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Database: UniProt
Entry: A0A4Y7KBY0_PAPSO
LinkDB: A0A4Y7KBY0_PAPSO
Original site: A0A4Y7KBY0_PAPSO 
ID   A0A4Y7KBY0_PAPSO        Unreviewed;       304 AA.
AC   A0A4Y7KBY0;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   02-APR-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   ORFNames=C5167_033508 {ECO:0000313|EMBL:RZC70397.1};
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469 {ECO:0000313|EMBL:RZC70397.1, ECO:0000313|Proteomes:UP000316621};
RN   [1] {ECO:0000313|EMBL:RZC70397.1, ECO:0000313|Proteomes:UP000316621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HN1 {ECO:0000313|Proteomes:UP000316621};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RZC70397.1};
RX   PubMed=30166436; DOI=.1126/science.aat4096;
RA   Guo L., Winzer T., Yang X., Li Y., Ning Z., He Z., Teodor R., Lu Y.,
RA   Bowser T.A., Graham I.A., Ye K.;
RT   "The opium poppy genome and morphinan production.";
RL   Science 362:343-347(2018).
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   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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DR   EMBL; CM010721; RZC70397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Y7KBY0; -.
DR   STRING; 3469.A0A4Y7KBY0; -.
DR   EnsemblPlants; RZC70397; RZC70397; C5167_033508.
DR   Gramene; RZC70397; RZC70397; C5167_033508.
DR   OMA; SRCSIKH; -.
DR   Proteomes; UP000316621; Chromosome 7.
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:InterPro.
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   Gene3D; 1.20.120.1750; -; 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; 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   SMART; SM00647; IBR; 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:UP000316621};
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          48..265
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          52..96
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          270..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..293
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  34656 MW;  B45998E1FA08E7D0 CRC64;
     MDQVVALREK FEICNIILLT RNDVKFAIKL ARDAIDCQIT ASAESSSANE TCNICLEEKD
     IMQIFSVDGC LHRYCCSCMK QHAEVKLLHG LVPGCPHEGC QTQLIADSCK KFLTPKFIEM
     MTLRLKEASV PVTEKLYCPY PKCSTLMSKS EVLSSNDLFG TANRSGAYKC IKCHGLFCIN
     CKVPWHHGMS CLEYKRLNPR GEEAKLKSLA SQQLWRQCVK CNHMIELAEG CYHMTCRCGF
     EFCYTCGAEW KNKKATCNCP LWNEDNILYD DSDEGEDEEW YDEEEWDSED DEYVNAPRSV
     SNIG
//
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