ID A0A3B6SFM5_WHEAT Unreviewed; 228 AA.
AC A0A3B6SFM5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=E3 ubiquitin-protein ligase {ECO:0000313|EnsemblPlants:TraesCS7B02G147600.1.cds1};
GN ORFNames=CFC21_102498 {ECO:0000313|EMBL:KAF7101102.1};
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:TraesCS7B02G147600.1.cds1};
RN [1] {ECO:0000313|EMBL:KAF7101102.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7101102.1};
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:TraesCS7B02G147600.1.cds1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7B02G147600.1.cds1};
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:TraesCS7B02G147600.1.cds1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7101102.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7101102.1};
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: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. It probably triggers the ubiquitin-mediated
CC degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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DR EMBL; CM022230; KAF7101102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6SFM5; -.
DR STRING; 4565.A0A3B6SFM5; -.
DR EnsemblPlants; TraesCS7B02G147600.1; TraesCS7B02G147600.1.cds1; TraesCS7B02G147600.
DR Gramene; TraesCS7B02G147600.1; TraesCS7B02G147600.1.cds1; TraesCS7B02G147600.
DR Gramene; TraesCS7B03G0401600.1; TraesCS7B03G0401600.1.CDS1; TraesCS7B03G0401600.
DR Gramene; TraesROB_scaffold_009832_01G000100.1; TraesROB_scaffold_009832_01G000100.1; TraesROB_scaffold_009832_01G000100.
DR Gramene; TraesWEE_scaffold_022531_01G000100.1; TraesWEE_scaffold_022531_01G000100.1; TraesWEE_scaffold_022531_01G000100.
DR OMA; YEPRDHE; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Chromosome 7B.
DR Proteomes; UP000815260; Chromosome 7B.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044286; SINL_plant.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR PANTHER; PTHR46632:SF36; SIAH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT DOMAIN 44..102
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
SQ SEQUENCE 228 AA; 24409 MW; F826AC8A2E86952E CRC64;
MQCAAGCHTA CSRCQSKLPG KRCHSCDQGG AYVRCPVMDG IVCSARVRCA YHQHGCPSYV
PYYEPRDHES VCPHAPCSCT EPGCAFVGSP RRFLAHLIDA HSWPVHTIRY GTHLGLGVRA
SEPRVLLVAA EEDEAVFLLA IGALGPARAV SVVCVRANGE AGQQYGLKLW AHASNERAIT
LDCEVTSSAA PGEVAVETVE FLTVPPAKMT GPQADKEMVI TVCIDKSF
//
