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Links from Protein

Items: 5

1.

CRISPR-associated nuclease/helicase Cas3, C-terminal

This entry represents the C-terminal domain of CRISPR-associated nuclease/helicase Cas3 subtype I-F/YPEST from Pseudomonas aeruginosa (Cas3), a DNA-degradation enzyme that forms part of the CRISPR-Cas bacterial immune system. Cas3 contains a Cas2 domain, an HD nuclease domain (Pfam:PF18019), RecA1, RecA2, a long linker region, and a C-terminal domain (this entry). This domain contains two alpha-helices and two six-stranded beta-blades [6]. Paper describing PDB structure 1gm5. [1]. 11595187. Structural analysis of DNA replication fork reversal by RecG. Singleton MR, Scaife S, Wigley DB;. Cell. 2001;107:79-89. Paper describing PDB structure 1t5i. [2]. 15296731. Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export. Zhao R, Shen J, Green MR, MacMorris M, Blumenthal T;. Structure. 2004;12:1373-1381. Paper describing PDB structure 1wp9. [3]. 15642269. Crystal structure and functional implications of Pyrococcus furiosus hef helicase domain involved in branched DNA processing. Nishino T, Komori K, Tsuchiya D, Ishino Y, Morikawa K;. Structure. 2005;13:143-153. Paper describing PDB structure 1yks. [4]. 16051820. Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing. Wu J, Bera AK, Kuhn RJ, Smith JL;. J Virol. 2005;79:10268-10277. Paper describing PDB structure 2bhr. [5]. 16051821. Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A. Xu T, Sampath A, Chao A, Wen D, Nanao M, Chene P, Vasudevan SG, Lescar J;. J Virol. 2005;79:10278-10288. [6]. 27455460. Structural basis o. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-10-16
Family Accession:
NF046773.1
Method:
HMM
2.

DEAD/H associated

This domain is found in ATP-dependent helicases as well as a number of hypothetical proteins together with the helicase conserved C-terminal domain (Pfam:PF00270) and the Pfam:PF00271 domain. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Molecular Function:
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides (GO:0016818)
Date:
2024-08-14
Family Accession:
NF020083.5
Method:
HMM
3.

DEAD/DEAH box helicase family protein

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
ATP binding (GO:0005524)
Molecular Function:
hydrolase activity (GO:0016787)
Date:
2024-08-14
Family Accession:
NF016724.5
Method:
HMM
4.

DEAD/DEAH box helicase

Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression. [1]. 10322435. Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. de la Cruz J, Kressler D, Linder P;. Trends Biochem Sci 1999;24:192-198. [2]. 9862990. The DEAD box RNA helicase family in Arabidopsis thaliana. Aubourg S, Kreis M, Lecharny A;. Nucleic Acids Res 1999;27:628-636. (from Pfam)

GO Terms:
Molecular Function:
nucleic acid binding (GO:0003676)
Molecular Function:
ATP binding (GO:0005524)
Date:
2024-10-16
Family Accession:
NF012492.5
Method:
HMM
5.

helicase-related protein

The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase. (from Pfam)

Date:
2024-08-14
Family Accession:
NF012493.5
Method:
HMM
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