AC PRU01239; DC Domain; TR PROSITE; PS51891; CENPV_GFA; 1; level=0 XX Names: CENP-V/GFA domain Function: At the C-terminal end, CENP-V possesses an evolutionally conserved domain that comprises an array of seven cysteines and shows high structural similarity to glutathione-dependent formaldehyde-activating enzyme (Gfa), an enzyme responsible for formaldehyde detoxification in prokaryotes. CENP-V could be an enzyme that scavenges the formaldehyde produced in histone demethylation reactions. XX case and CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit else case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; end case XX case or GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS51891 FT DOMAIN from..to FT /note="CENP-V/GFA" FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="structural" FT Group: 1; Condition: C FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="structural" FT Group: 1; Condition: C FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: C FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: C FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: C FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="structural" FT Group: 1; Condition: C FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="structural" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 110-155; Related: None; Repeats: 1; Topology: Undefined; Example: Q7Z7K6; Scope: Eukaryota Bacteria; Pseudomonadota Comments: None; XX # Revision 1.5 2023/01/26 //