Protein Family Models

This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold. (from Pfam)

Date:

2024-08-14

Members of this family belong to the PD-(D/E)XK nuclease superfamily [1]. 15972856. Identification of novel restriction endonuclease-like fold families among hypothetical proteins. Kinch LN, Ginalski K, Rychlewski L, Grishin NV;. Nucleic Acids Res. 2005;33:3598-3605. (from Pfam)

Date:

2024-10-16

The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyse ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family. Structure of Swiss:P09980. [1]. 9288744. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G;. Cell 1997;90:635-647. (from Pfam)

Date:

2024-10-16

The RecBCD holoenzyme is a multifunctional nuclease with potent ATP-dependent exodeoxyribonuclease activity. Ejection of RecD, as occurs at chi recombinational hotspots, cripples exonuclease activity in favor of recombinagenic helicase activity. All proteins in this family for which functions are known are DNA-DNA helicases that are used as part of an exonuclease-helicase complex (made up of RecBCD homologs) that function to generate substrates for the initiation of recombination and recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Gene:

recB

Date:

2024-05-30