ID A0A061FZX0_THECC Unreviewed; 817 AA.
AC A0A061FZX0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:EOY22801.1};
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:EOY22801.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY22801.1, 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; EOY22801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FZX0; -.
DR EnsemblPlants; EOY22801; EOY22801; TCM_014867.
DR Gramene; EOY22801; EOY22801; TCM_014867.
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:EOY22801.1};
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 460..752
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 746..817
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 168..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 381..413
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 277..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 817 AA; 91821 MW; 39F8390C6D064B2A CRC64;
MEKKEIVEAE GEPVPVLPPP PTLNIGIAIN GNRKSKYVVK WALEKFITEE NVMFKLLHVR
AKITTVPTPT AAYKKEVEWQ TNEMLLPYKK MCAQRKGQVD VIVIESNDVA NAIAEEVTKS
TITKLVIGAT SRGMFTRKLK KNNLSSRISV CTPSFCTVYA VSKGQLSSIR PSDSETNVST
KDDSSETSVS CKSSSSYTFS SETELGSVAS YATFHSPSLP VQRFQALSTI NQTFLHSSTS
SLEINQSRSL ESTQSRSPDI NHSRCHSLDI VAGKDDMSTC RSSSETRQAV SRSSSCRSLP
TDQQSVLSDQ ISTSDVLTDN SFSEHQVYVN FELEKLRTEL RHVQGMYAIA QSETIDASRK
LNALRKHRLE EAMKFKEISF KEEKAEELAR QEKEKYEAAR REVEHVKECA DREASQRREA
EMKAFHDAKE KEKLENVLIG SVQQYQKFTW EEIVSATSSF SEDLKVGMGA YGTVYKCMLH
HTAVAVKVLR SKENSRTKQF QQELEILSKI RHPHLLLLLG ACPEFPDHGC LVYEYMENGS
LEERLLRKNN TPPIPWFERY RIAWEVASAL NFLHNSKPEP IIHRDLKPAN ILLDRNFVSK
IGDVGLSMML NADPLSSSTM YRDTGPVGTL CYIDPEYQRT GLISPKSDVY AFGMVILQLL
TAKPAIALTH VVETAIDDGN LPGILDSEAG PWPVEETREL AILGLSCAEL RRKDRPGLKD
QVLPVLERMK EVADRARISI SKVQSAPPNH FICPILKDVM DDPCVAADGY TYDRKAIEKW
LDGNDKSPMT NLPLLNKNLL PNYNLLSAIV EWKSRKQ
//
