ID   FYV10_PHANO             Reviewed;         405 AA.
AC   Q0TYW1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Protein FYV10;
GN   Name=FYV10; ORFNames=SNOG_15382;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Involved in the proteasome-dependent degradation of fructose-
CC       1,6-bisphosphatase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FYV10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT77315.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445361; EAT77315.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001805532.1; XM_001805480.1.
DR   AlphaFoldDB; Q0TYW1; -.
DR   SMR; Q0TYW1; -.
DR   STRING; 13684.SNOT_15382; -.
DR   GeneID; 5982461; -.
DR   KEGG; pno:SNOG_15382; -.
DR   eggNOG; KOG0396; Eukaryota.
DR   InParanoid; Q0TYW1; -.
DR   OrthoDB; 1087488at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:UniProt.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR013144; CRA_dom.
DR   InterPro; IPR024964; CTLH/CRA.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR027714; Fyv10/MAEA.
DR   InterPro; IPR045098; Fyv10_fam.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR044063; ZF_RING_GID.
DR   PANTHER; PTHR12170; PTHR12170; 1.
DR   PANTHER; PTHR12170:SF2; PTHR12170:SF2; 1.
DR   Pfam; PF10607; CLTH; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00668; CTLH; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS51867; ZF_RING_GID; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..405
FT                   /note="Protein FYV10"
FT                   /id="PRO_0000292464"
FT   DOMAIN          124..156
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          162..220
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   ZN_FING         326..387
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
SQ   SEQUENCE   405 AA;  45418 MW;  0F7ABAF92AA89179 CRC64;
     MAELTSMKLN AESHLLLDQP LLRMPYELSR RNFKNAQRVI EHSSANMTTS LAAATKAASK
     SASPDATLDS LDAMISKMQV LKRKLEGLHE EETRIHKSAK ARLRHLQDLY DVNSLVDVKY
     DEWSRTRLSR LLVDYLLREG YSESAAHLAQ SKEIEDLVDV DAFIACHKIE RSLREGMSTS
     LALDWCKEHS KELKKGGSML EFELRLQQYI ELVRQGGETK LVEARVHAKK YLSTSGDFEL
     LRKAAGLLAY KPWDDVEPYV SLYSPSRWAH LANLFLSTHH NLYSLPPRPL LHIALSAGLS
     ALKTPACHSA YTSSSANASS ATTSVCPICS TELNELARNV PYAHHTKSIV KNDPVVLPNG
     RIYGRDQLTA FNKKVGTESG WVRDPVDGIK GEAWSESEVR KVYIM