ID A0A0E0NYG1_ORYRU Unreviewed; 1097 AA.
AC A0A0E0NYG1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI03G27550.2, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI03G27550.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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; A0A0E0NYG1; -.
DR EnsemblPlants; ORUFI03G27550.2; ORUFI03G27550.2; ORUFI03G27550.
DR Gramene; ORUFI03G27550.2; ORUFI03G27550.2; ORUFI03G27550.
DR HOGENOM; CLU_283774_0_0_1; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
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; 2.
DR CDD; cd22586; Rcat_RBR_ARI1-like; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 2.
DR Gene3D; 1.20.120.1750; -; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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:SF322; OS03G0625933 PROTEIN; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 2.
DR Pfam; PF01485; IBR; 3.
DR SMART; SM00647; IBR; 3.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 5.
DR PROSITE; PS51873; TRIAD; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022};
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 140..367
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 144..177
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 670..883
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 674..717
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 120203 MW; D52B3E5DF4E323C9 CRC64;
MSSDDEECFY DYDEEEEEEE EEEPGWDDGG GGDTMLVEEE AALPERPVDC WAITEESLPA
AQQQDLSMVM NLLYIKQHQA RALLIHHRWK MESILDHFDR KGRDRMLRET GVVIQQQAEE
KNGGGMAMAA SPSPPPRPRS SVTCYVCFED VSSDAVSTMD CGHCFCNDCW TEHFFACVNG
GQKQIRCMAV GCAAVCDEDV AQRLLGGRYP GAARRLRGAL LASYVEDNAA ARWCPSAPHC
GRAVRVDGGG GRWCCEVSCP CGASFCFGCA APAHSPCPCA MWERWEAKCR GESMNVDWIL
ANTKSCPNWL CGAATGLAHN WTSIDGHSCN RYDDAAEKRK VDGARRKVLR YAHYYERYKA
HGDSRRAEAE KLGPAIEARA RRLREDPDPA TAPASGDAAE ALAAAHRALL ASRDVLSRSY
AFAYHMFGGE ERTLKAAAPE SEVATAQALF EDHQEMAERH VEKLSGLLAA DAPPAPATAG
DAALRRAKQD AVALTAVVEK HCGEMHKCIQ DELLPMLVEP ISDDAAAMDG SDDECCYYYD
AVDSDGDEEE EEEIIMLDED DVGLLDGAAL PPPEEEVEHR AICWAITKES LAAAQEQDLS
MVMNLVNVER HNARALLAHH RWKMERIYDR LDMMGRDALL RDAGVVVLPE KSSSSGSSMA
MAKTNPPGSV AVTCNVCFEE YPLGSVSAMD CGHCFCNDCW TEYFAAAVSD GSKQMRCMEV
KCTVICDEAV VRRLLHGKHP GAAARLDRRL LEAYVEASDA VRWCPSAPHC GRAIRVDGGG
GGEERYAEVS CPCGAIFFFR CGGGAHSPCP CPMWDKWGAM RGGGEVDNLK WIVANTKSCP
KCSKPIEKNG GCNHVTCTCG QHLCYACGAA TGTLYMHICN RYKEEGGGGG VKVEMTAGGR
QRLRFMHYYE RFEIHTESYK EEQGKLGPAI DALARRLEAD ATLPWSGTRD ARWPSAAHRR
LLRCRQVLPR SYVLAYYMFG GGAATRRQRE EAAAQNRFED LQGQLEHHVE VLSRTLAAAA
RPADAAEVVK AKRDADNLAR VVEGLCAGMY RCVQDELLPL LVEPMNIAAY HPDGPAMAKE
FPPATSVTGG APPATRH
//
