UvrC protein functions as
Prokaryotic NER incision step requires UvrC protein possessing two distinct nuclease domains. N-terminal GIY-YIG domain and C-terminal RNase H-like domain coordinate magnesium ions to cleave phosphodiester bonds at defined distances from lesion. After UvrAB creates open complex around damage verifying lesion, UvrC binds and makes 3' incision 4-5 nucleotides downstream and 5' incision 8 nucleotides upstream generating 12-13 nucleotide oligonucleotide containing damage. It therefore acts as dual endonuclease not helicase, ligase, or polymerase. Helicase activity resides in UvrB and UvrD removing
Ref: Lodish et al., Molecular Cell Biology, 9th ed., Chapter 12: UvrC Function as Endonuclease in NER
