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Database: UniProt
Entry: R0G1N0_9BRAS
LinkDB: R0G1N0_9BRAS
Original site: R0G1N0_9BRAS 
ID   R0G1N0_9BRAS            Unreviewed;       413 AA.
AC   R0G1N0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   02-APR-2025, entry version 50.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE   Flags: Fragment;
GN   ORFNames=CARUB_v10025598mg {ECO:0000313|EMBL:EOA29317.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA29317.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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}.
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DR   EMBL; KB870808; EOA29317.1; -; Genomic_DNA.
DR   RefSeq; XP_006296419.1; XM_006296357.1.
DR   AlphaFoldDB; R0G1N0; -.
DR   STRING; 81985.R0G1N0; -.
DR   KEGG; crb:17889211; -.
DR   eggNOG; KOG1812; Eukaryota.
DR   OrthoDB; 541961at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
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; cd22582; BRcat_RBR_unk; 1.
DR   CDD; cd22584; Rcat_RBR_unk; 1.
DR   FunFam; 3.30.40.10:FF:000230; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.420.10:FF:000076; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
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; PF01485; IBR; 1.
DR   Pfam; PF13456; RVT_3; 1.
DR   SMART; SM00647; IBR; 1.
DR   SMART; SM00184; RING; 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; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
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          184..395
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          188..235
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   NON_TER         413
FT                   /evidence="ECO:0000313|EMBL:EOA29317.1"
SQ   SEQUENCE   413 AA;  46942 MW;  F1631687372C89DF CRC64;
     MEDEGTLVRE RVYDLKHAGN PSPSRSSPYS LYFKGLVSEN TTELSGEFRV AICGYKDGLM
     FQMKGPIYEP AITLLEAELI ALKSGLTEAA RLGINHISIC CDHNQIYEWV MERSTPEQEN
     IALLIRDVQG IRKRFTSSKA VLVTRKQVEF AYKLGMEAIS SKTNVAMATL FHPIKTNLPA
     RIHLKKTCSI CFEDVNADEM FLVHTCHHMF CSECVKNHIE VRLAEGYMMT CPQYKCKTKL
     VYNDCVNILT PKVKEMWEQR NIEESIPVTD RVYCPNPTCS ALMSVTNFSQ LNEVKQCCVK
     CGEFFCVNCK VPWHSDLSCH GYKKLHPNPT ENDKKLQNLA DCKRWRQCSK CKQMIERSDG
     CFFLLCRCGH KFCYQCGADA GYCYHLGLGN DFEPEDTTSI DIAVGFAIVV LLV
//
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