##gff-version 3
Q8WXX5	UniProtKB	Chain	1	260	.	.	.	ID=PRO_0000071063;Note=DnaJ homolog subfamily C member 9	
Q8WXX5	UniProtKB	Domain	15	82	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
Q8WXX5	UniProtKB	Region	171	249	.	.	.	Note=Required for histone binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Region	185	208	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8WXX5	UniProtKB	Compositional bias	188	208	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8WXX5	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:19690332,PMID:20068231,PMID:23186163,PMID:24275569	
Q8WXX5	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q8WXX5	UniProtKB	Mutagenesis	43	45	.	.	.	Note=Increased binding to histones H3 and H4. Less integration of histones H3 and H4 in chromatin. Increased recruitment of histone deposition factors to chromatin. Trapped on chromatin throughout the cell cycle in a manner depending on histone-binding. Released from chromatin trap%3B when associated with Ala-224%3B Ala-227%3B Ala-238 and Ala-242. HPD->QPN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Mutagenesis	195	200	.	.	.	Note=Reduces the co-chaperone complex formation with MCM2%3B histone H3.3 and H4. EEAKEA->AAAKAE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Mutagenesis	216	220	.	.	.	Note=Disrupts the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4. LKAAI->AKAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Mutagenesis	224	242	.	.	.	Note=Abolishes the interaction with MCM2%2C TONSL and histones H3.3 and H4. Disrupts the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4. QKDRQKEMDNFLAQMEAKY->AKDAQKEMDNFLAQAEAKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Mutagenesis	224	227	.	.	.	Note=Partial loss of histone dimer H3-H4 interaction. Reduces the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4. QKDR->AKDA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Mutagenesis	234	235	.	.	.	Note=Reduces the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4. FL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Mutagenesis	238	242	.	.	.	Note=Partial loss of histone dimer H3-H4 interaction. Reduces the co-chaperone complex formation with MCM2%3B histone H3.3 and H4. MEAKY->AEAKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Mutagenesis	243	243	.	.	.	Note=Does not affect interaction with histones. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33857403;Dbxref=PMID:33857403	
Q8WXX5	UniProtKB	Helix	175	207	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7CJ0	
Q8WXX5	UniProtKB	Helix	213	242	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7CIZ	
Q8WXX5	UniProtKB	Helix	244	247	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7CJ0