FYV10_ASPTN
ID FYV10_ASPTN Reviewed; 406 AA.
AC Q0CA25;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Protein fyv10;
GN Name=fyv10; ORFNames=ATEG_09459;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU30596.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476607; EAU30596.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001218081.1; XM_001218080.1.
DR AlphaFoldDB; Q0CA25; -.
DR SMR; Q0CA25; -.
DR STRING; 341663.Q0CA25; -.
DR EnsemblFungi; EAU30596; EAU30596; ATEG_09459.
DR GeneID; 4353767; -.
DR eggNOG; KOG0396; Eukaryota.
DR OrthoDB; 1087488at2759; -.
DR Proteomes; UP000007963; 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 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_0000292453"
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; 46437 MW; B9EBC75106C40D56 CRC64;
MAAELTSTKL NAENHLLLDQ PLLRLPHELA RRNFKSVQRL VEREKEYVLP ALKETANASL
SQSQTPDQTL AALDAMISRM QGLKRKMENL QQEEKKIHAQ SRKRIQHLEC LHHIPSLADV
KYDQWSRIRL DRLIVDQMLR SGYTESAQQL AQEKDIEDLV DLNVFIQCQR IAESLRRGET
KDALQWCNEN KAALRKSQYN LEFELRLQQY IEMIRTGDKG KLVEARAHAR KYLTPFIETQ
SAEIHRAAGL LAFPKDTKAE PYKSMYAPER WHHLSDLFVR THHELLSLPS WPLLHIALSA
GLSALKTPSC HSAYTSPSSN SLSTTTSVCP ICSTELNELA RNMPYAHHTK SYVESDPIVL
PNGRIYGQQR LLEMSKKVGC VEAGKVKDPT TGEVFDESEM KKVYIM