##gff-version 3
Q9D967	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000068828;Note=Magnesium-dependent phosphatase 1	
Q9D967	UniProtKB	Active site	11	11	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9D967	UniProtKB	Active site	13	13	.	.	.	Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9D967	UniProtKB	Binding site	11	11	.	.	.	.	
Q9D967	UniProtKB	Binding site	12	12	.	.	.	.	
Q9D967	UniProtKB	Binding site	13	13	.	.	.	.	
Q9D967	UniProtKB	Binding site	13	13	.	.	.	.	
Q9D967	UniProtKB	Binding site	20	20	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9D967	UniProtKB	Binding site	69	69	.	.	.	.	
Q9D967	UniProtKB	Binding site	70	70	.	.	.	.	
Q9D967	UniProtKB	Binding site	70	70	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9D967	UniProtKB	Binding site	100	100	.	.	.	.	
Q9D967	UniProtKB	Binding site	123	123	.	.	.	.	
Q9D967	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Abolishes enzymatic activity. D->N%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601995;Dbxref=PMID:11601995	
Q9D967	UniProtKB	Mutagenesis	13	13	.	.	.	Note=92%25 loss of enzymatic activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601995;Dbxref=PMID:11601995	
Q9D967	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Abolishes enzymatic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601995;Dbxref=PMID:11601995	
Q9D967	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Abolishes enzymatic activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601995;Dbxref=PMID:11601995	
Q9D967	UniProtKB	Mutagenesis	103	103	.	.	.	Note=50%25 decrease in enzymatic activity. H->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10889041;Dbxref=PMID:10889041	
Q9D967	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Abolishes enzymatic activity. D->N	
Q9D967	UniProtKB	Mutagenesis	123	123	.	.	.	Note=Abolishes enzymatic activity. D->N	
Q9D967	UniProtKB	Mutagenesis	127	127	.	.	.	Note=50%25 decrease in enzymatic activity. N->D	
Q9D967	UniProtKB	Mutagenesis	138	138	.	.	.	Note=No effect on enzymatic activity. C->S%2CA%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10889041;Dbxref=PMID:10889041	
Q9D967	UniProtKB	Beta strand	6	10	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Turn	13	15	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Helix	51	60	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Beta strand	65	69	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Helix	74	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Helix	87	89	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Beta strand	90	98	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Helix	100	111	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Beta strand	118	123	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Helix	125	132	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Turn	133	135	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Beta strand	137	140	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Beta strand	142	144	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Helix	147	160	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7O	
Q9D967	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7P