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Database: UniProt
Entry: E7CEG1_SOLHA
LinkDB: E7CEG1_SOLHA
Original site: E7CEG1_SOLHA 
ID   E7CEG1_SOLHA            Unreviewed;       629 AA.
AC   E7CEG1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Receptor-like protein kinase 2.33 {ECO:0000313|EMBL:ADV29685.1};
DE   Flags: Fragment;
OS   Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=62890 {ECO:0000313|EMBL:ADV29685.1};
RN   [1] {ECO:0000313|EMBL:ADV29685.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=384b {ECO:0000313|EMBL:ADV29685.1}, 385a
RC   {ECO:0000313|EMBL:ADV29686.1}, and 386a {ECO:0000313|EMBL:ADV29688.1};
RA   Merino C.G., Tellier A.L., Staedler T., Stephan W.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV29685.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=384b {ECO:0000313|EMBL:ADV29685.1}, 385a
RC   {ECO:0000313|EMBL:ADV29686.1}, and 386a {ECO:0000313|EMBL:ADV29688.1};
RX   PubMed=21245893; DOI=10.1038/hdy.2010.175;
RA   Tellier A., Fischer I., Merino C., Xia H., Camus-Kulandaivelu L.,
RA   Stadler T., Stephan W.;
RT   "Fitness effects of derived deleterious mutations in four closely related
RT   wild tomato species with spatial structure.";
RL   Heredity 107:189-199(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the RLP family. {ECO:0000256|ARBA:ARBA00009592}.
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DR   EMBL; GU951346; ADV29685.1; -; Genomic_DNA.
DR   EMBL; GU951347; ADV29686.1; -; Genomic_DNA.
DR   EMBL; GU951349; ADV29688.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7CEG1; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
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   PANTHER; PTHR47986:SF13; OS04G0685900 PROTEIN; 1.
DR   PANTHER; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   Pfam; PF08263; LRRNT_2; 2.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:ADV29685.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000313|EMBL:ADV29685.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000313|EMBL:ADV29685.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        492..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          594..629
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          435..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADV29685.1"
FT   NON_TER         629
FT                   /evidence="ECO:0000313|EMBL:ADV29685.1"
SQ   SEQUENCE   629 AA;  67512 MW;  5A1D644BD307F642 CRC64;
     AFASLVFTVT DPNDLSVINE FRKGLENPEV LKWPENGGDP CGSPVWPHIV CSGSRIQQIQ
     VMGLGLKGPL PQNLNKLSRL THLGLQKNQF SGKLPSFSGL SELSFAYLDF NQFDTIPLDF
     FDGLVNLQVL ALDENPLNAT SGWSLPNGLQ DSAQLINLTM INCNLAGPLP EFLGTMSSLE
     VLLLSTNRLS GPIPGTFKDA VLKMLWLNDQ SGDGMSGSID VVATMVSLTH LWLHGNQFSG
     KIPVEIGNLT NLKDLNVNTN NLVGLIPESL ANMPSLDNLD LNNNHFMGPV PKFKATNVSF
     MSNSFCQTKQ GAVCAPEVMA LLEFLDGVNY PSRLVESWSG NNPCDGRWWG ISCDDNQKVS
     VINLPKSNLS GTLSPSIANL ETVTRIYLES NNLSGFVPSS WTSLKSLSIL DLSNNNISPP
     LPKFTTPLKL VLNGNPKLTS NPPGANPSPN NSTTPADSPT SSVPSSRPNS SSSVIFKPGE
     QSPEKKDSKS KIAIVVVPIA GFLLLVFLAI PLYIYVCKKS KDKHQAPTAL VVHPRDPSDS
     DNVVKIAIAN QTNGSLSTVN ASGSASIQSG ESHMIEAGNL LISVQVLRNV TKNFSPENEL
     GRGGFGVVYK GELDDGTQIA VKRMEAGIV
//
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