ID I1QW20_ORYGL Unreviewed; 844 AA.
AC I1QW20;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA10G0140300.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA10G0140300.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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|RuleBase:RU365038};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC ECO:0000256|RuleBase:RU365038}.
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DR AlphaFoldDB; I1QW20; -.
DR STRING; 4538.I1QW20; -.
DR EnsemblPlants; ORGLA10G0140300.1; ORGLA10G0140300.1; ORGLA10G0140300.
DR Gramene; ORGLA10G0140300.1; ORGLA10G0140300.1; ORGLA10G0140300.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_0_1; -.
DR OMA; YSNIDTR; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:EnsemblPlants.
DR GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
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 CDD; cd16499; RING-HC_Bre1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF7; E3 UBIQUITIN-PROTEIN LIGASE BRE1-LIKE 2; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 792..830
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 244..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..37
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 163..239
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 291..454
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 561..595
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 701..789
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 96569 MW; 233DA04996D4F3D9 CRC64;
MDAAALQYEN QKLVQQLEAQ KSKMRALEGK FKELRDEQCS YDNTLICLNK MWNQLIDDLV
LLGVRAGGDL NGLQALDHEE MSEESLESCP SEEIFLFRLL NSRNFRNNDD SSLSKLVEEA
LALRYSTTVT LMKSLQEAFA VQQARSESLS LALNGQNSSE DVIVALENHN DYLKEVVDNL
RQAVSIINRK HEKYLDEIEA FKNNQSRELH EVKCLSGELE ESMAELEESR RKLAVLQLQT
GGGSLMNTSA PNGVNGSVST DKSSDKGMGW RDLKDAVEEA KTLAANRLFE LHETQEDNLI
LSKQLEDIQD QLKDENYIVT SKPYTILSDQ LHHLNAEIER YRGLVEVLQN EKDQLMQKEE
EMLAKAESVD AVQQSITTYK AKIEDLEHEI QKLMAEKNDL EIKAEEALQD SGKKDFKDEI
HVMAASLSKE MELLDNQMNR SKDAASEALA LREEADYLRT LLAKKIDEQK EISDRYNTQV
TEIKSLKALI ETLDQEKQEL QFIVDMLGKE CSESRAISEI EESENRARKQ AEYLRKCLEE
HNLELRVKAA NEAETACQQR LSIAEVELED LRAKVDASER DVMKLKESIR IKEAEVDGHI
SEIETIGQAY EDMQTQNQHL LQQVADRDDF NIKLVSDSVK MKQAYGSLLA EKNMLQKQLQ
HVNSSLESSK LKITSGEEQM KTYVAQAMKS SSENRHLAIS LERTMLEVSD AEKELKWLRS
ATGSAEKEYE INQKKIAELK MELERERNER RKLEEEYEEV KNEVSELTSE TEETTIQKLQ
DEIKECKAIL KCGVCFDRPK EVVITKCFHL FCSPCIQRNL EIRHRKCPGC GTPFGQSDVR
EVKI
//
