ID A0A061DUG8_THECC Unreviewed; 878 AA.
AC A0A061DUG8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=TCM_005636 {ECO:0000313|EMBL:EOX96385.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX96385.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX96385.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001879; EOX96385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DUG8; -.
DR STRING; 3641.A0A061DUG8; -.
DR EnsemblPlants; EOX96385; EOX96385; TCM_005636.
DR Gramene; EOX96385; EOX96385; TCM_005636.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_0_1; -.
DR InParanoid; A0A061DUG8; -.
DR OMA; THIEIMT; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000026915; Chromosome 1.
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:SF3; E3 UBIQUITIN-PROTEIN LIGASE BRE1-LIKE 1; 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 Reference proteome {ECO:0000313|Proteomes:UP000026915};
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 826..864
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..74
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 242..272
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 580..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 685..726
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 755..803
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 100477 MW; 2AFAE2E2BFD07A12 CRC64;
MGSTGEADRK RRHFSSISPT AVAAKKQPFL PISEEKRLDA TVLQYQNQKL IQKLEAQKFE
RSALENKLSQ LKEKQKPYDS TLKVVNKSWE ALLTDLESCS AHTRESSRQD VGCAPSMEDG
ASSPTEDAFL SRLMETGATE SSSSNNCPEQ MEEDREQIAS EKTRNILHNI VIAINNLWHL
KDGLYAAVLN EHPKDGSCKQ KASSELESEV KNLRLAIGDI HLKHRSLARE LQSHRDIDAK
NKVELKRIKG ELESALAELQ ESNCKLATLR VEKDATKGAF FPVLNLGSKH VTGDKAKDKQ
RALQEMESTL KEMLEQASSR LTELKGLHEE RIKLLQHSLN LQNTLKSVKC ISSSQLYLLV
RDQLEKSKSE VFQYQDLFEK LQVEKDNLAW REKELSIKND IADVFRRSFA VADSRASHLG
AEIQRQIEER KRIEAKLEEA SREPGRKEII AEFKSLLSSF PEEMSSMQSQ LGKYKEAAVD
IHSLRADVQS LSSVLDRKVR ECENLSVKSA DQVAEMHKLQ AMVQDLKDSD VELKLILEMY
RREFTDSRDV LEARDSEYKA WAHVQSLKSS LDEQNLELRV KTANEAEARS QQRLAAAEAE
IADLRQKLEA SKRDTARLSD ALKSKNEENE AYLSEIESIG QAYDDMQTQN QQLLQQITER
DDYNIKLVLE GVKAKQLQDA LLLEKHTMEK EIQQASASLD FYEMKAARIE DQLRFFSDQA
QKLAEERFQN SVSLENTQKR LSEVRISSHQ ARESLEDSQS RIEKSRVALT ELQIEIERER
FNKKRLEEEL GVVKRKVLRL RAETEGSSIV ERLQQELREY KEILKCSICL DRPKEVVITR
CYHLFCNPCV QKITESRHRK CPVCAASFGA NDVKPVYI
//