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Database: UniProt
Entry: B7SQ95_PEA
LinkDB: B7SQ95_PEA
Original site: B7SQ95_PEA 
ID   B7SQ95_PEA              Unreviewed;       622 AA.
AC   B7SQ95;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Putative LysM receptor kinase K1B {ECO:0000313|EMBL:ACE81762.1};
GN   Name=K1 {ECO:0000313|EMBL:ACE81762.1};
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888 {ECO:0000313|EMBL:ACE81762.1};
RN   [1] {ECO:0000313|EMBL:ACE81762.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18986256; DOI=10.1094/MPMI-21-12-1600;
RA   Zhukov V., Radutoiu S., Madsen L.H., Rychagova T., Ovchinnikova E.,
RA   Borisov A., Tikhonovich I., Stougaard J.;
RT   "The pea Sym37 receptor kinase gene controls infection-thread initiation
RT   and nodule development.";
RL   Mol. Plant Microbe Interact. 21:1600-1608(2008).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
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DR   EMBL; EU564091; ACE81762.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7SQ95; -.
DR   SMR; B7SQ95; -.
DR   GO; GO:0005886; C:plasma 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:0019199; F:transmembrane receptor protein kinase activity; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR044812; CERK1/LYK3-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR46204; CHITIN ELICITOR RECEPTOR KINASE 1-RELATED; 1.
DR   PANTHER; PTHR46204:SF15; LYSM DOMAIN RECEPTOR-LIKE KINASE 3; 1.
DR   Pfam; PF01476; LysM; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51782; LYSM; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACE81762.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:ACE81762.1};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..622
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002861466"
FT   TRANSMEM        230..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..147
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          323..602
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          273..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   622 AA;  68753 MW;  580D8A7963507588 CRC64;
     MKLKNGLLLF FLLVECAFFK VDSKCVKGCD IALASYYVMP LVELSNITTF MQSKLVTNSS
     DVLNRYNKVL VTNHGNIFSY FRINIPFPCE CIGGEFLGHV FEYTTKKGDT YDLIANNYYV
     SLTSVELLKK FNSYDPNHIP AKAKVNVTVN CSCGNSQISK DYGLFVTYPL RSTDSLEKIA
     NESKLDEGLI QNFNPDVNFS RGSGIVFIPG RDKNGEYVPL YPKTGVGKGV AIGISIAGVF
     AVLLFVICIY VKYFQKKEEE KTILPQVSKA LSTQDGNASS SGEYETSGSS GHGTGSAAGL
     TGIMVAKSTE FSYQELAKAT DNFSLDNKIG QGGFGAVYYA ELRGEKTAIK KMNVQASSEF
     LCELKVLTHV HHLNLVRLIG YCVEGSLFLV YEHIDNGNLG QYLHGKDKEP LPWSSRVQIA
     LDSARGLEYI HEHTVPVYIH RDVKSANILI DKNLRGKVAD FGLTKLIEVG NSTLHTRLVG
     TFGYMPPEYA QYGDVSPKID VYAFGVVLYE LISAKNAVLK TGEESVAESK GLVALFEKAL
     NQIDPSEALR KLVDPRLKEN YPIDSVLKMA QLGRACTRDN PLLRPSMRSL VVDLMTLSSP
     FEDCDDDTSY ENQTLINLLS VR
//
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