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Database: UniProt
Entry: A0A059C7F4_EUCGR
LinkDB: A0A059C7F4_EUCGR
Original site: A0A059C7F4_EUCGR 
ID   A0A059C7F4_EUCGR        Unreviewed;       854 AA.
AC   A0A059C7F4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=EUGRSUZ_E02757 {ECO:0000313|EMBL:KCW74121.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW74121.1};
RN   [1] {ECO:0000313|EMBL:KCW74121.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW74121.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KK198757; KCW74121.1; -; Genomic_DNA.
DR   RefSeq; XP_010057113.1; XM_010058811.2.
DR   AlphaFoldDB; A0A059C7F4; -.
DR   STRING; 71139.A0A059C7F4; -.
DR   EnsemblPlants; KCW74121; KCW74121; EUGRSUZ_E02757.
DR   GeneID; 104445017; -.
DR   Gramene; KCW74121; KCW74121; EUGRSUZ_E02757.
DR   KEGG; egr:104445017; -.
DR   eggNOG; KOG0978; Eukaryota.
DR   InParanoid; A0A059C7F4; -.
DR   OMA; THIEIMT; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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; 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:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 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          802..840
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          19..46
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          273..315
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          564..780
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   854 AA;  97085 MW;  9BBBC3B4FABC1A36 CRC64;
     MGSPELYFKR DIAVLQFQNQ KLVQKLESQK VEHAALESKL SQLTEQQLGY DSRLEVVKNS
     WDELLSKLQS RSVCVGESGG SAAVGQDVES LANSKDEDHP LPEDIFLSRL IETGVDGSSS
     VDSCSNNPHD DPEIASEKAV KTILRNIALA IDGIYHEKEG LHSAVLDGLP PDDSGRQRTS
     MDLAMQLKDS RALLGELHLK HRLLARELQS HRDIDAKNKA ELKRLKGELE STISELEESH
     SKLATLKVTK DSIRGVSFPV LNFGNKHTPI EKVRDKQRDL QEMESVLKEL QDQAASRLEE
     LKALYEERVK ILQQLPTLQN KIKNLKCISS SQAFISLKDQ LEISKSEVLR YQALYEKLQT
     ERGGLFWKEL ELSIKTDIID AYKRCSAVAE SRMIELETEV KKQMEDRNII ETKQKEASNE
     AGRQDIVNDF RALVSSFPEE MGAMQSELSK YKEAAVNIHS LRADVQCFSR ALDRMVKECE
     ILSETSASEV AEIEKLKTVV QDSEGSILEL KLILEMYRRE STDSRVVEEA KDSEYKAWAQ
     VESLKCSLNE HQLELRVKTA IEAEALSQQK LAAAEAEIAD LRQKLEASKR EISQLADVLK
     SKNEENEAYL SEIESIGQEY DDMQTQNQHL LQQIAERDDY NIKLVLEGVR ARQVRDSLSA
     EKQTLAREIQ LANASVDFLN MKVVRVEDQL NICTEKVQKL AEDRLQGSNA LDNTQKRLSD
     VRRMSHQIRE SLEELQSKVD KSRGTAGELQ AELERERFKK KRLEEELEVV RRKAIHLQAQ
     VVTPVVEKLQ EELRGYQDIL KCSICRDRPK EVVITKCYHL FCNTCIQNLA ETRHRKCPSC
     GASFGPNDVK PVYF
//
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