| Primary Identifier | IPR031490 | Type | Domain |
| Short Name | UBZ2_FAAP20 |
| description | The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating β-β-α fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families [, ]. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1) [, , ], type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex [, ], type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta [, , ], and type 4 UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase-interacting protein 1 (WRNIP1), and Rad18 [, , ]. The UBZ domain consists of two short antiparallel β-strands followed by one α-helix. The α-helix packs against the β-strands with a zinc ion sandwiched between the α-helix and the β-strands. The zinc ion is coordinated by two cysteines located on the fingertip formed by the β-strands and two histidines [, ]or one histidine and one cysteine []on the α-helix [].This domain is the type 2 UBZ found in Fanconi anemia-associated protein of 20kDa (FAAP20) [, , , ]. |
