##gff-version 3
P60848	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60849	
P60848	UniProtKB	Chain	2	97	.	.	.	ID=PRO_0000151711;Note=DNA/RNA-binding protein Alba 1	
P60848	UniProtKB	Binding site	16	16	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:24307170,ECO:0007744|PDB:3WBM;Dbxref=PMID:24307170	
P60848	UniProtKB	Binding site	17	17	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:24307170,ECO:0007744|PDB:3WBM;Dbxref=PMID:24307170	
P60848	UniProtKB	Binding site	22	22	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:24307170,ECO:0007744|PDB:3WBM;Dbxref=PMID:24307170	
P60848	UniProtKB	Binding site	42	42	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:24307170,ECO:0007744|PDB:3WBM;Dbxref=PMID:24307170	
P60848	UniProtKB	Binding site	44	44	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:24307170,ECO:0007744|PDB:3WBM;Dbxref=PMID:24307170	
P60848	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60849	
P60848	UniProtKB	Modified residue	16	16	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60849	
P60848	UniProtKB	Modified residue	16	16	.	.	.	Note=N6-methylated lysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:F0NHH1	
P60848	UniProtKB	Mutagenesis	8	8	.	.	.	Note=No effect on cis-trans isomerization of dimer. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14523014;Dbxref=PMID:14523014	
P60848	UniProtKB	Mutagenesis	16	16	.	.	.	Note=Decreases binding affinity for RNA. Significantly decreases binding affinity for RNA%3B when associated with A-22 or A-44. Abolishes binding of RNA with no significant effects on oligomerization%3B when associated with A-22 and A-44. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	17	17	.	.	.	Note=No significant effects on binding affinity for RNA. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	20	20	.	.	.	Note=Reduces ability to form higher order oligomers with no significant effects on binding affinity for RNA%3B when associated with E-24 and E-27. No significant effects on binding affinity for RNA%3B when associated with E-24%3B E-27 and E-60. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	22	22	.	.	.	Note=Decreases binding affinity for RNA. Decreases binding affinity for RNA%3B when associated with A-44. Significantly decreases binding affinity for RNA%3B when associated with A-16. Abolishes binding of RNA with no significant effects on oligomerization%3B when associated with A-16 and A-44. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Reduces ability to form higher order oligomers with no significant effects on binding affinity for RNA%3B when associated with E-20 and E-27. No significant effects on binding affinity for RNA%3B when associated with E-20%3B E-27 and E-60. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Reduces ability to form higher order oligomers with no significant effects on binding affinity for RNA%3B when associated with E-20 and E-24. No significant effects on binding affinity for RNA%3B when associated with E-20%3B E-24 and E-60. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Moderately decreases binding affinity for RNA. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Decreases binding affinity for RNA. Decreases binding affinity for RNA%3B when associated with A-16 or A-22. Abolishes binding of RNA with no significant effects on oligomerization%3B when associated with A-16 and A-22. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	60	60	.	.	.	Note=No significant effects on binding affinity for RNA and oligomerization. Reduces ability to form higher order oligomers with no significant effects on binding affinity for RNA%3B when associated with E-20%3B E-24 and E-27. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24307170;Dbxref=PMID:24307170	
P60848	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Loss of cis-trans isomerization of dimer. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14523014;Dbxref=PMID:14523014	
P60848	UniProtKB	Beta strand	9	13	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WBM	
P60848	UniProtKB	Helix	19	31	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WBM	
P60848	UniProtKB	Beta strand	36	42	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WBM	
P60848	UniProtKB	Helix	45	59	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WBM	
P60848	UniProtKB	Turn	62	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WBM	
P60848	UniProtKB	Beta strand	65	76	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WBM	
P60848	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Y9X	
P60848	UniProtKB	Beta strand	86	96	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WBM