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Database: UniProt
Entry: E7CEL8_9SOLN
LinkDB: E7CEL8_9SOLN
Original site: E7CEL8_9SOLN 
ID   E7CEL8_9SOLN            Unreviewed;       628 AA.
AC   E7CEL8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Receptor-like protein kinase 2.33 {ECO:0000313|EMBL:ADV29742.1};
DE   Flags: Fragment;
OS   Solanum arcanum.
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=376710 {ECO:0000313|EMBL:ADV29742.1};
RN   [1] {ECO:0000313|EMBL:ADV29742.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=432a {ECO:0000313|EMBL:ADV29742.1}, 434a
RC   {ECO:0000313|EMBL:ADV29746.1}, 434b {ECO:0000313|EMBL:ADV29747.1}, and
RC   435a {ECO:0000313|EMBL:ADV29748.1};
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:ADV29742.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=432a {ECO:0000313|EMBL:ADV29742.1}, 434a
RC   {ECO:0000313|EMBL:ADV29746.1}, 434b {ECO:0000313|EMBL:ADV29747.1}, and
RC   435a {ECO:0000313|EMBL:ADV29748.1};
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; GU951403; ADV29742.1; -; Genomic_DNA.
DR   EMBL; GU951407; ADV29746.1; -; Genomic_DNA.
DR   EMBL; GU951408; ADV29747.1; -; Genomic_DNA.
DR   EMBL; GU951409; ADV29748.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7CEL8; -.
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; 5.
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:ADV29742.1};
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:ADV29742.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000313|EMBL:ADV29742.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        491..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          593..628
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          434..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         621
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:ADV29742.1"
FT   NON_TER         628
FT                   /evidence="ECO:0000313|EMBL:ADV29742.1"
SQ   SEQUENCE   628 AA;  67400 MW;  6C87F4608019AB6F CRC64;
     AFASLVFTVT DPNDLSVINE LRKGLENPEV LKWPENGGDP CGSPVWPHIV CSGSRIQQIQ
     VMGLGLKGPL PQNLNKLSRL THLGLQKNQF SGKLPSFSGL SELSFAYLDF NQFDTIPLDF
     FDGLVNLQVL ALDENPLNAT SGWSLPNGLQ DSAQLINLTM INCNLAGPLP EFLGTMSSLE
     VLLLSTNRLS GPIPGTFKDA VLKMLWLNDQ SGDGMSGSID VVATMVSLTH IWLHGNQFSG
     KIPVEIGNLT NLKDLSVNTN NLVGLIPESL ANMPLDNLDL NNNHFMGPVP KFKAANVSFM
     SNSFCQTKQG AVCAPEVMAL LEFLDGVNYP SRLVESWSGN NPCDGRWWGI SCDDNQKVSV
     INLPKSNLSG TLSPSIANLE TVTRIYLESN NLSGFVPSSW TSLKSLSILD LSNNNISPPL
     PKFTTPLKLV LNGNPKLTSN PPGANPSPNN STTPADSPTS SVPSSRPNSS SSVIFKPIEQ
     SPEKKDSESK IAIVVVPIAG FLLLVFLAIP LYIYVCKKSK DKHQAPTALV VHPRDPSDSD
     NVVKIAIANQ TNGSLSTVNA SGSASIHSGE SHMIEAGNLL ISVQVLRNVT KNFSPENELG
     RGGFGVVYKG ELDDGTQIAV KRMEAGIV
//
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