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Database: UniProt
Entry: A0A0D9YWS7_9ORYZ
LinkDB: A0A0D9YWS7_9ORYZ
Original site: A0A0D9YWS7_9ORYZ 
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
//
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