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Database: UniProt
Entry: W9QXB6_9ROSA
LinkDB: W9QXB6_9ROSA
Original site: W9QXB6_9ROSA 
ID   W9QXB6_9ROSA            Unreviewed;       830 AA.
AC   W9QXB6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN   ORFNames=L484_016423 {ECO:0000313|EMBL:EXB57371.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB57371.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000641};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|PIRNR:PIRNR000641};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR   EMBL; KE344346; EXB57371.1; -; Genomic_DNA.
DR   RefSeq; XP_010094842.1; XM_010096540.1.
DR   AlphaFoldDB; W9QXB6; -.
DR   STRING; 981085.W9QXB6; -.
DR   GeneID; 21399471; -.
DR   KEGG; mnt:21399471; -.
DR   eggNOG; ENOG502QRWA; Eukaryota.
DR   OrthoDB; 364069at2759; -.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR   PANTHER; PTHR47974:SF9; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 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|PIRNR:PIRNR000641};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW   Lectin {ECO:0000313|EMBL:EXB57371.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000313|EMBL:EXB57371.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000641};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..830
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004930998"
FT   DOMAIN          16..137
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          139..257
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          480..756
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          795..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         508
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   830 AA;  90414 MW;  479D560C1BB8B2B2 CRC64;
     MAFHLSLLLA LLPMAAVSIS PGSSLYASNL NQTWSSPNKT YSLGFLPSDP STSPPSFIAA
     IFYSGRVPIW SASSAAVDSR GALNFDSSGN LLLVNGSGAK LWESGTSGRH VSSLDLDDTG
     NLALRNGSST VWSSFDHPTD SIVPSQNFTV GKVLRSGLYS FSLLKNGNLS LKWNDSIVYW
     NQGLNSSYEK NLSSPSLVLQ PIGILSISDT SLSSSLIVAY SSDYAEGSDI LRFLKLDNDG
     NLKIFSSARG SGTKMGRWAA VADQCEVYGY CGNMGICSYN ESDPVCGCPS QNFEPVDPKD
     SRKGCRRKVE IADCPGSPTM LDMEHTQLLT YPPEYEAQVF FVGISACRLN CLVSGSCDAS
     TSLSDGTGLC FYKTPSFLSG YQSPAMMSSS YIKVCGPVVQ NPLPSVGEGK SSVWKVRPWI
     VAVVVLATLG GLVMLEGGLW FWFCRNRPNF GGLSAHYALL EYASGAPVQF SYKELQRATK
     GFKEKLGAGG FGAVYRGILA NKMVAAVKQL EGIEQGEKQF RMEVATISST HHLNLVRLIG
     FCSEGRHRLL VYEFMKNGSL DAFLFKTDEN SGRLLNWEYR FNIALGTARG ITYLHEECRD
     CIVHCDIKPE NILLDENYCS KVSDFGLAKL INPKDHRYRT LKSVRGTRGY LAPEWLANLP
     ITSKSDVYSY GMVLLEIVSG RRNFEVSAET NHKKFSMWAY EEFEKGNVQG IVDNRIVEEV
     DMDQVMRAVQ VSFWCIQEQP SHRPMMGKVV QMLEGITEIE RPPAPKAATE LSASGTSIHA
     STNTSTLSTI AASAPAPSSF SSFQTPGLSP LASGISSEKA SSSLLYSDLK
//
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