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    <!-- http://purl.obolibrary.org/obo/SO_0000372 -->

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        <rdfs:label>enzymatic_RNA</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/SO_0000386 -->

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        <rdfs:label>RNase_P_RNA</rdfs:label>
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        <oboInOwl:hasExactSynonym>RNase P RNA</oboInOwl:hasExactSynonym>
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        <oboInOwl:hasExactSynonym>INSDC_qualifier:RNase_P_RNA</oboInOwl:hasExactSynonym>
        <oboInOwl:hasBroadSynonym>INSDC_feature:ncRNA</oboInOwl:hasBroadSynonym>
        <ns3:IAO_0000115>The RNA component of Ribonuclease P (RNase P), a ubiquitous endoribonuclease, found in archaea, bacteria and eukarya as well as chloroplasts and mitochondria. Its best characterized activity is the generation of mature 5 prime ends of tRNAs by cleaving the 5 prime leader elements of precursor-tRNAs. Cellular RNase Ps are ribonucleoproteins. RNA from bacterial RNase Ps retains its catalytic activity in the absence of the protein subunit, i.e. it is a ribozyme. Isolated eukaryotic and archaeal RNase P RNA has not been shown to retain its catalytic function, but is still essential for the catalytic activity of the holoenzyme. Although the archaeal and eukaryotic holoenzymes have a much greater protein content than the bacterial ones, the RNA cores from all the three lineages are homologous. Helices corresponding to P1, P2, P3, P4, and P10/11 are common to all cellular RNase P RNAs. Yet, there is considerable sequence variation, particularly among the eukaryotic RNAs.</ns3:IAO_0000115>
        <rdfs:comment>Moved under enzymatic_RNA on 18 Nov 2021. See GitHub Issue #533.</rdfs:comment>
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