ID A0A1Z5TBA4_HORWE Unreviewed; 763 AA.
AC A0A1Z5TBA4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=RING-Gid-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BTJ68_06421 {ECO:0000313|EMBL:OTA33141.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA33141.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA33141.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA33141.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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:OTA33141.1}.
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DR EMBL; MUNK01000080; OTA33141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TBA4; -.
DR STRING; 1157616.A0A1Z5TBA4; -.
DR VEuPathDB; FungiDB:BTJ68_06421; -.
DR InParanoid; A0A1Z5TBA4; -.
DR OrthoDB; 208500at2759; -.
DR Proteomes; UP000194280; 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; cd16652; dRING_Rmd5p-like; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR037683; Rmd5_dRing.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_euk.
DR PANTHER; PTHR12170:SF3; GH10162P; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50897; CTLH; 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:UP000194280};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 215..273
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 405..447
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 405..447
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT REGION 170..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 84540 MW; B45B318341A2CD07 CRC64;
MDPLLASHST LEKKANLSKA LADVQKLIDQ LSSTRDAVTT NPDMAALHMA KLKQPVKQSF
DKIEEDLKEV NKGLNQYQKA LKEKFKNSSL PTAGGVGEGL GEGEKKALVE RAVGMHLLRE
GMFGVADIFA REAKTRNERL GKVSGDGDVD MEEEDGKLRA ERKQEWLNNF MQSERNEVMG
DGDGYEEDED EEDLYAPGDR PLSSSSRFPS KLQARFADMY HILDALRNHR NLAPAIDWAR
MHSHELEHRG SNLEFELARL KFVELYTSST ASDTNPYTGP LQALEYARQV FPTFTSRYNH
ETSSLLGSLA FAPDLAQSPY VALFHNNHAW EETAASFTRE YCGLLGLSEK SPLYTAITAG
GIALPVLSKV EKIMTQTRGQ WTSVNELPVE TPLPPGYLFH SIFVCPVSKE QATDANPPMM
LPCGHVIAKE SLEGTSKGKV RVKCPYCPQE CRVGDARRLH EFKTALQTLR SIRAPLKLVI
AGNHDFTLDV PAFKRKLSAI DPPLDDALVK REYGTFGEAR ALLESEEAKA AGIHLLDEGT
HTFQLANGST LTVFASPYTC SLSADWGFQY RPDEEHEWPL QPGTDIAITH SPPHGVLDRT
DDGKRAGSPS LFAAVASSRP QVHCFGHIHE SWGAKKVHWR DEAPDSPRTH FTSIDNDRSP
LIETLARMTV KATDTAETKR DKETRLAACI ANGHCSAARH DIKAGAQTLF VNAAIEGPEE
GMQQPPWLVE IKLPRTGVTS ASNEERHSRK RRRTSERSSG AVE
//
