BBR_ARATH
ID BBR_ARATH Reviewed; 340 AA.
AC Q9LT17; Q8LG55;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=E3 ubiquitin ligase BIG BROTHER-related;
DE Short=AtBBR;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8L649};
DE AltName: Full=RING-type E3 ubiquitin transferase BIG BROTHER-related {ECO:0000305};
GN Name=BBR; OrderedLocusNames=At3g19910; ORFNames=MPN9.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-ligase probably involved in organ size
CC regulation. {ECO:0000250|UniProtKB:Q8L649}.
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:0000250|UniProtKB:Q8L649};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q8L649}.
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DR EMBL; AB025631; BAB01306.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76307.1; -; Genomic_DNA.
DR EMBL; AY045590; AAK73948.1; -; mRNA.
DR EMBL; AY045984; AAK76658.1; -; mRNA.
DR EMBL; AY079353; AAL85084.1; -; mRNA.
DR EMBL; AY084453; AAM61025.1; -; mRNA.
DR RefSeq; NP_566651.1; NM_112881.5.
DR AlphaFoldDB; Q9LT17; -.
DR SMR; Q9LT17; -.
DR STRING; 3702.AT3G19910.1; -.
DR iPTMnet; Q9LT17; -.
DR PaxDb; Q9LT17; -.
DR PRIDE; Q9LT17; -.
DR ProteomicsDB; 241129; -.
DR EnsemblPlants; AT3G19910.1; AT3G19910.1; AT3G19910.
DR GeneID; 821529; -.
DR Gramene; AT3G19910.1; AT3G19910.1; AT3G19910.
DR KEGG; ath:AT3G19910; -.
DR Araport; AT3G19910; -.
DR TAIR; locus:2092271; AT3G19910.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_059266_1_0_1; -.
DR InParanoid; Q9LT17; -.
DR OMA; HANDPQD; -.
DR OrthoDB; 1191740at2759; -.
DR PhylomeDB; Q9LT17; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LT17; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LT17; baseline and differential.
DR Genevisible; Q9LT17; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR043312; AtBBR-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47530; PTHR47530; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..340
FT /note="E3 ubiquitin ligase BIG BROTHER-related"
FT /id="PRO_0000396944"
FT ZN_FING 288..329
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 235
FT /note="W -> R (in Ref. 4; AAM61025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37263 MW; 6619727E1AFC9737 CRC64;
MPMENDNGPH VGNVVVTAEQ ATKINETDGR LPENRQTGVV SDTGSGSERG EQGVGESAVA
VAVPVEESGS ISVGELPAPR SSSARVPFTN LSQIDADLAL ARTLQEQERA YMMLTMNSEI
SDYGSWETGS YVYDEDEFDD PENEDEDDDE DEYETDDDPQ EDGLDVNVHA NEDDQEDDGN
SDIEEVAYTD DEAYARALQE AEERDMAARL SALSGLANRV VEDLEDESHT SQDAWDEMDP
DELSYEELLA LGDIVGTESR GLSADTIASL PSKRYKEGDN QNGTNESCVI CRLDYEDDED
LILLPCKHSY HSECINNWLK INKVCPVCSA EVSTSTSGQS