ID A0A0D3BHK6_BRAOL Unreviewed; 361 AA.
AC A0A0D3BHK6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=106336306 {ECO:0000313|EnsemblPlants:Bo3g132730.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo3g132730.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo3g132730.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo3g132730.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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 RefSeq; XP_013630550.1; XM_013775096.1.
DR AlphaFoldDB; A0A0D3BHK6; -.
DR STRING; 109376.A0A0D3BHK6; -.
DR EnsemblPlants; Bo3g132730.1; Bo3g132730.1; Bo3g132730.
DR GeneID; 106336306; -.
DR Gramene; Bo3g132730.1; Bo3g132730.1; Bo3g132730.
DR KEGG; boe:106336306; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_040377_0_0_1; -.
DR OMA; TETHCAV; -.
DR OrthoDB; 469114at2759; -.
DR Proteomes; UP000032141; Chromosome C3.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR CDD; cd16667; RING-H2_RNF126-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR010543; DUF1117.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF225; E3 UBIQUITIN-PROTEIN LIGASE RDUF1; 1.
DR Pfam; PF06547; DUF1117; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 188..229
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 55..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 39535 MW; 28D809DD58DD9575 CRC64;
MMPSRSATTT AAPTTTETTT SYWCYSCTRF VSVSTGGYVL CPYCNGGFIE DSSAAEAPTT
TTPVSQVEDS HRSVIRRRRS NRRTSFNPVI VLHGGAGGER VENEEGDRRP YEFYYDDGSG
SGLRPLPDSV SEILMGSGFE RLLEQLSQIE ASGNGIGRSG NPPASKSAIE SLPRVEMGDF
HIKAEANCAV CTEVFEAGAE GREMPCKHIF HGDCIVPWLS IRNSCPVCRF ELPSDPVQRS
IEEEHAVGMT IWRLPGGGFA VGRFNAAMRE GERILPVVLT EVDGGGLGSN EGPRRISWVR
DHGTPEISRN AARAGRLRRA ARGMVSFMRR MRPNRGSSSS NVIDLDTNVM NRSTSLIRRF
F
//
