ID A0A061FK60_THECC Unreviewed; 852 AA.
AC A0A061FK60;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN ORFNames=TCM_036647 {ECO:0000313|EMBL:EOY17466.1};
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:EOY17466.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY17466.1, 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|PIRNR:PIRNR000641};
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|PIRNR:PIRNR000641};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR EMBL; CM001886; EOY17466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FK60; -.
DR EnsemblPlants; EOY17466; EOY17466; TCM_036647.
DR Gramene; EOY17466; EOY17466; TCM_036647.
DR eggNOG; ENOG502QRWA; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; A0A061FK60; -.
DR OMA; AGNIPIW; -.
DR Proteomes; UP000026915; Chromosome 8.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR PANTHER; PTHR47974:SF2; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 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|PIRNR:PIRNR000641};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 444..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..161
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 506..781
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 826..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 852 AA; 92856 MW; 1ABA3D5ADF6E69E7 CRC64;
MMVWTIKKGK ESSLENMAKL SPFLLLQLHL LFVVSSSSTI IPLGSTLHAS DANQSWSSPS
STFSFSFIPV TPSSYVAAIT YSVGVTVWSA GDGSNSAGAV VDSGGTLRLL LTGALRLVNG
SGTIIWDSGT ADRGVSHASL DDTGNFQLLN NDSSPIWSSF ENPTDTLVPS QNFSVGKILR
SGSYSLSLNE IGNLTLKWNN SIEYWNLGFN SSSKGNLTSP RYVLQSAGIL RGFDPSFSSG
MIMAYSTDYG EGNGVFRFLR MDSDGNLRIY STSKGSGNIT PTWAAVTDQC QVFGYCGNMG
ICSYKDVNPI CGCPSQNFEL IDANDRRKGC KRKVEIEDCP GDFTMLELGH AKFLTYPPEV
SSQTFIVGIV ACRMNCLGSD SCIASTLVAD GSGSCYMKTP DFVSGYQNAI LPSTSFVKVC
GPAVPNASPY QDIAGNDNIS RSSVLIVAVV VLAILLILVA LLIGFWCCCY PSSPKFGHKS
AQYVLVDYAS GAPVKFSYKE LQQYTKGFSE RLGEGGFGAV HKGTLANRMV VAVKQLEGIE
QGEKQFRMEV ATISSTHHLN LVRLVGFCTD GRHRLLVYEF MKNGSLDNFL FMSKDKGKSL
NWENRFNIAL GTAKGITYLH EECRDCIIHC DIKPENILLD ESYTAKVSDF GLAKLMNPKD
NRYLSLASIR GTRGYLAPEW LANLPITSKC DVYSYGMVLL EIVSGTRNFE VSTETDGKRF
SLWAYEEFEK GNIEGIVDKR LEEVDIEQVV RAIMVSFWCI QEQPSQRPMM GKVVQMLEGV
IDIERPGAPK VVAEGATRGT GTTVNSNISA FSTYASSSSQ SIGVLPFRSE RDMGRESSSL
LGLERSETDP HS
//
