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Database: UniProt
Entry: A0A061GDD6_THECC
LinkDB: A0A061GDD6_THECC
Original site: A0A061GDD6_THECC 
ID   A0A061GDD6_THECC        Unreviewed;      1005 AA.
AC   A0A061GDD6;
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=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=TCM_029616 {ECO:0000313|EMBL:EOY27895.1};
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:EOY27895.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY27895.1, 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; EOY27895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061GDD6; -.
DR   EnsemblPlants; EOY27895; EOY27895; TCM_029616.
DR   Gramene; EOY27895; EOY27895; TCM_029616.
DR   eggNOG; ENOG502QW9B; Eukaryota.
DR   HOGENOM; CLU_000288_114_2_1; -.
DR   InParanoid; A0A061GDD6; -.
DR   OMA; HVVKIAF; -.
DR   Proteomes; UP000026915; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR021720; Malectin_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
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:SF72; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE RFK1-RELATED; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1005
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001602739"
FT   TRANSMEM        607..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          663..940
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          963..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..1005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  112745 MW;  6A3B74CEE8FC2DDF CRC64;
     MVTKKLFVFL IIAVGCFRLL RFAESKVPQE EVDALQEITA TMGSTYWKFN GDSCEVEMVG
     VTQEPPKNSE HEISCERETN SNVCHIVRIV LKRHNLPGML PPQLVKLPHL REIDFAYNYL
     NGTLPSEWAS MKLTSISVLV NRLSGEIPKH LGNITTLTNL SLEANQFSGA IPPELGNLIN
     LKTLMLSSNQ LTGNLPLTFA LLRNLTDFRI NDNNFNGTIP SFIQKWEQLS RLEMHASGLE
     GPIPTSISLL SNLVELRISD INGPNQGFPM VRNMTGIVRL VLRNCNIFGE IPAYVWAMKN
     LEMLDVSFNK LVGKIPTSIR ADRLRFVFLS GNMLSGDVPD SILKQGTSID LSYNNFTWQG
     PEKPVCHENM NLNLNLFRSS SSRNNLRGAL PCRKDFTCPQ YSNCLHVNCG GKDTRINTNL
     LYEGDGDVEG GAAKYYIRAD GNWGFSSTGD FMDDNDFQNT RYTVSKLSLN ISELYTTARR
     APISLTYFHY CLENGNYTIT LDFAEIQFTT DETYNSLGRR MFDIYVQEKL LWKDFNIESV
     ARSAQKPLVK QVPNVSVTNN FLEIRFYWAG KGTTRIPIRG VYGPLVSAIS VVSDFKQCSN
     GRNKGTAYII VGVVISCLVF FILGILWWKR SLLGKYWRKE DTKGDMSSGT FTLKQIKVAT
     DDFNSANKIG EGGFGPVYKG QLPDGTKIAV KQLSSKSRQG NREFLNEIGM ISCLQHPNLV
     KLHGFCVEGD QLLLVYEYME NNSLARALFG PEHNQLELDW ATRLKICIGI ARGLAFLHEE
     SRLKIVHRDI KATNVLLDSD LNPKISDFGL ARLDEEEKTH ITTRIAGTIG YMAPEYALWG
     HLTHKADVYS YGVVVMEIVT GKNNNNFMPS EKFVCLLDWA CHLQQTGSLI GLLDERLRSE
     VKKEEAELVV KVALLCTNAS ASLRPTMSEA VSMLEGRMTV PDLIPEPGNY TEDLRFKAMR
     DLRQQKEDQS SSGSQTQNST TVHTIYSSST SHSSNEINPV SRFGT
//
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