Protein Family Models

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)

Date:

2024-08-14

This domain is found in at the C terminus of group 3 Schlafen proteins from mammals, and represents the DNA/RNA helicase domain [2]. Schlafen proteins are involved in the control of cell proliferation, induction of immune responses, and in the regulation of viral replication [1,2,3]. These proteins inhibit DNA replication and promote cell death in response to DNA damage. They play a role in genome surveillance to kill cells with defective replication [3]. This domain is also found in various uncharacterised prokaryotic proteins fused to a DNA helicase, GIY-YIG or PD-(D/E)XK catalytic domain or HsdR-N(terminal) domain, which are similar to AAA DNA helicase, Type III restriction enzyme ATPase, RecD and RuvB helicase [3]. [1]. 23570387. The schlafen family of proteins and their regulation by interferons. Mavrommatis E, Fish EN, Platanias LC;. J Interferon Cytokine Res. 2013;33:206-210. [2]. 18355440. Subcellular localization of the Schlafen protein family. Neumann B, Zhao L, Murphy K, Gonda TJ;. Biochem Biophys Res Commun. 2008;370:62-66. [3]. 31504772. A protein architecture guided screen for modification dependent restriction endonucleases. Lutz T, Flodman K, Copelas A, Czapinska H, Mabuchi M, Fomenkov A, He X, Bochtler M, Xu SY;. Nucleic Acids Res. 2019;47:9761-9776. (from Pfam)

Date:

2024-10-16

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

Date:

2024-08-14

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)

Date:

2024-10-16

This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase activity, and a Walker B motif. In tRNA(Met) cytidine acetyltransferase (TmcA) it may function as an RNA helicase motor (driven by ATP hydrolysis) which delivers the wobble base to the active centre of the GCN5-related N-acetyltransferase (GNAT) domain [1]. It is found in the bacterial exodeoxyribonuclease V alpha chain (RecD), which has 5'-3' helicase activity. It is structurally similar to the motor domain 1A in other SF1 helicases [2]. [1]. 19322199. RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon. Chimnaronk S, Suzuki T, Manita T, Ikeuchi Y, Yao M, Suzuki T, Tanaka I;. EMBO J. 2009;28:1362-1373. [2]. 15538360. Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks. Singleton MR, Dillingham MS, Gaudier M, Kowalczykowski SC, Wigley DB;. Nature. 2004;432:187-193. (from Pfam)

Date:

2024-10-16

ATP-dependent DNA helicase belonging to the DEAD/DEAH box superfamily, utilizes the energy from ATP hydrolysis to unwind double-stranded DNA

Date:

2025-01-08