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Database: UniProt
Entry: A0A165Q3D1_EXIGL
LinkDB: A0A165Q3D1_EXIGL
Original site: A0A165Q3D1_EXIGL 
ID   A0A165Q3D1_EXIGL        Unreviewed;       787 AA.
AC   A0A165Q3D1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   02-APR-2025, entry version 35.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
GN   ORFNames=EXIGLDRAFT_636660 {ECO:0000313|EMBL:KZW03026.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03026.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW03026.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03026.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; KV425885; KZW03026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165Q3D1; -.
DR   STRING; 1314781.A0A165Q3D1; -.
DR   InParanoid; A0A165Q3D1; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   CDD; cd20339; BRcat_RBR_RNF216; 1.
DR   CDD; cd20353; Rcat_RBR_RNF216; 1.
DR   CDD; cd16630; RING-HC_RBR_RNF216; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047545; BRcat_RBR_RNF216.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR051628; LUBAC_E3_Ligases.
DR   InterPro; IPR047546; Rcat_RBR_RNF216.
DR   InterPro; IPR047544; RING-HC_RBR_RNF216.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22770:SF47; E3 UBIQUITIN-PROTEIN LIGASE RNF216; 1.
DR   PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          357..573
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          711..774
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   787 AA;  87667 MW;  A151735087B2F12B CRC64;
     MATRRTTRSM SREPGSSRST KPAKRRAAPT LDPVIDLTLS DDDDPDIVQV AGPSKATSRI
     HKPRDDGQRV LIELNDPPQP KPGPALSRTG SRVLAELNKS VNDKENARDS GAVPSVDPGL
     EVISVAAPMV EPRPVANPTP AGDQVPAEPV PGPAQPEVEV VDPLARVLEI VPDVDLEHAQ
     KLIDAHIATY GPEKVVQPVL HLLLEDPSYP KAQRNKGKRK ADVEAEANNK KIKIDYASAD
     RPFAGSNAYF EAAVTQLTVD YPYIPKADLR RFLLDRNSLY APTFLFIREE EKKPLSERPY
     KLKKSATPNK GKGRAVEYED DELAREVKWV KEFVTGNFAP VADEDDGDGS LEAPEGEGVE
     CGCCFGEYRF DTMIQCPDAH LFCISCVRAY AGTKLADGHA DIPCPSSSDP PCKMHFSESE
     LRRALKEGQM DLWGRVRARR DLESAKIDGL EECPFCDYAC VVENPDEKLF RCARVEECGE
     VSCRKCKKRD HLPKSCKEAE QDNVLDAQHA VEEAMTKALM RNCPKCSKAF VKETGCNKMS
     CPYCHTLSCY VCRQIIIGYD HFDQMPGGQR RPAGNKAGKC PLWDEGQNVE LRHRAEVEAA
     AKRALAEVRA ANPEVDAQAI KVDMPAPPPQ PRGHVHGGPA PVLGHFHGVH AVPMAGHGWN
     GAQFVHVPPP PVFPAAHHHY HHHPPPPPPP PPVVYHHHHH DYEDDMWDED EDDEEEEMMR
     LLEQEEEARR VRIQAEREQA RAQQAALLAE ERILRNLERQ QAEMREHVRR MAALRPPPAP
     VPRARRR
//
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