3.6.4.B8: clamp-loader complex
This is an abbreviated version!
For detailed information about clamp-loader complex, go to the full flat file.
Word Map on EC 3.6.4.B8
-
3.6.4.B8
-
chromatin
-
slide
-
sliding
-
fork
-
helicase
-
polymerases
-
orc1
-
single-stranded
-
mitosis
-
rad9
-
pre-replication
-
pre-rcs
-
schizosaccharomyces
-
pombe
-
s-phase
-
license
-
minichromosome
-
prereplicative
-
rpa
-
encircle
-
cdt1
-
ring-shaped
-
replisome
-
heterochromatin
-
firing
-
hydroxyurea
-
unwind
-
telomeres
-
primer-template
-
okazaki
-
translesion
-
primase
-
mating-type
-
pcna-binding
-
winged-helix
-
rad3-related
-
atr-mediated
-
mcm3
-
pcna-dependent
-
geminin
-
atr-dependent
-
replicases
-
chromatin-bound
-
dnax
-
atr-chk1
-
lagging-strand
-
template-primer
-
fen1
-
topbp1
-
claspin
- 3.6.4.B8
- chromatin
-
slide
-
sliding
-
fork
- helicase
- polymerases
- orc1
-
single-stranded
-
mitosis
- rad9
-
pre-replication
-
pre-rcs
- schizosaccharomyces
- pombe
-
s-phase
-
license
-
minichromosome
-
prereplicative
- rpa
-
encircle
- cdt1
-
ring-shaped
- replisome
- heterochromatin
-
firing
- hydroxyurea
-
unwind
-
telomeres
-
primer-template
-
okazaki
-
translesion
- primase
-
mating-type
-
pcna-binding
-
winged-helix
- rad3-related
-
atr-mediated
- mcm3
-
pcna-dependent
- geminin
-
atr-dependent
-
replicases
-
chromatin-bound
- dnax
-
atr-chk1
-
lagging-strand
-
template-primer
- fen1
-
topbp1
- claspin
Reaction
Synonyms
9-1-1 loader, ATP-dependent clamp loader complex, ATPase, cell cycle checkpoint protein, clamp loader, clamp loader complex, CLC, CTF18-RFC, ELG1-RFC, gamma clamp loader, gamma clamp loader complex, MacRFC complex, ORC, origin recognition complex, PCNA unloader, primary PCNA loader, RAD17, replication factor C, RF-C/activator 1 homolog, RFC, RFC clamp loader complex, RFC complex, RFC1, secondary PCNA loader, SsoRFC-complex
ECTree
Advanced search results
Substrates Products
Substrates Products on EC 3.6.4.B8 - clamp-loader complex
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REACTION DIAGRAM
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
-
-
-
?
ATP + H2O
ADP + phosphate
Q8TSX5; Q8TUC8; Q8TPU4
the clamp loader complex reconstituted from the three subunits MacRFCS1, MacRFCS2, and MacRFCL stimulates DNA synthesis by a cognate DNA polymerase in the presence of its sliding clamp. Mac-RFCS1 is critical to the clamp loading activity of the Methanosarcina acetivorans clamp loader
-
-
?
ATP + H2O
ADP + phosphate
Q8TSX5; Q8TUC8; Q8TPU4
the clamp loader complex reconstituted from the three subunits MacRFCS1, MacRFCS2, and MacRFCL stimulates DNA synthesis by a cognate DNA polymerase in the presence of its sliding clamp. Mac-RFCS1 is critical to the clamp loading activity of the Methanosarcina acetivorans clamp loader
-
-
?
ATP + H2O
ADP + phosphate
ATPase activity is activated by primed DNA templates, such as poly(dA)-oligo(dT). The SsoRFC-complex binds poly(dA)-oligo(dT), but not the unprimed homopolymer
-
-
?
