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Information on EC 2.7.7.102 - DNA primase AEP
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2.7.7.102 DNA primase AEPIUBMB Comments
The enzyme, which is found in eukaryota and archaea, catalyses the synthesis of short RNA or DNA sequences which are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase.
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
+
n
=
ssDNA/pppN(pN)n-1 hybrid
+
(n-1)
+
n
=
ssDNA/pppdN(pdN)n-1 hybrid
+
(n-1)
Synonyms
protein orf904, ccdc111, prislx, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AEP
-
-
-
-
archaeo-eukaryotic primase
PriL
PrimPol
PriS
PriSLX
Sso0079
SSO0557
SSO1048
archaeo-eukaryotic primase
-
-
-
-
PrimPol
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ssDNA + n dNTP = ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate
(2)
-
-
-
ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
(1)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(deoxy)nucleotide 5'-triphosphate:single-stranded DNA (deoxy)nucleotidyltransferase (DNA or DNA-RNA hybrid synthesizing)
The enzyme, which is found in eukaryota and archaea, catalyses the synthesis of short RNA or DNA sequences which are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-CTTCTTCTGTGC-3' + n dNTP
5'-CTTCTTCTGTGC-3'/pppdN(pdN)n-1 + (n-1) diphosphate
i.e. minimal substrate which supports synthesis of the full-length primer. The base 3' to the central GTG motif is critical for primer synthesis and the bases 5' of the GTG determine the length of the primer or run-off product
-
-
?
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3' + n dNTP
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3'/pppdN(pdN)n-1 + n-1 diphosphate
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3' + n NTP
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3'/pppN(dN)n-1 + n-1 diphosphate
5'-TTTTTTTTGTGCACTTT + n dNTP
5'-TTTTTTTTGTGCACTTT/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
?
bacteriophage M13 ssDNA + n NTP
bacteriophage M13 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
M13 ssDNA + n ATP
M13 ssDNA/pppN(pA)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n dATP
M13 ssDNA/pppdN(pdA)n-1 + (n-1) diphosphate
-
-
-
?
M13mp18 ssDNA + n dNTP
M13mp18 ss DNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
?
M13mp18 ssDNA + n dNTP
M13mp18 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
-
?
poly(dC)2500 + n GTP
poly(dC)2500/pppG(pG)n-1 + n-1 diphosphate
-
-
-
?
poly(dT)220 + n ATP
poly(dT)220/pppdA(pdA)n-1 + (n-1) diphosphate
-
-
-
?
poly(dT)400 + n ATP
poly(dT)400/pppA(pA)n-1 + n-1 diphosphate
-
-
-
?
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3' + n dNTP
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3'/pppdN(pdN)n-1 + n-1 diphosphate
-
-
-
?
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3' + n dNTP
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3'/pppdN(pdN)n-1 + n-1 diphosphate
-
-
-
?
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3' + n NTP
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3'/pppN(dN)n-1 + n-1 diphosphate
-
-
-
?
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3' + n NTP
5'-FAM-AAAAAAAAAAATCAGCGGACAAAAAAAAAAAA-3'/pppN(dN)n-1 + n-1 diphosphate
-
-
-
?
ATP + 7 dNTP
A(pdN)7 + 7 diphosphate
enzyme synthesizes short (8 nt-long) primers in the presence of single-stranded M13 DNA. The 12-bases-long substrate with the sequence 5'-CTTCTTCTGTGC-3' represents the minimal substrate which supports synthesis of the full-length primer. The base 3' to the central GTG motif is critical for primer synthesis and that the bases 5' of the GTG determine the length of the primer or run-off product but do not appear to be important for the efficiency of primer synthesis
-
-
?
