ID A0A0E0KAY9_ORYPU Unreviewed; 612 AA.
AC A0A0E0KAY9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC03G09210.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC03G09210.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC03G09210.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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 -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR AlphaFoldDB; A0A0E0KAY9; -.
DR STRING; 4537.A0A0E0KAY9; -.
DR EnsemblPlants; OPUNC03G09210.1; OPUNC03G09210.1; OPUNC03G09210.
DR Gramene; OPUNC03G09210.1; OPUNC03G09210.1; OPUNC03G09210.
DR eggNOG; KOG1815; Eukaryota.
DR HOGENOM; CLU_009823_2_0_1; -.
DR OMA; HRFCMIC; -.
DR Proteomes; UP000026962; Chromosome 3.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd22586; Rcat_RBR_ARI1-like; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
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:SF371; E3 UBIQUITIN-PROTEIN LIGASE ARI2-RELATED; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF21235; ARI1_UBAl; 1.
DR Pfam; PF19422; Ariadne; 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:UP000026962};
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 133..347
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 137..185
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 70110 MW; C96C87A1E9F50E43 CRC64;
MVTDAEEVSP TASSSELEQE DDDDDCYLSD QEDDALEESV LQVLEDERDE DCHWSSTSVI
TKESLLAAQR EDLRKVMELL GLREHHARTL LIHYRWDVER IFELLDQKGR DRLFSEAGIP
LQPANNAGSP SSTEVTCNVC YDDVPLSDAS KMDCGHNYCN ECWTGYFIVK INEGQSRRIK
CMAPKCNTIC DEAIVRKLVN AKRPDIAERF ERFLLESYIE DNDTVKWCPS TPHCGNAIRV
KGDIHCEVEC TCGRQFCFNC SSEAHSPCSC VMWELWIKKC RDESETVNWI TVNTKPCPKC
HKPVEKNGGC NLVACICGQA FCWLCGGATG RDHTWSSISG HSCGRFTEDQ SKKTEQARRN
LYRYMHYHNR YKAHTDSLKQ EAKLKGDIQG KISISENKDS KIKDYSWVIN GLNRLFRSRR
VLSYSYPFAF YMFGDEIFKD EMTSDERELK QNLFEDQQQQ LEFNVERLSG FLERDFQNFS
DDEVMDTMKH VINLSNVVDR LCKQMYQCIE NDLLYPLRTP HNIAPYKSKG LDRASELNVC
WDSSEQGLQP MKYSQDEYKS QSGLSGSSIF GKRQPGSSSN NNGRPHKRER NDAHGGAALF
DLNVPAEVAD KI
//
