ID A0A0L6WS84_9AGAR Unreviewed; 406 AA.
AC A0A0L6WS84;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Macrophage erythroblast attacher {ECO:0000313|EMBL:KNZ78316.1};
GN ORFNames=J132_01096 {ECO:0000313|EMBL:KNZ78316.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ78316.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) 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}.
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DR EMBL; KQ412480; KNZ78316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6WS84; -.
DR STRING; 1306850.A0A0L6WS84; -.
DR OrthoDB; 1429623at2759; -.
DR Proteomes; UP000053712; 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 CDD; cd16659; RING-Ubox_Emp; 1.
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 SMART; SM00668; CTLH; 1.
DR SUPFAM; SSF57850; RING/U-box; 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:UP000053712};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 161..217
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 313..391
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 313..391
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 406 AA; 45882 MW; 6F741B834659EFBC CRC64;
MNTKLNVEGV LLFEQPFARV PYENYRKVFR TSQKNVERDL GFVQNSSAEL MQRRSKEILG
KDEALNSINN MIGRVDSLKS KLSDLQETAG KPTQDVMRER IHHLTIIETI ATPGGSEYGD
WADTRLDRWL VDWCLRSGME KTARRIARDK NIETLVDIDL FMDIRRIEDA LLKHSCMEAL
AWCNENKVAL RKIKSPLEFD LRLQEFIELS RARKSEEAIA YAKKHLVGWQ ETHLQQIRTA
SALLAFSSNT TCAPYKRLYD PSRWHNLILT FRTAIYSLNT LPTEPLLHLG LYAGLASLKL
PACYDPSTKN VDCPVCDDEA GSGTQGPGLA QLAQEVPFSH HANSTIVCRI SGKIMDEDNP
PMAFPNGNVY SREALEEMAS KNSGLVICPR SGTTCELSML RKVFIS
//
