Update rloc.md

Issue #184 (closed)

Problem with experimental validation. Says: Penner et al 95 and E. coli system in E. coli. But I think , this paper is more relevant https://onlinelibrary.wiley.com/doi/full/10.1111/j.1365-2958.2008.06387.x Here system come from Geobacillus kaustophilus. But i did not see any antiphage activity. Check what I did to explain and see how you want to deal with it !

content/3.defense-systems/rloc.md

@@ -10,9 +10,24 @@ tableColumns:
     Activator: Unknown
     Effector: Nucleic acid degrading
     PFAM: PF13166
+
+contributors: 
+  - Aude Bernheim
+relevantAbstracts:
+  - doi: 10.1111/j.1365-2958.2008.06387.x
+
 ---
 
 # RloC
+
+## Description
+
+RloC is a distant homologue of the tRNALys anticodon nuclease (ACNase) [PrrC](/defense-systems/prrc). RloC shares the ABC ATPase motifs and catalytic ACNase triad with PrrC, but it possesses a unique zinc-hook/coiled-coil insert. This distinctive feature results in its ATPase domain bearing similarity to Rad50 and other DNA repair proteins.Contrary to PrrC RloC is rarely linked to a type I R-M system. RloC activity was not directly demonstrated on phages but hypothesized through its similar features to PrrC :ref{doi=10.1111/j.1365-2958.2008.06387.x}.
+
+## Molecular Mechanism
+
+RloC was shown to function by tRNA cleavage (wobble nucleotide-excising and Zn++-responsive tRNase) :ref{doi=10.1006/jmbi.1995.0343}. However such activity was not directly shown on a phage. Zinc hook seems to regulate the nuclease function.
+
 ## Example of genomic structure
 
 The RloC system is composed of one protein: RloC.
@@ -67,14 +82,4 @@ end
     style Title3 fill:none,stroke:none,stroke-width:none
     style Title4 fill:none,stroke:none,stroke-width:none
 </mermaid>
-## Relevant abstracts
-
-::relevant-abstracts
----
-items:
-    - doi: 10.1111/j.1365-2958.2008.06387.x
-    - doi: 10.1111/mmi.13074
-
----
-::