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FYV10_ASPFU
ID   FYV10_ASPFU             Reviewed;         411 AA.
AC   Q4WTQ4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein fyv10;
GN   Name=fyv10; ORFNames=AFUA_5G05720;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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=EAL92022.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000003; EAL92022.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_754060.1; XM_748967.1.
DR   AlphaFoldDB; Q4WTQ4; -.
DR   SMR; Q4WTQ4; -.
DR   STRING; 746128.CADAFUBP00005216; -.
DR   GeneID; 3510767; -.
DR   KEGG; afm:AFUA_5G05720; -.
DR   eggNOG; KOG0396; Eukaryota.
DR   HOGENOM; CLU_027445_2_0_1; -.
DR   InParanoid; Q4WTQ4; -.
DR   OrthoDB; 1087488at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
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   SMART; SM00667; LisH; 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..411
FT                   /note="Protein fyv10"
FT                   /id="PRO_0000292451"
FT   DOMAIN          133..165
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          171..228
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   ZN_FING         334..396
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
SQ   SEQUENCE   411 AA;  47045 MW;  8EA9E0B970011B31 CRC64;
     MAAELTSTKL NAENHLLLDQ PLLRLPHELA RRNFKSVQRL VEREREYVIP ALKEAANASL
     SNAQTPDQTL AALDSMLARM QNLKRKMESI QQEEKKVQNQ SRKRIQHLEH LHQIPSLADV
     KYDQWSRIRL DRLVVDHMLR SGYTESAQQL AQEKGIEDLV DLDVFVQCQR IAQSLRRGET
     KDALQWCNEN KAALKKSQFN LEFELRLQQY IEMLRTGDRG KLMDAMAHAK RYLTPYTETQ
     SKEIHRAAGL LAFPQDTKAE PYKLTDLQSM YSFDRWNYLS DLFIRTHHEL LSLPSSPLLH
     IALSAGLSAL KTPSCHSAYT SSSSNFLSTT TSVCPICSTE LNELARNMPY AHHAKSYVES
     DPIVLPNGRI YGQQRLLDMS KKLGCVETGK VKDPTTGEIF DKSEMKKVYI M
 
 
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