ATP + H2O
ADP + phosphate
-
model of the clamp loading process: ATP-bound replication factor C forms a complex with replication factor C. This results in in-plane opening of a single interface of Proliferating-Cell-Nuclear-Antigen (PCNA) and allowing entry of DNA
-
-
?
ATP + H2O
ADP + phosphate
ATPase activity is activated by primed DNA templates, such as poly(dA)-oligo(dT). The SsoRFC-complex binds poly(dA)-oligo(dT), but not the unprimed homopolymer
-
-
?
?
-
the three gamma or tau subunits are the active ATPases, and each binds one molecule of ATP
-
-
-
additional information
?
-
-
the three gamma or tau subunits are the active ATPases, and each binds one molecule of ATP
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
loading of human DNA sliding clamp PCNA (proliferating cell nuclear antigen) by the clamp loader complex RFC
-
-
-
additional information
?
-
-
loading of human DNA sliding clamp PCNA (proliferating cell nuclear antigen) by the clamp loader complex RFC
-
-
-
additional information
?
-
DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
-
DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
-
DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
DNA loading substrate of Rad17 is 9-1-1
-
-
-
additional information
?
-
schematic model of substrate proliferating-cell-nuclear-antigen (PCNA) loading by RFC: the homotrimeric ring of PCNA has a head-to-tail configuration of subunits. Substrate PCNA is a hub protein That connects DNA replication and peripheral chromosomal reactions. The ring has asymmetric side surfaces known as the N face and C face. PCNA protomer has two repetitive domains, 1 and 2 that are bridged by IDCL, which is located on the C face. In the presence of ATP, RFC attaches to the C face, opens one interface between the subunits, and binds to the 3' primer-template junction. Upon ATP hydrolysis, the structure of RFC changes to dissociate from PCNA and DNA, leaving a closed PCNA ring that is loaded on the duplex DNA with the C face directed to the 3' end of the primer. Poldelta then binds to the 3' primer end using the C face of PCNA as its docking surface and synthesizes lagging-strand DNA processively. After completion of the DNA elongation, FEN1 and DNA ligase 1 are tethered sequentially to ligate the lagging strands. The dynamic status of PCNA on dsDNA is determined by structural analyses, single-molecule imaging, and molecular-dynamics simulations. PCNA moves along dsDNA in a diffusive fashion in both directions. Most of the time, PCNA tracks rotationally the helical pitch of dsDNA by tilting with the DNA axis. This rotational motion of the tilted PCNA on DNA facilitates formation of a large number of electrostatic interactions between DNA backbone and the positively charged residues lining the PCNA inner surface, and it may provide a structure that captures a proper PCNA-binding partner
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
schematic model of substrate proliferating-cell-nuclear-antigen (PCNA) loading by RFC: the homotrimeric ring of PCNA has a head-to-tail configuration of subunits. Substrate PCNA is a hub protein That connects DNA replication and peripheral chromosomal reactions. The ring has asymmetric side surfaces known as the N face and C face. PCNA protomer has two repetitive domains, 1 and 2 that are bridged by IDCL, which is located on the C face. In the presence of ATP, RFC attaches to the C face, opens one interface between the subunits, and binds to the 3' primer-template junction. Upon ATP hydrolysis, the structure of RFC changes to dissociate from PCNA and DNA, leaving a closed PCNA ring that is loaded on the duplex DNA with the C face directed to the 3' end of the primer. Poldelta then binds to the 3' primer end using the C face of PCNA as its docking surface and synthesizes lagging-strand DNA processively. After completion of the DNA elongation, FEN1 and DNA ligase 1 are tethered sequentially to ligate the lagging strands. The dynamic status of PCNA on dsDNA is determined by structural analyses, single-molecule imaging, and molecular-dynamics simulations. PCNA moves along dsDNA in a diffusive fashion in both directions. Most of the time, PCNA tracks rotationally the helical pitch of dsDNA by tilting with the DNA axis. This rotational motion of the tilted PCNA on DNA facilitates formation of a large number of electrostatic interactions between DNA backbone and the positively charged residues lining the PCNA inner surface, and it may provide a structure that captures a proper PCNA-binding partner
-
-
-
additional information
?
