ID A0A0D9X8I5_9ORYZ Unreviewed; 531 AA.
AC A0A0D9X8I5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR08G13890.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR08G13890.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR08G13890.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR08G13890.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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 -!- 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 AlphaFoldDB; A0A0D9X8I5; -.
DR STRING; 77586.A0A0D9X8I5; -.
DR EnsemblPlants; LPERR08G13890.1; LPERR08G13890.1; LPERR08G13890.
DR Gramene; LPERR08G13890.1; LPERR08G13890.1; LPERR08G13890.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_518168_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 8.
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:InterPro.
DR CDD; cd22582; BRcat_RBR_unk; 2.
DR CDD; cd22584; Rcat_RBR_unk; 2.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR027370; Znf-RING_euk.
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 PANTHER; PTHR11685:SF225; RING ZN FINGER-CONTAINING PROTEIN; 1.
DR Pfam; PF01485; IBR; 4.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00647; IBR; 4.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 6.
DR PROSITE; PS51873; TRIAD; 2.
DR PROSITE; PS00518; ZF_RING_1; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
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 106..323
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 110..160
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 319..531
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 323..371
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 531 AA; 57556 MW; 1612765827377F7E CRC64;
MASGSGSSSS SDADLTVLVD DFYFSVLSHG RNGDDGDDDD ELFPISDEKY ASELQLQEVI
MSSSAIVASS RRTMTPSIES QQVIFIGESS SSKAASSSSA AATTVAMVFC KICMDAVPEA
DAHQASWGCD HAFCGGCLAG YIAAKIQENR IAGVNCPEER CRGELDPELC QGIIPREVFD
RWGAALCEAM LLGAKRTYCP FKDCSAMMLD DGGEVVTESE CPSCRRLFCA ACDVPWHAGA
DCAAYRKLGK GDRGKEDLML LEMAKGRKWK RCPKCKFFVE KSEGCLHITC RCGFEFCYGC
GGQWGITHSK EEKAGKQQRH PSCSICMEPM PPTEAHRGGV GCAHEFCRAC LAGHVRAKLD
SSGSAGAVRC PDASCGGALD PELCRVALPS DVFERWCAAL CEAMFVGARR TYCPFPGCSE
MMVADDDGEE GSCVTQTECQ GCRRLFCARC GVPWHAGVSC GEFERLGEGE RGREDLLLVE
AARNGKWKRC PRCRFYVEKS NGCLHITCRC GFEFCYGCGK PWQLIHDGCS G
//
