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Conserved domains on  [gi|1909717562|ref|WP_190599409|]
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MULTISPECIES: bifunctional nuclease family protein [Synechocystis]

Protein Classification

bifunctional nuclease family protein( domain architecture ID 10003218)

bifunctional nuclease family protein similar to plant bifunctional nucleases that have both DNase and RNase activities

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1259 COG1259
Bifunctional DNase/RNase [General function prediction only];
1-138 7.55e-63

Bifunctional DNase/RNase [General function prediction only];


:

Pssm-ID: 440871  Cd Length: 138  Bit Score: 190.03  E-value: 7.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1909717562   1 MIEMRVAGIALDAVSRSPIVLLKDGSERRALPIYISQDQARSIIGALENQKPSRPLTHDLMVNLLTTWDVDLKKIIIHSL 80
Cdd:COG1259     1 MIELEVVGVRVDPPSGSPVVLLKEEDGRRVLPIWIGPFEAQAIALALEGEKPPRPLTHDLLKNILEALGARLERVVIDDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1909717562  81 QDNTFYAVLCCVQGDQIREIDCRPSDAISLALRMDSPIWVMEEVLADASIPVDRDADE 138
Cdd:COG1259    81 KDGVFYARLVLKDGGEEVEIDARPSDAIALALRTGAPIYVAEEVLDEAGIPLEEEEEE 138
 
Name Accession Description Interval E-value
COG1259 COG1259
Bifunctional DNase/RNase [General function prediction only];
1-138 7.55e-63

Bifunctional DNase/RNase [General function prediction only];


Pssm-ID: 440871  Cd Length: 138  Bit Score: 190.03  E-value: 7.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1909717562   1 MIEMRVAGIALDAVSRSPIVLLKDGSERRALPIYISQDQARSIIGALENQKPSRPLTHDLMVNLLTTWDVDLKKIIIHSL 80
Cdd:COG1259     1 MIELEVVGVRVDPPSGSPVVLLKEEDGRRVLPIWIGPFEAQAIALALEGEKPPRPLTHDLLKNILEALGARLERVVIDDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1909717562  81 QDNTFYAVLCCVQGDQIREIDCRPSDAISLALRMDSPIWVMEEVLADASIPVDRDADE 138
Cdd:COG1259    81 KDGVFYARLVLKDGGEEVEIDARPSDAIALALRTGAPIYVAEEVLDEAGIPLEEEEEE 138
BFN_dom pfam02577
Bifunctional nuclease domain; This entry represents the bifunctional nuclease (BFN) domain ...
 20-133 1.04e-51

Bifunctional nuclease domain; This entry represents the bifunctional nuclease (BFN) domain which is specific to bacteria and plant organizms. It has both RNase and DNase activities. The dimer of the BFN domain forms a wedge, each monomer being a basic triangular shape. The BFN domain is composed of an eight-stranded, distorted beta-sheet consisting of a four-stranded antiparallel beta-sheet, and a four-stranded mixed beta-sheet. This domain can be found in M. tuberculosis Carbon monoxide resistance (Cor) proteins. Cor consists entirely of this domain with homologs in a variety of organizms, including most mycobacteria, Bacteroides sp., Chlamydia sp., Streptomyces sp., and Rhodococcussp. One of the homologs from Oryza minuta protein OmBBD was reported to exhibit DNase and RNAse activity in vitro. OmBBD carries a C-terminal UvrB domain that is absent in the mycobacterial sequences. UvrB is one component of the UvrABC endonuclease system. Hence, it was proposed that OmBBD's observed nuclease activity may come not from this domain but from an interaction of the C-terminal UvrB with the catalytic UvrC nuclease.


Pssm-ID: 426845  Cd Length: 112  Bit Score: 160.69  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1909717562  20 VLLKDGSERRALPIYISQDQARSIIGALENQKPSRPLTHDLMVNLLTTWDVDLKKIIIHSLQDNTFYAVLCCVQGDqiRE 99
Cdd:pfam02577   1 VLLREEEGRRVLPIWIGAFEAQAIALALEGVKPPRPLTHDLLKSLLEALGARVERVVITDLRDGTFYAELVLDDGE--IE 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1909717562 100 IDCRPSDAISLALRMDSPIWVMEEVLADASIPVD 133
Cdd:pfam02577  79 IDARPSDAIALALRTGAPIYVDEEVLEEAGIPVE 112
 
Name Accession Description Interval E-value
COG1259 COG1259
Bifunctional DNase/RNase [General function prediction only];
1-138 7.55e-63

Bifunctional DNase/RNase [General function prediction only];


Pssm-ID: 440871  Cd Length: 138  Bit Score: 190.03  E-value: 7.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1909717562   1 MIEMRVAGIALDAVSRSPIVLLKDGSERRALPIYISQDQARSIIGALENQKPSRPLTHDLMVNLLTTWDVDLKKIIIHSL 80
Cdd:COG1259     1 MIELEVVGVRVDPPSGSPVVLLKEEDGRRVLPIWIGPFEAQAIALALEGEKPPRPLTHDLLKNILEALGARLERVVIDDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1909717562  81 QDNTFYAVLCCVQGDQIREIDCRPSDAISLALRMDSPIWVMEEVLADASIPVDRDADE 138
Cdd:COG1259    81 KDGVFYARLVLKDGGEEVEIDARPSDAIALALRTGAPIYVAEEVLDEAGIPLEEEEEE 138
BFN_dom pfam02577
Bifunctional nuclease domain; This entry represents the bifunctional nuclease (BFN) domain ...
 20-133 1.04e-51

Bifunctional nuclease domain; This entry represents the bifunctional nuclease (BFN) domain which is specific to bacteria and plant organizms. It has both RNase and DNase activities. The dimer of the BFN domain forms a wedge, each monomer being a basic triangular shape. The BFN domain is composed of an eight-stranded, distorted beta-sheet consisting of a four-stranded antiparallel beta-sheet, and a four-stranded mixed beta-sheet. This domain can be found in M. tuberculosis Carbon monoxide resistance (Cor) proteins. Cor consists entirely of this domain with homologs in a variety of organizms, including most mycobacteria, Bacteroides sp., Chlamydia sp., Streptomyces sp., and Rhodococcussp. One of the homologs from Oryza minuta protein OmBBD was reported to exhibit DNase and RNAse activity in vitro. OmBBD carries a C-terminal UvrB domain that is absent in the mycobacterial sequences. UvrB is one component of the UvrABC endonuclease system. Hence, it was proposed that OmBBD's observed nuclease activity may come not from this domain but from an interaction of the C-terminal UvrB with the catalytic UvrC nuclease.


Pssm-ID: 426845  Cd Length: 112  Bit Score: 160.69  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1909717562  20 VLLKDGSERRALPIYISQDQARSIIGALENQKPSRPLTHDLMVNLLTTWDVDLKKIIIHSLQDNTFYAVLCCVQGDqiRE 99
Cdd:pfam02577   1 VLLREEEGRRVLPIWIGAFEAQAIALALEGVKPPRPLTHDLLKSLLEALGARVERVVITDLRDGTFYAELVLDDGE--IE 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1909717562 100 IDCRPSDAISLALRMDSPIWVMEEVLADASIPVD 133
Cdd:pfam02577  79 IDARPSDAIALALRTGAPIYVDEEVLEEAGIPVE 112
 
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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