ATP + 7 dNTP
A(pdN)7 + 7 diphosphate
formation of a ribonucleotide primer when ORF904 is incubated with ribonucleotides and single-stranded M13 DNA. Effcient dNTP incorporation is strongly dependent on the presence of ATP. The non-hydrolysable analogues beta,gamma-imino-ATP and beta,gamma-methylene-ATP are active in stimulation of primer formation. alpha,beta-methylene-ATP does not enhance primer formation. The stimulatory effect is also seen for GTP and UTP but not for ADP or dATP. The majority of the primers have a length of eight nucleotides. Protein ORF904 shows ATPase, DNA polymerase and primase activity
-
-
?
bacteriophage M13 ssDNA + n NTP
bacteriophage M13 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
-
-
?
bacteriophage M13 ssDNA + n NTP
bacteriophage M13 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n dNTP
M13 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n dNTP
M13 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
Q9V292; Q9V291
-
-
-
?
M13 ssDNA + n dNTP
M13 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n dNTP
M13 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n dNTP
M13 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n dNTP
M13 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n dNTP
M13 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n NTP
M13 ssDNA/pppN(pN)n-1 + (n-1) diphosphate
Q9V292; Q9V291
-
-
-
?
M13 ssDNA + n NTP
M13 ssDNA/pppN(pN)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n NTP
M13 ssDNA/pppN(pN)n-1 + (n-1) diphosphate
-
-
-
?
M13 ssDNA + n NTP
M13 ssDNA/pppN(pN)n-1 + (n-1) diphosphate
-
-
-
?
NTP + 7 dNTP
N(pdN)7 + 7 diphosphate
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
-
-
?
NTP + 7 dNTP
N(pdN)7 + 7 diphosphate
formation of a ribonucleotide primer when ORF904 is incubated with ribonucleotides and single-stranded M13 DNA. Effcient dNTP incorporation is strongly dependent on the presence of ATP. The non-hydrolysable analogues beta,gamma-imino-ATP and beta,gamma-methylene-ATP are active in stimulation of primer formation. alpha,beta-methylene-ATP does not enhance primer formation. The stimulatory effect is also seen for GTP and UTP but not for ADP or dATP. The majority of the primers have a length of eight nucleotides. Protein ORF904 shows ATPase, DNA polymerase and primase activity
-
-
?
NTP + 7 dNTP
N(pdN)7 + 7 diphosphate
the enzyme synthesizes a mixed primer consisting of a single ribonucleotide at the 5' end followed by seven deoxynucleotides. Ribonucleotides and deoxynucleotides are strictly required at the respective positions within the primer. The primase can initiate primer synthesis with an ATP regardless of the base 5' of the GTG motif and then proceed to synthesize a primer made up of dNTPs. The primase activity is highly sequence-specific and requires the trinucleotide motif GTG in the template. Primer synthesis starts outside of the recognition motif, immediately 5' to the recognition motif
-
-
?
phage X174 ssDNA + n NTP
phage X174 ssDNA/pppN(pN)n-1 + (n-1) diphosphate
-
-
-
?
phage X174 ssDNA + n NTP
phage X174 ssDNA/pppN(pN)n-1 + (n-1) diphosphate
-
-
-
?
ssDNA + n dNTP
ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate
primases have a fundamental role in DNA replication. They synthesize a primer that is then extended by DNA polymerases
-
-
?
ssDNA + n dNTP
ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate
a small helical bundle prepares primer synthesis by binding two nucleotides that enhance sequence-specific recognition of the DNA template. Archaeoeukaryotic primases require for synthesis a catalytic and an accessory domain. For the pRN1 archaeal primase, this domain is a 115-amino acid helix bundle domain (HBD). Only the HBD binds the DNA template. DNA binding becomes sequence-specific after a major allosteric change in the HBD, triggered by the binding of two nucleotide triphosphates
-
-
?
additional information
?
-
a template oligonucleotide in which sequence GTCC is flanked by thymine residues is also recognized as substrate, with preferential formation of initiating dinucleotides 5'-A-dG-3' or 5'-dA-dG-3'
-
-
?
additional information
?
-
no substrate: poly(A). In the pH range 6.0-7.6, main products are oilgoribonucleotides of 7 and 14 bases. At pH 8.1 and pH 8.5, longer products are also detected
-
-
?
additional information
?
