FYV10_CHAGB
ID FYV10_CHAGB Reviewed; 441 AA.
AC Q2H991;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Protein FYV10;
GN Name=FYV10; ORFNames=CHGG_03213;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408030; EAQ91278.1; -; Genomic_DNA.
DR RefSeq; XP_001229729.1; XM_001229728.1.
DR AlphaFoldDB; Q2H991; -.
DR SMR; Q2H991; -.
DR STRING; 38033.XP_001229729.1; -.
DR EnsemblFungi; EAQ91278; EAQ91278; CHGG_03213.
DR GeneID; 4389687; -.
DR eggNOG; KOG0396; Eukaryota.
DR HOGENOM; CLU_027445_2_0_1; -.
DR InParanoid; Q2H991; -.
DR OMA; DVKYDEW; -.
DR OrthoDB; 1087488at2759; -.
DR Proteomes; UP000001056; 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..441
FT /note="Protein FYV10"
FT /id="PRO_0000292456"
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 364..426
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT REGION 312..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 49130 MW; 05477878D2E86B96 CRC64;
MADLEAANIN HDNHLLLDQP CLRLPYELLR KNFRSVHYPF EWDSTSVKNV VKETANGLIS
GKASPQDAVE NLDQMLVKMR GLKRKLTAAA KEEDRLYRQM DSRVAHLREL ADLHTVDDVR
YEAWSRQRLD RLLVDYMLRH GYDSSAIALA DERGMRDLVD IDTFVVMSRI RKSLEGGSVQ
EALNWCNENK KELRKMQSNL EFLLRCQQYI EMMRTDSPAK MAEAIHHARK YITPFTETYP
VEISSIAGLL AYRPGTISEP YASLYSASRW QKLADTFVEA HLKLLGLPMT PLLHIALSSG
LSALKTPACH STQLQVPTQP EESQPVNGAG DGAATATAAA ASSTTSTAIP HHHHGTASLT
TRVCPICSTE LNALARSVRY AHHGKSRLLE QDLVLLPNGR VYGKARLDEY AAKSGLPAGQ
IKDLVTGEVF SGEEGRKVFV T