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
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lagging-strand
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template-primer
- fen1
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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
3.6.4.B8 clamp-loader complexAdvanced search results
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results (Engineering
Engineering on EC 3.6.4.B8 - clamp-loader complex
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D125A
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC5 at the ATP-binding site
D159A
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC4 at the ATP-binding site. The mutation of the ORC4 Walker-B motif has little effect on ATPase activity
D620A
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC1 at the ATP-binding site. Disrupting the ORC1 Walker-B motif effectively abolishes ATPase activity
D620A/D159A
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunits ORC1 and ORC4 at the ATP-binding site. The double mutation of the Walker-B motif of both ORC1 and ORC4 abolishes activity
R261Q
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC3 at the ATP-binding site
R69V
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC4 at the ATP-binding site
R720Q
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC1 at the ATP-binding site. The mutation abolishes ATPase activity of the motor module, and this mutation exists in a single heterozygous individual with a wild-type allele
R98Q
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC3 at the ATP-binding site
Y174C
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC4 at the ATP-binding site. The ORC4-Y174C mutation in the ORC4 tether, which disrupts its hydrogen bond to an ORC1 Walker-B side chain (ORC1-E621), renders the motor module hyperactive for ATPase activity. The ORC4 MGS mutant Y174C has reduced activity (at about 50% of wild-type) in the context of ORC1-5. The hyperactivity of this mutant observed in the context of the motor module alone suggests that binding of ORC2-ORC3 modulates the ATPase activity of the ORC motor
R84A/R90A/T120A/K149A
additional information
R84A/R90A/T120A/K149A
site-directed mutagenesis, quadruple mutant of RFCS small subunit
R84A/R90A/T120A/K149A
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site-directed mutagenesis, quadruple mutant of RFCS small subunit
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additional information
O28219; O29072
mutation of the proposed arginine finger in the small subunits results in a complex that can still bind ATP but has impaired clamp-loading activity
additional information
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mutation of the proposed arginine finger in the small subunits results in a complex that can still bind ATP but has impaired clamp-loading activity
additional information
P35251; P35250; P40938; P35249; P40937
deletion of its N-terminal DNA binding domain does not affect the activity of the wild-type RFC complex, leading to generate a truncated RFC1DELTA555 construct, that is easier to purify in the RFC pentamer
additional information
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deletion of its N-terminal DNA binding domain does not affect the activity of the wild-type RFC complex, leading to generate a truncated RFC1DELTA555 construct, that is easier to purify in the RFC pentamer
additional information
Q8TSX5; Q8TUC8; Q8TPU4
site-directed mutagenesis in the Walker A and SRC motifs is performed to examine the contribution of each subunit to the function of the Methanosarcina acetivorans clamp loader. Mutations in the large subunit MacRFCL and the small subunit MacRFCS2 do not impair clamp loading activity. Any mutant clamp loader harboring a mutation in MacRFCS1 is devoid of the clamp loading property
additional information
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site-directed mutagenesis in the Walker A and SRC motifs is performed to examine the contribution of each subunit to the function of the Methanosarcina acetivorans clamp loader. Mutations in the large subunit MacRFCL and the small subunit MacRFCS2 do not impair clamp loading activity. Any mutant clamp loader harboring a mutation in MacRFCS1 is devoid of the clamp loading property
additional information
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site-directed mutagenesis in the Walker A and SRC motifs is performed to examine the contribution of each subunit to the function of the Methanosarcina acetivorans clamp loader. Mutations in the large subunit MacRFCL and the small subunit MacRFCS2 do not impair clamp loading activity. Any mutant clamp loader harboring a mutation in MacRFCS1 is devoid of the clamp loading property
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