Protein Family Models

This helix-turn-helix domain is often found in transferases and is likely to be DNA-binding. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

Tc3 is transposase with a specific DNA-binding domain which contains three alpha-helices, two of which form a helix-turn-helix motif which makes four base-specific contacts with the major groove. The N-terminus makes contacts with the minor groove. There is a base specific recognition between Tc3 and the transposon DNA. The DNA binding domain forms a dimer in which each monomer binds a separate transposon end. This implicates that the dimer has a role in synapsis and is necessary for the simultaneous cleavage of both transposon termini [1]. [1]. 9312061. Crystal structure of the specific DNA-binding domain of Tc3 transposase of C.elegans in complex with transposon DNA. van Pouderoyen G, Ketting RF, Perrakis A, Plasterk RH, Sixma TK;. EMBO J 1997;16:6044-6054. (from Pfam)

Date:

2024-10-16

Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain Pfam:PF02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain Pfam:PF00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyses the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site [1]. [1]. 7801124. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases [see comments]. Dyda F, Hickman AB, Jenkins TM, Engelman A, Craigie R, Davies DR;. Science 1994;266:1981-1986. (from Pfam)

Date:

2024-10-16

transposase binds to the end of a transposon and catalyzes the movement of the transposon to another part of the genome by a cut and paste mechanism or a replicative transposition mechanism

Date:

2024-05-15

Date:

2021-03-03

Date:

2019-09-10