##gff-version 3
P55824	UniProtKB	Chain	1	2778	.	.	.	ID=PRO_0000080688;Note=Probable ubiquitin carboxyl-terminal hydrolase FAF	
P55824	UniProtKB	Domain	1668	2062	.	.	.	Note=USP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01035	
P55824	UniProtKB	Region	1	85	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P55824	UniProtKB	Region	1065	1094	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P55824	UniProtKB	Region	2568	2632	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P55824	UniProtKB	Region	2644	2691	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P55824	UniProtKB	Compositional bias	1065	1085	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P55824	UniProtKB	Compositional bias	2568	2584	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P55824	UniProtKB	Compositional bias	2605	2626	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P55824	UniProtKB	Active site	1677	1677	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093,ECO:0000305|PubMed:23919485;Dbxref=PMID:23919485	
P55824	UniProtKB	Active site	1986	1986	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
P55824	UniProtKB	Modified residue	924	924	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18327897;Dbxref=PMID:18327897	
P55824	UniProtKB	Alternative sequence	2705	2778	.	.	.	ID=VSP_005269;Note=In isoform 3. KCRRVIIKKLVESKDEEDATTATTAATTEVTTSPATAIATAATLEPAGMSELTTMVEKNLIISQENPQAKSSLQ->VTRANNV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1295747;Dbxref=PMID:1295747	
P55824	UniProtKB	Mutagenesis	1677	1677	.	.	.	Note=Loss of enzymatic activity. Increased susceptibility to infections by E.cloacae. No effect on binding and polyubiquitination of imd. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23919485;Dbxref=PMID:23919485	
P55824	UniProtKB	Sequence conflict	234	234	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P55824	UniProtKB	Sequence conflict	2725	2725	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305