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Conserved domains on  [gi|1720392864|ref|XP_030106281|]
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DNA endonuclease RBBP8 isoform X2 [Mus musculus]

Protein Classification

SAE2 C-terminal domain-containing protein( domain architecture ID 10554153)

SAE2 C-terminal domain-containing protein that may be involved in DNA repair; the C-terminus of DNA endonuclease SAE2 is important to its function in DNA-end resection during double-strand break repair via the homologous recombination pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAE2 pfam08573
DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing ...
 519-582 1.58e-13

DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing meiotic and mitotic double-strand breaks in DNA. It has been shown to negatively regulate DNA damage checkpoint signalling. SAE2 is homologous to the CtIP proteins in mammals and an homologous protein in plants. Crucial sequence motifs that are highly conserved are the CxxC and the RHR motifs in this C-terminal part of the protein. In budding yeast, genetic evidence suggests that the SAE2 protein is essential for the processing of hairpin DNA intermediates and meiotic double-strand breaks by Mre11/Rad50 complexes. SAE2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. Hairpin structures are not processed at the tip by SAE2 but rather at single-stranded DNA regions adjacent to the hairpin. The catalytic activities of SAE2 are important for its biological functions. Although proteins containing this domain were described as endonucleases, it is now known that they actually function as endonuclease activators. This domain contains highly conserved residues at its 15-residue extreme that are indispensable for MRN (Mre11-Rad50-Nbs1) complex activation, through the stimulation of Mre11 endonuclease activity.


:

Pssm-ID: 462525  Cd Length: 108  Bit Score: 67.00  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392864 519 EVVRKKEERRKLLGHTCKEC--EIYYA------------------------------DLPAEERE--------KKLASC- 557
Cdd:pfam08573   4 EVVRGKDERKCLPGCTCPCCcgDYFRAmaplpgrlrqkeedqklledylgdeayklgTMSAEEREellveaktRKLANKy 83

                          90       100
                  ....*....|....*....|....*
gi 1720392864 558 SRHRFRYIPPNTPENFWEVGFPSTQ 582
Cdd:pfam08573  84 GRHRHHFERAPTPPGFWRTDFPSTQ 108
 
Name Accession Description Interval E-value
SAE2 pfam08573
DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing ...
 519-582 1.58e-13

DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing meiotic and mitotic double-strand breaks in DNA. It has been shown to negatively regulate DNA damage checkpoint signalling. SAE2 is homologous to the CtIP proteins in mammals and an homologous protein in plants. Crucial sequence motifs that are highly conserved are the CxxC and the RHR motifs in this C-terminal part of the protein. In budding yeast, genetic evidence suggests that the SAE2 protein is essential for the processing of hairpin DNA intermediates and meiotic double-strand breaks by Mre11/Rad50 complexes. SAE2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. Hairpin structures are not processed at the tip by SAE2 but rather at single-stranded DNA regions adjacent to the hairpin. The catalytic activities of SAE2 are important for its biological functions. Although proteins containing this domain were described as endonucleases, it is now known that they actually function as endonuclease activators. This domain contains highly conserved residues at its 15-residue extreme that are indispensable for MRN (Mre11-Rad50-Nbs1) complex activation, through the stimulation of Mre11 endonuclease activity.


Pssm-ID: 462525  Cd Length: 108  Bit Score: 67.00  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392864 519 EVVRKKEERRKLLGHTCKEC--EIYYA------------------------------DLPAEERE--------KKLASC- 557
Cdd:pfam08573   4 EVVRGKDERKCLPGCTCPCCcgDYFRAmaplpgrlrqkeedqklledylgdeayklgTMSAEEREellveaktRKLANKy 83

                          90       100
                  ....*....|....*....|....*
gi 1720392864 558 SRHRFRYIPPNTPENFWEVGFPSTQ 582
Cdd:pfam08573  84 GRHRHHFERAPTPPGFWRTDFPSTQ 108
 
Name Accession Description Interval E-value
SAE2 pfam08573
DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing ...
 519-582 1.58e-13

DNA endonuclease activator SAE2/CtIP C-terminus; SAE2 is a protein involved in repairing meiotic and mitotic double-strand breaks in DNA. It has been shown to negatively regulate DNA damage checkpoint signalling. SAE2 is homologous to the CtIP proteins in mammals and an homologous protein in plants. Crucial sequence motifs that are highly conserved are the CxxC and the RHR motifs in this C-terminal part of the protein. In budding yeast, genetic evidence suggests that the SAE2 protein is essential for the processing of hairpin DNA intermediates and meiotic double-strand breaks by Mre11/Rad50 complexes. SAE2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. Hairpin structures are not processed at the tip by SAE2 but rather at single-stranded DNA regions adjacent to the hairpin. The catalytic activities of SAE2 are important for its biological functions. Although proteins containing this domain were described as endonucleases, it is now known that they actually function as endonuclease activators. This domain contains highly conserved residues at its 15-residue extreme that are indispensable for MRN (Mre11-Rad50-Nbs1) complex activation, through the stimulation of Mre11 endonuclease activity.


Pssm-ID: 462525  Cd Length: 108  Bit Score: 67.00  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392864 519 EVVRKKEERRKLLGHTCKEC--EIYYA------------------------------DLPAEERE--------KKLASC- 557
Cdd:pfam08573   4 EVVRGKDERKCLPGCTCPCCcgDYFRAmaplpgrlrqkeedqklledylgdeayklgTMSAEEREellveaktRKLANKy 83

                          90       100
                  ....*....|....*....|....*
gi 1720392864 558 SRHRFRYIPPNTPENFWEVGFPSTQ 582
Cdd:pfam08573  84 GRHRHHFERAPTPPGFWRTDFPSTQ 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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