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Database: UniProt
Entry: APF2_GIBF5
LinkDB: APF2_GIBF5
Original site: APF2_GIBF5 
ID   APF2_GIBF5              Reviewed;         389 AA.
AC   S0DPL8;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Apicidin F cluster transcription factor apf2 {ECO:0000303|PubMed:25058475};
DE   AltName: Full=Apicidin F synthesis protein 2 {ECO:0000303|PubMed:25058475};
GN   Name=apf2 {ECO:0000303|PubMed:25058475}; ORFNames=FFUJ_00012;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=24195442; DOI=10.1021/np4006053;
RA   von Bargen K.W., Niehaus E.M., Bergander K., Brun R., Tudzynski B.,
RA   Humpf H.U.;
RT   "Structure elucidation and antimalarial activity of apicidin F: an
RT   apicidin-like compound produced by Fusarium fujikuroi.";
RL   J. Nat. Prod. 76:2136-2140(2013).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND SUBCELLULAR LOCATION.
RX   PubMed=25058475; DOI=10.1371/journal.pone.0103336;
RA   Niehaus E.M., Janevska S., von Bargen K.W., Sieber C.M., Harrer H.,
RA   Humpf H.U., Tudzynski B.;
RT   "Apicidin F: characterization and genetic manipulation of a new secondary
RT   metabolite gene cluster in the rice pathogen Fusarium fujikuroi.";
RL   PLoS ONE 9:E103336-E103336(2014).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       gene cluster that mediates the biosynthesis of apicidin F
CC       (PubMed:23825955, PubMed:25058475). Binds to the eight-base-pair motif
CC       5'-TGACGTGA-3' called the 'Api-box' that is found in all promoters of
CC       the apicidin F cluster except in the promoter region of apf2 itself
CC       (PubMed:25058475). {ECO:0000269|PubMed:23825955,
CC       ECO:0000269|PubMed:25058475}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25058475}.
CC   -!- DOMAIN: Contains a basic DNA-binding region at the N-terminus which is
CC       usually found in bZIP transcription factors, but does not contain the
CC       characteristic leucine zipper domain (PubMed:25058475). Instead, four
CC       C-terminal ankyrin repeats were identified that were shown to confer
CC       protein-protein interaction of regulatory proteins (PubMed:25058475).
CC       {ECO:0000305|PubMed:25058475}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the loss of apicidin F production
CC       (PubMed:25058475). {ECO:0000269|PubMed:25058475}.
CC   -!- BIOTECHNOLOGY: Apicidin F, like the other known apicidins, is a cyclic
CC       tetrapeptides with anti-malarial properties via histone deacetylase
CC       inhibitory activity (PubMed:24195442). {ECO:0000269|PubMed:24195442}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Highly divergent.
CC       {ECO:0000305}.
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DR   EMBL; HF679023; CCT63352.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0DPL8; -.
DR   SMR; S0DPL8; -.
DR   STRING; 1279085.S0DPL8; -.
DR   EnsemblFungi; CCT63352; CCT63352; FFUJ_00012.
DR   VEuPathDB; FungiDB:FFUJ_00012; -.
DR   HOGENOM; CLU_709899_0_0_1; -.
DR   OrthoDB; 1880983at2759; -.
DR   Proteomes; UP000016800; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd14688; bZIP_YAP; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR24178:SF9; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   ANK repeat; DNA-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..389
FT                   /note="Apicidin F cluster transcription factor apf2"
FT                   /id="PRO_0000437168"
FT   REPEAT          241..270
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          274..303
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          307..336
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          357..386
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          12..38
FT                   /note="Basic DNA-binding region"
FT                   /evidence="ECO:0000305|PubMed:25058475"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  42375 MW;  C1A6BA2C2EE4CD1B CRC64;
     MSPPSQDWST ITDANERRKA QNRVAQRNYR SRQKLRVELA EAILYDMPSW RTAVGLKRKR
     WLETPQSVED HDTNPDSATP KPSLSSQVIQ YHEEGQLVQN PTDFSMSADA DVTADVSSGG
     ESSDLSLGVF TPGDDWMNAE IDWTAAMTLA GDTSASEPDL RHRAVGPGND IHAQPPVSIP
     VQAASGQHRT LTAPTPAESM SLRTEPPETA VITVTSNREV PNLGDSNEGS RSISTTKQPS
     EFKTPVLTAI AKGKLDIARL LISSGANIDT RDMHGRTNLH YAVSRSDAKT VRSLLELGAD
     LLMSDASGVT ALHMAVGADD QDMVKLLLGW CEQQDRTASS TDHKTTLKQC INSRDGQNMT
     PLHLCVVMER MDMLKILLDY GADVNIGCD
//
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