ID   FYV10_YARLI             Reviewed;         564 AA.
AC   Q6C435;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Protein FYV10;
GN   Name=FYV10; OrderedLocusNames=YALI0E30085g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382131; CAG80181.1; -; Genomic_DNA.
DR   RefSeq; XP_504577.1; XM_504577.1.
DR   AlphaFoldDB; Q6C435; -.
DR   SMR; Q6C435; -.
DR   STRING; 4952.CAG80181; -.
DR   EnsemblFungi; CAG80181; CAG80181; YALI0_E30085g.
DR   GeneID; 2911468; -.
DR   KEGG; yli:YALI0E30085g; -.
DR   VEuPathDB; FungiDB:YALI0_E30085g; -.
DR   HOGENOM; CLU_027445_2_0_1; -.
DR   InParanoid; Q6C435; -.
DR   OMA; YARRSEN; -.
DR   Proteomes; UP000001300; Chromosome E.
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..564
FT                   /note="Protein FYV10"
FT                   /id="PRO_0000292467"
FT   DOMAIN          128..160
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          166..224
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   ZN_FING         487..549
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT   REGION          322..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  63970 MW;  CF0712267A10CC3E CRC64;
     MIKADNALLL EEPLLRVPYE MLRKNLKTVH KHMTQESTMV EQTLSKLQQS TQHVAAEYGE
     KQQEEARESL DQLISRVRGL KRKIATLKDE QNETLTTTKA RVEHLNVIFD NEKETDPEKQ
     KETEKKWLRT RLERLLTDYF LRQGFSETAK SFAQNRGITS LVDVTILDQC ISVETSLRQR
     HSTAECLAWC SENRSFLRKT RSSLEFEVRL QHYVELVKSG RVEDALKYCQ RFLSKNADIH
     LREIQQAAGL LAFPPGTEGS PYKDLYACER WNQLSRKFVQ TFADVHGLSD GSSLLYTLST
     GLSVLKTHSC RNFGAPAELP ITADKDEDMD PSLTSSARPY ARRSENLPSV FGSGFSIRMY
     GSDEIRGLDT LPVIPPRALA NLSSMRRDIA MQNNLDLEES IEDDNEESEE RTSGDGERDS
     DGAVPVEELE ELPDAPPELL SAEYLARRIE EATKENTDII PKTTLDMFNH FYPGCCTSHQ
     LSRADACPVC SVELNSLAEN LPYAHHIRSH LDADPVVLPN SRIFGRAKLM EYSHKMMKAA
     PNTVVDPTSF ECFKIDELIT AYPS