EC Number   |
General Information |
Reference |
|---|
   2.7.7.102 | physiological function |
computational study of the protein sequences and structures of the superfamily of archaeo-eukaryotic primases. Comparison of the enzymes from Pyrococcus furiosus, Sulfolobus islandicus, and others |
751714 |
| 2.7.7.102 | physiological function |
does not catalyze by itself the synthesis of short RNA primers but preferentially utilizes deoxynucleotides to synthesize DNA fragments up to several kilobases in length. PriS does not require primers for the synthesis of long DNA strands. PriS interacts with replication protein A |
750365 |
| 2.7.7.102 | physiological function |
isoform PRIMPOL gene silencing or ablation impairs mitochondrial DNA replication. PrimPol is proposed to facilitate replication fork progression by acting as a translesion DNA polymerase or as a specific DNA primase reinitiating downstream of lesions that block synthesis during both mitochondrial and nuclear DNA replication |
751551 |
| 2.7.7.102 | physiological function |
primase/polymerase PolpTN2 is encoded by the pTN2 plasmid and exhibits primase, polymerase and nucleotidyl transferase activities. It specifically incorporates dNTPs, to the exclusion of rNTPs. PolpTN2 can efficiently prime DNA synthesis by PolB DNA polymerase. The N-terminal PriS-like domain of PolpTN2 exhibits all activities of the full-length enzyme but is much less efficient in priming cellular DNA polymerases. The N-terminal domain possesses reverse transcriptase activity |
751720 |
| 2.7.7.102 | physiological function |
primases are specialized DNA-dependent RNA polymerases that synthesize a short oligoribonucleotide complementary to single-stranded template DNA. In the context of cellular DNA replication, primases are indispensable since DNA polymerases are not able to start DNA polymerization de novo |
720578 |
| 2.7.7.102 | physiological function |
primases have a fundamental role in DNA replication. They synthesize a primer that is then extended by DNA polymerases |
760821 |
| 2.7.7.102 | physiological function |
PriSL is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. Products range from dinucleotides to DNA molecules in excess of 7 kb and RNA up to 1 kb in length. PriSL has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides |
-, 751319 |
| 2.7.7.102 | physiological function |
replication protein A directly interacts with primase subunit PrimS |
751009 |
| 2.7.7.102 | physiological function |
the C-terminal domain of the large subunit Prim2 plays a major role in template-primer binding and also defines the elements of the DNA template and the RNA primer that interact with the domain. The interaction with a template-primer involving the terminal 5'-triphosphate of RNA and the 3'-overhang of DNA results in a stable complex between the C-terminal domain of Prim2 and the DNA/RNA duplex |
751078 |
| 2.7.7.102 | physiological function |
the complex between subunits PriS and PriL shows higher DNA binding activity than the catalytic PriS subunit alone. The amount of DNA synthesized by the complex is much more abundant and shorter in length than that by PriS alone. The activity for RNA primer synthesis is not detected with PriS alone but observed using the complex in vitro |
751010 |
