2.7.7.B17: primase (sequence-specific)
This is an abbreviated version!
For detailed information about primase (sequence-specific), go to the full flat file.
Word Map on EC 2.7.7.B17
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2.7.7.B17
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fork
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translesion
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polymerases
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primase-polymerase
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repriming
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stall
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primases
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restart
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poldip2
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error-free
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replisome
- 2.7.7.B17
-
fork
-
translesion
- polymerases
-
primase-polymerase
-
repriming
-
stall
- primases
-
restart
- poldip2
-
error-free
-
replisome
Reaction
Synonyms
AEP, archaeo-eukaryotic primase, DNA primase/polymerase protein, ORF904, PolpTN2, primase, PrimPol
ECTree
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Engineering
Engineering on EC 2.7.7.B17 - primase (sequence-specific)
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additional information
in-frame deletions of orf 56 and orf904 from pRSP1 generating pRSP10 and pRSP9, respectively. Each of the genes is placed under the control of the putative promoter elements of the cotranscribed genes located at the 5'-end of orf56, in-trans complementation of orf56 and orf904 deletion mutants of pRSP1. Construction of pRN1-based shuttle vectors, comprising orf56 and orf904 as minmal sequence, methylation and transformation, overview
additional information
-
in-frame deletions of orf 56 and orf904 from pRSP1 generating pRSP10 and pRSP9, respectively. Each of the genes is placed under the control of the putative promoter elements of the cotranscribed genes located at the 5'-end of orf56, in-trans complementation of orf56 and orf904 deletion mutants of pRSP1. Construction of pRN1-based shuttle vectors, comprising orf56 and orf904 as minmal sequence, methylation and transformation, overview
additional information
-
in-frame deletions of orf 56 and orf904 from pRSP1 generating pRSP10 and pRSP9, respectively. Each of the genes is placed under the control of the putative promoter elements of the cotranscribed genes located at the 5'-end of orf56, in-trans complementation of orf56 and orf904 deletion mutants of pRSP1. Construction of pRN1-based shuttle vectors, comprising orf56 and orf904 as minmal sequence, methylation and transformation, overview
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additional information
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to better understand the functions of the two domains of PolpTN2, a shorter form of this enzyme was engineered by removing the PriL-like domain. The truncated enzyme PolpTN2DELTA311-923 is less susceptible to proteolysis than the native one and retains the DNA polymerase, primase and nucleotidyl transferase activities of the intact protein, confirming that the catalytic activity resides in the N-terminal PriS-like domain. The truncated protein displays a reverse transcriptase activity, which is not observed with the intact enzyme