Literature summary for 2.7.7.102 extracted from

Bocquier, A.; Liu, L.; Cann, I.; Komori, K.; Kohda, D.; Ishino, Y.
Archaeal primase Bridging the gap between RNA and DNA polymerases (2001), Curr. Biol., 11, 452-456 .

Search for more literature for 2.7.7.102

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	little activity in presence of Mg2+	Pyrococcus furiosus
Mn2+	5 mM, required	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	Q9P9H1	small subunit PriS	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
M13mp18 ssDNA + n dNTP	-	Pyrococcus furiosus	M13mp18 ss DNA/pppdN(pdN)n-1 + (n-1) diphosphate	-	?
additional information	enzyme is specific for dNTPs	Pyrococcus furiosus	?	-	?
poly(dT)220 + n ATP	-	Pyrococcus furiosus	poly(dT)220/pppdA(pdA)n-1 + (n-1) diphosphate	-	?

Subunits

Subunits	Comment	Organism
?	x * 40772, calculated from sequecne	Pyrococcus furiosus

Synonyms

Synonyms	Comment	Organism
PriS	-	Pyrococcus furiosus

General Information

General Information	Comment	Organism
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	Pyrococcus furiosus

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Release 2023.1 (January 2023)