##gff-version 3
P00433	UniProtKB	Signal peptide	1	30	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1001465;Dbxref=PMID:1001465	
P00433	UniProtKB	Chain	31	338	.	.	.	ID=PRO_0000023739;Note=Peroxidase C1A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1001465;Dbxref=PMID:1001465	
P00433	UniProtKB	Propeptide	339	353	.	.	.	ID=PRO_0000023740	
P00433	UniProtKB	Active site	72	72	.	.	.	Note=Proton acceptor	
P00433	UniProtKB	Binding site	73	73	.	.	.	.	
P00433	UniProtKB	Binding site	76	76	.	.	.	.	
P00433	UniProtKB	Binding site	78	78	.	.	.	.	
P00433	UniProtKB	Binding site	80	80	.	.	.	.	
P00433	UniProtKB	Binding site	82	82	.	.	.	.	
P00433	UniProtKB	Binding site	94	94	.	.	.	.	
P00433	UniProtKB	Binding site	169	169	.	.	.	.	
P00433	UniProtKB	Binding site	200	200	.	.	.	Note=Axial binding residue	
P00433	UniProtKB	Binding site	201	201	.	.	.	.	
P00433	UniProtKB	Binding site	252	252	.	.	.	.	
P00433	UniProtKB	Binding site	255	255	.	.	.	.	
P00433	UniProtKB	Binding site	260	260	.	.	.	.	
P00433	UniProtKB	Site	68	68	.	.	.	Note=Transition state stabilizer	
P00433	UniProtKB	Modified residue	31	31	.	.	.	Note=Pyrrolidone carboxylic acid;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00297,ECO:0000269|PubMed:1001465;Dbxref=PMID:1001465	
P00433	UniProtKB	Glycosylation	43	43	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1001465;Dbxref=PMID:1001465	
P00433	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1001465;Dbxref=PMID:1001465	
P00433	UniProtKB	Glycosylation	188	188	.	.	.	Note=N-linked (GlcNAc...) asparagine	
P00433	UniProtKB	Glycosylation	216	216	.	.	.	Note=N-linked (GlcNAc...) asparagine	
P00433	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine	
P00433	UniProtKB	Glycosylation	244	244	.	.	.	Note=N-linked (GlcNAc...) asparagine	
P00433	UniProtKB	Glycosylation	285	285	.	.	.	Note=N-linked (GlcNAc...) asparagine	
P00433	UniProtKB	Glycosylation	298	298	.	.	.	Note=N-linked (GlcNAc...) asparagine	
P00433	UniProtKB	Disulfide bond	41	121	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00297,ECO:0000269|PubMed:1001465;Dbxref=PMID:1001465	
P00433	UniProtKB	Disulfide bond	74	79	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00297,ECO:0000269|PubMed:1001465;Dbxref=PMID:1001465	
P00433	UniProtKB	Disulfide bond	127	331	.	.	.	.	
P00433	UniProtKB	Disulfide bond	207	239	.	.	.	.	
P00433	UniProtKB	Turn	34	40	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	44	58	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	62	74	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Beta strand	78	81	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Beta strand	89	91	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	94	96	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Turn	98	103	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	107	120	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Turn	122	124	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	127	141	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	161	167	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	175	184	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	190	197	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	198	201	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Beta strand	204	206	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	207	210	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	211	215	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	217	219	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Beta strand	220	222	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	229	238	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Beta strand	248	251	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Beta strand	253	255	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1H5F	
P00433	UniProtKB	Helix	262	268	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	275	282	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Turn	284	288	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	289	298	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Helix	300	314	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU	
P00433	UniProtKB	Beta strand	324	326	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GWU