-
enzyme can synthesize DNA, RNA, and mixed DNA-RNA primers in vitro. At physiologically relevant ratios of substrate, the primase is almost exclusively a RNA synthetic enzyme. There is little discrimination in the initiation site for ATP over dATP, but the inclusion of dATP results in a general decrease of primer length
-
-
?
additional information
?
-
enzyme can synthesize DNA, RNA, and mixed DNA-RNA primers in vitro. At physiologically relevant ratios of substrate, the primase is almost exclusively a RNA synthetic enzyme. There is little discrimination in the initiation site for ATP over dATP, but the inclusion of dATP results in a general decrease of primer length
-
-
?
additional information
?
-
multifunctional replication protein with primase, DNA polymerase and helicase activity. The minimal region required for primase activity encompasses amino-acid residues 40370
-
-
?
additional information
?
-
homopolymers as substrates do not yield detectable primase activity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NTP + 7 dNTP
N(pdN)7 + 7 diphosphate
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
-
-
?
ssDNA + n dNTP
ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate
primases have a fundamental role in DNA replication. They synthesize a primer that is then extended by DNA polymerases
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
cluster is buried deeply within the protein core
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
5fold and 2fold activation on substrates poly(dT) and poly(dC), respectively, at 20 mM
Mg2+
Mn2+
Zn2+
Mg2+
or Mn2+, required. Optimum concentration 10 mM
Mn2+
or Mg2+, required. Optimum concentration 11 mM
Zn2+
sequence contains a zinc-finger stem. The zinc ion is tightly bound
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
in the presence of Mg2+, primase activity is inhibited almost 4fold by increasing the KCl concentration from 15 mM to 150 mM. In the presence of Mn2+, KCl stimulates RNA synthesis
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
in the presence of Mg2+, primase activity is inhibited almost 4fold by increasing the KCl concentration from 15 mM to 150 mM. In the presence of Mn2+, KCl stimulates RNA synthesis
Mn2+
significantly enhances the binding of nucleotide to primase,which correlates with higher catalytic efficiency in vitro
ATP
ATP binding enhances sequence-specific DNA recognition for primase anchoring
ATP
ATP-induced structural switch that mediates specific DNA recognition in an archaeoeukaryotic primase
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
5'-CTTCTTCTGTGC-3'
50°C, pH 7.5, synthesis of full-length primer
additional information
additional information
pH 7.5, 50°C, kinetic properties of the primase activity
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
5'-CTTCTTCTGTGC-3'
50°C, pH 7.5, synthesis of full-length primer
additional information
additional information
pH 7.5, 50°C, kinetic properties of the primase activity
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
5'-CTTCTTCTGTGC-3'
50°C, pH 7.5, synthesis of full-length primer
additional information
additional information
pH 7.5, 50°C, kinetic properties of the primase activity
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q9V292 i.e. small subunit PriS, Q9V291 i.e. large subunit PriL
Q9V292; Q9V291
SwissProt
brenda
Saccharolobus solfataricus DSM 16170
Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e. large subunit PriL
UniProt
brenda
P49642 i.e. small subunit Prim1, P09884, i.e. large catalytic subunit
UniProt
brenda
P49642 i.e. small subunit Prim1, P49643 i.e. large subunit Prim2
UniProt
brenda
P49642 i.e. subunit Prim1, P49643 i.e. large subunit Prim2
UniProt
brenda
Q97Z83 i. e. small subunit PriS, Q9UWW1 i.e. large subunit PriL
UniProt
brenda
Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e large subunit PriL
UniProt
brenda
Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e. large subunit PriL
UniProt
brenda
Q9UWW1: DNA primase large subunit PriL, Q97Z83: DNA primase small (catalytic) subunit PriS, Q97ZS7: PriX domain-containing protein
UniProt
brenda
Q97Z83 i. e. small subunit PriS, Q9UWW1 i.e. large subunit PriL
UniProt
brenda
Q9UWW1: DNA primase large subunit PriL, Q97Z83: DNA primase small (catalytic) subunit PriS, Q97ZS7: PriX domain-containing protein
UniProt
brenda
Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e large subunit PriL
UniProt
brenda
Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e. large subunit PriL
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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
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
