Protein Family Models for Protein (Select 529016911) - Protein Family Models

Select item 4240241.

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)

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Molecular Function:: hydrolase activity (GO:0016787)

Date:: 2024-08-14

Family Accession:: NF024754.5
Method:: HMM

Select item 4221812.

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)

Date:: 2024-08-14

Family Accession:: NF024928.5
Method:: HMM

Select item 4221643.

AAA family ATPase

Date:: 2024-08-14

Family Accession:: NF024642.5
Method:: HMM

Select item 4121224.

Viral (Superfamily 1) RNA helicase

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)

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Date:: 2024-10-16

Family Accession:: NF013601.5
Method:: HMM

Select item 4112215.

UvrD-helicase domain-containing protein

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)

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Date:: 2024-10-16

Family Accession:: NF012789.5
Method:: HMM

Select item 4000096.