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Database: UniProt
Entry: A0A428U2V8_9HYPO
LinkDB: A0A428U2V8_9HYPO
Original site: A0A428U2V8_9HYPO 
ID   A0A428U2V8_9HYPO        Unreviewed;       935 AA.
AC   A0A428U2V8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0000259|PROSITE:PS50048};
GN   ORFNames=CEP52_004545 {ECO:0000313|EMBL:RSM08595.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM08595.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM08595.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM08595.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:RSM08595.1}.
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DR   EMBL; NKCK01000033; RSM08595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428U2V8; -.
DR   STRING; 1325735.A0A428U2V8; -.
DR   Proteomes; UP000287144; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR48075:SF3; 3-HYDROXYACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287144}.
FT   DOMAIN          14..54
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50048"
FT   REGION          61..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  103722 MW;  6476F5AE0D76CBE1 CRC64;
     MPGGLVTRRT QFSSCDECRR SRVACDAAQS RNAAAGEAPA SCTRCRNRHK SCTFKWIQDA
     KASGSGNTSG GVKRKGRRRI ASHHPSSDTS STQGSRASAG NEGFVLGSER GAHRESVTTS
     VLSTPFVAPS PTYSTITAQN TGLLSEADSR WLETLYREGF EAVFGSWMGR YSCPFLFGHN
     LADKYVSISD LCCHLDGCMA DAAANNGQSP GRGSERCCLI EQSLQRTIAS FSARWLPISS
     RTALSENDHR VLVQALWRHA RRDMLRIINR PSYRSMLSLL LFALTPIPDG ISEEEEADGI
     SGQACVHAAL QQIQTLRARQ KNLQFSGSKV SPSLKSQGIV TTPESIETSG FINAESTAYW
     AALTFDTSAS LTLNCRPLLS SGLFGFESEL PWRLVRTCAK MFDETAKHWS RGSSDMTDER
     ANQIIAAGAS WKLLGWKLTA IFKEALRDGH DESEVRKAYL AVVDSIKQFG TVYRPLLDEC
     HKRMQFLGQQ TKLRWFSLML HYHLSILMLV DVMEVTDRHD LLADIADIST DAENTVMNTL
     AFGLHNTFTL RRPPDPDTLG QEGPRDTTFT VPIVSIDPYP HHAVAGVQLL RKAIDRDFGV
     GKITDETYQS LLSTLERTLK HLPQSSKSVQ AAIAKFSLGI YPEFDCSLIF IDKMVLSVTP
     KTSVALIGAG TQGRRLAFMW SSRGNDVHLV DGQETQLEAS LKAIDDFQKD SGKKNSQWGR
     IITHSPKTLR EALKTAWLVV ECVPEQLALK QKVIVELDAL AGEDTIIASN SSSYSCSEIL
     EGISLKNERR FLSAHSYWPP ETPEIEIMGH ETTNPSYIPL MMEQCKAHGF SPFQVKTPSM
     GYIYNRIWAA IKREALLAAS EGVATPEEID AMFKGILKTP KGPFEQMDVV GLDVVLDIEQ
     HYADARGDIP SAPREYLQKV SREWTSWCQE WTWFL
//
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