##gff-version 3
Q9NRC8	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000110271;Note=NAD-dependent protein deacetylase sirtuin-7	
Q9NRC8	UniProtKB	Domain	82	329	.	.	.	Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
Q9NRC8	UniProtKB	Region	1	27	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NRC8	UniProtKB	Region	354	380	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NRC8	UniProtKB	Compositional bias	9	27	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NRC8	UniProtKB	Compositional bias	354	369	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NRC8	UniProtKB	Active site	187	187	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:16618798,ECO:0000269|PubMed:22722849,ECO:0000269|PubMed:26867678,ECO:0000269|PubMed:30944854;Dbxref=PMID:16618798,PMID:22722849,PMID:26867678,PMID:30944854	
Q9NRC8	UniProtKB	Binding site	107	126	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NXA8	
Q9NRC8	UniProtKB	Binding site	167	170	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NXA8	
Q9NRC8	UniProtKB	Binding site	195	195	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
Q9NRC8	UniProtKB	Binding site	198	198	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
Q9NRC8	UniProtKB	Binding site	225	225	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
Q9NRC8	UniProtKB	Binding site	228	228	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
Q9NRC8	UniProtKB	Binding site	268	270	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NXA8	
Q9NRC8	UniProtKB	Binding site	297	299	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NXA8	
Q9NRC8	UniProtKB	Binding site	315	315	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NXA8	
Q9NRC8	UniProtKB	Modified residue	388	388	.	.	.	Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30420520;Dbxref=PMID:30420520	
Q9NRC8	UniProtKB	Modified residue	388	388	.	.	.	Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:30420520,ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315,PMID:30420520	
Q9NRC8	UniProtKB	Alternative sequence	1	30	.	.	.	ID=VSP_044396;Note=In isoform 3. MAAGGLSRSERKAAERVRRLREEQQRERLR->MPGPRRRSPSACP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q9NRC8	UniProtKB	Alternative sequence	162	183	.	.	.	ID=VSP_008736;Note=In isoform 2. QHVVSQNCDGLHLRSGLPRTAI->RALGGWYTCQGPGRAPWCPVGN;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q9NRC8	UniProtKB	Alternative sequence	184	400	.	.	.	ID=VSP_008737;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q9NRC8	UniProtKB	Alternative sequence	336	400	.	.	.	ID=VSP_044397;Note=In isoform 3. WQDPIFSLATPLRAGEEGSHSRKSLCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT->VL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q9NRC8	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Catalytically inactive mutant%3B abolishes activation of pre-rRNA synthesis. Abolishes deacetylation of DDB1. Abolished histone desuccinylase activity%3B when associated with Y-187. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16618798,ECO:0000269|PubMed:22586326,ECO:0000269|PubMed:27436229,ECO:0000269|PubMed:28886238;Dbxref=PMID:16618798,PMID:22586326,PMID:27436229,PMID:28886238	
Q9NRC8	UniProtKB	Mutagenesis	187	187	.	.	.	Note=Abolishes deacylase and deacetylase activities and activation of pre-rRNA synthesis. Abolished histone desuccinylase activity%3B when associated with A-111. H->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16618798,ECO:0000269|PubMed:22722849,ECO:0000269|PubMed:26867678,ECO:0000269|PubMed:27436229,ECO:0000269|PubMed:30944854;Dbxref=PMID:16618798,PMID:22722849,PMID:26867678,PMID:27436229,PMID:30944854	
Q9NRC8	UniProtKB	Mutagenesis	388	388	.	.	.	Note=Mimics methylation status%3B impaired histone deacetylase activity. R->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30420520;Dbxref=PMID:30420520	
Q9NRC8	UniProtKB	Mutagenesis	388	388	.	.	.	Note=Decreased methylation%3B does not affect histone deacetylase activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30420520;Dbxref=PMID:30420520	
Q9NRC8	UniProtKB	Sequence conflict	71	71	.	.	.	Note=L->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9NRC8	UniProtKB	Sequence conflict	384	384	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9NRC8	UniProtKB	Helix	8	37	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5IQZ	
Q9NRC8	UniProtKB	Helix	40	42	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5IQZ	
Q9NRC8	UniProtKB	Helix	45	52	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5IQZ	
Q9NRC8	UniProtKB	Helix	55	60	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5IQZ