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 [1,2]. Type 1 UBZs are CCHH-type zinc fingers
found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1) [3,4,5], type
2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the
Fanconi anemia (FA) core complex [6,7], type 3 UBZs are CCHH-type zinc fingers
found only in the Y-family translesion polymerase eta [8,9,10], and type 4
UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase
kappa, Werner helicase-interacting protein 1 (WRNIP1), and Rad18 [11,12,13].
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 (see <PDB:4BMJ>) [1,8] or one hisidine and one
cysteine (see <PDB:2MUQ>) [6] on the α-helix [2].
The profiles we developed cover the entire UBZ1-, UBZ2-, UBZ3-, and UBZ4-type
zinc fingers.
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