ID A0A8B8QGI4_9MYRT Unreviewed; 564 AA.
AC A0A8B8QGI4;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC115752227 {ECO:0000313|RefSeq:XP_030546185.1};
OS Rhodamnia argentea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Myrteae;
OC Australasian group; Rhodamnia.
OX NCBI_TaxID=178133 {ECO:0000313|Proteomes:UP000694854, ECO:0000313|RefSeq:XP_030546185.1};
RN [1] {ECO:0000313|RefSeq:XP_030546185.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) 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 -!- 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 ---------------------------------------------------------------------------
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 RefSeq; XP_030546185.1; XM_030690325.1.
DR KEGG; rarg:115752227; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000694854; Unplaced.
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; 1.20.120.1750:FF:000019; RBR-type E3 ubiquitin transferase; 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; IPR012337; RNaseH-like_sf.
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; 2.
DR Pfam; PF13456; RVT_3; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
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:UP000694854};
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 310..528
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 314..358
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 535..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 63633 MW; 3712AFAB87AAC656 CRC64;
MGSRSSIDDD LRSLVDEQHR ELMAAQALES DLDLAYRLQL EEALAASLSL LPSSSSPPSQ
TLAPPDDVVS PSFVSLQSDE LSRFQREFKD RELSEAEARR VREDLHRRIH DQKVATEIMT
IPDDDWGDWG DEFERPFGEG CSKDFGGGGG EVVDVFSLYC KGLVSDETVE GQKCNSVFAG
VGIAVCDFKG NLIFEVRKPL VGPGTSKSKV VVEAKALVEG LNAAVALELK RIVFYCDYFP
LFQFITRRWM PKQRKVAALV EQATLLRRKF DQCNFLLVAR NEFKFAFKLA RDAITSQIVR
RVDSVASKNP KETCVICLED TDVSQIFAID GCLHRYCLSC MRQHVEVKLL HGMVPRCPHE
GCKSDLNVSS CSKFLTPKLI EMMTQRLKEA SIPVTEKIYC PYPTCSALMS KSEVSESSIT
SGAGAARSGA RKCIKCHGLF CINCKVPWHS SLTCLAYKKL HPHPPAEDAK LKSLASRNLW
RQCIKCNHMI ELSEGCYHMT CRCGYEFCYN CGAEWKDKKP TCSCPLWEED NILYDDDRDF
DDDDDDDDEE DEEWYTDSDE DYLI
//
