ID A0A2J6QDJ8_9HELO Unreviewed; 701 AA.
AC A0A2J6QDJ8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 02-APR-2025, entry version 26.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=NA56DRAFT_595779 {ECO:0000313|EMBL:PMD24344.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD24344.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD24344.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD24344.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KZ613473; PMD24344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6QDJ8; -.
DR STRING; 1745343.A0A2J6QDJ8; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000235672; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR054694; Parkin-like_IBR.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22605; IBR_2; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000235672};
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 510..701
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 236..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 392..509
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 253..271
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 79368 MW; A616F269C7979CD5 CRC64;
MENIEDTVVT SVLTDALSRY MRYIEVEQEL HESSQPRRGK GVQTDTDLAR TEYFRARTVT
TGFCLHFVGQ IAENVKRWAT GEAEVKDVGR GKEKEKKVDF GIRDQDLIDF NENIPLSPDD
CFKPVWEDED DEPYINPMTG QWITPVTSKS AGPSNSQWMY ENPSRKASAG QVLKADESLF
PTTDEVREAN IPNILVDLQR RVQPKDVSVV PQLPPLSIFP KLIDLDDDDQ LPYDALLPGA
ILPPTNPFSN PLPSRRSSTN TSGSNTPNTS SRDTDHEPED IFLDSANGRQ QIVNLQSECA
LDNDHLQNTL QFAFPLEDAT TTSRFDLDRL AALKLQAQFD NEAQQTSHFR SQDGYAGQLE
QEERTGVLGF SADTEAAKRL ALEWEAQDGI YEQNLEKLRK EWAEEDRRLE EQAAFADAMR
RDEEARDEAI RRDQAAAMAA LNQWEQERRE AEDSTRRLRE QIEREEEEEM ERMRAAIEQA
RRLAEELERQ EEEERQRLAA EAAEAERRER QADCVVCMEP SDKVDMCSLS CEHYYCEDCV
IAAFNTALSS RAPFTCCTRD PIPASVATDF LPAQTVIQYD LMVLELTTPN PRYCSNRNCR
LFIPPNSVHG PLAICPSCHT RTCSLCNNAE HAGVCAEDRE GAAVVAMARG MGWKPCPRCG
ALVEKHGGCL HMTCKISSCR AQWCWECLRD WGICNSTCRR A
//
