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Database: UniProt
Entry: A0A061GQD9_THECC
LinkDB: A0A061GQD9_THECC
Original site: A0A061GQD9_THECC 
ID   A0A061GQD9_THECC        Unreviewed;       374 AA.
AC   A0A061GQD9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Kinase superfamily protein isoform 2 {ECO:0000313|EMBL:EOY31706.1};
GN   ORFNames=TCM_038772 {ECO:0000313|EMBL:EOY31706.1};
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:EOY31706.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY31706.1, 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   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; CM001887; EOY31706.1; -; Genomic_DNA.
DR   RefSeq; XP_007014087.1; XM_007014025.2.
DR   AlphaFoldDB; A0A061GQD9; -.
DR   SMR; A0A061GQD9; -.
DR   EnsemblPlants; EOY31706; EOY31706; TCM_038772.
DR   EnsemblPlants; Tc09v2_t016810.3; Tc09v2_p016810.3; Tc09v2_g016810.
DR   GeneID; 18589165; -.
DR   Gramene; EOY31706; EOY31706; TCM_038772.
DR   Gramene; Tc09v2_t016810.3; Tc09v2_p016810.3; Tc09v2_g016810.
DR   HOGENOM; CLU_000288_21_1_1; -.
DR   OrthoDB; 1209183at2759; -.
DR   Proteomes; UP000026915; Chromosome 9.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45621; OS01G0588500 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR45621:SF15; SERINE_THREONINE-PROTEIN KINASE PBL17-RELATED; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOY31706.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..288
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          311..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   374 AA;  41997 MW;  EC89C601431F8B74 CRC64;
     MRLVTKQFRP DYILGEGGFG VVYKGVIDEN TRPGYKSMAV AVKELNPDGF QGDREWLAEV
     NYLGQLSHPN LVKLIGYCCE DEHRLLVYEY MASGSLEKHL FRRVGCSLTW SKRMKIALDA
     AKGLAFLHGA ERPIIYRDFK TSNILLDADF NAKLSDFGLA KDGPMGDQTH VSTRVMGTYG
     YAAPEYVMTG HLTARSDVYG FGVVLLEMLL GRRAMDKSRP SREHNLVDWA RPLLNHNKKL
     MRILDPRMEG QYSARTAMKV ANLAYQCLSQ NPKGRPLMSQ VVELLETFQT KEVSNEEAML
     HTGASGITLY EAPSNCPHTP AKKSNPARSE SHREGDAHRR KPGNGRSKSE PPKECDLYDP
     PHFEAEDKSE SNRG
//
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