ID A0A367YFB9_9ASCO Unreviewed; 503 AA.
AC A0A367YFB9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Protein FYV10 {ECO:0000256|ARBA:ARBA00018741};
DE AltName: Full=Protein fyv10 {ECO:0000256|ARBA:ARBA00017917};
GN Name=FYV10_0 {ECO:0000313|EMBL:RCK64575.1};
GN ORFNames=Cantr_00274 {ECO:0000313|EMBL:RCK64575.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK64575.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK64575.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK64575.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the proteasome-dependent degradation of fructose-
CC 1,6-bisphosphatase. {ECO:0000256|ARBA:ARBA00002343}.
CC -!- SIMILARITY: Belongs to the FYV10 family.
CC {ECO:0000256|ARBA:ARBA00010615}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCK64575.1}.
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DR EMBL; QLNQ01000022; RCK64575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367YFB9; -.
DR STRING; 5486.A0A367YFB9; -.
DR Proteomes; UP000253472; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR045098; Fyv10_fam.
DR InterPro; IPR044063; ZF_RING_GID.
DR PANTHER; PTHR12170:SF2; E3 UBIQUITIN-PROTEIN TRANSFERASE MAEA; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR SMART; SM00757; CRA; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000253472};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 214..251
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 422..488
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 422..488
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 503 AA; 58114 MW; 5196359CD875197A CRC64;
MTEPTLNFHI QTHQTQFKIP VELIKKNFKT IQKLIEKQKK QLTDDISKIK RAQALSSAAK
LELIQRLIRN FEAFQKKLTL AVKKDEEFRS RLITRLENLL ELLRFVAGLE TKGGEEGAGA
GEGTGGNGDD EADKVLDLHN PNLINWYRDQ TNLLIIDYLI KSNTRSDANI GLLLLKNLAE
TNPKLMKLID YDLFENFNQV FVSIVQDHDL TMIIAWFNEN RNALKKISSN LEFEINYCKF
LTLIEKGDIN EAINYSRENL SSYGNKENYS DQDNVNHAMN LERLKSLGGL LVFRSMEQEE
NSNSLTFSNK LMINSVQFKE YQKLLSNERW ESLSQCFIEN FTKLYGITKN YPIYIYLSAG
LSSLKTKSCY HNAENTVFKD PNAVLDAMEM DKGGGEEEKM LTDRKYRGPN HYYQILNKIN
NCPVCSPELF KLSQNLPYAQ LITSIFNNPF KLPNGNIYPF DKLLSPNDKY LLEKNTLLRL
NKIKDPLTKE IFYIDHCIRV FPA
//
