ID A0A0F4Z8F4_9PEZI Unreviewed; 449 AA.
AC A0A0F4Z8F4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Protein FYV10 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TD95_002925 {ECO:0000313|EMBL:KKA26620.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA26620.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA26620.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA26620.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) 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:KKA26620.1}.
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DR EMBL; LAEV01002060; KKA26620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4Z8F4; -.
DR OrthoDB; 1429623at2759; -.
DR Proteomes; UP000033483; 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; IPR006594; LisH.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 163..220
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 373..434
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 373..434
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT COILED 65..92
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 449 AA; 50934 MW; 046F82162D2D975B CRC64;
MADHNNIAIK HADHLLLEQQ LVRLPYELLR KNFRSAHFAI EKENANLRSA AESAAKAAMR
QTADKQATLQ SLDTMIEQAE ALKRKLNDFV AEEEKIATNL EKRLDYMGAI YNMNTYEDVG
YESWSRTRLD RLMVEYMLQQ GFIESGLALA RSREIEHLID AEPFLQCNKI IESLRNHSVT
EALAWCSENK KELRKMSCNL EFMLRYQQYI ELLRGGNPAR FNKAIFHARK YILPMRDTYP
AEVLQACGLI AFRPDPASPS TENSPIWSAT RWDTLVAIFR KAFHEFFGIH DRPLLHVALS
AGLSALKTPA CQQKRGKPPA AQQKSEIELL EERLLGTSSE DTASSTPGIR FQLGPDYLNM
TYVEGYGARE LLCPICSPEL SDLAAPMPYA NHTRSHIDHD AVRLPTGNVF SKQKLLDFAK
KARLPEGKIK DLRSGSVFDV SEMGKVFIT
//
