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DESCRIBE <http://purl.uniprot.org/SHA-384/8AB7F714132C6F52D41F7B5CFDF05E89B4FB3165E0227C779DBCE87B69E8288AB75661B863A6C34E1BAB9C89FCFE5BB7>
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http://purl.uniprot.org/SHA-384/8AB7F714132C6F52D41F7B5CFDF05E89B4FB3165E0227C779DBCE87B69E8288AB75661B863A6C34E1BAB9C89FCFE5BB7
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/8AB7F714132C6F52D41F7B5CFDF05E89B4FB3165E0227C779DBCE87B69E8288AB75661B863A6C34E1BAB9C89FCFE5BB7
http://www.w3.org/2000/01/rdf-schema#comment
"Results show that Glycine 38 is crucial for the full catalytic activity of the human enzyme on duplex RNA as its substitution with aspartate or alanine results in a drastic reduction in the dsRNA cleavage activity of HPR."
xsd:string
http://purl.uniprot.org/uniprot/#_D441730F418166AC092EDC3A96C51B5B7C9E2035E6261A9DC87557BF0D769A6B22EB4FC085624A905363824DE90152FE
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/8AB7F714132C6F52D41F7B5CFDF05E89B4FB3165E0227C779DBCE87B69E8288AB75661B863A6C34E1BAB9C89FCFE5BB7
http://purl.uniprot.org/uniprot/W0UV93
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/8AB7F714132C6F52D41F7B5CFDF05E89B4FB3165E0227C779DBCE87B69E8288AB75661B863A6C34E1BAB9C89FCFE5BB7
http://purl.uniprot.org/uniprot/#_W0UV93-mappedCitation-12237131
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/8AB7F714132C6F52D41F7B5CFDF05E89B4FB3165E0227C779DBCE87B69E8288AB75661B863A6C34E1BAB9C89FCFE5BB7