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Database: UniProt
Entry: A0A395SJD4_FUSSP
LinkDB: A0A395SJD4_FUSSP
Original site: A0A395SJD4_FUSSP 
ID   A0A395SJD4_FUSSP        Unreviewed;      1024 AA.
AC   A0A395SJD4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=2og-fe oxygenase superfamily {ECO:0000313|EMBL:RGP72179.1};
GN   ORFNames=FSPOR_2851 {ECO:0000313|EMBL:RGP72179.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP72179.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP72179.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP72179.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RGP72179.1}.
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DR   EMBL; PXOF01000036; RGP72179.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395SJD4; -.
DR   STRING; 5514.A0A395SJD4; -.
DR   Proteomes; UP000266152; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR47256:SF1; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR   PANTHER; PTHR47256; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 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   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          390..422
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50048"
FT   REGION          354..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1024 AA;  115807 MW;  A7C9C9B02D42E84C CRC64;
     MPSATQLYQY NHVPETKANL DWADLPTIDL SLYGTESGNA ELAETLIEAI RTKGFFYVTN
     YGISQEEVDT QFALGQHFYE LPLEEKIKYQ PNLEAGDYNG YRPAGRRVLS GGIKDKTEVW
     NMATNDGRIT QPLPELLQKN KTLIENFSKD LHDKVLDPLL HLIAIALELP ADFFTKLHQW
     NVHDESHLRY MKYSKFSPEE REKLSDGLWS LGHTDLGTIT LLFRQPVAAL QIKDHKTGEW
     KWAKPLDGSL TVNTCDALSF LTGGYIKSTV HRVSAPPKDQ EHVDRLGLLY FARPQNDLVL
     NTIDSPVLKR AGYTQNEFEA GNHKVPTMGE FTTLKQTWQQ KRGKVYKEED GAEILPGFQG
     PDQQDPAPSD NGSNGPGRQL VSKRKHTPTA CGVCRRRKTR CGGERPTCFA CIRNGRSAEC
     TYETKPTETK SQALKRKYSA ADGENNIHRR FVDILRTHPA QDVNDILNRL RGGASVDELV
     RHIESGDVLL ELSVAPEVLW RNNPGNLSNI PDLLKTAGNP YVRSLIYQWK FDSSIPARPR
     PPMMGLHALY NAPYHTATMV SSIIDNCEPS KWTTVSKDDE LLREILRHYF TSIYIFFPFF
     HKDYFLYDML HERRRFCSSL LVNTVLAAGC YKFLSEARRL WELSAGERTI TRVQAAIALN
     FEHGLNGQDK LGFSLCITAV ALAQDLGLFD DYPATMSNAQ RAVRTMTAWA LFASQSLQSY
     HHEKPPLITS PPSIALPTAD GDFGEIWLKY AASHSPIPIR FSDMFITLAK FRTVLNEIAD
     RLYSPANSDK VVNIYEASIF YRRLQGWYRE LPSHLDAFNL VFPAHFNMHM HYWLVVERLF
     TPHIAEASSS SPITLAINPG KIVDDARICM RTLIRLFYGS HGDDGYELFG IITAQHVGFA
     ALERISTMQQ ATERSLQEAN DSDALISACI LRGQGRMALF GDMVFRVMYK FAPLDLASKI
     SRFTNITKDD NTSTPLPPVQ GEWPMYVGDI QQKDDRRVGN LLRAMAEISV EDRDSGEEEE
     EASI
//
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