Protein Family Models

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

Date:

2023-12-12

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)

Date:

2023-12-12

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)

Date:

2024-04-03

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

Date:

2022-08-31

This HMM describes the helicase DnaB, a homohexameric protein required for DNA replication. The homohexamer can form a ring around a single strand of DNA near a replication fork. An intein of > 400 residues is found at a conserved location in DnaB of Synechocystis PCC6803, Rhodothermus marinus (both experimentally confirmed), and Mycobacterium tuberculosis. The intein removes itself by a self-splicing reaction. The seed alignment contains inteins so that the model built from the seed alignment will model a low cost at common intein insertion sites.

Gene:

dnaB

Date:

2021-05-12