FYV10_ASPCL
ID FYV10_ASPCL Reviewed; 406 AA.
AC A1C9R2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein fyv10;
GN Name=fyv10; ORFNames=ACLA_009000;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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}.
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DR EMBL; DS027049; EAW12480.1; -; Genomic_DNA.
DR RefSeq; XP_001273906.1; XM_001273905.1.
DR AlphaFoldDB; A1C9R2; -.
DR SMR; A1C9R2; -.
DR STRING; 5057.CADACLAP00000972; -.
DR EnsemblFungi; EAW12480; EAW12480; ACLA_009000.
DR GeneID; 4706351; -.
DR KEGG; act:ACLA_009000; -.
DR VEuPathDB; FungiDB:ACLA_009000; -.
DR eggNOG; KOG0396; Eukaryota.
DR HOGENOM; CLU_027445_2_0_1; -.
DR OMA; DVKYDEW; -.
DR OrthoDB; 1087488at2759; -.
DR Proteomes; UP000006701; 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_0000292450"
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; 46483 MW; C61BC51A693C31B1 CRC64;
MAAELTSTKL NAENHLLLDQ PLLRVPHELA RRNFKSVQRL VEREREYVLP ALKEAANASL
ANTQTPDQTL AALDAMISRM QGLKRKMESL QEEEKRIQEQ SRKRIQHLEC LHQIPSLADV
KYDQWSRVRL DRLVIDHMLR SGYTASAQQL AQEKGIVDLV DLDVFTQCQR IAQSLRHGET
RDALQWCNEN KAALKKSRFN LEFELRLQQY IEIIRTGDRG RFIDAMAHAK RYLTPYIETQ
SMEIHRAAGL LAFPRDTKAD PYKSMYSSDR WTYLSDLFIR THHELLSLSS RPLLHIALSA
GLSALKTPSC HSEYTSPSSN SLSTTTSVCP ICSTELKELA RNMPYAHHAK SYVENDPIIL
PNGRIYGQQR LLDMSKKVGC VETGKVKDPT TGEIFDESEM KKVYIM