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AAA family ATPase
This family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B. (from Pfam)
ATP-binding domain-containing protein
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)
PIF1-like helicase
This family includes homologues of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated [1-4]. This family includes a large number of largely uncharacterised plant proteins. This entry includes a P-loop motif that is involved in nucleotide binding. [1]. 17172855. Human PIF helicase is cell cycle regulated and associates with telomerase. Mateyak MK, Zakian VA;. Cell Cycle. 2006;5:2796-2804. [2]. 16522649. The human Pif1 helicase, a potential Escherichia coli RecD homologue, inhibits telomerase activity. Zhang DH, Zhou B, Huang Y, Xu LX, Zhou JQ;. Nucleic Acids Res. 2006;34:1393-1404. [3]. 30698796. Structural and functional analysis of the nucleotide and DNA binding activities of the human PIF1 helicase. Dehghani-Tafti S, Levdikov V, Antson AA, Bax B, Sanders CM;. Nucleic Acids Res. 2019;47:3208-3222. [4]. 29202194. Insights into the structural and mechanistic basis of multifunctional S. cerevisiae Pif1p helicase. Lu KY, Chen WF, Rety S, Liu NN, Wu WQ, Dai YX, Li D, Ma HY, Dou SX, Xi XG;. Nucleic Acids Res. 2018;46:1486-1500. (from Pfam)
ATP-dependent DNA helicase
ATP-dependent DNA helicase belonging to the DEAD/DEAH box superfamily, utilizes the energy from ATP hydrolysis to unwind double-stranded DNA
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