LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry corresponds to the N-terminal domain found in CD-NTase associated protein 4 (Cap4) from Enterobacter cloacae. This is the effector domain which has dsDNA nuclease activity, sharing structural homology with type II restriction endonucleases and it has the putative active-site conserved residues required for divalent metal coordination. It has a mixed β-sheet arrangement with α-helical bundles on the sides. This domain is inactive as a monomer; after Cap4 signal recognition through its C-terminal SAVED domain, it oligomerizes to closely locate two nuclease effector domains. This domain does not participate in ligand specificity and it has a promiscuous DNA cleavage response [ ]. This domain can also be found in uncharacterised proteins from bacteria and archaea. CD-NTase-associated protein 4 (Cap4) is a member of a diverse family of bacterial receptors that specifically recognises nucleotide second messenger signals synthesised by cGAS/DncV-like nucleotidyltransferases (CD-NTases), that functions in CBASS immunity. It plays an essential role protecting bacteria from phage infections degrading dsDNA through its DNA endonuclease domain which is activated after ligand-induced oligomerization [ ]. This domain is found in LmuA and AbpA proteins, which confer resistance to phage infections. |
| Short Name | Cap4-like_endonuclease_dom |
