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Conserved domains on  [gi|2733464697|ref|WP_346266107|]
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DddA-like double-stranded DNA deaminase toxin, partial [Glycomyces rutgersensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DddA-like super family cl16874
Double-stranded DNA deaminase toxin A; Members of this family are predicted to function as ...
 12-122 2.71e-11

Double-stranded DNA deaminase toxin A; Members of this family are predicted to function as toxins in bacterial polymorphic toxin systems, including DddA from Burkholderia cenocepacia. DddA is part of the cellular contact- dependent growth inhibition (CDI) system that allows bacteria to communicate with and inhibit the growth of closely related neighbouring bacteria in a contact-dependent fashion. Its deaminase domain has double-stranded DNA cytidine deaminase activity and can be used for CRISPR-free mitochondrial base editing.


The actual alignment was detected with superfamily member pfam14428:

Pssm-ID: 433948  Cd Length: 136  Bit Score: 56.68  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733464697  12 GNLFFTSGKQNDQPLKASPGTTKFHPGEIKPGWQHTKP--AQGHIEGNAAADMLHAGVQRAVLFLNAEPCDHDGNGCKTN 89
Cdd:pfam14428  28 GQLFRPDGRPISPELVSGRGEPASRVNSILRGTGYPRPytTAGHVEGKAAAWMRDNGIREASLVINNGPCGDPLKGCDTL 107

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2733464697  90 TAHYLKPRTELIVKVCDTEGRLRLRkkitGTGE 122
Cdd:pfam14428 108 VEHILPEGSTLTVHGPNGDGPVGLR----GTGE 136
 
Name Accession Description Interval E-value
DddA-like pfam14428
Double-stranded DNA deaminase toxin A; Members of this family are predicted to function as ...
 12-122 2.71e-11

Double-stranded DNA deaminase toxin A; Members of this family are predicted to function as toxins in bacterial polymorphic toxin systems, including DddA from Burkholderia cenocepacia. DddA is part of the cellular contact- dependent growth inhibition (CDI) system that allows bacteria to communicate with and inhibit the growth of closely related neighbouring bacteria in a contact-dependent fashion. Its deaminase domain has double-stranded DNA cytidine deaminase activity and can be used for CRISPR-free mitochondrial base editing.


Pssm-ID: 433948  Cd Length: 136  Bit Score: 56.68  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733464697  12 GNLFFTSGKQNDQPLKASPGTTKFHPGEIKPGWQHTKP--AQGHIEGNAAADMLHAGVQRAVLFLNAEPCDHDGNGCKTN 89
Cdd:pfam14428  28 GQLFRPDGRPISPELVSGRGEPASRVNSILRGTGYPRPytTAGHVEGKAAAWMRDNGIREASLVINNGPCGDPLKGCDTL 107

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2733464697  90 TAHYLKPRTELIVKVCDTEGRLRLRkkitGTGE 122
Cdd:pfam14428 108 VEHILPEGSTLTVHGPNGDGPVGLR----GTGE 136
 
Name Accession Description Interval E-value
DddA-like pfam14428
Double-stranded DNA deaminase toxin A; Members of this family are predicted to function as ...
 12-122 2.71e-11

Double-stranded DNA deaminase toxin A; Members of this family are predicted to function as toxins in bacterial polymorphic toxin systems, including DddA from Burkholderia cenocepacia. DddA is part of the cellular contact- dependent growth inhibition (CDI) system that allows bacteria to communicate with and inhibit the growth of closely related neighbouring bacteria in a contact-dependent fashion. Its deaminase domain has double-stranded DNA cytidine deaminase activity and can be used for CRISPR-free mitochondrial base editing.


Pssm-ID: 433948  Cd Length: 136  Bit Score: 56.68  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733464697  12 GNLFFTSGKQNDQPLKASPGTTKFHPGEIKPGWQHTKP--AQGHIEGNAAADMLHAGVQRAVLFLNAEPCDHDGNGCKTN 89
Cdd:pfam14428  28 GQLFRPDGRPISPELVSGRGEPASRVNSILRGTGYPRPytTAGHVEGKAAAWMRDNGIREASLVINNGPCGDPLKGCDTL 107

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2733464697  90 TAHYLKPRTELIVKVCDTEGRLRLRkkitGTGE 122
Cdd:pfam14428 108 VEHILPEGSTLTVHGPNGDGPVGLR----GTGE 136
 
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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