Dna2 and its plant homologue JHS1 are DNA replication factors with single-stranded DNA-dependent ATPase, ATP-dependent nuclease, (5'-flap endonuclease) and helicase activities. It is required for Okazaki fragment processing and is involved in DNA repair pathways [, ]. The helicase activity is weak and its function remains unclear [, , , ].
This domain contains the ATP-binding region of DNA2. DNA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Proteins containing this domain also include Nam7 and other helicases. Dna2 is a DNA replication factor with single-stranded DNA-dependent ATPase, ATP-dependent nuclease, (5'-flap endonuclease) and helicase activities [, ]. Nam7 (also known as Upf1) is an ATP-dependent RNA helicase involved in the nonsense-mediated mRNA decay (NMD) pathway []. This domain is known as AAA_11 in Pfam.
This domain contains a P-loop motif that is characteristic of the AAA superfamily. Proteins containing this domain are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA [, , ].Proteins containing this domain include helicases, such as Dna2 an Nam7. Dna2 is a DNA replication factor with single-stranded DNA-dependent ATPase, ATP-dependent nuclease, (5'-flap endonuclease) and helicase activities [, ]. Nam7 (also known as Upf1) is an ATP-dependent RNA helicase involved in the nonsense-mediated mRNA decay (NMD) pathway []. This domain can also be found in some virus polyproteins. This domain is also known as HelicC.
Retinoblastoma-binding protein 8 (RBBP8), also known as CtIP, is an endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in processing meiotic and mitotic double-strand breaks (DSBs) by ensuring both resection and intrachromosomal association of the broken ends [, ]. CtIP interacts with the BRCA1 tumour suppressor []. BRCA1 and CtIP are required to recruit Dna2 at DSBs in homologous recombination, ensuring robust DSB resection []. CtIP it is not a tumuor suppressor itself, instead, it can promote tumourigenesis. This is probably related to its role in the formation of chromosomal rearrangements through the microhomology-mediated end joining (MMEJ) pathway, a relatively error-prone pathway of DSB repair [].
This entry represents a group of helicases, including DNA2 and Nam7. Proteins in this family contain a conserved domain with s a P-loop motif that is characteristic of the AAA superfamily. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA [, , ].Dna2 is a DNA replication factor with single-stranded DNA-dependent ATPase, ATP-dependent nuclease, (5'-flap endonuclease) and helicase activities [, ]. Nam7 (also known as Upf1) is an ATP-dependent RNA helicase involved in the nonsense-mediated mRNA decay (NMD) pathway [].
