FYV10_NEOFI
ID FYV10_NEOFI Reviewed; 406 AA.
AC A1CZJ5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein fyv10;
GN Name=fyv10; ORFNames=NFIA_037390;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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=EAW24165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS027686; EAW24165.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001266062.1; XM_001266061.1.
DR AlphaFoldDB; A1CZJ5; -.
DR SMR; A1CZJ5; -.
DR STRING; 331117.A1CZJ5; -.
DR EnsemblFungi; EAW24165; EAW24165; NFIA_037390.
DR GeneID; 4592695; -.
DR KEGG; nfi:NFIA_037390; -.
DR OrthoDB; 1087488at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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; 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..406
FT /note="Protein fyv10"
FT /id="PRO_0000292462"
FT DOMAIN 126..158
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 164..221
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 329..391
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 406 AA; 46513 MW; 87A3C7EFFB1B3C20 CRC64;
MAAELTSTKL NAENHLLLDQ PLLRLPHELA RRNFKSVQRL VEREREYVIH ALKEAANASL
SNDQTPDQTL AALDSMLARM QNLKRKMESI QQEEKKIQNQ SRKRIQHLEH LHQIPSLADV
KYDQWSRIRL DRLVVDHMLR SGYTESAQRL AQEKGIEDLV DLDVFVQCQR IAQSLRRGET
KDALRWCNEN KAALKKSQFN LEFELRLQQY IEMLRTGDRG KLMDAMAHAK RYLTPYTETQ
SKEIHRAAGL LAFPQDTKAE PYKSMYSFDR WNHLSDLFIR THHELLSLPS SPLLHIALSA
GLSALKTPSC HSAYTSSSSN SLSTATSVCP ICSTELNELA RNMPYAHHAK SYVESDPIVL
PNGRIYGQQR LLDMSKKLGC VETGKVKDPT TGEIFDESEM KKVYIM