ID A0A061FHQ6_THECC Unreviewed; 1079 AA.
AC A0A061FHQ6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Leucine-rich receptor-like protein kinase family protein isoform 1 {ECO:0000313|EMBL:EOY16875.1};
GN ORFNames=TCM_035808 {ECO:0000313|EMBL:EOY16875.1};
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:EOY16875.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY16875.1, 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. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001886; EOY16875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FHQ6; -.
DR EnsemblPlants; EOY16875; EOY16875; TCM_035808.
DR Gramene; EOY16875; EOY16875; TCM_035808.
DR Proteomes; UP000026915; Chromosome 8.
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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48053; LEUCINE RICH REPEAT FAMILY PROTEIN, EXPRESSED; 1.
DR PANTHER; PTHR48053:SF64; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE RGI5; 1.
DR Pfam; PF00560; LRR_1; 8.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOY16875.1};
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}; Receptor {ECO:0000313|EMBL:EOY16875.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1079
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001598058"
FT TRANSMEM 718..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 786..1072
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 815
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1079 AA; 117819 MW; E74268A494D76FA7 CRC64;
MARPNHFART YFLFFLFLLS IAMSRTLFVT ALSPDGEAVL SLLAAADPSA KASSSILFSW
NPKSQTPCSW QGITCSPQDR VISLSLPNTF LNLSSLPPQL SSLSSLQLLN LSSTNISGTI
PPSFGQLTHL RLLDLSSNSL SGPIPQELGQ LSLLQFLFLN SNKLIGRIPQ QLANLTLLQV
LCLQDNLLNG SIPYQLGSLV SLQQFRVGGN PYLTGEIPSQ LGLLTNLTTF GAAATGLSGV
IPPTFGNLIN LQTIALYDTE VFGSIPPELG LCSELRNLYL HMNNLSGNIP PQLGKLQKLT
SLLLWGNALS GSIPAELSNC SSLVVLDASA NDLTGEIPGD IGKLVVLEQL HLSDNSLTGL
IPWQLSNCTI LTALQLDKNQ LSGAIPWQVG NLKYLQSFFL WGNSVSGTIP SSFGNCTELY
ALDLSRNKLT GSIPEEIFSL KKLSKLLLLG NSLSGGLPRS VANCQSLVRL RLGENQLSGQ
IPKEIGQLQN LVFLDLYMNH FSGGLPLEIA NITVLELLDV HNNYITGEIP SQLGELVNLE
QLDLSRNSFT GEIPPSFGNF SYLNKLILNN NLLTGSIPNS FRNLQKLTLL DLSYNSLSGE
IPPEIGYVTS LTISLDLSSN LFAGEIPESM SRLTQLQSLD LSHNMLHGRI KVLSSLTSLT
YLNISFNNFS GPIPVTPFFS TLSSNSYLQN PNLCESIDGS TCSSRLVRKS GLRSTKTVAL
ISVILASVTI VVLASWFLVA RNHRYMVEKS AGASSSSPGA EDFSYPWTFI PFQKLNFTID
NILDCLKDEN VIGKGCSGVV YKAEMPSGEL IAVKKLWKTK RDEEPAVDSF AAEIQILGHI
RHRNIVKLLG YCSNKSVKLL LYNYIPNGNL QQLLRGNRNL DWETRYKIAV GSAQGLAYLH
HDCVPAILHR DVKCNNILLD SKFDAYLADF GLAKLMNSPN YHHAMSRVAG SYEYGYTMNI
TEKSDVYSYG VVLLEILSGR SAVESQVGDG MHIVEWVKKK MGSFEPAASI LDTKLQGLPD
QMVQEMLQTL GIAMFCVNSS PAERPTMKEV VALLMEVKSP PEEWGKTSQP LIKQSSNQS
//