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Links from Protein

Items: 13

1.

Bacteriophage T7 DNA helicase/primase, N-terminal a+b fold

Date:
2024-07-16
Family Accession:
NF044437.1
Method:
HMM
2.

AAA family ATPase

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

Date:
2024-07-14
Family Accession:
NF024872.4
Method:
HMM
3.

toprim domain-containing protein

This is a family or Toprim-like proteins. (from Pfam)

Date:
2024-07-14
Family Accession:
NF024554.4
Method:
HMM
4.

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:
2024-07-10
Family Accession:
NF015736.4
Method:
HMM
5.

toprim domain-containing protein

This is a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins [1]. Both DnaG motifs IV and V are present in the alignment, the DxD (V) motif may be involved in Mg2+ binding and mutations to the conserved glutamate (IV) completely abolish DnaG type primase activity [1]. DNA primase EC:2.7.7.6 is a nucleotidyltransferase it synthesises the oligoribonucleotide primers required for DNA replication on the lagging strand of the replication fork; it can also prime the leading stand and has been implicated in cell division [2]. This family also includes the atypical archaeal A subunit from type II DNA topoisomerases [4]. Type II DNA topoisomerases catalyse the relaxation of DNA supercoiling by causing transient double strand breaks. [1]. 9722641. Toprim--a conserved catalytic domain in type IA and II. topoisomerases, DnaG-type primases, OLD family nucleases and. RecR proteins.. Aravind L, Leipe DD, Koonin EV;. Nucleic Acids Res 1998;26:4205-4213.. [2]. 9224947. Cloning and analysis of the dnaG gene encoding Pseudomonas. putida DNA primase.. Szafranski P, Smith CL, Cantor CR;. Biochim Biophys Acta 1997;1352:243-248.. [3]. 8294018. The Haemophilus influenzae dnaG sequence and conserved bacterial. primase motifs.. Versalovic J, Lupski JR;. Gene 1993;136:281-286.. [4]. 9121560. An atypical topoisomerase II from Archaea with implications for. meiotic recombination.. Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A,. Forterre P;. Nature 1997;386:414-417. (from Pfam)

Date:
2024-07-09
Family Accession:
NF013878.4
Method:
HMM
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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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.
new record, indexing in progress
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