ID A0A3B5YSQ5_WHEAT Unreviewed; 597 AA.
AC A0A3B5YSQ5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=RBR-type E3 ubiquitin transferase {ECO:0000313|EnsemblPlants:TraesCS1B02G065800.1};
GN ORFNames=CFC21_005288 {ECO:0000313|EMBL:KAF6987667.1};
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:TraesCS1B02G065800.1};
RN [1] {ECO:0000313|EMBL:KAF6987667.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF6987667.1};
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:TraesCS1B02G065800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS1B02G065800.1};
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|EnsemblPlants:TraesCS1B02G065800.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF6987667.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF6987667.1};
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; CM022212; KAF6987667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B5YSQ5; -.
DR STRING; 4565.A0A3B5YSQ5; -.
DR PaxDb; 4565-Traes_1DS_7DCFDE673-1; -.
DR EnsemblPlants; TraesCS1B02G065800.1; TraesCS1B02G065800.1; TraesCS1B02G065800.
DR Gramene; TraesCS1B02G065800.1; TraesCS1B02G065800.1; TraesCS1B02G065800.
DR Gramene; TraesCS1B03G0163600.1; TraesCS1B03G0163600.1.CDS; TraesCS1B03G0163600.
DR Gramene; TraesPAR_scaffold_042296_01G000100.1; TraesPAR_scaffold_042296_01G000100.1; TraesPAR_scaffold_042296_01G000100.
DR OMA; KHACRDD; -.
DR OrthoDB; 4338126at2759; -.
DR Proteomes; UP000019116; Chromosome 1B.
DR Proteomes; UP000815260; Chromosome 1B.
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 CDD; cd23134; RING-HC_ITT1-like; 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; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685:SF237; E3 UBIQUITIN-PROTEIN LIGASE RNF14; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 3.
DR SMART; SM00184; RING; 3.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF57850; RING/U-box; 4.
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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 93..234
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 288..508
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 COILED 411..438
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 597 AA; 67726 MW; EBB7517A38E02375 CRC64;
MPRKYWKPRG GPGCVAPAPE LHWKALNPNP VPAEVPECSR SRAAEVSDDD AFVDVPATAE
DAVVEEEIAT KLVGIHMELS QEELRANHQM QEDEIFALEA IFGDSIVILN KKEGQRSFQV
HVHIEIPDDG IDVSARLDYG TGTLNYGETC DGDASDNLVY KFRVEHLPPI LLTCYLPSSY
PSHQPPSFTI STEWLDTVKI SSLCQMLDMI WEEQQGMEVI YQWVQWLQNS LLSHLGFADE
IILSKGDLTC HEDGRDKHAC RDDSAPDVII TRIMRYDDDK RHEAFLHDIH DCMICFSEFP
GVDFVTLPCH HFFCRKCIQT YCKIHVKEGT VLKLTCPDTK CEGVVSPHIL KTLLAEDEYE
RWEKLLLQRT LDAMNDLVYC PRCETACLED ESNDAVCPSC LFSFCTLCTS HRHVGKQCMT
AEEKIRKLEE RLKSRQERGD QNLTDEVLSL QAIMRDAKQC PRCKIAIYKI SGCNKMTCSN
CGHYFCYQCN FAIVGYEHFR PGACDLFSRE EIRRWEARMN PGRGRVEDAP APAPLPQGRY
RHPCPTCGKG TPKIGNNNHI SCGSCQTGFC ALCRKTVHKT SQHFGPRGCK QHTPDRD
//
