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Links from Protein

Items: 15

1.

SWI2/SNF2 ATPase

A SWi2/SNF2 ATPase found in polyvalent proteins [1]. [1]. 28559295. Polyvalent Proteins, a Pervasive Theme in the Intergenomic. Biological Conflicts of Bacteriophages and Conjugative Elements.. Iyer LM, Burroughs AM, Anand S, de Souza RF, Aravind L;. J Bacteriol. 2017; [Epub ahead of print] (from Pfam)

Date:
2024-04-03
Family Accession:
NF037510.4
Method:
HMM
2.

DNA/RNA helicase domain-containing protein

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:
2024-04-03
Family Accession:
NF021375.4
Method:
HMM
3.

type I restriction-modification enzyme R subunit C-terminal domain-containing protein

The restriction enzyme EcoEI recognises 5'-GAGN(7)ATGC-3' and is composed of the three proteins R, M, and S. The domain described here is found at the C-terminus of the R protein (HsdR) which is required for both nuclease and ATPase activity [1,2]. [1]. 8412658. Conservation of motifs within the unusually variable polypeptide. sequences of type I restriction and modification enzymes.. Murray NE, Daniel AS, Cowan GM, Sharp PM;. Mol Microbiol 1993;9:133-143.. [2]. 10449767. Regulation of endonuclease activity by proteolysis prevents. breakage of unmodified bacterial chromosomes by type I. restriction enzymes.. Makovets S, Doronina VA, Murray NE;. Proc Natl Acad Sci U S A 1999;96:9757-9762. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
catalytic activity (GO:0003824)
Biological Process:
DNA modification (GO:0006304)
Date:
2024-04-03
Family Accession:
NF020052.4
Method:
HMM
4.

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:
2023-12-12
Family Accession:
NF016724.4
Method:
HMM
5.

restriction endonuclease subunit S

This domain is also known as the target recognition domain (TRD). Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity subunit (this family), two modification (M) subunits and two restriction (R) subunits [2]. [1]. 8336674. Biology of DNA restriction.. Bickle TA, Kruger DH;. Microbiol Rev 1993;57:434-450.. [2]. 9837717. The DNA recognition subunit of the type IB. restriction-modification enzyme EcoAI tolerates circular. permutions of its polypeptide chain.. Janscak P, Bickle TA;. J Mol Biol 1998;284:937-948. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Biological Process:
DNA modification (GO:0006304)
Date:
2024-04-03
Family Accession:
NF013579.4
Method:
HMM
6.

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:
2024-04-03
Family Accession:
NF012492.4
Method:
HMM
7.

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:
2023-12-12
Family Accession:
NF012493.4
Method:
HMM
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.

type I restriction-modification system endonuclease

Gene:
hsdR
Date:
2020-10-26
Family Accession:
NF008521.0
Method:
HMM
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