ID A0A0D9YWS7_9ORYZ Unreviewed; 1271 AA.
AC A0A0D9YWS7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G29350.5};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G29350.5}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G29350.5}
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 -!- 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; A0A0D9YWS7; -.
DR EnsemblPlants; OGLUM02G29350.5; OGLUM02G29350.5; OGLUM02G29350.
DR Gramene; OGLUM02G29350.5; OGLUM02G29350.5; OGLUM02G29350.
DR HOGENOM; CLU_263960_0_0_1; -.
DR Proteomes; UP000026961; 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; cd20341; BRcat_RBR_RNF14; 1.
DR CDD; cd20336; Rcat_RBR; 1.
DR CDD; cd20354; Rcat_RBR_RNF14; 2.
DR Gene3D; 1.20.120.1750; -; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047548; Rcat_RBR_RNF14.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685:SF257; -; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF05773; RWD; 3.
DR SMART; SM00647; IBR; 3.
DR SMART; SM00184; RING; 4.
DR SMART; SM00591; RWD; 3.
DR SUPFAM; SSF57850; RING/U-box; 6.
DR SUPFAM; SSF54495; UBC-like; 3.
DR PROSITE; PS50908; RWD; 3.
DR PROSITE; PS51873; TRIAD; 2.
DR PROSITE; PS00518; ZF_RING_1; 2.
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:UP000026961};
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 73..212
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 263..487
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 267..312
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 625..764
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 805..1074
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1136..1271
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 142918 MW; 980C88862759C61E CRC64;
MSSEASSSAA AGVAVRDVGD DKPLPSAEVD ITYWAAQEEA AALLESMAAT ARARGEDDLS
EEQLQANNQL QEDEVIALQA IFGDDMVILE NKDNLRFIQI FVHYTLPDSI RVFLNLRRSG
AMVGTDDSEN HNGGELYHAC RLQHLPPVVL TCLLPRSYPS ICAPYFTISA KWLDEPKVSY
LCAALDEVWT ELPGQEVIYR WVDWLNSSSW SSIALNDEIV LDPDKTSKIG DERAIARRIL
VESTIPLMQS YSEKRSHKIF LESLLVCGIC LSEDVGKNFI KLPCHHSFCL KCMESHCKIH
VKEGNLTQLA CPDTNCRNPL PPSVLKSLLR DDGYAQWESF ALQKLLDAMP DLVYCPRCSA
ACLEVDNDAQ CPGCFFTFCT LCKRRRHVGD TCITPEEKIR ILKERQKLYS IPEEQLLKEQ
REIDELINIQ EALRDSKQCP RCKMAISKIE GCNKMTCGNC GRFFCYRCNK AIGGYDHFWN
GNCDMFEREQ DENPQQQDDE NFDGDPDEDA ELLEPEWVLL TYPCPNCGRR NEKRLAISKH
QSKRSEQSIP WEIPMSSEAS SSSSAAVAVR DLGDDNPSAS PEVDTTYWTA QEEAAALLES
MAARVRGEEE LSEEQLQANE QLQEDEVIAL EAIFGGDMVI LENKDSLRFI QIFVHYSLPD
GIRVFLNLRR SGALVGTGDN ENHNGGEVCY ACRLQHLPPV VLTCLLPRSY PSTCAPYFTI
SAKWLDEPKV SYLCAALDEI WTELPGQEVI YRWVDWLNSS SWSFIALNDE IVLSPDRTSK
FGDERAIARR ILVESTIPLM QIYSEEISQG INFIKHLSFC YCILLGINFV KLPCHHFFCV
KCMEAHCKIH VKERNLTQLT CPDTNCRSPL PPSLLKSLLR DDGYAQWESF ALKKLLDAMP
DLERQKLHSM PAEQLLKERR ELEELMNIQE ALRSSKQCPH CKMAISKIEG CNKMICVNCG
GYFCYSCNQA IKGYEHFWGG NCVLFGTHAH YQIRNPQQQR DENPGDHAEL LEQRVQLTYP
CPNCGSRNEK LGTNNHISCP GCRGHYCALC RKRVLKCSQH FGPRDEGQVS SGSLVAAVEI
TMMTPGSSST SVPGDEADAG NWDAGVETAA RLEAMVHAED ELSEEQIQAN NQTQEDELLA
LQAIYGDDLV IFDNKDGLRF FQISLHYQLA GDIRVYLNVC PNGRTETGAE NDDDDDSDRL
LYACSLQHLP PVVLTCLLPR LYPSHRAPYF VVAAKWLDEP EVSSFCSLRE RVDAAACAED
DGAMATCGSM P
//