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Database: UniProt
Entry: A0A3B6EUS2_WHEAT
LinkDB: A0A3B6EUS2_WHEAT
Original site: A0A3B6EUS2_WHEAT 
ID   A0A3B6EUS2_WHEAT        Unreviewed;       359 AA.
AC   A0A3B6EUS2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=E3 ubiquitin-protein ligase {ECO:0000313|EnsemblPlants:TraesCS3A02G505400.1};
GN   ORFNames=CFC21_038359 {ECO:0000313|EMBL:KAF7026242.1};
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:TraesCS3A02G505400.1};
RN   [1] {ECO:0000313|EMBL:KAF7026242.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7026242.1};
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:TraesCS3A02G505400.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS3A02G505400.1};
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:TraesCS3A02G505400.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7026242.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7026242.1};
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; CM022217; KAF7026242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6EUS2; -.
DR   STRING; 4565.A0A3B6EUS2; -.
DR   EnsemblPlants; TraesCS3A02G505400.1; TraesCS3A02G505400.1; TraesCS3A02G505400.
DR   Gramene; TraesCAD_scaffold_092151_01G000100.1; TraesCAD_scaffold_092151_01G000100.1; TraesCAD_scaffold_092151_01G000100.
DR   Gramene; TraesCLE_scaffold_039974_01G000100.1; TraesCLE_scaffold_039974_01G000100.1; TraesCLE_scaffold_039974_01G000100.
DR   Gramene; TraesCS3A02G505400.1; TraesCS3A02G505400.1; TraesCS3A02G505400.
DR   Gramene; TraesCS3A03G1187600.1; TraesCS3A03G1187600.1.CDS; TraesCS3A03G1187600.
DR   Gramene; TraesPAR_scaffold_072626_01G000100.1; TraesPAR_scaffold_072626_01G000100.1; TraesPAR_scaffold_072626_01G000100.
DR   Gramene; TraesRN3A0101216100.1; TraesRN3A0101216100.1; TraesRN3A0101216100.
DR   OMA; ICIGREY; -.
DR   OrthoDB; 383958at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000019116; Chromosome 3A.
DR   Proteomes; UP000815260; Chromosome 3A.
DR   GO; GO:0005737; C:cytoplasm; 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: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:SF29; RING-TYPE E3 UBIQUITIN TRANSFERASE; 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          92..158
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
FT   REGION          318..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  36949 MW;  3415231B6A154543 CRC64;
     MGLGGGGGEG VLAVVPMEAI PMAEPQIVAG GKIVGLRADL LDCHNCRLPL KPPIFKCDAE
     HLVCSSCRGL HGEACGGRAA VHSALADIFA AAATVPCGYE RYGCDAGGVV YHEAADHRRA
     CQHAPCCCPD RAGAAGIGGC GFVGSRQDLL DHISGPDHSR PIIVVRYGQP WNLSLPLSRR
     WHILVGEEDK AVAAAAGAER HRNLFLVSLG ERGATTAVSL VCVRVDGTAP SAPQFACKLA
     VESDGCRLTL ESPLVCSSSL SGGLPAEVKC LPVPKDFLSG DSVPLSIHIE KLPAPPAPPL
     GLGVAPACTS PVAATPPPCP AATIPPSRPS SGSSDNVAVK TVITDQSYKK RKSANPRKL
//
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