ID A0A1D5UU75_WHEAT Unreviewed; 594 AA.
AC A0A1D5UU75;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=RBR-type E3 ubiquitin transferase {ECO:0000313|EnsemblPlants:TraesCS2D02G444400.1};
GN ORFNames=CAMPLR22A2D_LOCUS4455 {ECO:0000313|EMBL:SPT19830.1},
GN CFC21_031555 {ECO:0000313|EMBL:KAF7018254.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2D02G444400.1};
RN [1] {ECO:0000313|EMBL:KAF7018254.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7018254.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS2D02G444400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS2D02G444400.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EMBL:SPT19830.1, ECO:0000313|Proteomes:UP000280104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Thind KAUR A.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblPlants:TraesCS2D02G444400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [5] {ECO:0000313|EMBL:KAF7018254.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7018254.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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 -!- 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; CM022216; KAF7018254.1; -; Genomic_DNA.
DR EMBL; LS480641; SPT19830.1; -; Genomic_DNA.
DR STRING; 4565.A0A1D5UU75; -.
DR EnsemblPlants; TraesCS2D02G444400.1; TraesCS2D02G444400.1; TraesCS2D02G444400.
DR Gramene; TraesCAD_scaffold_118104_01G000100.1; TraesCAD_scaffold_118104_01G000100.1; TraesCAD_scaffold_118104_01G000100.
DR Gramene; TraesCLE_scaffold_109201_01G000100.1; TraesCLE_scaffold_109201_01G000100.1; TraesCLE_scaffold_109201_01G000100.
DR Gramene; TraesCS2D02G444400.1; TraesCS2D02G444400.1; TraesCS2D02G444400.
DR Gramene; TraesCS2D03G0997000.1; TraesCS2D03G0997000.1.CDS; TraesCS2D03G0997000.
DR Gramene; TraesPAR_scaffold_138279_01G000100.1; TraesPAR_scaffold_138279_01G000100.1; TraesPAR_scaffold_138279_01G000100.
DR Gramene; TraesROB_scaffold_106498_01G000100.1; TraesROB_scaffold_106498_01G000100.1; TraesROB_scaffold_106498_01G000100.
DR Gramene; TraesWEE_scaffold_165453_01G000100.1; TraesWEE_scaffold_165453_01G000100.1; TraesWEE_scaffold_165453_01G000100.
DR OMA; QCITAEQ; -.
DR OrthoDB; 4338126at2759; -.
DR Proteomes; UP000019116; Chromosome 2D.
DR Proteomes; UP000280104; Chromosome ii.
DR Proteomes; UP000815260; Chromosome 2D.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
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; cd20341; BRcat_RBR_RNF14; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 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; IPR006575; RWD_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
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:SF297; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS50908; RWD; 1.
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:UP000019116};
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 101..237
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 288..504
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 292..340
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 67050 MW; D3850B110C936882 CRC64;
MAAASAVSSS SRALGPHRDV PAHRFSAKAF SSSSSRPVEA RPVLCGGGGG EDDVLDLDFP
WVAEGEAESR LEEAAAAGLH LRAEEAGDED EIRDNRQRQE DELMALEAIY GDDLVEFESK
GGLRYFQIYI HYDLHDGAEV CAKLSSASAN RKDGGCQPDE FSYTCNFEHL PPLILTCLLP
KSYPSKDPPY FNVTVKWMDG HNVSQLCEML DTIWAELPGQ EVVYQWVEWI RSSSLSHLMF
DGKITLGSDC PTHKGDNRAI SRSLSLESVI PSMLNYSSKK HYEAFLENLH TCRICLNQSK
GSNFVRLPCQ HLFCVKCMET LCRMHVKEGT VFHLVCPETK CNASIPPYLL KRLLREEEFE
RWDRLALEKA LDSMSDVVYC PKCAIGCLED EDNNAQCPKC SFIFCSFCKD PRHPGKQCIT
AEQKLQRKQA SGRMTEWEMV KEMLSIKKLY RDAILCPKCK VPISRTEGCN KIECGNCGQF
LCFRCGKAIT GYDHFRSKGC QLFAPVDNDT TVWQRRMEVL KNERGMRAQR RQVAGSDTVK
CPKCRQEVLK DDDKYIYCWT CRASYSTRSK QHGQGSSRSR MRGKGAIKDD HGDA
//
