##gff-version 3 C0LGT1 UniProtKB Signal peptide 1 31 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 C0LGT1 UniProtKB Chain 32 613 . . . ID=PRO_0000387560;Note=Probable LRR receptor-like serine/threonine-protein kinase At5g10290 C0LGT1 UniProtKB Topological domain 32 225 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 C0LGT1 UniProtKB Transmembrane 226 246 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 C0LGT1 UniProtKB Topological domain 247 613 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 C0LGT1 UniProtKB Repeat 95 117 . . . Note=LRR 1 C0LGT1 UniProtKB Repeat 119 141 . . . Note=LRR 2 C0LGT1 UniProtKB Repeat 143 166 . . . Note=LRR 3 C0LGT1 UniProtKB Repeat 167 189 . . . Note=LRR 4 C0LGT1 UniProtKB Domain 290 569 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 C0LGT1 UniProtKB Active site 417 417 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 C0LGT1 UniProtKB Binding site 296 304 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 C0LGT1 UniProtKB Binding site 318 318 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 C0LGT1 UniProtKB Modified residue 287 287 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9LSI9 C0LGT1 UniProtKB Modified residue 313 313 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94F62 C0LGT1 UniProtKB Modified residue 371 371 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94AG2 C0LGT1 UniProtKB Modified residue 390 390 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94AG2 C0LGT1 UniProtKB Modified residue 450 450 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94F62 C0LGT1 UniProtKB Modified residue 451 451 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94F62 C0LGT1 UniProtKB Modified residue 456 456 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94F62 C0LGT1 UniProtKB Modified residue 464 464 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94AG2 C0LGT1 UniProtKB Modified residue 466 466 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94AG2 C0LGT1 UniProtKB Modified residue 467 467 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94AG2 C0LGT1 UniProtKB Modified residue 471 471 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94AG2 C0LGT1 UniProtKB Modified residue 547 547 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q94AG2 C0LGT1 UniProtKB Glycosylation 81 81 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 C0LGT1 UniProtKB Glycosylation 116 116 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 C0LGT1 UniProtKB Glycosylation 155 155 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 C0LGT1 UniProtKB Glycosylation 193 193 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 C0LGT1 UniProtKB Sequence conflict 537 537 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305