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Database: UniProt
Entry: S0E930_GIBF5
LinkDB: S0E930_GIBF5
Original site: S0E930_GIBF5 
ID   S0E930_GIBF5            Unreviewed;       536 AA.
AC   S0E930;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   08-NOV-2023, entry version 53.
DE   RecName: Full=Transcriptional adapter 2 {ECO:0000256|PIRNR:PIRNR025024};
GN   ORFNames=FFUJ_08807 {ECO:0000313|EMBL:CCT71145.1};
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 {ECO:0000313|EMBL:CCT71145.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., 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., Munsterkotter M., Freitag M., Humpf H.U., Guldener 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).
CC   -!- FUNCTION: Functions as component of the transcription regulatory
CC       histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is
CC       involved in RNA polymerase II-dependent transcriptional regulation.
CC       {ECO:0000256|PIRNR:PIRNR025024}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR025024}.
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DR   EMBL; HF679029; CCT71145.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0E930; -.
DR   STRING; 1279085.S0E930; -.
DR   EnsemblFungi; CCT71145; CCT71145; FFUJ_08807.
DR   VEuPathDB; FungiDB:FFUJ_08807; -.
DR   HOGENOM; CLU_018273_1_0_1; -.
DR   OrthoDB; 206414at2759; -.
DR   Proteomes; UP000016800; Chromosome 7.
DR   GO; GO:0140671; C:ADA complex; IEA:EnsemblFungi.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000124; C:SAGA complex; IEA:EnsemblFungi.
DR   GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0001786; F:phosphatidylserine binding; IEA:EnsemblFungi.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IEA:EnsemblFungi.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0035065; P:regulation of histone acetylation; IEA:InterPro.
DR   GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:EnsemblFungi.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:EnsemblFungi.
DR   CDD; cd02335; ZZ_ADA2; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR041983; ADA2-like_ZZ.
DR   InterPro; IPR016827; Ada2/TADA2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR12374:SF20; TRANSCRIPTIONAL ADAPTER 2-ALPHA; 1.
DR   PANTHER; PTHR12374; TRANSCRIPTIONAL ADAPTOR 2 ADA2 -RELATED; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR   SMART; SM00717; SANT; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
DR   PROSITE; PS51293; SANT; 1.
DR   PROSITE; PS50934; SWIRM; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR025024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR025024};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR025024}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          16..75
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          77..130
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   DOMAIN          82..126
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   DOMAIN          448..536
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          165..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  60311 MW;  E53408EEED857FA4 CRC64;
     MGVIRKKTIT RGGEGGVKYV CDVCSSDITS TVRIRCADSD CSDFDLCVSC FAKGESRNAH
     DPATHSFRVI EQNSFPIFEK EWGADEELLL LEGAEIYGLG SWADIADHIG GFREKDEVRD
     HYLSTYVDSP HFPLPKRCSP HDCELANEIP REEFQARKKR RIEERRDAAK NAPALQPKTK
     PTASVPSCHE IQGYMPGRLE FETEYANEAE EAVQLMQFDP GDGLNPRTGE LEPEMELKLT
     VMDIYNARLT QRVERKKVIF EHNLLEYREN TKLEKRRTKE ERDLLQKAKP FARMMNQQDF
     EELNQGLLDE LNLRQAITQL QEWRNMRIGD LRSGEKYENE KASRIQKAIP MGSMDRERLA
     SAQRSKQPPP PEPPSGSALL IAPELPARLL PTPAAEVNGD VKPLTNGHTD GLANGQTNGQ
     VNGVTNGING VNGVNGHAAP KQRYTAQPIS GVQPMPMTQD TAPDLHLLTP EEVKLCEIIR
     LQPKPYLMIK EQILKEALKT NGTLKKKQAK EICRLDSQKG GRIFDFFINS GWVGKA
//
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