ID   FYV10_DEBHA             Reviewed;         511 AA.
AC   Q6BYF0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Protein FYV10;
GN   Name=FYV10; OrderedLocusNames=DEHA2A10076g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382133; CAG84732.2; -; Genomic_DNA.
DR   RefSeq; XP_456769.2; XM_456769.1.
DR   AlphaFoldDB; Q6BYF0; -.
DR   SMR; Q6BYF0; -.
DR   STRING; 4959.XP_456769.2; -.
DR   PRIDE; Q6BYF0; -.
DR   EnsemblFungi; CAG84732; CAG84732; DEHA2A10076g.
DR   GeneID; 2899592; -.
DR   KEGG; dha:DEHA2A10076g; -.
DR   VEuPathDB; FungiDB:DEHA2A10076g; -.
DR   eggNOG; KOG0396; Eukaryota.
DR   HOGENOM; CLU_027445_2_0_1; -.
DR   InParanoid; Q6BYF0; -.
DR   OMA; DVKYDEW; -.
DR   OrthoDB; 1087488at2759; -.
DR   Proteomes; UP000000599; Chromosome A.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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; 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   PROSITE; PS50897; CTLH; 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..511
FT                   /note="Protein FYV10"
FT                   /id="PRO_0000292458"
FT   DOMAIN          200..258
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   ZN_FING         430..496
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT   REGION          117..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  59413 MW;  7CE6CF78F2F6ACF2 CRC64;
     MSEPTVNFHI QTRLTEFKIP TELIKKNFKA VQKQIEKQKK SIGEDVAKVK KNNKLPTAMK
     IEMINKLIKS FEIFQKRLRT SINRDEVFRS RIIARLENLS ELANYTVKTN VVLESNASPI
     DSDDNRDESS VTPKSMEDED RPLDLHNVNL INWYRDQTNL LIIDYLIKSN TRSDQNIGLQ
     LLKSISQTNP KFTKLIDYDL YDNFNKVFVS IIENHDLSLV IAWFNENRSF LKKANSNLEF
     EINYCKFLSL IEEGDVNEAI KFSQVNLSPY GNKGNYQSQE FMNHESNLNK LKEIGGLLVY
     MAINEKANAQ IDKSIPFSSS LVINSPRFKE YKKLLSNERW DSLSQCFIEN FTKLYGISRN
     YPLFIYLSAG LSSLKTKSCY CNTENTIFKQ YEESSESNKN IYKKDLAVLT DKKYRGPNKY
     YKLLNKINHC PVCSPELYKL SKNLPYAQLI TSIFNNPFKL PNGNIYPFDK LLNPSEKYLS
     EKNTLLRMGK IKDPLTREIF LIDDCVRVYP A