ID S1RU19_THECC Unreviewed; 499 AA.
AC S1RU19;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Serine-threonine protein kinase, plant-type, putative {ECO:0000313|EMBL:EOY20463.1};
GN ORFNames=TCM_046330 {ECO:0000313|EMBL:EOY20463.1};
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:EOY20463.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY20463.1, 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:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; KE133228; EOY20463.1; -; Genomic_DNA.
DR AlphaFoldDB; S1RU19; -.
DR EnsemblPlants; EOY20463; EOY20463; TCM_046330.
DR Gramene; EOY20463; EOY20463; TCM_046330.
DR eggNOG; ENOG502QWMW; Eukaryota.
DR HOGENOM; CLU_000288_35_4_1; -.
DR InParanoid; S1RU19; -.
DR OMA; QCIETIT; -.
DR Proteomes; UP000026915; Unassembled WGS sequence.
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 Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47973; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 3; 1.
DR PANTHER; PTHR47973:SF19; OS11G0470500 PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 2.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOY20463.1};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004507702"
FT TRANSMEM 272..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..134
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 140..249
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 334..499
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 499 AA; 55213 MW; 0B1FEDDDA0FD1594 CRC64;
MQPKTAYLTC LLTIIWWLFL EESASASEGQ FNLLNSGCSQ YNVTNFREFS SNLNSTFLQL
REQLMNSDNK YFATAQQARG SDPAYAMVQC RKYLSSADCL ACFEAALSRI RNCSANGARV
IYDDCFLRYE SNDFYNQTTQ EGHSMMCGNQ SASEPSAFEA AVQGLLADLQ TATPRIDGYF
AATKKEVVGG GTGISATVYG VAQCIETITE SGCRECMQVV TSDIQRCPPN TNGRAVDVGC
FLRYSDSPFF ADNQTIDIRP FLRSGSSSKK KAIIIGGVVG GASLLLLVIT ALLVWFKLST
RQRGTLRGDI LGATELQGPL NYKYKDLMSA TKNFGEEYKL GEGGFGDVYK GVLKNGKIVA
VKKLAVLQSR RAKLDFDSEV RLISNVHHRN LIRLLGCCSK GLELLLVYEY MANSSLDKFL
FGERRGSLNW KQRYGIILGT ARGLAYLHEE FHVCIIHRDI KSSNILLDDD LQPKIADFGL
ARLLPEDKSH LSTKFAGTL
//
