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http://purl.uniprot.org/SHA-384/F078868A8EBF48636FCC00BED6E1D2B39D22D2A3CCE73DB831646D3329DBC799D9B24158686F9F14BCB4CE79FF06502Chttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/F078868A8EBF48636FCC00BED6E1D2B39D22D2A3CCE73DB831646D3329DBC799D9B24158686F9F14BCB4CE79FF06502Chttp://www.w3.org/2000/01/rdf-schema#comment"The finding that a threading mechanism like that used by hFEN1 is also used by hEXO1 unifies the mode of operation for members of the 5'-nuclease superfamily that act on discontinuous substrates. As with hFEN1 intrinsic disorder of the arch region of the protein may explain how flaps can be threaded without a need for a coupled energy source."xsd:string
http://purl.uniprot.org/uniprot/#_252023F5831CE92719277D2F1F558A1883C42935DDAF514F262E770908474A5E8E4EC46595EC4EE296F09C2F719EE53Bhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/F078868A8EBF48636FCC00BED6E1D2B39D22D2A3CCE73DB831646D3329DBC799D9B24158686F9F14BCB4CE79FF06502C
http://purl.uniprot.org/uniprot/Q9UQ84http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/F078868A8EBF48636FCC00BED6E1D2B39D22D2A3CCE73DB831646D3329DBC799D9B24158686F9F14BCB4CE79FF06502C
http://purl.uniprot.org/uniprot/#_Q9UQ84-mappedCitation-28682061http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/F078868A8EBF48636FCC00BED6E1D2B39D22D2A3CCE73DB831646D3329DBC799D9B24158686F9F14BCB4CE79FF06502C