##gff-version 3
Q8ILQ7	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000259967;Note=Glutathione S-transferase	
Q8ILQ7	UniProtKB	Domain	3	87	.	.	.	Note=GST N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8ILQ7	UniProtKB	Domain	89	211	.	.	.	Note=GST C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8ILQ7	UniProtKB	Binding site	58	59	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12972411;Dbxref=PMID:12972411	
Q8ILQ7	UniProtKB	Binding site	71	72	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12972411;Dbxref=PMID:12972411	
Q8ILQ7	UniProtKB	Binding site	105	105	.	.	.	Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:3FR9	
Q8ILQ7	UniProtKB	Binding site	117	117	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12972411;Dbxref=PMID:12972411	
Q8ILQ7	UniProtKB	Binding site	121	121	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12972411;Dbxref=PMID:12972411	
Q8ILQ7	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Greater than 10-fold decrease in activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16385005;Dbxref=PMID:16385005	
Q8ILQ7	UniProtKB	Mutagenesis	15	15	.	.	.	Note=10-fold decrease in substrate affinity and 20-fold decrease in activity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16385005;Dbxref=PMID:16385005	
Q8ILQ7	UniProtKB	Mutagenesis	71	71	.	.	.	Note=3-fold decrease in substrate affinity and 2-fold decrease in activity. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16385005;Dbxref=PMID:16385005	
Q8ILQ7	UniProtKB	Mutagenesis	101	101	.	.	.	Note=2-fold decrease in substrate affinity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16385005;Dbxref=PMID:16385005	
Q8ILQ7	UniProtKB	Mutagenesis	211	211	.	.	.	Note=2-fold increase in activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16385005;Dbxref=PMID:16385005	
Q8ILQ7	UniProtKB	Sequence conflict	1	1	.	.	.	Note=M->MKL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8ILQ7	UniProtKB	Beta strand	5	12	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Turn	14	16	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Helix	17	26	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Beta strand	31	35	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Helix	41	51	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Beta strand	61	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Beta strand	67	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Helix	72	82	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Helix	90	111	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Turn	115	118	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Helix	120	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Helix	128	141	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q4J	
Q8ILQ7	UniProtKB	Helix	160	175	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Turn	179	182	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1OKT	
Q8ILQ7	UniProtKB	Helix	184	194	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG	
Q8ILQ7	UniProtKB	Helix	197	205	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZXG