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Database: UniProt
Entry: A0A061FZI1_THECC
LinkDB: A0A061FZI1_THECC
Original site: A0A061FZI1_THECC 
ID   A0A061FZI1_THECC        Unreviewed;       456 AA.
AC   A0A061FZI1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=RING domain ligase2 isoform 1 {ECO:0000313|EMBL:EOY22287.1};
GN   ORFNames=TCM_014506 {ECO:0000313|EMBL:EOY22287.1};
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:EOY22287.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY22287.1, 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; CM001881; EOY22287.1; -; Genomic_DNA.
DR   EMBL; CM001881; EOY22288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061FZI1; -.
DR   EnsemblPlants; EOY22287; EOY22287; TCM_014506.
DR   EnsemblPlants; EOY22288; EOY22288; TCM_014506.
DR   Gramene; EOY22287; EOY22287; TCM_014506.
DR   Gramene; EOY22288; EOY22288; TCM_014506.
DR   eggNOG; KOG1327; Eukaryota.
DR   HOGENOM; CLU_035766_1_0_1; -.
DR   InParanoid; A0A061FZI1; -.
DR   OMA; HIGEEQN; -.
DR   Proteomes; UP000026915; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd01459; vWA_copine_like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR010734; Copine_C.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45751; COPINE FAMILY PROTEIN 1; 1.
DR   PANTHER; PTHR45751:SF38; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EOY22287.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          413..446
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  50829 MW;  6359C12360F4C745 CRC64;
     MGGVTSKRSA TAQSSSVGSN SHSWDHQRYA QPSYAPSSRD YSWDHQRYAQ PSYAPSSRDY
     VPQQHYAPPL QSYGGRAPES NRRLERKYSK IDDNYNSLEQ VTEALARAGL ESSNLIVGID
     YTKSNEWTGA RSFHRRSLHH IGDEQNPYEQ AISIIGKTLS SFDEDNLIPC FGFGDASTHD
     QEVFSFYPDE TFCNGFEEVL RRYRELVPNL RLAGPTSFAP IIEMAITIVE QSGGQYHVLL
     IIADGQVTRS VDTERGQLSP QEMKTVEAIV RASDYPLSII LVGVGDGPWD MMREFDDNIP
     ARAFDNFQFV NFTEIMSKNM DRSRKEAEFA LAALMEIPSQ YKATLELSIL GTSRGKDIDR
     VPLPPPLYGA ASFSNSKPSR SSSFRPTPPS SGRYDAPVRT TPSASSASDN HVCPICLCNP
     KDMAFGCGHQ TCCECGQDLQ LCPICRSTID TRIRLY
//
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