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http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.4.24.-
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.4.-.-
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.-.-.-
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#comment"Belongs to peptidase family M48."xsd:string
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#comment"The enzyme hydrolyzes proteins that terminate with a CaaX motif in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids."xsd:string
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#comment"Differs from EC 3.4.26.1 in its catalytic mechanism and substrate preference."xsd:string
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#comment"Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane-anchor."xsd:string
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2000/01/rdf-schema#comment"The enzyme is one of two enzymes that can catalyze this processing step for mating a-factor in yeast."xsd:string
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2004/02/skos/core#prefLabel"Ste24 endopeptidase"xsd:string
http://purl.uniprot.org/enzyme/3.4.24.84http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11581258
http://purl.uniprot.org/enzyme/3.4.24.84http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9015299
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2004/02/skos/core#altLabel"CAAX prenyl protease 1"xsd:string
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2004/02/skos/core#altLabel"prenyl protein-specific endoprotease 1"xsd:string
http://purl.uniprot.org/enzyme/3.4.24.84http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/3.4.24.84#SIP27DAFCF77B4153A6
http://purl.uniprot.org/enzyme/3.4.24.84http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/3.4.24.-
http://purl.uniprot.org/uniprot/A0A9P7MTU1http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.24.84
http://purl.uniprot.org/uniprot/A0A9P7Q5I9http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.24.84
http://purl.uniprot.org/uniprot/A0A811VC84http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.24.84
http://purl.uniprot.org/uniprot/A0A8J2HET4http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.24.84
http://purl.uniprot.org/uniprot/A0A8J6DZ30http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.24.84
http://purl.uniprot.org/uniprot/A0A8S3SXT8http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.24.84
http://purl.uniprot.org/uniprot/A0A9P6SZ76http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.24.84
http://purl.uniprot.org/uniprot/A0A9P4PCA2http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.24.84