ID A0A150UXG8_9PEZI Unreviewed; 420 AA.
AC A0A150UXG8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Protein FYV10 {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_6692 {ECO:0000313|EMBL:KYG42994.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG42994.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG42994.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG42994.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG42994.1}.
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DR EMBL; JPDO01000372; KYG42994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150UXG8; -.
DR STRING; 766039.A0A150UXG8; -.
DR Proteomes; UP000075602; 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; 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; 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:UP000075602};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 158..215
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 339..400
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 339..400
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..97
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 420 AA; 46339 MW; 7D9CE64EEF6B314A CRC64;
MAEQLASTKL DHDAHLLLDQ PLLRLPHELL RKNLKTAQRQ IEIANKAITS SISAAITASP
TDVLANLDAT IQKAQTLKRK LEALHEEEKT LHRQQKARIR HLQALHEIPG LADVKYDAWA
HVRLDRLLVD YLLRRGYAES AVALAREKGI EELVDIGVFA ECGRIERSLQ RGEVKEALAW
CLENKQALRK INSTLEPELR LQQFIELART GDMPKLMEAI MHARKHLSTP PDAPSSAQDS
FDPLDPDSET SDFGLRAAGL LAHTPDTLVE PYRTLYSPAR YASLAARFLR THHALFALPA
APLLHIALSA GLSALKTPAC HSVHAVSTGS GPTTSAAMCP ICAPELNELA RNVPYAHHTK
SFVDEDAVVL PNGRVFGREK LRALNEKLGV PPGRVRDPTM VGSTEAVEWD EGVLKKVYIS
//
