO:0000303|PubMed:10975654}; DE AltName: Full=AK-toxin biosynthesis regulator 2 {ECO:0000303|PubMed:10975654}; GN Name=AKTR-2 {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], AND FUNCTION. 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: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:10975654). The CDCs are not essential for saprophytic growth CC but controls host-selective pathogenicity (PubMed:10975654). CC {ECO:0000269|PubMed:10975654}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB035493; BAB07812.1; -; Genomic_DNA. DR AlphaFoldDB; Q9P4U8; -. DR SMR; Q9P4U8; -. 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; Zn(2)-C6 fungal-type DNA-binding domain; 1. DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd. DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf. DR PANTHER; PTHR31069:SF31; ARGININE METABOLISM REGULATION PROTEIN II; 1. DR PANTHER; PTHR31069; OLEATE-ACTIVATED TRANSCRIPTION FACTOR 1-RELATED; 1. DR Pfam; PF00172; Zn_clus; 1. DR PRINTS; PR00755; AFLATOXINBRP. DR SMART; SM00066; GAL4; 1. DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 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 AKTR-2" FT /id="PRO_0000444842" FT DNA_BIND 16..43 FT /note="Zn(2)-C6 fungal-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227" FT REGION 49..103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 70..89 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 435 AA; 48235 MW; AAD028C78F51A1C9 CRC64; MLQCAPKKNE RLRGSCDFCT QSKLRCNKNK PSCRRCTIQQ QVCVYSVARR TGRPPKHPRR ADDSQETSGQ HGHQDPMTSA PADSCEQQSS HLDLEGDDTD FTLVDGRTTA EGRATVAPPV LDNAFLMGET FEFNSLLDDP LVQSEDIFSF SPHIPRGEKG VHMASFHALN ESTSPCSPSA LLSIDVPQLP TNFRFLESFI GSELHGRNEP HPVEQPDEME KTYDKGSILL GLDSAINAIT NNGKDEPSIS GWTVARPHSK HLCFCSMSMS KLQVLVSHPA LCRQNSRTPF DMVLFLEEFV FGIHSDVLRC LICQSRSLHS LASLCICTDW VVEALVDVAQ DLSLGQDNLG GLRAEICPPK NGSSIYVGRL ILADQFRESC TRSLVKYRLR KLIPIMDTMI KLNYRGAGGA LSQAIRTMVE DVRHKIESAL GMMEL //