ID I1IVA4_BRADI Unreviewed; 583 AA.
AC I1IVA4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN Name=100828328 {ECO:0000313|EnsemblPlants:PNT65620};
GN ORFNames=BRADI_4g45200v3 {ECO:0000313|EMBL:PNT65620.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:PNT65620.1};
RN [1] {ECO:0000313|EMBL:PNT65620.1, ECO:0000313|EnsemblPlants:PNT65620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT65620.1,
RC ECO:0000313|EnsemblPlants:PNT65620};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:PNT65620.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT65620.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:PNT65620}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT65620};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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 EMBL; CM000883; PNT65620.1; -; Genomic_DNA.
DR RefSeq; XP_010238832.1; XM_010240530.2.
DR AlphaFoldDB; I1IVA4; -.
DR STRING; 15368.I1IVA4; -.
DR EnsemblPlants; PNT65620; PNT65620; BRADI_4g45200v3.
DR GeneID; 100828328; -.
DR Gramene; PNT65620; PNT65620; BRADI_4g45200v3.
DR KEGG; bdi:100828328; -.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_022048_8_3_1; -.
DR InParanoid; I1IVA4; -.
DR OMA; WGDCFER; -.
DR OrthoDB; 2943236at2759; -.
DR Proteomes; UP000008810; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd22582; BRcat_RBR_unk; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
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:SF459; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF13456; RVT_3; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
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:UP000008810};
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 289..510
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 293..339
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..541
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 64885 MW; 1107F4072BB702FE CRC64;
MASAAADDDL DLAFRLQLAE ALQASLRLDT RNPSSSKTPA IASSSTSSSS SRPGPLDSDA
AYALALHAAD LRRAEEDHRY AKACRAYHAR AAASVRVAAH DAVFARELAA VPEDRWADDG
DNIERPLESS AAAGPLFRVF FKGMSSKEVV APRDRDPGVA ALAVAICGPQ GEVVLRVQKP
VQAFVGGRMT LEVMALNEGL HAALGLGIQS VKIVTDYRSL SNHLLGYWHP TQKKVIDVLN
QAASLRKKFQ RCQISLVQRN QLDYVMKLAR DSIDSQVAKA AAMDASKEKR ETCTICLEDT
DVTKIHAVEG CGHRFCFSCM KEHVKVKLLD GTLPACPQDG CTTKLSVEGS KIFLSPRLLD
IMVQRIREAQ IPPTQKIYCP YPKCSALMSL SEVIRPMQES SSKYTIADAA TLRNCVKCRG
SFCISCKVPW HDRMSCYDYK RRYPHARPED AKLQNLARQQ LWRQCIKCKH MIELAEGCYH
MTCVCGYEFC YTCGKEWKEK KATCSCPLWD EGNIIHDDSD EDDDDDDDDY DEDEDDDDDY
YPANQDHGRH HGGGGAQVHY GYNNNPGRHR RGGAPRIFYN YNN
//
