##gff-version 3
Q9BQ65	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000274391;Note=U6 snRNA phosphodiesterase 1	
Q9BQ65	UniProtKB	Region	1	72	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9BQ65	UniProtKB	Compositional bias	1	15	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9BQ65	UniProtKB	Compositional bias	16	30	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9BQ65	UniProtKB	Active site	120	120	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03040,ECO:0000269|PubMed:23190533,ECO:0000269|PubMed:30215753;Dbxref=PMID:23190533,PMID:30215753	
Q9BQ65	UniProtKB	Active site	208	208	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03040,ECO:0000269|PubMed:23190533,ECO:0000269|PubMed:30215753;Dbxref=PMID:23190533,PMID:30215753	
Q9BQ65	UniProtKB	Binding site	120	122	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:30215753,ECO:0007744|PDB:6D31;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Binding site	164	164	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:28887445,ECO:0007744|PDB:5V1M;Dbxref=PMID:28887445	
Q9BQ65	UniProtKB	Binding site	202	202	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:30215753,ECO:0007744|PDB:6D31;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Binding site	202	202	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:28887445,ECO:0007744|PDB:5V1M;Dbxref=PMID:28887445	
Q9BQ65	UniProtKB	Binding site	204	210	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:30215753,ECO:0007744|PDB:6D31;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Binding site	206	210	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:28887445,ECO:0007744|PDB:5V1M;Dbxref=PMID:28887445	
Q9BQ65	UniProtKB	Alternative sequence	150	265	.	.	.	ID=VSP_042936;Note=In isoform 3. RFFFTANQVKIYTNQEKTRTFIGLEVTSGHAQFLDLVSEVDRVMEEFNLTTFYQDPSFHLSLAWCVGDARLQLEGQCLQELQAIVDGFEDAEVLLRVHTEQVRCKSGNKFFSMPLK->SPHPGPHCLIGTKDAPVTQEIPKDLGALRQEPGSQTR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q9BQ65	UniProtKB	Alternative sequence	150	167	.	.	.	ID=VSP_042878;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q9BQ65	UniProtKB	Natural variant	115	115	.	.	.	ID=VAR_053822;Note=R->K;Dbxref=dbSNP:rs35025252	
Q9BQ65	UniProtKB	Natural variant	250	250	.	.	.	ID=VAR_030277;Note=Q->E;Dbxref=dbSNP:rs16959641	
Q9BQ65	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Abolishes exoribonuclease activity. Does not restore U6 snRNA processing when expressed in deleted mpn1 yeast cells%3B when associated with A-208. Increases the accumulation of unspliced pre-mRNAs when expressed in deleted mpn1 yeast cells%3B when associated with A-208. Slows growth in the cold when expressed in deleted mpn1 yeast cells%3B when associated with A-208. Abolishes exoribonuclease activity%3B when associated with A-208. Decreases U6 and U6atac motility. H->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23022480,ECO:0000269|PubMed:23190533,ECO:0000269|PubMed:26213367;Dbxref=PMID:23022480,PMID:23190533,PMID:26213367	
Q9BQ65	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Significantly decreases exonuclease activity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30215753;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Significantly decreases exonuclease activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30215753;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Mutagenesis	202	202	.	.	.	Note=Significantly decreases exonuclease activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30215753;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Abolishes exoribonuclease activity. Does not rescue the molecular phenotype caused by USB1 depletion. Does not restore U6 snRNA processing when expressed in deleted mpn1 yeast cells%3B when associated with A-120. Increases the accumulation of unspliced pre-mRNAs when expressed in deleted mpn1 yeast cells%3B when associated with A-120. Slows growth in the cold when expressed in deleted mpn1 yeast cells%3B when associated with A-120. Abolishes exoribonuclease activity%3B when associated with A-120. Decreases U6 and U6atac motility. H->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22899009,ECO:0000269|PubMed:23022480,ECO:0000269|PubMed:23190533,ECO:0000269|PubMed:26213367;Dbxref=PMID:22899009,PMID:23022480,PMID:23190533,PMID:26213367	
Q9BQ65	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Loss of exonuclease activity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30215753;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Loss of exonuclease activity. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30215753;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Significantly decreases exonuclease activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30215753;Dbxref=PMID:30215753	
Q9BQ65	UniProtKB	Sequence conflict	89	89	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9BQ65	UniProtKB	Sequence conflict	209	209	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9BQ65	UniProtKB	Beta strand	80	89	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Helix	93	107	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Beta strand	117	122	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Beta strand	127	130	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Helix	134	145	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Beta strand	155	162	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Beta strand	166	175	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Helix	179	195	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Beta strand	208	216	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Helix	219	222	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Helix	225	235	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Helix	241	244	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Beta strand	245	247	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6D30	
Q9BQ65	UniProtKB	Beta strand	250	255	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W	
Q9BQ65	UniProtKB	Beta strand	258	263	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H7W