##gff-version 3
O42893	UniProtKB	Chain	1	735	.	.	.	ID=PRO_0000173797;Note=Cytosolic neutral trehalase	
O42893	UniProtKB	Region	1	55	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O42893	UniProtKB	Active site	457	457	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13482	
O42893	UniProtKB	Active site	652	652	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13482	
O42893	UniProtKB	Binding site	97	97	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32356	
O42893	UniProtKB	Binding site	99	99	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32356	
O42893	UniProtKB	Binding site	101	101	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32356	
O42893	UniProtKB	Binding site	103	103	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32356	
O42893	UniProtKB	Binding site	108	108	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32356	
O42893	UniProtKB	Binding site	283	283	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13482	
O42893	UniProtKB	Binding site	290	291	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13482	
O42893	UniProtKB	Binding site	327	327	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13482	
O42893	UniProtKB	Binding site	336	338	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13482	
O42893	UniProtKB	Binding site	336	336	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O42893	UniProtKB	Binding site	455	455	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13482	
O42893	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18257517;Dbxref=PMID:18257517	
O42893	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18257517;Dbxref=PMID:18257517	
O42893	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18257517;Dbxref=PMID:18257517	
O42893	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18257517;Dbxref=PMID:18257517	
O42893	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Abolishes activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15965643;Dbxref=PMID:15965643	
O42893	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Decreases activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15965643;Dbxref=PMID:15965643	
O42893	UniProtKB	Mutagenesis	51	51	.	.	.	Note=Abolishes activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15965643;Dbxref=PMID:15965643	
O42893	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1. S->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15965643;Dbxref=PMID:15965643	
O42893	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Abolishes calcium binding. Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12943532;Dbxref=PMID:12943532	
O42893	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Decreases calcium binding. Decreases activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12943532;Dbxref=PMID:12943532	
O42893	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Abolishes calcium binding. Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12943532;Dbxref=PMID:12943532