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Links from Protein

Items: 17

1.

3'-5' exonuclease

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
2.

AAA family ATPase

Date:
2024-08-14
Family Accession:
NF024642.5
Method:
HMM
3.

PD-(D/E)XK nuclease family protein

Members of this family belong to the PD-(D/E)XK nuclease superfamily [1]. 15972856. Identification of novel restriction endonuclease-like fold families among hypothetical proteins. Kinch LN, Ginalski K, Rychlewski L, Grishin NV;. Nucleic Acids Res. 2005;33:3598-3605. (from Pfam)

Date:
2024-10-16
Family Accession:
NF024117.5
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.

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
6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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16.

helicase-exonuclease AddAB subunit AddA

helicase-exonuclease AddAB subunit AddA, with AddB, forms a heterodimer that acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease; recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination

Date:
2020-06-18
Family Accession:
11494990
Method:
Sparcle
17.

helicase-exonuclease AddAB subunit AddA

AddAB, also called RexAB, substitutes for RecBCD in several bacterial lineages. These DNA recombination proteins act before synapse and are particularly important for DNA repair of double-stranded breaks by homologous recombination. The term AddAB is used broadly, with AddA homologous between the Firmicutes (as modeled here) and the alphaproteobacteria, while the partner AddB proteins show no strong homology across the two groups of species.

Gene:
addA
GO Terms:
Biological Process:
double-strand break repair via homologous recombination (GO:0000724)
Molecular Function:
DNA helicase activity (GO:0003678)
Biological Process:
double-strand break repair (GO:0006302)
Molecular Function:
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides (GO:0016818)
Date:
2024-05-29
Family Accession:
TIGR02785.1
Method:
HMM
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