ID A0A3B6B6M6_WHEAT Unreviewed; 595 AA.
AC A0A3B6B6M6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=CFC21_019712 {ECO:0000313|EMBL:KAF7004505.1};
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:TraesCS2A02G526800.2};
RN [1] {ECO:0000313|EMBL:KAF7004505.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7004505.1};
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:TraesCS2A02G526800.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS2A02G526800.2};
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:TraesCS2A02G526800.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7004505.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7004505.1};
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 -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR EMBL; CM022214; KAF7004505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6B6M6; -.
DR STRING; 4565.A0A3B6B6M6; -.
DR EnsemblPlants; TraesCS2A02G526800.2; TraesCS2A02G526800.2; TraesCS2A02G526800.
DR Gramene; TraesCS2A02G526800.2; TraesCS2A02G526800.2; TraesCS2A02G526800.
DR Gramene; TraesCS2A03G1221700.2; TraesCS2A03G1221700.2.CDS; TraesCS2A03G1221700.
DR Proteomes; UP000019116; Chromosome 2A.
DR Proteomes; UP000815260; Chromosome 2A.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
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:SF281; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR SMART; SM00184; RING; 3.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..595
FT /note="RING-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039989161"
FT TRANSMEM 111..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..275
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 372..417
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 176..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 63865 MW; 93F90570089444AF CRC64;
MPSAGIVSSS AAAFLLLLFV LLGEGQPAEG FMSKNGSEAF LAPEPEVRYC YRRSVTDGEA
KLTKTVAVGP IELGLGAVPT SKTTAVPADT QAPTPPALAP PAAETGLSWR AKAWCCWVLA
VATVVLVFVV RPETFLVSPR IDGMFITDGE GDPPVDGNQH TTMDMDTVPD ILKVSVDSSE
TRRERGSSPM PRPQPRDPML IADSNGDSPV DGHHAYDGRG ELFYCPMCME TAPIILKSRF
GSCDDHVFCS SCVAKYVAVK QRQDVALPVE CPDCKDDASL NSDGEGNEDS PADGDGKRFY
CAKCMHVVPC ACIRPSFTSC AHDLCSSCVS QQLQGRRRQA GKLPRHQPAD LLPKPKGNGD
LPVDVDGELL DCAICMELVP GTLRFRVNSC AHAFCSSCVA QYIAAKLDDM VARIECPHPG
CEDGAVEPES CHGIIPTDLL DKWGLLLCEL AVGAKSNTGQ EDVLPVPGML GAPARRQRGG
VPALPPAFLR PVRRAVARRL GVRRVPEARA GRARPGGPLA PASRRQGGLA AVPRVPDVRG
EIGRVQLHQM QVWIQLLLPM RIRVVRAKPL LQQVQALIST VWLAMEGRFL PPTTT
//
