ID A0A6P4A1Y1_ZIZJJ Unreviewed; 321 AA.
AC A0A6P4A1Y1;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC107422495 {ECO:0000313|RefSeq:XP_015887437.1};
OS Ziziphus jujuba (Chinese jujube) (Ziziphus sativa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rhamnaceae; Paliureae; Ziziphus.
OX NCBI_TaxID=326968 {ECO:0000313|Proteomes:UP000515210, ECO:0000313|RefSeq:XP_015887437.1};
RN [1] {ECO:0000313|RefSeq:XP_015887437.1}
RP IDENTIFICATION.
RC TISSUE=In vitro plantlets {ECO:0000313|RefSeq:XP_015887437.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates.
CC {ECO:0000256|ARBA:ARBA00003976}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR RefSeq; XP_015887437.1; XM_016031951.2.
DR RefSeq; XP_015887437.3; XM_016031951.4.
DR AlphaFoldDB; A0A6P4A1Y1; -.
DR GeneID; 107422495; -.
DR KEGG; zju:107422495; -.
DR InParanoid; A0A6P4A1Y1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000515210; Chromosome 7.
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:UniProtKB-UniPathway.
DR CDD; cd22582; BRcat_RBR_unk; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR FunFam; 1.20.120.1750:FF:000018; RBR-type E3 ubiquitin transferase; 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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000515210};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 105..321
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 109..163
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 68..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..104
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 321 AA; 36458 MW; E32563F8B0427D5B CRC64;
MAKQQLVSDL LLEDDVTISL SDVMLFNEDD HDHHDHDQNF PIPDEKYAEE FQFQEALMAS
LITSQKKTAS SSSSSPSFII TENSEKQEPE MGSSSSSSSP SSSTSRCFCE ICAEKKQTEG
MFNNNNNNNN KCAYSFCTDC IIKHISIRVQ HNKFINSSTV SCPGFDCLDH VLELEACSSF
LPKQVIEEWD EALCESAIFG SDKFYCPFKD CSAMLIIDGE EAITQCECPI CHRLFCATCY
IPWHSGVDCE EFQRMNEDER GREDLMVKEL AKEKNWKRCP HCKYYVEKTE GCLHITCRCN
FQFCYACGSE WTSTHGGCQP N
//
