BRE1A_ORYSI
ID BRE1A_ORYSI Reviewed; 884 AA.
AC A2XW69; B8ASX7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1-like 1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8RXD6};
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1-like 1 {ECO:0000305};
GN Name=BRE1A; ORFNames=OsI_16895;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that monoubiquitinates H2B to
CC form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for H3K4me and
CC maybe H3K79me. It thereby plays a central role in histone code and gene
CC regulation. Forms a ubiquitin ligase complex in cooperation with the E2
CC enzyme UBC2/RAD6. {ECO:0000250|UniProtKB:Q8RXD6}.
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:Q8RXD6};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8RXD6}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR EMBL; CM000129; EEC77758.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XW69; -.
DR SMR; A2XW69; -.
DR STRING; 39946.A2XW69; -.
DR PRIDE; A2XW69; -.
DR EnsemblPlants; BGIOSGA014597-TA; BGIOSGA014597-PA; BGIOSGA014597.
DR Gramene; BGIOSGA014597-TA; BGIOSGA014597-PA; BGIOSGA014597.
DR HOGENOM; CLU_002640_1_0_1; -.
DR OMA; THIEIMT; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:EnsemblPlants.
DR GO; GO:0051301; P:cell division; IEA:EnsemblPlants.
DR GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR GO; GO:0033523; P:histone H2B ubiquitination; IEA:EnsemblPlants.
DR GO; GO:0010390; P:histone monoubiquitination; IEA:EnsemblPlants.
DR GO; GO:0045087; P:innate immune response; IEA:EnsemblPlants.
DR GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:EnsemblPlants.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblPlants.
DR GO; GO:0010162; P:seed dormancy process; IEA:EnsemblPlants.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..884
FT /note="E3 ubiquitin-protein ligase BRE1-like 1"
FT /id="PRO_0000293111"
FT ZN_FING 832..871
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..86
FT /evidence="ECO:0000255"
FT COILED 216..541
FT /evidence="ECO:0000255"
FT COILED 580..663
FT /evidence="ECO:0000255"
FT COILED 696..762
FT /evidence="ECO:0000255"
FT COILED 789..827
FT /evidence="ECO:0000255"
FT COMPBIAS 107..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 100399 MW; 2B2CB3E6D8F58A78 CRC64;
MGSTGEPDRK RRLSSSVAPG GGAPVSPAKR LAVAPTSEDK KLDFTVLKYK NQKLSEQLEA
HKFEYRALEN KFAGLKEKQR THNETLSLVN SSWEQLVADL KSRSFCKSGS PNSSPGSGHN
NVQKDGTCAP IERDTLRSLV ESGATESSGC LPGCHLGSDA PPLHLSTANA LGDIFFPSSD
LLQANEECAL AALTKLPEND RSKQLQSTSS NLLSSLNNVV QALSNLQLKH KQLAEDYQNQ
RDSSARKRAE HRRLKEELAS AASELEETNY KLAALKAQRD NTQGARIPYP TLGNKSMPED
KVRDKQREMQ DLEATHKELS ELISKRLVEI KRLHEERIEI LNKIATFQNI LMDFKSIRSS
KAFQLVNDRL QKSQAELDHY QTLLEKLQVD KDKFVWQERQ FNLKVDLAEI PERVSTYCES
SIADLKKDIQ KLRDEKNMLI LKLEEASREP GRNQVITKFK ALVSSIPREM GAMQSEMTKH
KEASLELNSL RAEVHSLSRI LSRKERDNEE ASCRSARAGS DITQLQSVIS DLKQTNKELK
LFADMYKRES TDSREIMESR DREFLEWAHV HALKSSLDES KLEQRVKAAN EAEAITQQRL
ATAEAEIAES GQKLGTSRKD LVSLSHMLKS KQEECEAYRV EVECIGQAYE DIQAQNQQLL
QQIIERDDDN TKIFMEGVKA KQTQDALHLE TYSLRRNLQQ ESSLMDLYNQ KIVSLEDQLK
MWSDRVGKLQ EDGWQQSVSL SNYQRKLVDV HRDAQKLMQS LDGIQANVGS SRLEVADLLI
ELEKERFSKK RIEDDLEVMS RKASSLRAKA RESAVLEKLR HEVKEYRGIL KCGICHDRQK
EVVITKCYHL FCNQCIQKSL GNRQRRCPSC SLSFGANDVK PIYI
