ID M1BDZ2_SOLTU Unreviewed; 589 AA.
AC M1BDZ2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Ubiquitin-protein ligase {ECO:0000313|EnsemblPlants:PGSC0003DMT400043038};
GN Name=102585691 {ECO:0000313|EnsemblPlants:PGSC0003DMT400043038};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400043038, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400043038}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400043038};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; M1BDZ2; -.
DR EnsemblPlants; PGSC0003DMT400043038; PGSC0003DMT400043038; PGSC0003DMG400016690.
DR Gramene; PGSC0003DMT400043038; PGSC0003DMT400043038; PGSC0003DMG400016690.
DR HOGENOM; CLU_454492_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1BDZ2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00084; HMG-box_SF; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
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:SF13; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT DOMAIN 57..126
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 407..465
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT DNA_BIND 57..126
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 65831 MW; 8056A57F83F3EE56 CRC64;
MVEVEASPPD LNDKASSPHH TMIMVPTEGE FAMGKRKDQG ISEPEGSRKK KKKQVATPRP
ACSWVHFSRD FIKEYSATHP ESSGLKAATK AASDAWKLMG PEEKAKYTTR AREVWDKYLS
SAPARAPKPR RQTKLVTRCS PGRLLNVLQR LTPDQKEAVK SMGFGNILGL RCRTLRRSLC
LWLLERFNTV RRSLEICGER IPLTPRDVEL VMGLPASGKD VVNSGSDELI LQLRKRYNAT
NRGISVRLLE ERLAAPEAGE DFKRSFVLYV MGTLLCPTAR LDVSPSFLHF LTNMDVLHQY
NWGKFLLDRL VREISRFRQG KQRAVGGCLL FLQVVCMDRG LGMGSLGYKA QTDSMPLRAV
EPMQEVSHAQ DMEDQEYEDT FTEQEHAHTD SIEGNVVCAE IEVVAGSGPV PCGNIKYGCT
EIVDYSKKRD HEEACPYAPC PCPLQNCKFV DSSKQLSSHF SSKHWDSGRH FQYDCPLPIS
LSKKETFLVL QAEKDGILFL LSKGTQSIGH TIVITCIGPR SSKECYLYDV VSEKGSSSLR
LKSSAHSFPG RFQGLPPVDF LLVPFAHLDS SGQLDLEICI WSPTEPGSE
//
