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Conserved domains on  [gi|61679896|pdb|1SJ5|A]
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Chain A, Crystal structure of a duf151 family protein (tm0160) from thermotoga maritima at 2.8 A resolution

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];
13-159 1.99e-48

Bifunctional DNase/RNase [General function prediction only];


:

Pssm-ID: 440871  Cd Length: 138  Bit Score: 153.05  E-value: 1.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SJ5_A       13 MRKAWVKTLALDRVSNTPVVILGIEGTNRVLPIWIGAAEGHALALAMEKMEFPRPLTHDLLLSVLESLEARVDKVIIHSL 92
Cdd:COG1259   1 MIELEVVGVRVDPPSGSPVVLLKEEDGRRVLPIWIGPFEAQAIALALEGEKPPRPLTHDLLKNILEALGARLERVVIDDL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1SJ5_A       93 KDNTFYATLVIRDltytdeedeEAALIDIDSRPSDAIILAVKTGAPIFVSDNLVEKHSIELEVNERD 159
Cdd:COG1259  81 KDGVFYARLVLKD---------GGEEVEIDARPSDAIALALRTGAPIYVAEEVLDEAGIPLEEEEEE 138
 
Name Accession Description Interval E-value
COG1259 COG1259
Bifunctional DNase/RNase [General function prediction only];
13-159 1.99e-48

Bifunctional DNase/RNase [General function prediction only];


Pssm-ID: 440871  Cd Length: 138  Bit Score: 153.05  E-value: 1.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SJ5_A       13 MRKAWVKTLALDRVSNTPVVILGIEGTNRVLPIWIGAAEGHALALAMEKMEFPRPLTHDLLLSVLESLEARVDKVIIHSL 92
Cdd:COG1259   1 MIELEVVGVRVDPPSGSPVVLLKEEDGRRVLPIWIGPFEAQAIALALEGEKPPRPLTHDLLKNILEALGARLERVVIDDL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1SJ5_A       93 KDNTFYATLVIRDltytdeedeEAALIDIDSRPSDAIILAVKTGAPIFVSDNLVEKHSIELEVNERD 159
Cdd:COG1259  81 KDGVFYARLVLKD---------GGEEVEIDARPSDAIALALRTGAPIYVAEEVLDEAGIPLEEEEEE 138
BFN_dom pfam02577
Bifunctional nuclease domain; This entry represents the bifunctional nuclease (BFN) domain ...
 32-154 8.17e-43

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: 137.97  E-value: 8.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SJ5_A         32 VILGIEGTNRVLPIWIGAAEGHALALAMEKMEFPRPLTHDLLLSVLESLEARVDKVIIHSLKDNTFYATLVIRDLTYTde 111
Cdd:pfam02577   1 VLLREEEGRRVLPIWIGAFEAQAIALALEGVKPPRPLTHDLLKSLLEALGARVERVVITDLRDGTFYAELVLDDGEIE-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
1SJ5_A        112 edeeaalidIDSRPSDAIILAVKTGAPIFVSDNLVEKHSIELE 154
Cdd:pfam02577  79 ---------IDARPSDAIALALRTGAPIYVDEEVLEEAGIPVE 112
 
Name Accession Description Interval E-value
COG1259 COG1259
Bifunctional DNase/RNase [General function prediction only];
13-159 1.99e-48

Bifunctional DNase/RNase [General function prediction only];


Pssm-ID: 440871  Cd Length: 138  Bit Score: 153.05  E-value: 1.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SJ5_A       13 MRKAWVKTLALDRVSNTPVVILGIEGTNRVLPIWIGAAEGHALALAMEKMEFPRPLTHDLLLSVLESLEARVDKVIIHSL 92
Cdd:COG1259   1 MIELEVVGVRVDPPSGSPVVLLKEEDGRRVLPIWIGPFEAQAIALALEGEKPPRPLTHDLLKNILEALGARLERVVIDDL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1SJ5_A       93 KDNTFYATLVIRDltytdeedeEAALIDIDSRPSDAIILAVKTGAPIFVSDNLVEKHSIELEVNERD 159
Cdd:COG1259  81 KDGVFYARLVLKD---------GGEEVEIDARPSDAIALALRTGAPIYVAEEVLDEAGIPLEEEEEE 138
BFN_dom pfam02577
Bifunctional nuclease domain; This entry represents the bifunctional nuclease (BFN) domain ...
 32-154 8.17e-43

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: 137.97  E-value: 8.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SJ5_A         32 VILGIEGTNRVLPIWIGAAEGHALALAMEKMEFPRPLTHDLLLSVLESLEARVDKVIIHSLKDNTFYATLVIRDLTYTde 111
Cdd:pfam02577   1 VLLREEEGRRVLPIWIGAFEAQAIALALEGVKPPRPLTHDLLKSLLEALGARVERVVITDLRDGTFYAELVLDDGEIE-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
1SJ5_A        112 edeeaalidIDSRPSDAIILAVKTGAPIFVSDNLVEKHSIELE 154
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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