-
-
schematic model of substrate proliferating-cell-nuclear-antigen (PCNA) loading by RFC: the homotrimeric ring of PCNA has a head-to-tail configuration of subunits. Substrate PCNA is a hub protein That connects DNA replication and peripheral chromosomal reactions. The ring has asymmetric side surfaces known as the N face and C face. PCNA protomer has two repetitive domains, 1 and 2 that are bridged by IDCL, which is located on the C face. In the presence of ATP, RFC attaches to the C face, opens one interface between the subunits, and binds to the 3' primer-template junction. Upon ATP hydrolysis, the structure of RFC changes to dissociate from PCNA and DNA, leaving a closed PCNA ring that is loaded on the duplex DNA with the C face directed to the 3' end of the primer. Poldelta then binds to the 3' primer end using the C face of PCNA as its docking surface and synthesizes lagging-strand DNA processively. After completion of the DNA elongation, FEN1 and DNA ligase 1 are tethered sequentially to ligate the lagging strands. The dynamic status of PCNA on dsDNA is determined by structural analyses, single-molecule imaging, and molecular-dynamics simulations. PCNA moves along dsDNA in a diffusive fashion in both directions. Most of the time, PCNA tracks rotationally the helical pitch of dsDNA by tilting with the DNA axis. This rotational motion of the tilted PCNA on DNA facilitates formation of a large number of electrostatic interactions between DNA backbone and the positively charged residues lining the PCNA inner surface, and it may provide a structure that captures a proper PCNA-binding partner
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
solution dynamics of the substrate human clamp protein in proliferating cell nuclear antigen (PCNA). Computational modeling (molecular dynamic simulations and MM/GBSA binding energy decomposition analyses) is used to identify conserved networks of hydrophobic residues critical for clamp stability and ring-opening dynamics, subunit interface dynamics, substrate structure, detailed overview
-
-
-
additional information
?
-
-
solution dynamics of the substrate human clamp protein in proliferating cell nuclear antigen (PCNA). Computational modeling (molecular dynamic simulations and MM/GBSA binding energy decomposition analyses) is used to identify conserved networks of hydrophobic residues critical for clamp stability and ring-opening dynamics, subunit interface dynamics, substrate structure, detailed overview
-
-
-
additional information
?
-
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
the ORC motor module displays robust ATPase activity, which is independent of DNA binding, nucleotide-binding site analysis, overview. In the context of the motor module, only the ORC1/4 interface is a functional ATPase. The RecA-fold and lid domains of HsORC1 form a classic ATPase site
-
-
-
additional information
?
-
-
the ORC motor module displays robust ATPase activity, which is independent of DNA binding, nucleotide-binding site analysis, overview. In the context of the motor module, only the ORC1/4 interface is a functional ATPase. The RecA-fold and lid domains of HsORC1 form a classic ATPase site
-
-
-
additional information
?
-
the enzyme stimulates the synthetic activity of Sulfolobus solfataricus B1-type DNA polymerase in reactions containing primed M13mp18 DNA, ATP, and either of the two poliferating cell nuclear antigen-like processivity factors of Sulfolobus solfataricus (039p and 048p)
-
-
?
additional information
?
-
-
the enzyme stimulates the synthetic activity of Sulfolobus solfataricus B1-type DNA polymerase in reactions containing primed M13mp18 DNA, ATP, and either of the two poliferating cell nuclear antigen-like processivity factors of Sulfolobus solfataricus (039p and 048p)
-
-
?
additional information
?
-
the enzyme stimulates the synthetic activity of Sulfolobus solfataricus B1-type DNA polymerase in reactions containing primed M13mp18 DNA, ATP, and either of the two poliferating cell nuclear antigen-like processivity factors of Sulfolobus solfataricus (039p and 048p)
-
-
?