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
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
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
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
physiological function
replication protein A directly interacts with primase subunit PrimS
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
physiological function
Q9P9H1; Q8U4H7
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
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
physiological function
The minimal region of the protein required for primase activity encompasses amino-acid residues 40-370. The C-terminal part of the minimal region folds into a compact domain with six helices and is stabilized by a disulfide bond. The C-terminal helix of the helix bundle domain is required for primase activity
physiological function
the primase activity synthesizes a mixed primer consisting of a single ribonucleotide at the 5' end followed by seven deoxynucleotides. Ribonucleotides and deoxynucleotides are strictly required at the respective positions within the primer. The primase activity is highly sequence-specific and requires the trinucleotide motif GTG in the template. Primer synthesis starts outside of the recognition motif, immediately 5' to the recognition motif. Non-complementary bases are not incorporated into the primer
physiological function
Q9V292; Q9V291
the small subunit PrimS alone has no RNA synthesis activity but can synthesize up to 3 kb long DNA strands. Addition of the large subunit increases the rate of DNA synthesis but decreases the length of the DNA fragments synthesized and confers RNA synthesis capability. The primase has comparable affinities for ribonucleotides and deoxyribonucleotides. DNA primase also displays DNA polymerase, gapfilling, and strand-displacement activities
physiological function
primases have a fundamental role in DNA replication. They synthesize a primer that is then extended by DNA polymerases
physiological function
the enzyme plays a role in DNA damage tolerance rather than initiation of DNA replication. Because of its ability to carry out translesion synthesis and to bypass template lesions such as thymine dimers, PrimPol is important for re-priming and resolution of stalled replication forks. Physiologically, PrimPol resolves stalled replication forks that occur if DNA lesions such as UV-induced cyclobutane thymine dimers and (6-4) thymine dimers obstruct the replisome function
physiological function
Saccharolobus solfataricus DSM 16170
-
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
-
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PRI1_HUMAN
420
0
49902
Swiss-Prot
other Location (Reliability: 1)
PRI1_MOUSE
417
0
49295
Swiss-Prot
other Location (Reliability: 1)
PRI1_PLAF7
452
0
53489
Swiss-Prot
other Location (Reliability: 1)
PRI1_PLAFK
452
0
53489
Swiss-Prot
other Location (Reliability: 1)
PRI1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
454
0
52009
Swiss-Prot
other Location (Reliability: 1)
PRIL_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
394
0
45949
Swiss-Prot
-
PRI1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
409
0
47690
Swiss-Prot
Secretory Pathway (Reliability: 3)
PRIS_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
350
0
41802
Swiss-Prot
-
PRIPO_HUMAN
560
0
64412
Swiss-Prot
other Location (Reliability: 5)
PRIS_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
347
0
40772
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
?
Q9V292; Q9V291
x * 41000, subunit PrimS, plus x * 46000, subunit PrimL, claculated from sequence
?
x * 35700, subunit PriL, plus x * 37600, subunit PriS
heterotrimer
1 * 35734 (subunit PriS) + 1 * 37598 (subunit PriL) and 1 * 18029 (subunit PriX), calculated from sequence. PriX is essential for primer synthesis and is structurally related to the Fe-S cluster domain of eukaryotic PriL. PriX contains a nucleotide-binding site required for primer synthesis. A primase chimera, where PriX is fused to a truncated version of PriL lacking the Fe-S cluster domain retains wild type levels of primer synthesis
heterotrimer
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1 * 35734 (subunit PriS) + 1 * 37598 (subunit PriL) and 1 * 18029 (subunit PriX), calculated from sequence. PriX is essential for primer synthesis and is structurally related to the Fe-S cluster domain of eukaryotic PriL. PriX contains a nucleotide-binding site required for primer synthesis. A primase chimera, where PriX is fused to a truncated version of PriL lacking the Fe-S cluster domain retains wild type levels of primer synthesis
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