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
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3.6.4.B8
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chromatin
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slide
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sliding
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fork
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helicase
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polymerases
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orc1
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single-stranded
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mitosis
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rad9
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pre-replication
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pre-rcs
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schizosaccharomyces
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pombe
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s-phase
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license
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minichromosome
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prereplicative
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rpa
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encircle
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cdt1
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ring-shaped
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replisome
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heterochromatin
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firing
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hydroxyurea
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unwind
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telomeres
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primer-template
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okazaki
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translesion
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primase
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mating-type
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pcna-binding
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winged-helix
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rad3-related
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atr-mediated
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mcm3
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pcna-dependent
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geminin
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atr-dependent
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replicases
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chromatin-bound
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dnax
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atr-chk1
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lagging-strand
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template-primer
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fen1
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topbp1
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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
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Activating Compound
Activating Compound on EC 3.6.4.B8 - clamp-loader complex
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DNA
ATPase activity is activated by primed DNA templates, such as poly(dA)-oligo(dT). ATPase activity of the SsoRFC-complex is substantially stimulated by the primed homopolymer, whereas no effect is detected in the presence of poly(dA)400. The maximal activation (about tenfold) of the ATP-hydrolyzing activity is measured in the presence of poly(dA)4000-oligo(dT)45 at 140 nM
dsDNA
Q8TSX5; Q8TUC8; Q8TPU4
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 12fold by dsDNA
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proliferating cell nuclear antigen
Q8TSX5; Q8TUC8; Q8TPU4
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 3fold by Methanosarcina acetivorans proliferating cell nuclear antigen
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singly primed single-stranded DNA
Q8TSX5; Q8TUC8; Q8TPU4
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 58fold by singly primed single-stranded DNA
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ssDNA
Q8TSX5; Q8TUC8; Q8TPU4
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 33fold by ssDNA
P35251; P35250; P40938; P35249; P40937
clamp substrate PCNA proteins are assayed for stimulation of the ATPase activity of the RFC clamp loader complex in the presence of DNA
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additional information
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clamp substrate PCNA proteins are assayed for stimulation of the ATPase activity of the RFC clamp loader complex in the presence of DNA
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