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DESCRIBE <http://purl.uniprot.org/SHA-384/EC309893A84BB8B33139FB6E20D130CE25C7DDDAA9019167842D3FBD5722A1118C8CF73CEAAC707366A6C1EEE274F828>
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http://purl.uniprot.org/SHA-384/EC309893A84BB8B33139FB6E20D130CE25C7DDDAA9019167842D3FBD5722A1118C8CF73CEAAC707366A6C1EEE274F828
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/EC309893A84BB8B33139FB6E20D130CE25C7DDDAA9019167842D3FBD5722A1118C8CF73CEAAC707366A6C1EEE274F828
http://www.w3.org/2000/01/rdf-schema#comment
"Characterization of full-length enzymes with defective hybrid binding domain indicates that this domain dramatically enhances both the specific activity and processivity of RNase H1."
xsd:string
http://purl.uniprot.org/uniprot/#_594BA8B01069E0F4913C155946BD4C6D76F9B76263436ED88A1B89A27B1C84CB3EE3B117497A32E4C811447994C9B846
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/EC309893A84BB8B33139FB6E20D130CE25C7DDDAA9019167842D3FBD5722A1118C8CF73CEAAC707366A6C1EEE274F828
http://purl.uniprot.org/uniprot/O60930
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/EC309893A84BB8B33139FB6E20D130CE25C7DDDAA9019167842D3FBD5722A1118C8CF73CEAAC707366A6C1EEE274F828
http://purl.uniprot.org/uniprot/#_O60930-mappedCitation-18337749
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/EC309893A84BB8B33139FB6E20D130CE25C7DDDAA9019167842D3FBD5722A1118C8CF73CEAAC707366A6C1EEE274F828