##gff-version 3
P22087	UniProtKB	Chain	1	321	.	.	.	ID=PRO_0000148507;Note=RRNA 2'-O-methyltransferase fibrillarin	
P22087	UniProtKB	Region	1	87	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P22087	UniProtKB	Region	274	306	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22087	UniProtKB	Binding site	172	173	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y9U3	
P22087	UniProtKB	Binding site	191	192	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.31	
P22087	UniProtKB	Binding site	216	217	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.31	
P22087	UniProtKB	Binding site	236	239	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.31	
P22087	UniProtKB	Modified residue	8	8	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22509	
P22087	UniProtKB	Modified residue	15	15	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22509	
P22087	UniProtKB	Modified residue	21	21	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22509	
P22087	UniProtKB	Modified residue	24	24	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22509	
P22087	UniProtKB	Modified residue	27	27	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22509	
P22087	UniProtKB	Modified residue	102	102	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
P22087	UniProtKB	Modified residue	121	121	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569	
P22087	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
P22087	UniProtKB	Modified residue	205	205	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Modified residue	206	206	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Cross-link	84	84	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
P22087	UniProtKB	Cross-link	102	102	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
P22087	UniProtKB	Cross-link	109	109	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
P22087	UniProtKB	Cross-link	131	131	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
P22087	UniProtKB	Cross-link	143	143	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
P22087	UniProtKB	Cross-link	158	158	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
P22087	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Mimics acetylation%3B impaired ability to methylate histone H2A%3B when associated with Q-121 and 205-Q-Q-206. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Decreased acetylation%3B restores ability to methylate histone H2A%3B when associated with R-121 and 205-R-R-206. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Mimics acetylation%3B impaired ability to methylate histone H2A%3B when associated with Q-102 and 205-Q-Q-206. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Decreased acetylation%3B restores ability to methylate histone H2A%3B when associated with R-102 and 205-R-R-206. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Mutagenesis	205	206	.	.	.	Note=Mimics acetylation%3B impaired ability to methylate histone H2A%3B when associated with Q-102 and Q-121. KK->QQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Mutagenesis	205	206	.	.	.	Note=Decreased acetylation%3B restores ability to methylate histone H2A%3B when associated with R-102 and R-121. KK->RR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30540930;Dbxref=PMID:30540930	
P22087	UniProtKB	Sequence conflict	132	132	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P22087	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	106	109	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	117	119	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	130	136	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Turn	139	141	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Helix	143	149	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	162	166	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Helix	172	181	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	185	190	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Helix	194	206	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	210	213	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Helix	220	222	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Helix	224	226	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	230	235	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Helix	242	253	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	254	265	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Helix	266	269	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	271	273	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IPX	
P22087	UniProtKB	Helix	275	288	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	291	298	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Turn	300	302	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7	
P22087	UniProtKB	Beta strand	303	313	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SE7