##gff-version 3
Q93091	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P81649	
Q93091	UniProtKB	Chain	24	150	.	.	.	ID=PRO_0000030892;Note=Ribonuclease K6	
Q93091	UniProtKB	Active site	38	38	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64438	
Q93091	UniProtKB	Active site	145	145	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64438	
Q93091	UniProtKB	Binding site	61	65	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q93091	UniProtKB	Binding site	86	86	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q93091	UniProtKB	Binding site	105	105	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q93091	UniProtKB	Site	24	24	.	.	.	Note=Important for bactericidal activity%2C bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27089320;Dbxref=PMID:27089320	
Q93091	UniProtKB	Site	36	36	.	.	.	Note=Important for bactericidal activity%2C bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27089320;Dbxref=PMID:27089320	
Q93091	UniProtKB	Site	59	59	.	.	.	Note=Facilitates cleavage of polynucleotide substrates;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27013146;Dbxref=PMID:27013146	
Q93091	UniProtKB	Site	61	61	.	.	.	Note=Critical for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H1E1	
Q93091	UniProtKB	Glycosylation	55	55	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q93091	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q93091	UniProtKB	Disulfide bond	46	104	.	.	.	Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4X09	
Q93091	UniProtKB	Disulfide bond	60	114	.	.	.	Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4X09	
Q93091	UniProtKB	Disulfide bond	78	129	.	.	.	Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4X09	
Q93091	UniProtKB	Disulfide bond	85	92	.	.	.	Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4X09	
Q93091	UniProtKB	Natural variant	89	89	.	.	.	ID=VAR_012048;Note=R->Q;Dbxref=dbSNP:rs1045922	
Q93091	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Moderately impairs bactericidal activity%2C bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS). W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27089320;Dbxref=PMID:27089320	
Q93091	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Strongly impairs bactericidal activity%2C bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS). I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27089320;Dbxref=PMID:27089320	
Q93091	UniProtKB	Mutagenesis	38	38	.	.	.	Note=Significantly reduced activity towards dinucleotides UpA and CpA. Slightly reduced activity towards polymeric substrates poly(U) and poly(U):poly(A). No effect on bactericidal activity. Significantly reduced activity towards poly(U) and poly(U):poly(A)%3B when associated with R-59. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27013146,ECO:0000269|PubMed:27089320;Dbxref=PMID:27013146,PMID:27089320	
Q93091	UniProtKB	Mutagenesis	59	59	.	.	.	Note=No significant effect on activity towards dinucleotides UpA and CpA. Reduced activity towards polymeric substrates poly(U) and poly(U):poly(A). Significantly reduced activity towards poly(U) and poly(U):poly(A)%3B when associated with A-38. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27013146;Dbxref=PMID:27013146	
Q93091	UniProtKB	Helix	30	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ENP	
Q93091	UniProtKB	Helix	46	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ENP	
Q93091	UniProtKB	Beta strand	62	67	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ENP	
Q93091	UniProtKB	Helix	71	77	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ENP	
Q93091	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ENP	
Q93091	UniProtKB	Beta strand	99	108	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ENP	
Q93091	UniProtKB	Beta strand	115	130	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ENP	
Q93091	UniProtKB	Beta strand	142	150	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ENP