| Product description |
catalytic activity:Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). cofactor:Magnesium. domain:The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity. Belongs to the DNA polymerase type-Y family. Contains 1 umuC domain. subcellular location:Accumulates at replication forks after DNA damage. subunit:Binds REV1L (By similarity). Binds POLH. tissue specificity:Ubiquitous. Highly expressed in testis. |
