GenomeNet

Database: UniProt
Entry: A0A6A1W9Y9_9ROSI
LinkDB: A0A6A1W9Y9_9ROSI
Original site: A0A6A1W9Y9_9ROSI 
ID   A0A6A1W9Y9_9ROSI        Unreviewed;       523 AA.
AC   A0A6A1W9Y9;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   18-JUN-2025, entry version 18.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=CJ030_MR3G015771 {ECO:0000313|EMBL:KAB1220518.1};
OS   Morella rubra.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Myricaceae; Morella.
OX   NCBI_TaxID=262757 {ECO:0000313|EMBL:KAB1220518.1, ECO:0000313|Proteomes:UP000516437};
RN   [1] {ECO:0000313|EMBL:KAB1220518.1, ECO:0000313|Proteomes:UP000516437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAB1220518.1};
RX   PubMed=29992702;
RA   Jia H.M., Jia H.J., Cai Q.L., Wang Y., Zhao H.B., Yang W.F., Wang G.Y.,
RA   Li Y.H., Zhan D.L., Shen Y.T., Niu Q.F., Chang L., Qiu J., Zhao L.,
RA   Xie H.B., Fu W.Y., Jin J., Li X.W., Jiao Y., Zhou C.C., Tu T., Chai C.Y.,
RA   Gao J.L., Fan L.J., van de Weg E., Wang J.Y., Gao Z.S.;
RT   "The red bayberry genome and genetic basis of sex determination.";
RL   Plant Biotechnol. J. 17:397-409(2019).
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAB1220518.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; RXIC02000021; KAB1220518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6A1W9Y9; -.
DR   OrthoDB; 10009520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000516437; Chromosome 3.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   FunFam; 1.20.120.1750:FF:000027; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 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   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF21235; UBA_ARI1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
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:UP000516437};
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..344
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          140..186
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          300..340
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   523 AA;  59776 MW;  0FE0FA4B3D023112 CRC64;
     MEETDFDSDR AAEDYYYSSA DDATRDGAVS EDADWNFDSM EEEDLLDSEH AESHKGSDRS
     YRILKKEDVR QRQEDAIAEV STVLSVPRPA ATILLHRFNW SVSQVHEGWF ADEDGVRKSV
     GFLDHTRPFS DIDASDRITC GICLDPYPPA EIFPAGCGHP FCRECWGGYI RTSINDGPGC
     LTLRCPEPSC RAAVDRDMID KLAPSEDEKK KYSEYLLRSY IDENKKIKWC PGPDCECAAE
     FDAGGGDSWD VSCPCYYSFC WNCLEDAHRP VDCQTVANWI SKNKDQSETQ LWILARTKPC
     PKCQRPIEKN MGCMHMTCNP SCGHEFCWTC LGDWNNHNSC NGYNGTDAME VDKHRKKANK
     YVAKYAHYYE RWAANDLLRQ LALATLHRMQ TEQLTRLSSV QGKAENDLWF ITEAWAQIVD
     CRRALKWTYV YGYYLSENEG AKRRLFEFLK GEAETGLERL QECADKELQQ FLDDDGPSKY
     FEEFNAKLKG LTAVTRTYFE KLIKALENGL SEVQTTGTSG EED
//
DBGET integrated database retrieval system