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Database: UniProt
Entry: A0A1Y2E9A8_9FUNG
LinkDB: A0A1Y2E9A8_9FUNG
Original site: A0A1Y2E9A8_9FUNG 
ID   A0A1Y2E9A8_9FUNG        Unreviewed;       329 AA.
AC   A0A1Y2E9A8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=RING-Gid-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LY90DRAFT_661049 {ECO:0000313|EMBL:ORY67894.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY67894.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY67894.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY67894.1,
RC   ECO:0000313|Proteomes:UP000193920};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY67894.1}.
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DR   EMBL; MCOG01000048; ORY67894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2E9A8; -.
DR   STRING; 1754190.A0A1Y2E9A8; -.
DR   OrthoDB; 208500at2759; -.
DR   Proteomes; UP000193920; 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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12170:SF3; GH10162P; 1.
DR   PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR   Pfam; PF10607; CTLH; 1.
DR   SMART; SM00668; CTLH; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS51867; ZF_RING_GID; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01215}.
FT   DOMAIN          98..155
FT                   /note="CTLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50897"
FT   DOMAIN          266..315
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51867"
FT   ZN_FING         266..315
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ   SEQUENCE   329 AA;  37859 MW;  80E82A55DE9932A8 CRC64;
     MEQISNEFEK LVKKQKLTNN QTQINIDKLI NHINDSIQKI DNDDSQSDTL WKPNVLSGKE
     DIINSILMSH FIREGQFDLA ETFSKESNIP ISDEKKNQFQ DLFNIVEAIK RKDLGPALKW
     ASEKRDILKR NNSNLEFELH KLQYVQYLIN NDIPSAIQYA KNIKRLVCSI LYIKHLDNSP
     YSDLLAPSLW DDIESQFKRD FCSIYGFSSE SPLFEAVMVG ASSIPPLIKI DTILKVTKNI
     DWSANSELPV EIPLLDSQRY HTVFTCPVSK EQVDCNGKDN YPTMLLCGHI ISKESLLGLC
     KGNNIYRHKF KCPYCPTESI EAQAKRVYF
//
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