ID A0A061GDG6_THECC Unreviewed; 1179 AA.
AC A0A061GDG6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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_029304 {ECO:0000313|EMBL:EOY27458.1};
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:EOY27458.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY27458.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; CM001884; EOY27458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061GDG6; -.
DR EnsemblPlants; EOY27458; EOY27458; TCM_029304.
DR Gramene; EOY27458; EOY27458; TCM_029304.
DR eggNOG; ENOG502QUW9; Eukaryota.
DR HOGENOM; CLU_000288_114_1_1; -.
DR InParanoid; A0A061GDG6; -.
DR OMA; GIFMWIK; -.
DR Proteomes; UP000026915; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR021720; Malectin_dom.
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; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR PANTHER; PTHR48006:SF34; OS08G0203400 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 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:EOY27458.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 590..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 648..922
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1179 AA; 129800 MW; 220E52EFBCF24C6A CRC64;
MNGKLTVRAL NSIFQQWETQ APDTWNISGE PCSGRALSDS DSVFEDSSNN PAIRCDCSFE
KGTICHITRL RVFSLEKRGQ IPEELLALRF LTFLKIDQNF FTGPLPAFIG SMSRLALLSV
AQNSLSGPIP KEIGNLKELY MLSLGINNFS GTLPPELGNL VELQQLYINS CGFTGEIPST
FANLRNLQIV LLNFRYASDN ALTGKIPDFI GNNWTKLASL KLEGNSFEGP IPSNIGNLTS
LTILRISGIY NGSSSLDFVR NLKNIADLVL RNVLLTGSIP TDIVEFQSLQ KLDLSFNNLT
GQIPSELFNK NSLTFLGNNS LSGTLPSQKS QSLKNIDVSY NHLSGNLPSW IDSSLQLLLP
GLQCLQRGFP CNRNAPRYAN FAIKCGGPQM TADGILFEAE NSTLGAATFN VTSTQKWAVS
NVGLYEDREN PLYVQNTFAQ VKSTNTPAIY QTSRISPVSL RYYGLGLENG PYTVNLFFAE
TAYPERSTQS WKSLGRRVFD IYIQGSLKVK DFDISKEAGG AERAITRNFT ANVTENHLEI
HLFWAGKGTC CVPEFGYYGP SISAISVVPD FKPTVSGLPP SSSNRKKQTA LIVGIIVPVG
VAALILICVI IFIKRRKEYD DDEEVLLAIG PRPNTFSYAE LKAATEDFSP SNKLGEGGFG
AVYKGTLSDG RVVAVKQLSV ASHQGKSQFI AEVATISAVQ HRNLVKLYGC CIEGKRHLLV
YEYLENKSLD QALFGRSDLH LDWATRFNIC LATARGLAYL HEESRPRIVH RDVKASNILL
DAELCPKISD FGLAKLYDDK KTHISTRVAG TIGYLAPEYA MRGHLTEKAD VFGFGIVALE
ILSGRPNTDN SLKDDKIYLL EWAWALHENN QSLDLVDPNL VGSDENEALR VMGVALLCTQ
GSPTMRPPMS RVVAMLAGDI EVSGVITKPS YLTDWDFKDL TGSFMTEDTQ NSIATENTDN
NSNININPGA APNLSSVNVT EFSDIIEGRY GHIKRDCPTK GDESNENKGE CAFVAEGDDC
DVLTISENMD ANSYWYLNSA SATHICYQKD CFDLLQEGVA GNLTLGNKSI VKVMGLEVVK
IKMFDGVVRS LDGMAYVPKM RKNLISLNLL NSKGYGYSAC DGVVKVTQRD MVLMRGNLHN
GLYHLECEAS KGWEQCTRDG SYQSEISFAE EVMKGWCRR
//
