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Database: UniProt
Entry: A0A061DUG8_THECC
LinkDB: A0A061DUG8_THECC
Original site: A0A061DUG8_THECC 
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
//
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