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Database: UniProt
Entry: A0A061GPC3_THECC
LinkDB: A0A061GPC3_THECC
Original site: A0A061GPC3_THECC 
ID   A0A061GPC3_THECC        Unreviewed;       367 AA.
AC   A0A061GPC3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=TCM_038630 {ECO:0000313|EMBL:EOY31655.1};
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:EOY31655.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY31655.1, 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|ARBA:ARBA00000900};
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DR   EMBL; CM001887; EOY31654.1; -; Genomic_DNA.
DR   EMBL; CM001887; EOY31655.1; -; Genomic_DNA.
DR   EMBL; CM001887; EOY31656.1; -; Genomic_DNA.
DR   EMBL; CM001887; EOY31657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061GPC3; -.
DR   EnsemblPlants; EOY31654; EOY31654; TCM_038630.
DR   EnsemblPlants; EOY31655; EOY31655; TCM_038630.
DR   EnsemblPlants; EOY31656; EOY31656; TCM_038630.
DR   EnsemblPlants; EOY31657; EOY31657; TCM_038630.
DR   Gramene; EOY31654; EOY31654; TCM_038630.
DR   Gramene; EOY31655; EOY31655; TCM_038630.
DR   Gramene; EOY31656; EOY31656; TCM_038630.
DR   Gramene; EOY31657; EOY31657; TCM_038630.
DR   eggNOG; KOG0800; Eukaryota.
DR   InParanoid; A0A061GPC3; -.
DR   OMA; DMDSHIQ; -.
DR   Proteomes; UP000026915; Chromosome 9.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd16667; RING-H2_RNF126-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR   PANTHER; PTHR15710:SF22; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF14369; zinc_ribbon_9; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          240..281
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          133..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  40889 MW;  054052CE1B51A8CB CRC64;
     MEEAMAARYW CHQCSRIVNP IMEVEIKCPV CETGFIEEMS SGTRDSEDID SDIGSDRALS
     LWAPILLGMM GNPRRRRRHR RIDFEEEDDD NDDGEARHGG DTDLDRELES IIRRRRRSSA
     TILQLLQGIR DGMASEAENS ENDRDRDTSR DRDRERERVI LINPFNQTII VQGSYDSNQG
     GQNQNSNHIG SLGDYFVGPG LDLLLQHLAE NDPNRYGTPP AQKEAIEAMP TVKIEENLQC
     SVCLDDFEAG SEAREMPCKH KFHSGCILPW LELHSSCPVC RYQMPADESK LDTERPRNNT
     NQRESENNVH GSGEEGEGDG RSGSGRRFSF PWPFNGLFSS GSQAGGGNSS SASSGSQSGS
     ASQADEN
//
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