ID A0A0E0KGH2_ORYPU Unreviewed; 532 AA.
AC A0A0E0KGH2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:OPUNC03G24290.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC03G24290.1}
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:OPUNC03G24290.1}
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; A0A0E0KGH2; -.
DR STRING; 4537.A0A0E0KGH2; -.
DR EnsemblPlants; OPUNC03G24290.1; OPUNC03G24290.1; OPUNC03G24290.
DR Gramene; OPUNC03G24290.1; OPUNC03G24290.1; OPUNC03G24290.
DR eggNOG; KOG1815; Eukaryota.
DR HOGENOM; CLU_009823_2_1_1; -.
DR OMA; EDECGYF; -.
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; 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; 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 PANTHER; PTHR11685:SF273; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
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 136..366
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 140..183
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 60504 MW; C9E2C29ADD58A3EA CRC64;
MASDHQRCHY YYEEEDEDDG DEEEVEWLAM EADEGDVGLL EEDDLHLRLP DDRRADCWAI
TQESLPAAQQ QDLSIVMNLL NIKQHHARTL LIHHRWKMHC INDHLDRKGR DRMLSEACIV
LPKNSMSAAS SRTSSTSVTC IVCFEDFSIT DVSTMDCGHY FCNDCWTEHF FASIKTGNKQ
IRCMEVKCKA ICDEDIVRRL LSLKYPAASK RFDCLLLESY LEDNDSVKWC PSAPHCGRAI
QIGTGERYCE VACPCGVSFC FNCTGQVHSP CPCAIWEKWK AKGHGDSDSV KWILANTKSC
PKCSKPIEKN GGCNLVHCKC GQCLCISGHS CNRYKEENGN KVDTSRQQMQ RYTHYWDRYN
IHTGSYKVEQ KDLGPAVEEQ VKKLESNLTG PRMNWDGSWL AMAYQSLLAS RQVLSRSYAF
AYYMFGGGEV KTHKSEQASL AVAQNLFEDR QEQLERHVEH LSKVLAADVL GLPEEILLKK
LEIVNLAKIV QAICGQLYRC IQDELLPLLV QPMNIAAYQP DGPNKAKEFI RA
//
