Early post-infection, the reverse transcriptase converts the viral RNA genome into double-stranded viral DNA. The RNase H domain of the reverse transcriptase performs two functions. It degrades the RNA template and specifically removes the RNA primer from the RNA/DNA hybrid. Following nuclear import, the integrase catalyzes the insertion of the linear, double-stranded viral DNA into the host cell chromosome. Endogenous Pol proteins may have kept, lost or modified their original function during evolution (By similarity). a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Endonucleolytic cleavage to 5'-phosphomonoester. This protein is synthesized as Gag-Pro and Gag-Pro-Pol polyprotein precursors. These polyproteins are thought, by similarity with type-B retroviruses, to be generated by -1 frameshifts occurring at the Gag-Pro and Pro-Pol genes boundaries. The LPQG and YXDD motifs are catalytically important and conserved among many retroviruses. Exact N-terminus of this protein has not been formally described. The 102 C-terminal amino acids differ from HERV-K(HML-2) Pol prototype due to a frameshift in position 867. Belongs to the beta type-B retroviral polymerase family. HERV class-II K(HML-2) pol subfamily.