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)

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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 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. (from Pfam)

Date:

2024-08-14

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)

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2024-10-16

Helicase activity for this family has been demonstrated [1] and NTPase activity [2]. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis [3]. This family is discussed pages 388-391. [1]. 8269709. Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences. Koonin EV, Dolja VV;. Crit Rev Biochem Mol Biol 1993;28:375-430. [2]. 10217401. RNA helicase activity of Semliki Forest virus replicase protein NSP2. Gomez de Cedron M, Ehsani N, Mikkola ML, Garcia JA, Kaariainen L;. FEBS Lett 1999;448:19-22. [3]. 8057461. ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2. Rikkonen M, Peranen J, Kaariainen L;. J Virol 1994;68:5804-5810. [4]. 10982322. Helicase and capping enzyme active site mutations in brome mosaic virus protein 1a cause defects in template recruitment, negative-strand RNA synthesis, and viral RNA capping. Ahola T, den Boon JA, Ahlquist P;. J Virol 2000;74:8803-8811. (from Pfam)

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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