##gff-version 3 P0C0V9 UniProtKB Signal peptide 1 14 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P0C0V9 UniProtKB Chain 15 416 . . . ID=PRO_0000045398;Note=Hemagglutinin-esterase P0C0V9 UniProtKB Topological domain 15 393 . . . Note=Virion surface;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0C0V9 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0C0V9 UniProtKB Topological domain 415 416 . . . Note=Intravirion;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0C0V9 UniProtKB Region 4 121 . . . Note=Esterase domain first part;Ontology_term=ECO:0000250;evidence=ECO:0000250 P0C0V9 UniProtKB Region 122 263 . . . Note=Receptor binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 P0C0V9 UniProtKB Region 264 379 . . . Note=Esterase domain second part;Ontology_term=ECO:0000250;evidence=ECO:0000250 P0C0V9 UniProtKB Active site 37 37 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 P0C0V9 UniProtKB Active site 325 325 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 P0C0V9 UniProtKB Active site 328 328 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 P0C0V9 UniProtKB Glycosylation 76 76 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Glycosylation 257 257 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Glycosylation 278 278 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Glycosylation 313 313 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Glycosylation 322 322 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Glycosylation 343 343 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Disulfide bond 41 57 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Disulfide bond 88 136 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Disulfide bond 200 246 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Disulfide bond 206 213 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Disulfide bond 304 309 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Disulfide bond 346 371 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Natural variant 29 29 . . . Note=F->S P0C0V9 UniProtKB Natural variant 114 114 . . . Note=D->G P0C0V9 UniProtKB Natural variant 133 133 . . . Note=T->I P0C0V9 UniProtKB Natural variant 152 152 . . . Note=Q->K P0C0V9 UniProtKB Natural variant 155 155 . . . Note=V->E P0C0V9 UniProtKB Natural variant 159 159 . . . Note=N->K P0C0V9 UniProtKB Natural variant 214 214 . . . Note=L->R P0C0V9 UniProtKB Natural variant 234 234 . . . Note=P->S P0C0V9 UniProtKB Natural variant 238 238 . . . Note=S->L P0C0V9 UniProtKB Natural variant 416 416 . . . Note=C->V P0C0V9 UniProtKB Mutagenesis 64 64 . . . Note=Strongly reduced activity toward 7%2C9-di-O-acetylated sialic acids and strongly increased activity toward 9-mono-O-acetylated sialic acids. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Mutagenesis 103 103 . . . Note=Strongly reduced activity toward both 7%2C9-di and 9-mono-O-acetylated sialic acids. Increased activity toward synthetic substrate (4-nitrophenyl)acetate. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Mutagenesis 109 109 . . . Note=Reduced lectin activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Mutagenesis 168 168 . . . Note=Reduced lectin activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Mutagenesis 170 170 . . . Note=Reduced lectin activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Mutagenesis 207 207 . . . Note=Loss of lectin activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19721004;Dbxref=PMID:19721004 P0C0V9 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 27 29 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 31 36 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 37 39 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Turn 44 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 54 59 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 60 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 68 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 90 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 102 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 108 111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 112 131 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 164 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 177 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 193 202 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 216 222 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 225 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 244 251 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 253 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 269 274 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 283 286 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 299 303 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Turn 306 308 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 309 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 320 325 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 328 330 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 331 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 338 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 345 348 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 351 353 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 357 361 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Beta strand 368 370 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26 P0C0V9 UniProtKB Helix 375 378 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I26