<?xml version="1.0"?>
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    <!-- http://purl.obolibrary.org/obo/TFClass_human.obo#2 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/TFClass_human.obo#2">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Zinc-coordinating DNA-binding domains</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/TFClass_human.obo#2.5 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/TFClass_human.obo#2.5">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">DM-type intertwined zinc finger factors</rdfs:label>
        <rdfs:subClassOf rdf:resource="http://purl.obolibrary.org/obo/TFClass_human.obo#2"/>
        <ns2:xref rdf:datatype="http://www.w3.org/2001/XMLSchema#string">CLASSLINK:http\://www.edgar-wingender.de/class 2.5.html</ns2:xref>
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        <ns3:def rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Class description: The known transcription factors exhibiting a DNA-binding domain of intertwined zinc fingers belong to the DM group of proteins, named after Drosophila Doublesex and C. elegans Meb-3. Intertwined are one zinc finger of C2HC and one of HCC2 type, each binding one zinc ion. Together, they follow the consensus pattern C--C--h--------H---C----c-c-c, where upper and lower case letter refer to either zinc finger, and dashes symbolize any other amino acid. The most C-terminal cysteine is part of a short alpha-helical structure, which extends into a carboxy-terminal tail that stably folds into an alpha helix upon binding to DNA. This recognition helix binds in the minor groove of the DNA. In contrast to other minor-groove binders, it does not induce a sharp bending of the DNA. (PMID 16382145)</ns3:def>
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