ID A0A061GM08_THECC Unreviewed; 1248 AA.
AC A0A061GM08;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=TCM_037655 {ECO:0000313|EMBL:EOY30453.1};
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:EOY30453.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY30453.1, 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=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; CM001887; EOY30453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061GM08; -.
DR EnsemblPlants; EOY30453; EOY30453; TCM_037655.
DR Gramene; EOY30453; EOY30453; TCM_037655.
DR HOGENOM; CLU_000288_24_2_1; -.
DR Proteomes; UP000026915; Chromosome 9.
DR GO; GO:0016020; C: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; PTHR47989; OS01G0750732 PROTEIN; 1.
DR PANTHER; PTHR47989:SF9; PROTEIN KINASE SUPERFAMILY PROTEIN; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOY30453.1};
KW Membrane {ECO:0000256|SAM:Phobius};
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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1248
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001602978"
FT TRANSMEM 759..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 851..1127
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 36..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 879
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1248 AA; 133259 MW; 9E012E9C25B51BDF CRC64;
MLYGMGMLMP LILQLARLCI IGFPLIVQES SEGIPSAVEQ RSDAPNTLSQ PNGSDLHSPP
ALPPLMSASV PETTEGHARS FSPSNSMELP PYNTAPPPVT VEEGVPSLAP STPAVLPPFD
TAPPPMLVQV HTPSKSPTAL QKKEPIMKSP PSVPDAPAPV ASPSRNLPQN SPAIHPFPSI
TPTQNSPENS PVVHQTPFAP PLRNPPQNSP PTQSSRRSAF PPISNQRNSS SNRAPVLEPT
APAPVAPPLR NPPQNSPAIH FSKPHALPPS ANQGNSSNKT EPVMEPIAPV PVATPSGNLP
RNQTAIHPRG PALAPSVPIP EPTAPVASPP RKLERTTPPV HSIMPPSILP VVSPPEESPH
ISPTIHPNVP EGTPSQLPDP DISPVSTPPS SINWKNDGIP VASPRNEIHK PMPPLSHTPE
NGSSSAKSPL APKAVRHPGN SPVSSLAPSN KGYNPPALSP SISFHKHQHK RNGRTSPAPA
SSYLISPPPL KQQGPVISPA FLPGRRRRHY APAPLHSVSP SHSAVPSSVG TVSPVPSPSP
MTASRQTKMP LSPPKVSPSV SPLRSPKVPP PPPVMSFPPP PPNEDCSTTI CTEPYTNTPP
GSPCGCVLPM QVGLRLSVAL YTFFPLVSEL ATEIAAGVFM KQSQVRIIGA NAASEQPEKT
VVLIDLVPLG EKFDNTTAFL TYQRFWHKQV AIKTSFFGDY EVLYVRYLGL PPSPPLPPSD
IDIMDAGPYS GNDNNARAIK PLGVDVHGKR HKNVPSGGVI AIIVLSALVA MVLCSAIAWV
LLFRRTNHAS QQAATTQPPQ TSLAKPSGSA GSMVGSGLSS TSLSFGSSIV AYTGSAKTFS
TSDIEKATNN FDASRILGEG GFGRVYSGVL EDGTKVAVKV LKRDDQQGGR EFLAEVEMLS
RLHHRNLVKL IGICTEERNR CLVYELIPNG SVESHLHGVD KDSAPLDWDA RIKIALGAAR
GLAYLHEDSS PRVIHRDFKS SNILLEHDFT PKVSDFGLAR TAMDEEGRHI STRVMGTFGY
VAPEYAMTGH LLVKSDVYSY GVVLLELLTG RKPVDMTQPP GQENLVAWAR PLLTTKEGLE
TIIDPSLSSD VPFDSVAKVA AIASMCVQPE VSHRPFMGEV VQALKLVCNE CDEAKEVGSR
CSSQDDLSID LDARVSTGSG QLADPLQSHY LIPNYDTGLD TERGLSVSDL FSSSARFGRQ
SSGSFRRHCS SGPLRTARGS RFWQKVQRLS RGSISEHGVM MRFWPGSH
//