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Database: UniProt
Entry: A0A565BSB2_9BRAS
LinkDB: A0A565BSB2_9BRAS
Original site: A0A565BSB2_9BRAS 
ID   A0A565BSB2_9BRAS        Unreviewed;       542 AA.
AC   A0A565BSB2;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   02-APR-2025, entry version 15.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=ANE_LOCUS14694 {ECO:0000313|EMBL:VVB04250.1};
OS   Arabis nemorensis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=586526 {ECO:0000313|EMBL:VVB04250.1, ECO:0000313|Proteomes:UP000489600};
RN   [1] {ECO:0000313|EMBL:VVB04250.1, ECO:0000313|Proteomes:UP000489600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dittberner H.;
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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; CABITT030000005; VVB04250.1; -; Genomic_DNA.
DR   OrthoDB; 10009520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000489600; Unassembled WGS sequence.
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; cd22586; Rcat_RBR_ARI1-like; 1.
DR   CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR   FunFam; 1.20.120.1750:FF:000013; 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; 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   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 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:UP000489600};
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          122..335
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          126..175
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  62172 MW;  C00E203B1EFA5909 CRC64;
     MDEEYYSVEE EDCYDSDDDS YNEEESDLQD LEDFDMEHVS TGKSTSQVIT KESLVAAQKX
     XXXXXXXXXX XXXNQARILL IHYQWNVDKL FSVFIDNGKD RLFSCAGLTV FDPSLITSRY
     XSTMSCDICM EDGLPSCNMT RMECGHCFCN DCWKEHFTVR INEGESKRIT CMAHKCNAVC
     DEDVVRKLVS PELAEKFDRF LVQSYVEDNR MVKWCPSTPH CGNAIRKLVD DGDDEVICSC
     GLQFCFSCLC ESHSPCSCLM WKLWRKKCEE ESETVTWITI NTRLCPNCNK PVHKIDGCNL
     MTCICKQHFC WLCGGATGFD HTWKTIAGHS CGKYSEDSVR QLERAKRDLD RYTHYHFRYK
     AHTDSLKLEG KLRASILEKA LSNSEKKDQS VFKEFSWITD GANLLFRSRR ILANSYPFAF
     YMFGEELFKD EMSDKEREIK KNLFEDQQQQ LEGNIEKLSG LLEEPFDGYS YDKVMGMKNQ
     ITNLCASVNH YCTKMYECIE NELLGPIPTG ANHNIAPYKA KGIEQAAEFR TDVGTSSDCG
     SS
//
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