Literature summary for 2.7.7.102 extracted from

Hu, J.; Guo, L.; Wu, K.; Liu, B.; Lang, S.; Huang, L.
Template-dependent polymerization across discontinuous templates by the heterodimeric primase from the hyperthermophilic archaeon Sulfolobus solfataricus (2012), Nucleic Acids Res., 40, 3470-3483 .

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Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	Q97Z83 and Q9UWW1	Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e. large subunit PriL	-
Saccharolobus solfataricus DSM 16170	Q97Z83 and Q9UWW1	Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e. large subunit PriL	-

Synonyms

Synonyms	Comment	Organism
SSO0557	large subunit	Saccharolobus solfataricus
SSO1048	small subunit	Saccharolobus solfataricus

General Information

General Information	Comment	Organism
physiological function	the enzyme is able to synthesize products far longer than templates in vitro. The long products result from template-dependent polymerization across discontinuous templates, which is initiated through either primer synthesis or terminal transfer, and occurs efficiently on templates containing contiguous dCs. The enzyme is able to promote strand annealing. PriSL catalyzes template-dependent polymerization across discontinuous templates with either dNTPs or rNTPs as the substrates but prefers the latter	Saccharolobus solfataricus

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Release 2023.1 (January 2023)