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    <!-- http://purl.obolibrary.org/obo/GO_0140797 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/GO_0140797">
        <rdfs:label>histone H3R17 arginine deiminase activity</rdfs:label>
        <rdfs:subClassOf rdf:resource="http://purl.obolibrary.org/obo/GO_0141057"/>
        <ns3:IAO_0000233 rdf:datatype="http://www.w3.org/2001/XMLSchema#anyURI">https://github.com/geneontology/go-ontology/issues/23152</ns3:IAO_0000233>
        <ns3:IAO_0000233 rdf:datatype="http://www.w3.org/2001/XMLSchema#anyURI">https://github.com/geneontology/go-ontology/issues/28520</ns3:IAO_0000233>
        <ns3:IAO_0000233 rdf:datatype="http://www.w3.org/2001/XMLSchema#anyURI">https://github.com/geneontology/go-ontology/issues/30578</ns3:IAO_0000233>
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        <oboInOwl:creation_date>2022-04-06T13:12:15Z</oboInOwl:creation_date>
        <ns3:IAO_0000115>Catalysis of the reaction: H2O + histone H3 L-arginyl (position 17)= histone H3 L-citrullyl (position 17) + NH4+, resulting in histone H3 citrullination at position 17.</ns3:IAO_0000115>
        <rdfs:comment>Comment: Note that the residue position corresponds to the canonical human H3 histone (UniProtKB:P84243); this residue is conserved across all eukaryotes. Residue 1 is the first residue following removal of the initiating Methionine (Met). Note that each histone is encoded by multiple genes, and sequences may vary across different genes within an organism. The substrate for histone deiminase may be methyl-arginine, rather than arginine (see PMID:35197210 and PMID:16567635).</rdfs:comment>
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