##gff-version 3 P30215 UniProtKB Signal peptide 1 16 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Chain 17 424 . . . ID=PRO_0000037144;Note=Hemagglutinin-esterase;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Topological domain 17 392 . . . Note=Virion surface;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Transmembrane 393 413 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Topological domain 414 424 . . . Note=Intravirion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Region 7 127 . . . Note=Esterase domain 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Region 128 266 . . . Note=Receptor binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Region 267 379 . . . Note=Esterase domain 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Active site 40 40 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Active site 326 326 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Active site 329 329 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 54 54 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 89 89 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 153 153 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 236 236 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 301 301 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 316 316 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 358 358 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Glycosylation 417 417 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Disulfide bond 44 65 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Disulfide bond 113 162 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Disulfide bond 197 276 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Disulfide bond 205 249 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Disulfide bond 307 312 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Disulfide bond 347 371 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_04207 P30215 UniProtKB Natural variant 158 158 . . . Note=In strain: Isolate ATCCVR-759 and Isolate clinical OC43-Paris. S->A P30215 UniProtKB Natural variant 379 379 . . . Note=In strain: Isolate ATCCVR-759 and Isolate clinical OC43-Paris. N->I P30215 UniProtKB Natural variant 403 404 . . . Note=In strain: Isolate ATCCVR-759 and Isolate clinical OC43-Paris. VI->IV P30215 UniProtKB Natural variant 418 418 . . . Note=In strain: Isolate ATCCVR-759 and Isolate clinical OC43-Paris. G->V