ID   W9R9P4_9ROSA            Unreviewed;       561 AA.
AC   W9R9P4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=L484_005891 {ECO:0000313|EMBL:EXB60292.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB60292.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) 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; KE344394; EXB60292.1; -; Genomic_DNA.
DR   RefSeq; XP_010095466.1; XM_010097164.1.
DR   AlphaFoldDB; W9R9P4; -.
DR   STRING; 981085.W9R9P4; -.
DR   GeneID; 21389343; -.
DR   KEGG; mnt:21389343; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   OrthoDB; 3084186at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd16773; RING-HC_RBR_TRIAD1; 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   PANTHER; PTHR11685:SF395; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
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:UP000030645};
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          163..373
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          167..215
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   561 AA;  65539 MW;  9BD618D2ED1C4677 CRC64;
     MEEYESIDNE SGYPDYEDDF EFVFVEECES TDNESGYPDY EDDFEFGFVE EYESSDNESG
     YPDYEDNFEF GLEEETRTIA GSQQIEVISK ESLLAAQRDD LLRVMDVLSL KEHDAWSLLI
     HYSWDVEKLL SVLVEKGEDE VYAEAGVTLM ERNEDLFSFM FSSSVMCMIC VKEVPGNKVT
     TMECGHYFCN TCWTEHFISK INESQSEQIR CMAHQCNAIC DISKVRTLVS TRDPHLAEKF
     DQLLLESYIE ANRKVKWCPS VPHCGNAIRV DGNVLCEVEC ACGLQFCFKC LSEAHSPCSC
     LMWELWNKSC QGKSETVKCI LEQTKICPEC YELFEKDGEC DLRTFVSGEP FCLLCGRHAY
     DSCGGFQKEK QVKIRHRNKD IWYYLHYHHR YRDQTQTFDL ERKLKQAAED MIFLFRENYF
     KSRVFCWVFD AFNRVSKARR ILSFTYPFAY CMFGPVLFKD HDMPKQEIRI KQNIFDAHLQ
     QLVENIERLS SLLEKPFEFY EEDSLMKLKM QIVNHSAVTD KLCKNLYDCI ENDLLGPLQS
     EIHNIAPYKS NGVEKASDHC L
//