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Database: UniProt
Entry: I1PNM2_ORYGL
LinkDB: I1PNM2_ORYGL
Original site: I1PNM2_ORYGL 
ID   I1PNM2_ORYGL            Unreviewed;       884 AA.
AC   I1PNM2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
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:ORGLA04G0179100.1, 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:ORGLA04G0179100.1}
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; I1PNM2; -.
DR   STRING; 4538.I1PNM2; -.
DR   EnsemblPlants; ORGLA04G0179100.1; ORGLA04G0179100.1; ORGLA04G0179100.
DR   Gramene; ORGLA04G0179100.1; ORGLA04G0179100.1; ORGLA04G0179100.
DR   eggNOG; KOG0978; Eukaryota.
DR   HOGENOM; CLU_002640_1_0_1; -.
DR   OMA; THIEIMT; -.
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:0051301; P:cell division; IEA:EnsemblPlants.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; 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:0006513; P:protein monoubiquitination; 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   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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR   PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 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          832..871
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
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          51..78
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          216..278
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          422..449
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          473..507
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          698..732
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        107..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   884 AA;  100426 MW;  8A157D16EC660B23 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 TLGNKNMPED
     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
//
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