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| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.-.- |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.21.- |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.-.-.- |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2000/01/rdf-schema#comment | "Belongs to peptidase family S26."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2000/01/rdf-schema#comment | "Cleaves a single bond -Ala-|-Ala- in M13 phage procoat protein, producing free signal peptide and coat protein."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2000/01/rdf-schema#comment | "Eukaryote signal peptidases that may have somewhat different specificity are known from the endoplasmic reticulum membrane and mitochondrial inner membrane."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2000/01/rdf-schema#comment | "Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2004/02/skos/core#prefLabel | "signal peptidase I"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8266095 |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16275749 |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8394311 |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9422718 |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7845215 |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7845216 |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8262975 |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2004/02/skos/core#altLabel | "SPase I"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2004/02/skos/core#altLabel | "bacterial leader peptidase I"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2004/02/skos/core#altLabel | "phage-procoat-leader peptidase"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/3.4.99.36 |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/3.4.21.89#SIPDC8666BB27B5962E |
| http://purl.uniprot.org/enzyme/3.4.21.89 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/3.4.21.- |
| http://purl.uniprot.org/uniprot/A0A9D6XV72 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/3.4.21.89 |
| http://purl.uniprot.org/uniprot/A0A948YCL7 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/3.4.21.89 |