ID A0A9D5BXA6_9LILI Unreviewed; 785 AA.
AC A0A9D5BXA6;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
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=J5N97_030236 {ECO:0000313|EMBL:KAJ0962408.1};
OS Dioscorea zingiberensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC Dioscorea.
OX NCBI_TaxID=325984 {ECO:0000313|EMBL:KAJ0962408.1, ECO:0000313|Proteomes:UP001085076};
RN [1] {ECO:0000313|EMBL:KAJ0962408.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0962408.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAJ0962408.1};
RA Li Z., Yang C.;
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ0962408.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0962408.1};
RX PubMed=36204203;
RA Li Y., Tan C., Li Z., Guo J., Li S., Chen X., Wang C., Dai X., Yang H.,
RA Song W., Hou L., Xu J., Tong Z., Xu A., Yuan X., Wang W., Yang Q., Chen L.,
RA Sun Z., Wang K., Pan B., Chen J., Bao Y., Liu F., Qi X., Gang D.R., Wen J.,
RA Li J.;
RT "The genome of Dioscorea zingiberensis sheds light on the biosynthesis,
RT origin and evolution of the medicinally important diosgenin saponins.";
RL Hortic Res 9:0-0(2022).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048679,
CC ECO:0000256|PIRNR:PIRNR000641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899,
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAJ0962408.1}.
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DR EMBL; JAGGNH010000010; KAJ0962408.1; -; Genomic_DNA.
DR OrthoDB; 643280at2759; -.
DR Proteomes; UP001085076; Miscellaneous, Linkage group lg10.
DR GO; GO:0016020; C: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:0048544; P:recognition of pollen; IEA:InterPro.
DR GO; GO:0051707; P:response to other organism; IEA:UniProtKB-ARBA.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR FunFam; 3.30.200.20:FF:000370; Receptor-like protein kinase 4; 1.
DR FunFam; 1.10.510.10:FF:000227; Serine/threonine-protein kinase; 1.
DR FunFam; 2.90.10.10:FF:000002; Serine/threonine-protein kinase; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
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:SF19; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF08276; PAN_2; 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; 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; PS50948; PAN; 1.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP001085076};
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};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..785
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039447164"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..149
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 341..423
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 488..785
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 785 AA; 87563 MW; 7724A576F2C49CE4 CRC64;
MTPVSRRIVL ILFLISLTIC ASHESDSINI NKPLSGDQKI TSKGGNFVLG FFTKDNSSRR
FYIGIWYKRV SELTPVWVAN RATPVSDPTK SLLHISHEGN LVLQDQLAKS LIWSTNATIS
SYSTVAVLQD NGNLVLRDGE NSSNVFWQSF ENPTHTWLSG GKLAFNKRTG VSQRLTSWKN
PENPAPGLFS LEIGQNGQYI SQWNMSKSYW TTGPWDGRTF SQVPVMAEHF MFDYTYVNNS
EEIYFSFSVI DNATIARLIM DVSGQMKFLK WVEAVRVWTQ FWCGPEAQCQ VTAFCGPFGS
CNEQRLRHKC TCVKGFSQRS LKDWDLSDYS GGCTRITPLQ CGGNTSAYVE EDKFLLISSV
RLPTDAQQFQ AGNVDECEQA CLNNCSCTAY SYGTTCSLWY GGLLNLQDQY DGADGGTLYL
RLAASELPRH HNNRRVPGII AGGVAASFVG ALVVWVLVTT WRRRERSWVL EKGALVVFRY
NDLQRVTHNF SDKLGAGSFG SVFKGVLPDS TIVAVKKLQG IRQGEKQFRA EVSTLGTIQH
VNLVSLRGFC AEGTERLLVF DYMPNGSLDS HLFHSNAKVL DWSTRYRIAL GIARGLAYLH
EKCRECIIHC DIKPENILLD AAFNPIVTDF GLAKLLGREF SHVLTSLRGT IGYISPEWIS
GLAITPKADV YSFGMMLLEI ISGKRNTKQI KCWVDYFPLK AAIQVREGMV DCLLDGRLQG
DANMDELNIA CKVACWCIQD MEIERPTMGM VVLMLEGLME VSIPPISAFL QGLVHPGEQN
VASSD
//
