ID W1NTK9_AMBTC Unreviewed; 823 AA.
AC W1NTK9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=AMTR_s00103p00133830 {ECO:0000313|EMBL:ERN00882.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN00882.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR EMBL; KI394805; ERN00882.1; -; Genomic_DNA.
DR RefSeq; XP_006838313.1; XM_006838250.2.
DR AlphaFoldDB; W1NTK9; -.
DR EnsemblPlants; ERN00882; ERN00882; AMTR_s00103p00133830.
DR GeneID; 18428954; -.
DR Gramene; ERN00882; ERN00882; AMTR_s00103p00133830.
DR KEGG; atr:18428954; -.
DR eggNOG; ENOG502QW3Z; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR OMA; QKICVAC; -.
DR OrthoDB; 1210474at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP 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; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47974:SF13; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE SD3-1; 1.
DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 2.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000641};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000256|PIRNR:PIRNR000641}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
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|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..823
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004806830"
FT TRANSMEM 442..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..152
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 328..408
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 496..768
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 778..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 90917 MW; AAF7A909B827513B CRC64;
MASFSLIIFC FYFSLPSIFD GFVSGISLGS SLAVNANNFW VSSPKGSFAF GFFNRSDEEP
NQYGLGIRYN SLLIPTSAQR VVWSAGGDVI VGPQASLQLT MEGDLVLLDP PKSLPAWTSN
TSKLSVSQAS LLDNGNLILL DSNNKMVWQS FETPSDTVLP GQNLTAQTLR AATRDTVSSY
YSLALDDTGQ LELKWETSIN YWRSGTASLG AIGLMIGSNG ALQLYDKEFR PVWLRFGEDH
DDPSVGFRHL RLDMDGNLRM YSWVKEIGSW REVWRAIENR CEVFATCGQQ GLCVLTPTGE
ALCRCPFKSS EISNSSENIK CLAPYQQCSS GTTLTALKHT VLYSLYPPHD AVNYLSLSQC
RDSCLSDETC TAVTVMADGS GECRMKTTRF VTGYKHASVP SISYVKDCLD PMALNPGIII
SQTPSVEPSS PKRRHGFCLP CLLGAACGTL LAFFVIQIGV CYCFLRHRRR KEKIHMERRA
MAISRGPIRL TYLEIKDLTK DFSEKLGSAV YKGVLPGNRL VAIKELERDV PEKQFRSVLS
MVGSIHHKNL VKLEGYCCDS EHRYMVYEYM KNGSLDSLLV GPRKKRRLSW RRRAEIWTGV
SRGLAYLHGE CHRFIGHGSL KLENILLDQD LVPHLTHFAL PDRQAPRAEI DVLAFGKLLL
EMVTGQVAGP TLCAWAYEEW AQGRVQGVLD ADLDGSKVAW GEVERVLRVA FWCLQARAGL
RPSIAEVVKV LEGLLTVDPP PFPFNGDHPL TENEGESPEN GGIGHVWSES CELGLPENGI
GGGYGGEGLG DDTMLENVGE SPKNDGDGPT WPDSGELRPH FET
//
