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Database: UniProt
Entry: A0A0B2R405_GLYSO
LinkDB: A0A0B2R405_GLYSO
Original site: A0A0B2R405_GLYSO 
ID   A0A0B2R405_GLYSO        Unreviewed;       810 AA.
AC   A0A0B2R405;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=D0Y65_015855 {ECO:0000313|EMBL:RZC09280.1}, glysoja_039330
GN   {ECO:0000313|EMBL:KHN28390.1};
OS   Glycine soja (Wild soybean).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN28390.1};
RN   [1] {ECO:0000313|EMBL:KHN28390.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Root {ECO:0000313|EMBL:KHN28390.1};
RA   Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT   "Identification of a novel salt tolerance gene in wild soybean by whole-
RT   genome sequencing.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RZC09280.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC09280.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) 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|ARBA:ARBA00001433,
CC         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|ARBA:ARBA00000775,
CC         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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KN652840; KHN28390.1; -; Genomic_DNA.
DR   EMBL; QZWG01000006; RZC09280.1; -; Genomic_DNA.
DR   OrthoDB; 501776at2759; -.
DR   Proteomes; UP000289340; Chromosome 6.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00028; B_lectin; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
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; IPR000742; EGF-like_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF219; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00473; PAN_AP; 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; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50948; PAN; 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|PIRNR:PIRNR000641};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000641, ECO:0000313|EMBL:KHN28390.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW   Receptor {ECO:0000313|EMBL:KHN28390.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289340};
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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..810
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040562883"
FT   DOMAIN          28..148
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          287..323
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          342..424
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          497..782
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   810 AA;  90779 MW;  AF8595E406AA2B02 CRC64;
     MKFILTLTSF ILYILFVSSL VVSIAADTSS ISQSQSLSFG RTIVSPNGVF ELGFFNLGNP
     NKSYLGIWFK NIPSQNIVWV ANGGNPINDS FAILSLNSSG HLVLTHNNTV VWSTSSLRET
     QNPVAKLLDS GNLVIRDENE VNQEAYLWQS FDYPSNTGLS GMKIGWYLKR NLSIHLTAWK
     SDDDPTPGDF TWGIVLHPYP EIYLMKGTKK YYRVGPWNGL SFGNGSPELN NSIYYHEFVS
     DEEEVSYTWN LKNASFLSKV VVNQTTEERP RYVWSETESW MLYSTRPEDY CDHYGVCGAN
     AYCSTTASPI CECLKGYTPK SPEKWKSMDR TQGCVLKHPL SCKYDGFAQV DDLKVPDTKR
     THVDQTLDIE QCRTKCLNDC SCMAYTNSNI SGAGSGCVMW FGDLLDIKLY SVAESGRRLH
     IRLPPSELES IKSKKSSKII IGTSVAAPLG VVLAICFIYR RNIADKSKTK KSIDRQLQDV
     DVPLFDMLTI TAATDNFLLN NKIGEGGFGP VYKGKLVGGQ EIAVKRLSSL SGQGITEFIT
     EVKLIAKLQH RNLVKLLGCC IKGQEKLLVY EYVVNGSLNS FIFDQIKSKL LDWPRRFNII
     LGIARGLLYL HQDSRLRIIH RDLKASNVLL DEKLNPKISD FGMARAFGGD QTEGNTNRVV
     GTYGYMAPEY AFDGNFSIKS DVFSFGILLL EIVCGIKNKS LCHENLTLNL VGYAWALWKE
     QNALQLIDSG IKDSCVIPEV LRCIHVSLLC VQQYPEDRPT MTSVIQMLGS EMDMVEPKEP
     GFFPRRILKE GNLKEMTSND ELTISLFSGR
//
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