ID A0A1B7NVR8_9EURO Unreviewed; 403 AA.
AC A0A1B7NVR8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Protein FYV10 {ECO:0000256|ARBA:ARBA00018741};
DE AltName: Full=Protein fyv10 {ECO:0000256|ARBA:ARBA00017917};
GN ORFNames=ACJ72_04806 {ECO:0000313|EMBL:OAX80859.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX80859.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX80859.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX80859.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-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:OAX80859.1}.
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DR EMBL; LGUA01000602; OAX80859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7NVR8; -.
DR STRING; 1658172.A0A1B7NVR8; -.
DR OrthoDB; 1429623at2759; -.
DR Proteomes; UP000091918; 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:UP000091918};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 164..221
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 326..388
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 326..388
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT COILED 73..100
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 403 AA; 45656 MW; A9938F31B384E8E4 CRC64;
MAAELTSIKL NPESHLLLDQ PLLRLPHELA RRNFKSVQRI VERERDHILP YLKETANASL
SGTQDATQTL TALDTMISRM QGLKRKMETL QDEEKKILTQ SRKRIQHLED LYKIPSLADV
KYEEWSRIRL NRLLVDHMLR SGYADSARQL AAEKGIEDLV DLGVFVQCQR IAESLGRGET
KEALTWCGEN KVGLKKIQSN LEFELRLQQY IEMVRAGDKA EARQHAKKFL SPHSETQATD
IRRAAGLLVF SPDTTAEPYK DMYSSSRWQH LSDLFIRTHH DLLALSSRPL LQIALSAGLS
ALKTPSCHSA YASSSSNPNS TTTSVCPICS TELNELARHM PYAHHTKSYV ENDPIVLPNG
RIYGRQRLLD MCKKSGFVAP GKVKDPTTGE EFDETEMKKV YIS
//
