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Conserved domains on  [gi|2327734129|ref|WP_265093045|]
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MULTISPECIES: hypothetical protein [Enterobacter]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NucC-like super family cl41770
cyclic oligonucleotide-based anti-phage signaling system-associated NucC nuclease and similar ...
14-41 2.20e-03

cyclic oligonucleotide-based anti-phage signaling system-associated NucC nuclease and similar proteins; Cyclic oligonucleotide-based anti-phage signaling system (CBASS)-associated NucC nuclease kills phage-infected cells through genome destruction. It is allosterically activated by a cyclic triadenylate (cA3) second messenger that is synthesized by CBASS upon infection. NucC is related to restriction endonucleases but it adopts a homotrimeric structure. Binding of cA3 causes two NucC homotrimers to assemble into a homohexamer, which brings together a pair of active sites to activate DNA cleavage. NucC has also been integrated into type III CRISPR/Cas systems as an accessory nuclease.


The actual alignment was detected with superfamily member cd21173:

Pssm-ID: 477763  Cd Length: 231  Bit Score: 33.11  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|....*....
gi 2327734129  14 MLARFKESG-FIHHSGDKGENREEFLMDF 41
Cdd:cd21173     2 LLAEYERIRkLIHHGLTKGRYREEILREF 30
 
Name Accession Description Interval E-value
NucC-like cd21173
cyclic oligonucleotide-based anti-phage signaling system-associated NucC nuclease and similar ...
14-41 2.20e-03

cyclic oligonucleotide-based anti-phage signaling system-associated NucC nuclease and similar proteins; Cyclic oligonucleotide-based anti-phage signaling system (CBASS)-associated NucC nuclease kills phage-infected cells through genome destruction. It is allosterically activated by a cyclic triadenylate (cA3) second messenger that is synthesized by CBASS upon infection. NucC is related to restriction endonucleases but it adopts a homotrimeric structure. Binding of cA3 causes two NucC homotrimers to assemble into a homohexamer, which brings together a pair of active sites to activate DNA cleavage. NucC has also been integrated into type III CRISPR/Cas systems as an accessory nuclease.


Pssm-ID: 411057  Cd Length: 231  Bit Score: 33.11  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|....*....
gi 2327734129  14 MLARFKESG-FIHHSGDKGENREEFLMDF 41
Cdd:cd21173     2 LLAEYERIRkLIHHGLTKGRYREEILREF 30
 
Name Accession Description Interval E-value
NucC-like cd21173
cyclic oligonucleotide-based anti-phage signaling system-associated NucC nuclease and similar ...
14-41 2.20e-03

cyclic oligonucleotide-based anti-phage signaling system-associated NucC nuclease and similar proteins; Cyclic oligonucleotide-based anti-phage signaling system (CBASS)-associated NucC nuclease kills phage-infected cells through genome destruction. It is allosterically activated by a cyclic triadenylate (cA3) second messenger that is synthesized by CBASS upon infection. NucC is related to restriction endonucleases but it adopts a homotrimeric structure. Binding of cA3 causes two NucC homotrimers to assemble into a homohexamer, which brings together a pair of active sites to activate DNA cleavage. NucC has also been integrated into type III CRISPR/Cas systems as an accessory nuclease.


Pssm-ID: 411057  Cd Length: 231  Bit Score: 33.11  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|....*....
gi 2327734129  14 MLARFKESG-FIHHSGDKGENREEFLMDF 41
Cdd:cd21173     2 LLAEYERIRkLIHHGLTKGRYREEILREF 30
 
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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