The domain within your query sequence starts at position 94 and ends at position 147; the E-value for the zf-CSL domain shown below is 1.6e-16.



PFAM accession number:PF05207
Interpro abstract (IPR007872):

This entry represents the DPH-type metal binding domain consists of a three-stranded beta-sandwich with one sheet comprising two parallel strands: (i) beta1 and (ii) beta6 and one anti-parallel strand: beta5. The second sheet in the beta-sandwich is comprised of strands beta2, beta3, and beta4 running anti-parallel to each other. The two beta-sheets are separated by a short stretch alpha-helix. It can be found in proteins such as DPH3 and DPH4. This domain is also found associated with N-terminal domain of heat shock protein DnaJ IPR001623 domain [ (PUBMED:15952786) (PUBMED:22367199) (PUBMED:25543256) ].

Diphthamide is a unique post-translationally modified histidine residue found only in translation elongation factor 2 (eEF-2). It is conserved from archaea to humans and serves as the target for diphteria toxin and Pseudomonas exotoxin A. These two toxins catalyse the transfer of ADP-ribose to diphtamide on eEF-2, thus inactivating eEF-2, halting cellular protein synthesis, and causing cell death [ (PUBMED:11595641) ]. The biosynthesis of diphtamide is dependent on at least five proteins, DPH1 to -5, and a still unidentified amidating enzyme. DPH3 and DPH4 share a conserved region, which encode a putative zinc finger, the DPH-type or CSL-type (after the conserved motif of the final cysteine) zinc finger and the next two residues) MB domain contains a Cys-X-Cys...Cys-X2-Cys motif which tetrahedrically coordinates both Fe and Zn. The Fe containing DPH-type MBD has an electron transfer activity [ (PUBMED:14527407) (PUBMED:15485916) (PUBMED:15952786) (PUBMED:18021800) (PUBMED:22367199) (PUBMED:25543256) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry zf-CSL