ID   FYV10_ASHGO             Reviewed;         516 AA.
AC   Q75AZ2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Protein FYV10;
GN   Name=FYV10; OrderedLocusNames=ADL222W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
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DR   EMBL; AE016817; AAS51698.1; -; Genomic_DNA.
DR   RefSeq; NP_983874.1; NM_209227.1.
DR   AlphaFoldDB; Q75AZ2; -.
DR   SMR; Q75AZ2; -.
DR   STRING; 33169.AAS51698; -.
DR   EnsemblFungi; AAS51698; AAS51698; AGOS_ADL222W.
DR   GeneID; 4620014; -.
DR   KEGG; ago:AGOS_ADL222W; -.
DR   eggNOG; KOG0396; Eukaryota.
DR   HOGENOM; CLU_027445_2_0_1; -.
DR   InParanoid; Q75AZ2; -.
DR   OMA; DVKYDEW; -.
DR   Proteomes; UP000000591; Chromosome IV.
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:EnsemblFungi.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:EnsemblFungi.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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   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..516
FT                   /note="Protein FYV10"
FT                   /id="PRO_0000292449"
FT   DOMAIN          203..261
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   ZN_FING         434..501
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT   REGION          143..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  59961 MW;  39E8985CD2503989 CRC64;
     MSVMNEPTVD FHLKLNEQQF HIPNELLKRN LKQCQKLIDK EATALEKSFE ELDRLVRNPQ
     NDESSMALLN EIIQKVERLE RKLTKRVNVE LQLLQRIDAR IKYYQQLDQI KQSGDRNRLL
     EWYQSYTNLL ISDYLTRNSM YEGEDDISCS STPPPARLKR KLSSASSQLT TATSNNDPDR
     SHVNPGVEYL KQQGLDLLLD YDILLTTNRI SKQLTINHEL GPLLDWIKEN ATYLKHTSSM
     LEFEARFQEY IEYVKVEDYS KAITCFQTHL VKFLYSNPLD LQQAAGLLVF IKACKSNISS
     YVPTPRHEEI VKQQTLLQSK EDFWSFFFLK LPKSSKKDHK TNIEVKNNEL AASVDIKRYM
     ELLDDRRWEK LNEMFLKAYY SMYGISYHDP LLIYLSLGIS SLKTKDCLHE RRAFVSPNNE
     LSEFLSSEVL RNACPVCSPE FAPIAQKLPY AHQVQSRLFE NPVMLPSGNV YDAEKLKALA
     QTLRKRKLVV MGEDEVLDPI AGHTYALTDF ITMYPT