Function and Biology Details
Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
SsDNA + n NTP = ssDNA/pppN(pN)(n-1) hybrid + (n-1) diphosphate
GTP + a 5'-diphospho-[mRNA] = diphosphate + a 5'-(5'-triphosphoguanosine)-[mRNA]
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- DNA-directed DNA polymerase, family B
- DNA primase large subunit, eukaryotic/archaeal
- DNA primase, large subunit, eukaryotic
- DNA primase, small subunit, eukaryotic/archaeal
- DNA polymerase alpha, subunit B
- NSP1 globular domain superfamily, betacoronavirus
- NSP1, globular domain, betacoronavirus
- NSP1, globular domain, alpha/betacoronavirus
14 more domains
Structure analysis Details
Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140800 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):