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Links from Protein

Items: 13

1.

AAA family ATPase

This AAA domain is found in a wide variety of presumed DNA repair proteins. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024872.5
Method:
HMM
2.

ATPase domain-containing protein

This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria [1]. [1]. 10064581. Physical interactions among circadian clock proteins KaiA, KaiB and KaiC in cyanobacteria. Iwasaki H, Taniguchi Y, Ishiura M, Kondo T;. EMBO J 1999;18:1137-1145. (from Pfam)

Date:
2024-10-16
Family Accession:
NF018455.5
Method:
HMM
3.

DnaB-like helicase C-terminal domain-containing protein

The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis. (from Pfam)

GO Terms:
Molecular Function:
DNA helicase activity (GO:0003678)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
DNA replication (GO:0006260)
Date:
2024-08-14
Family Accession:
NF015736.5
Method:
HMM
4.

DnaB-like helicase N-terminal domain-containing protein

The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. This N-terminal domain is required both for interaction with other proteins in the primosome and for DnaB helicase activity [1]. [1]. 10404598. Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Fass D, Bogden CE, Berger JM;. Structure Fold Des 1999;7:691-698. (from Pfam)

GO Terms:
Molecular Function:
DNA helicase activity (GO:0003678)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
DNA replication (GO:0006260)
Date:
2024-10-16
Family Accession:
NF012974.5
Method:
HMM
5.
new record, indexing in progress
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.

replicative DNA helicase

replicative DNA helicase unwinds the DNA duplex at the chromosome replication fork

Date:
2020-12-10
Family Accession:
11416751
Method:
Sparcle
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