<rdf:RDF
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:ns6="http://www.uniprot.org/uniprot/"
    xmlns:ns9="http://metadb.riken.jp/db/SciNetS_rib166i/"
    xmlns:rdfs="http://www.w3.org/2000/01/rdf-schema#"
    xmlns:ns4="http://metadb.riken.jp/meta/1.0/"
    xmlns:ns5="http://creativecommons.org/ns#"
    xmlns:ns8="http://metadb.riken.jp/db/SciNetS_ria349i/"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#"
    xmlns:ns1="http://metadb.riken.jp/db/SciNetS_ria214i/"
    xmlns:ns3="http://database.riken.jp/sw/item/">
  <ns1:cria214s2i rdf:about="http://metadb.riken.jp/db/SciNetS_ria214i/cria214s2ria214u70097i">
    <ns8:pria349s10i rdf:resource="http://metadb.riken.jp/db/SciNetS_rib166i/crib166u26rib166u615i"/>
    <ns5:attributionURL rdf:resource="http://www.uniprot.org/uniprot/Q9X981"/>
    <ns4:hasFile rdf:resource="http://metadb.riken.jp/dbfiles/SciNetS_ria214i/cria214s2i/cria214s2ria214u70097i/Q9X981.fasta"/>
    <ns1:pria214s6i xml:lang="en">Formamidopyrimidine-DNA glycosylase</ns1:pria214s6i>
    <ns1:pria214s2i xml:lang="en">mutM</ns1:pria214s2i>
    <rdfs:label xml:lang="en">FPG_SERMA</rdfs:label>
    <rdfs:seeAlso rdf:resource="http://database.riken.jp/sw/item/cria214s2ria214u70097i"/>
    <ns1:pria214s8i xml:lang="en">MPELPEVETSRRGIEPYLVGHSIQYAVVRNARLRWPVSEQILTLSDQPVLSVQRRAKYLLIELERGWIIVHLGMSGSLRMLREENEDEAGKHDHVDLVINNGMILRYTDPRRFGAWLWCEDLATSSVLAHLGPEPLSEAFNGDYLYEKSRNKRTLIKPWLMDNKLVVGVGNIYASESLFSAGILPDRPAGSLTKAEAALLAKTIKAVLQRSIEQGGTTLRDFLQSDGKPGYFAQELQVYGRAGEPCRTCGTPIESAKHGQRSTFFCRRCQR</ns1:pria214s8i>
    <ns1:pria214s4i>271</ns1:pria214s4i>
    <ns1:pria214s9i xml:lang="en">DNA-(apurinic or apyrimidinic site) lyase mutM</ns1:pria214s9i>
    <ns1:pria214u1i xml:lang="en">fpg</ns1:pria214u1i>
    <ns1:pria214s3i xml:lang="en">Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity).</ns1:pria214s3i>
  </ns1:cria214s2i>
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