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Database: UniProt
Entry: A0A2V1C718_9HELO
LinkDB: A0A2V1C718_9HELO
Original site: A0A2V1C718_9HELO 
ID   A0A2V1C718_9HELO        Unreviewed;       416 AA.
AC   A0A2V1C718;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   02-APR-2025, entry version 22.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE   Flags: Fragment;
GN   ORFNames=DL98DRAFT_416483 {ECO:0000313|EMBL:PVH81474.1};
OS   Cadophora sp. DSE1049.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Ploettnerulaceae; Cadophora.
OX   NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH81474.1, ECO:0000313|Proteomes:UP000244409};
RN   [1] {ECO:0000313|EMBL:PVH81474.1, ECO:0000313|Proteomes:UP000244409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE1049 {ECO:0000313|EMBL:PVH81474.1,
RC   ECO:0000313|Proteomes:UP000244409};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(2018).
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};
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DR   EMBL; KZ804138; PVH81474.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1C718; -.
DR   STRING; 1485229.A0A2V1C718; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000244409; 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   CDD; cd22584; Rcat_RBR_unk; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244409};
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          144..337
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PVH81474.1"
SQ   SEQUENCE   416 AA;  46431 MW;  64E6A68F15943726 CRC64;
     GSSKEPSEWE IVLKLHKDEL ERGLSTIRDR HISHSLARAV MIDANANNNA ISAAISQERL
     AESDRAVALR LAGLPVPPPI QQALAGLGTP TPPQTPRSTD TGFEKIIDLI GEQSVYTTSV
     KETKETDTPL KGSGTPKPLG SEGRLKGCVS CADEFEPAYI SQMPCKYDYC HFCVQRVVIN
     SLVDEARYPP RCCKQPFDMD SMRQALTLEL ISGFYEKKAE FETVDRTYCS NPTCSAFLYP
     VNIVGDKAAC PICFTKTCTI CKGPVHNGDC PQDTATQQVL ALANTEGWKR CENCKRMIEL
     KHGCNHITCA CRAEWCYICG VAWKNCGCRM WEENRLLDRA NEIAARNPQP AGPARQDQVA
     AIARAVTDNH ECDHDEWERV DGEWECDECG DELPYFIWRC TQCDIDACTR CRYNVL
//
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