FYV10_MAGO7
ID FYV10_MAGO7 Reviewed; 410 AA.
AC A4RK04; G4MUF7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Protein FYV10;
GN Name=FYV10; ORFNames=MGG_01665;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(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}.
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DR EMBL; CM001232; EHA54844.1; -; Genomic_DNA.
DR RefSeq; XP_003714651.1; XM_003714603.1.
DR AlphaFoldDB; A4RK04; -.
DR SMR; A4RK04; -.
DR STRING; 318829.MGG_01665T0; -.
DR PRIDE; A4RK04; -.
DR EnsemblFungi; MGG_01665T0; MGG_01665T0; MGG_01665.
DR GeneID; 2679342; -.
DR KEGG; mgr:MGG_01665; -.
DR VEuPathDB; FungiDB:MGG_01665; -.
DR eggNOG; KOG0396; Eukaryota.
DR HOGENOM; CLU_027445_2_0_1; -.
DR InParanoid; A4RK04; -.
DR OMA; DVKYDEW; -.
DR OrthoDB; 1087488at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; ISS:PAMGO_MGG.
DR GO; GO:0005829; C:cytosol; ISS:PAMGO_MGG.
DR GO; GO:0005634; C:nucleus; ISS:PAMGO_MGG.
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; ISS:PAMGO_MGG.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:PAMGO_MGG.
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..410
FT /note="Protein FYV10"
FT /id="PRO_0000292461"
FT DOMAIN 125..157
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 163..220
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 334..395
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 410 AA; 46740 MW; 587E63113CCADDFB CRC64;
MADHQTTKID KSNHLLLDQT LLRLPYDLMR KNFRNAHFVV EHESKAITKL LKDTATGSLK
GKHSSDDVLK NIDAMLAKAK GIKRKLQACS DEEARLYRQL GARIKHVGEV VSMETVDDVR
YEQWSRTRLD RLIVDYMLRH GYNESACALA DDRGIRDLVD IDTFIHMSRI QESLANRSVT
EALAWCHENK KELRKIDSNF EFMLRFQQYI ELVRSQTLPK VLEAITHARK YLIPFKETYP
HEVNQAAGLL AYPPEQTSDS YSNLWGQERW EMLSTLFIET HHRLLSLPSF PLLHIALSSG
LSALKTPACH TAGARDLADT PNSAPGNSLD SSMCPICSAE LNELAENVPY AHHSKSHVEH
DLVLLPNDRV YGKARLEEYA RKSGLPHNCV KDLRTGEIYP ASRMKKVFIT