<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/cria214s2ria214u273098i">
    <ns1:pria214u3i xml:lang="en">DR_1948</ns1:pria214u3i>
    <ns4:hasFile rdf:resource="http://metadb.riken.jp/dbfiles/SciNetS_ria214i/cria214s2i/cria214s2ria214u273098i/Q9RT21.fasta"/>
    <ns8:pria349s10i rdf:resource="http://metadb.riken.jp/db/SciNetS_rib166i/crib166u26rib166u1299i"/>
    <rdfs:seeAlso rdf:resource="http://database.riken.jp/sw/item/cria214s2ria214u273098i"/>
    <ns1:pria214s8i xml:lang="en">MAELISKEGNKVEFKVSVPAAEVNRAYDQVWAGLARDVRVPGFRPGKAPRKVIENRVGKGYVESQVRDRLLETHYSQGLRELGLNLVDATVDPQDVQSGQAFEFTVKGETYPEVKLGDWQGLKVSAQAPEITDEVLEQTLSDLRERNASFEKAERPIEAADQVTIQELGEGDSEEGGSYPIYLDMAEEHVRNALLGKSAGDVVDITVPAHQHGDHEHAEHTVRVKVVEVSSKKLQDLNDEFATSLNYESMDKLRTDLREELERRAQQEGDNLRREELVGHLVEGMTVEIPQALIDRRREGMMSEIQDDLRRQGVQWKEYEAFMQEQGKLDEFEADLTKNAETRVRRDLALEQLATDLNAQVNEAEFNQTLMNLAQANGMNVQQLVQQLGQDGVQSYYISLLRERGLQRALAQLSGEGQSTEAASPKATGTEAAGTEQSEPAQTETAQNDAGQTETAQSEGEQQSE</ns1:pria214s8i>
    <rdfs:label xml:lang="en">TIG_DEIRA</rdfs:label>
    <ns1:pria214s2i xml:lang="en">tig</ns1:pria214s2i>
    <ns1:pria214s4i>465</ns1:pria214s4i>
    <ns5:attributionURL rdf:resource="http://www.uniprot.org/uniprot/Q9RT21"/>
    <ns1:pria214s6i xml:lang="en">Trigger factor</ns1:pria214s6i>
    <ns1:pria214s3i xml:lang="en">Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation (By similarity). Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24, PubMed:16271892), exposing a hydrophobic crevice that is probably important for its chaperone activity (PubMed:16091460 and PubMed:16271892).</ns1:pria214s3i>
  </ns1:cria214s2i>
</rdf:RDF>