ID A0A1Y2LNB1_EPING Unreviewed; 434 AA.
AC A0A1Y2LNB1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 02-APR-2025, entry version 29.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=B5807_10214 {ECO:0000313|EMBL:OSS45230.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS45230.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS45230.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS45230.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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; KZ107854; OSS45230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2LNB1; -.
DR STRING; 105696.A0A1Y2LNB1; -.
DR InParanoid; A0A1Y2LNB1; -.
DR OMA; MGAKPCP; -.
DR Proteomes; UP000193240; 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; cd20336; Rcat_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; 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; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000193240};
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 98..336
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 47505 MW; 60179912C345686B CRC64;
MAPSTRLREQ PARRVDYRQN MAAGRVGSTR DPILIGDTPP PQEKPKHSAK TKQKAVSKPV
RASQGRFTKS ESPTNAKSGR SKVAKSAPPP KEQKPRPNKT ECTICATTKN TKRGFRASSL
VDTCEHFESI CDLCIQKQIK TRMAAHQLAE AHLPCMFPQC EIVLDHSALK KVTSKALFES
WNTAVTKHLL ATDPSYIACL NSECGVYFSA EGCGSKHEID IGNGEGKGKS KAKNDDSAVK
AVCPHCDHEL CLSCKRPWHL GSCNSARKKE DEESEKAIKN MGAKQCPKCG VNIEKQGGCD
HMTCKTCRHN FCWECLGAFT GNANNHAETC SHRRPMIAQD VGNWVPDNLN EQQINGIIER
AERERAAGRI PQNAMQLPPV HGAQPPPLHP QAQAWAQVQI PPQGGNGNAP AAPTLAPRDV
LQMIQNFVRQ LGVP
//
