##gff-version 3 P04963 UniProtKB Signal peptide 1 20 . . . . P04963 UniProtKB Chain 21 319 . . . ID=PRO_0000023631;Note=Chloroperoxidase P04963 UniProtKB Propeptide 322 373 . . . ID=PRO_0000023632 P04963 UniProtKB Active site 204 204 . . . . P04963 UniProtKB Binding site 50 50 . . . Note=Axial binding residue P04963 UniProtKB Binding site 125 125 . . . . P04963 UniProtKB Binding site 126 126 . . . . P04963 UniProtKB Binding site 129 129 . . . . P04963 UniProtKB Modified residue 21 21 . . . Note=Pyrrolidone carboxylic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8747463;Dbxref=PMID:8747463 P04963 UniProtKB Glycosylation 33 33 . . . Note=N-linked (GlcNAc...) asparagine P04963 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine P04963 UniProtKB Glycosylation 237 237 . . . Note=N-linked (GlcNAc...) asparagine P04963 UniProtKB Glycosylation 259 259 . . . Note=O-linked (Man) threonine P04963 UniProtKB Glycosylation 260 260 . . . Note=O-linked (Man) serine P04963 UniProtKB Glycosylation 262 262 . . . Note=O-linked (Man) serine P04963 UniProtKB Glycosylation 263 263 . . . Note=O-linked (Man) serine P04963 UniProtKB Glycosylation 269 269 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04963 UniProtKB Glycosylation 271 271 . . . Note=O-linked (Man) threonine P04963 UniProtKB Glycosylation 272 272 . . . Note=O-linked (Man) serine P04963 UniProtKB Glycosylation 273 273 . . . Note=O-linked (Man) threonine P04963 UniProtKB Glycosylation 296 296 . . . Note=O-linked (Man...) threonine P04963 UniProtKB Glycosylation 304 304 . . . Note=O-linked (Man...) threonine P04963 UniProtKB Glycosylation 314 314 . . . Note=O-linked (Man...) threonine P04963 UniProtKB Disulfide bond 100 108 . . . . P04963 UniProtKB Mutagenesis 50 50 . . . Note=Retains most of the chlorination%2C peroxidation%2C epoxidation%2C and catalase activities. C->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10535936;Dbxref=PMID:10535936 P04963 UniProtKB Helix 23 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Turn 27 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 51 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 71 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 86 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Beta strand 111 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 116 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Turn 121 124 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 153 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Turn 163 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Beta strand 167 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 171 188 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Turn 191 193 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 198 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Turn 218 222 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 228 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 242 244 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Helix 255 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CIW P04963 UniProtKB Turn 311 314 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CPO