ID A0A061FZ50_THECC Unreviewed; 831 AA.
AC A0A061FZ50;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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_014867 {ECO:0000313|EMBL:EOY22800.1};
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:EOY22800.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY22800.1, 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 -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|ARBA:ARBA00003861}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; CM001881; EOY22800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FZ50; -.
DR EnsemblPlants; EOY22800; EOY22800; TCM_014867.
DR Gramene; EOY22800; EOY22800; TCM_014867.
DR eggNOG; ENOG502QQ92; Eukaryota.
DR HOGENOM; CLU_000288_153_1_1; -.
DR InParanoid; A0A061FZ50; -.
DR OMA; DTTHSRA; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000026915; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR CDD; cd01989; STK_N; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR006016; UspA.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR PANTHER; PTHR45647:SF15; U-BOX DOMAIN-CONTAINING PROTEIN 35; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00582; Usp; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOY22800.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 474..766
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 760..831
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 182..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..427
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 291..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 831 AA; 93362 MW; CE5B126FCD6059F8 CRC64;
MEKKEIVEAE GEPVPVLPPP PTLNIGIAIN GNRKSKYVVK WALEKFITEE NVMFKLLHVR
AKITTVPTPM GNFIPISQVR NDVAAAYKKE VEWQTNEMLL PYKKMCAQRK GQVDVIVIES
NDVANAIAEE VTKSTITKLV IGATSRGMFT RKLKKNNLSS RISVCTPSFC TVYAVSKGQL
SSIRPSDSET NVSTKDDSSE TSVSCKSSSS YTFSSETELG SVASYATFHS PSLPVQRFQA
LSTINQTFLH SSTSSLEINQ SRSLESTQSR SPDINHSRCH SLDIVAGKDD MSTCRSSSET
RQAVSRSSSC RSLPTDQQSV LSDQISTSDV LTDNSFSEHQ VYVNFELEKL RTELRHVQGM
YAIAQSETID ASRKLNALRK HRLEEAMKFK EISFKEEKAE ELARQEKEKY EAARREVEHV
KECADREASQ RREAEMKAFH DAKEKEKLEN VLIGSVQQYQ KFTWEEIVSA TSSFSEDLKV
GMGAYGTVYK CMLHHTAVAV KVLRSKENSR TKQFQQELEI LSKIRHPHLL LLLGACPEFP
DHGCLVYEYM ENGSLEERLL RKNNTPPIPW FERYRIAWEV ASALNFLHNS KPEPIIHRDL
KPANILLDRN FVSKIGDVGL SMMLNADPLS SSTMYRDTGP VGTLCYIDPE YQRTGLISPK
SDVYAFGMVI LQLLTAKPAI ALTHVVETAI DDGNLPGILD SEAGPWPVEE TRELAILGLS
CAELRRKDRP GLKDQVLPVL ERMKEVADRA RISISKVQSA PPNHFICPIL KDVMDDPCVA
ADGYTYDRKA IEKWLDGNDK SPMTNLPLLN KNLLPNYNLL SAIVEWKSRK Q
//