ID A0A6J0MY47_RAPSA Unreviewed; 523 AA.
AC A0A6J0MY47;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC108847874 {ECO:0000313|RefSeq:XP_018476738.1};
OS Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus.
OX NCBI_TaxID=3726 {ECO:0000313|Proteomes:UP000504610, ECO:0000313|RefSeq:XP_018476738.1};
RN [1] {ECO:0000313|Proteomes:UP000504610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WK10039 {ECO:0000313|Proteomes:UP000504610};
RX PubMed=30722041;
RA Yu H.J., Baek S., Lee Y.J., Cho A., Mun J.H.;
RT "The radish genome database (RadishGD): an integrated information resource
RT for radish genomics.";
RL Database 2019:5306501-5306501(2019).
RN [2] {ECO:0000313|RefSeq:XP_018476738.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_018476738.1};
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 -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC {ECO:0000256|ARBA:ARBA00044508}.
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DR RefSeq; XP_018476738.1; XM_018621236.2.
DR AlphaFoldDB; A0A6J0MY47; -.
DR GeneID; 108847874; -.
DR KEGG; rsz:108847874; -.
DR OrthoDB; 10009520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000504610; Chromosome 3.
DR GO; GO:0003676; F:nucleic acid binding; 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; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd20354; Rcat_RBR_RNF14; 1.
DR CDD; cd23141; RING-HC_ARI6-like; 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; IPR047548; Rcat_RBR_RNF14.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PS50158; ZF_CCHC; 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:UP000504610};
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:PRU00047}.
FT DOMAIN 123..332
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 127..173
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 249..262
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 504..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 60426 MW; 4DD9D1DF66AFB21F CRC64;
MDYSDDDVMV NTDSGEESLL SDNQVDSDYE FTDQDMDNAS ITKRSQLSYL VLKEDDIRKH
QRTDIEHVST VLSISQVEAI VLLLHYQWNV SKVQDEWFTD EEKVRELVGI LKEPVVDLND
REMNIECGIC FESYPQKEVA TVSCGHPYCN ACWTGYITTS INDGPGCLTV KCPEPSCSAV
ACQDMIDKVI TDKELKEKYY RYFVRSYVEA SGNKIKWCPS PGCENAIDFE SRSGSEHYDV
SCLCSHEFCW NCGEDAHRPV DCDTVSKWIA KNTDESENTN WILANTKPCP NCKRQIEKSM
GCNVMRCSIC KCMFCWNCLL PFTDHKKCNK FEGDDETDIN KRKRAKSAID RYMHYFERWA
SNQSSRVIAM ADLKKFQSVQ LKLLSLRQGT TESQLQFTIE AWRQIIECRR VLKWTYAYGY
YLPEQEQTKK QFFEYLQGEA EAGLERLHHC AEEELKHFVF KTQDSSKKFG DFRRKLTGLT
EATKTYFENL VKALENGLAD VALNESSKSE TNSKPATKRR KLK
//
