ID A0A1D5UHK6_WHEAT Unreviewed; 365 AA.
AC A0A1D5UHK6;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=E3 ubiquitin-protein ligase {ECO:0000313|EnsemblPlants:TraesCS2D02G600200.1};
GN ORFNames=CAMPLR22A2D_LOCUS1127 {ECO:0000313|EMBL:SPT16529.1},
GN CFC21_033183 {ECO:0000313|EMBL:KAF7020059.1};
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:TraesCS2D02G600200.1};
RN [1] {ECO:0000313|EMBL:KAF7020059.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7020059.1};
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:TraesCS2D02G600200.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS2D02G600200.1};
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:SPT16529.1, 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:TraesCS2D02G600200.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [5] {ECO:0000313|EMBL:KAF7020059.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7020059.1};
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; CM022216; KAF7020059.1; -; Genomic_DNA.
DR EMBL; LS480641; SPT16529.1; -; Genomic_DNA.
DR STRING; 4565.A0A1D5UHK6; -.
DR EnsemblPlants; TraesCS2D02G600200.1; TraesCS2D02G600200.1; TraesCS2D02G600200.
DR Gramene; TraesCS2D02G600200.1; TraesCS2D02G600200.1; TraesCS2D02G600200.
DR Gramene; TraesCS2D03G1265100.1; TraesCS2D03G1265100.1.CDS; TraesCS2D03G1265100.
DR OMA; HEMRQHE; -.
DR OrthoDB; 387406at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Chromosome 2D.
DR Proteomes; UP000280104; Chromosome ii.
DR Proteomes; UP000815260; Chromosome 2D.
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:SF17; RING-TYPE E3 UBIQUITIN TRANSFERASE; 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 180..238
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 41323 MW; D381ACF29B1586B6 CRC64;
MSYSGSGGGK RLRTSPSEAE GSPRRRRGSP SVYSPSPSPY RSPSPLPSPS TYRSLSHSPS
PCRSWSQRPP SNDDADDLSR SRGSDDLDRH GRRPAWRPHA NKELGEHGRT GEYSVRIDDY
DRLFTCKACR RMLSPPVYQC PFAHVTCSRC HEEVGDNRCS CCGSGNGYGR NRVVEEFLGR
IRFSCRNKVH ACEAFLPHHE MRQHEQTCRH EPIFCPVPQC GFASRAVALT THLTLRHHWD
TIRFHYDENF RASAFTSTIF QSRDDGELFF LDSFSEGRGI ALSTICIRPE NAREQEFVYE
LKTPVGNGGR RPWLQMQSTA RNTSLRHGLG EKEKVFLLVP KDLPGTEDGN VEVCIRKLGH
QRDSV
//
