ID A0A0D3CVT9_BRAOL Unreviewed; 379 AA.
AC A0A0D3CVT9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=106300936 {ECO:0000313|EnsemblPlants:Bo6g081050.1};
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:Bo6g081050.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo6g081050.1, 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:Bo6g081050.1}
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};
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DR RefSeq; XP_013592656.1; XM_013737202.1.
DR AlphaFoldDB; A0A0D3CVT9; -.
DR EnsemblPlants; Bo6g081050.1; Bo6g081050.1; Bo6g081050.
DR GeneID; 106300936; -.
DR Gramene; Bo6g081050.1; Bo6g081050.1; Bo6g081050.
DR KEGG; boe:106300936; -.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_035766_1_1_1; -.
DR OMA; QLISACC; -.
DR OrthoDB; 3641271at2759; -.
DR Proteomes; UP000032141; Chromosome C6.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45751; COPINE FAMILY PROTEIN 1; 1.
DR PANTHER; PTHR45751:SF16; E3 UBIQUITIN-PROTEIN LIGASE RGLG4; 1.
DR Pfam; PF07002; Copine; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 335..368
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 41369 MW; 637B3BFE4206F429 CRC64;
MSTGMGSGKG KSCPSPSDPS ISVSDKINAT REKYALIPDR FSSLDQVSKA LREAGLESSN
LILGIDFTKS NEWSGKTSFH GKSLHALGAT QNPYEKAIFV IGQTLAPFDE DNLIPCFGFG
DSTTHDEEVF SFHSDNSPCH GFEEVLSCYR RITPNLILSG PTSYGPLIHA AVDIVEKNNG
QFHVLVIVAD GQVTRGVDKA EGELSQQERT TIDAIVNASS YALSIVLIGV GDGPWEDMRK
FDDKIPKREF DNFQFVNFTE IMKRDSSESA KEAAFALAAL MEIPFQYQAA TELSLLGKTT
GLAKKINPRP PPTPYTPTIR TELPSPASEE HTQSCPICLT SQKDVAFGCG HMTCRDCGSR
IANCPICRVL ITSRLRLYT
//
