##gff-version 3
P47120	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03101,ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
P47120	UniProtKB	Chain	2	325	.	.	.	ID=PRO_0000203100;Note=Deoxyhypusine hydroxylase	
P47120	UniProtKB	Repeat	77	103	.	.	.	Note=HEAT-like PBS-type 1	
P47120	UniProtKB	Repeat	110	136	.	.	.	Note=HEAT-like PBS-type 2	
P47120	UniProtKB	Repeat	202	231	.	.	.	Note=HEAT-like PBS-type 3	
P47120	UniProtKB	Repeat	235	261	.	.	.	Note=HEAT-like PBS-type 4	
P47120	UniProtKB	Repeat	268	294	.	.	.	Note=HEAT-like PBS-type 5	
P47120	UniProtKB	Binding site	79	79	.	.	.	.	
P47120	UniProtKB	Binding site	80	80	.	.	.	.	
P47120	UniProtKB	Binding site	112	112	.	.	.	.	
P47120	UniProtKB	Binding site	113	113	.	.	.	.	
P47120	UniProtKB	Binding site	237	237	.	.	.	.	
P47120	UniProtKB	Binding site	238	238	.	.	.	.	
P47120	UniProtKB	Binding site	270	270	.	.	.	.	
P47120	UniProtKB	Binding site	271	271	.	.	.	.	
P47120	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03101,ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
P47120	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198	
P47120	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198	
P47120	UniProtKB	Modified residue	281	281	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
P47120	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	80	80	.	.	.	Note=Abolishes enzyme activity and impairs iron-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	113	113	.	.	.	Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Abolishes substrate-binding and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Reduces enzyme activity by 97%25. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	237	237	.	.	.	Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	238	238	.	.	.	Note=Abolishes substrate-binding%2C enzyme activity%2C and impairs iron-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	271	271	.	.	.	Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
P47120	UniProtKB	Mutagenesis	274	274	.	.	.	Note=Abolishes substrate-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996