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Conserved domains on  [gi|334350969|sp|B6QNP4|]
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RecName: Full=Probable endonuclease lcl3

Protein Classification

thermonuclease family protein( domain architecture ID 11445923)

thermonuclease family protein, may be a thermostable nuclease and catalyze the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond

CATH:  2.40.50.90
SCOP:  4001821

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
115-282 7.18e-28

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


:

Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 106.69  E-value: 7.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 115 RSLLGRVTSVGDGDNFRIfhtpggrlvgwgwlpwmkvptarkELKDKTVHIRLAGVDAPELAHFGRPAQPYAYEAHMWLT 194
Cdd:COG1525   22 ATLTAGVVRVIDGDTLRV------------------------RDDGKGERVRLAGIDAPELGQPCGPEQPCGEEARQALR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 195 SYLMNRRVR-AYVHRPDQYKRVIATVYVrrwldfpplRRRDVSYEMLRRGLATVYeaksgVEFGGTENERKYREAEMLAK 273
Cdd:COG1525   78 ALLAGKTVTlEPDEGRDRYGRLLAYVYV---------DGRDLNEELVREGLAWAY-----RRYSPDKYADRYLAAEAEAR 143

                 ....*....
gi 334350969 274 NRRQGLWKD 282
Cdd:COG1525  144 AARRGLWSD 152
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
115-282 7.18e-28

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 106.69  E-value: 7.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 115 RSLLGRVTSVGDGDNFRIfhtpggrlvgwgwlpwmkvptarkELKDKTVHIRLAGVDAPELAHFGRPAQPYAYEAHMWLT 194
Cdd:COG1525   22 ATLTAGVVRVIDGDTLRV------------------------RDDGKGERVRLAGIDAPELGQPCGPEQPCGEEARQALR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 195 SYLMNRRVR-AYVHRPDQYKRVIATVYVrrwldfpplRRRDVSYEMLRRGLATVYeaksgVEFGGTENERKYREAEMLAK 273
Cdd:COG1525   78 ALLAGKTVTlEPDEGRDRYGRLLAYVYV---------DGRDLNEELVREGLAWAY-----RRYSPDKYADRYLAAEAEAR 143

                 ....*....
gi 334350969 274 NRRQGLWKD 282
Cdd:COG1525  144 AARRGLWSD 152
SNc smart00318
Staphylococcal nuclease homologues;
119-282 3.42e-23

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 93.48  E-value: 3.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969   119 GRVTSVGDGDNFRIFHTPGgrlvgwgwlpwmkvptarkelkdKTVHIRLAGVDAPELAHFG----RPAQPYAYEAHMWLT 194
Cdd:smart00318   5 GVVERVIDGDTIRVRLPKG-----------------------PLITIRLSGIDAPETARPNkgdgTPDEPFGEEAKEFLK 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969   195 SYLMNRRVRAYVHRPDQYKRVIATVYVRRWldfpplrrRDVSYEMLRRGLATVYEAKSGVEFGGTEnerkYREAEMLAKN 274
Cdd:smart00318  62 KLLLGKKVQVEVDSKDRYGRFLGTVYLNGG--------NNIAEELVKEGLAKVYRYADKDEYVYDE----LLEAEEAAKK 129

                   ....*...
gi 334350969   275 RRQGLWKD 282
Cdd:smart00318 130 ARKGLWSD 137
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
165-282 2.20e-21

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 87.38  E-value: 2.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969  165 IRLAGVDAPELAHFGRPAQPYAYEAHMWLTSYLMNRRVRAYVHRPDQYKRVIATVYVrrwldfpplRRRDVSYEMLRRGL 244
Cdd:pfam00565   2 VRLVGIDAPETAKPNTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYL---------NGKNINEELVKEGL 72
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 334350969  245 ATVYEAKSGveFGGTENErkYREAEMLAKNRRQGLWKD 282
Cdd:pfam00565  73 AWVYKAYPP--NFKHYDE--LLAAEEEAKKKKKGLWSD 106
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
123-282 3.77e-18

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 79.24  E-value: 3.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 123 SVGDGDNFRIFHTPGgrlvgwgwlpwmkvptarkelkdKTVHIRLAGVDAPELAH----FGRPAQPYAYEAHMWLTSYLM 198
Cdd:cd00175    1 RVIDGDTIRVRLPPG-----------------------PLITVRLSGIDAPETARpnkgKSETDEPFGEEAKEFLKKLLL 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 199 NRRVRAYVHRPDQYKRVIATVYVrrwldfPPLrrRDVSYEMLRRGLATVYEAKSGVEFGGTEnerkYREAEMLAKNRRQG 278
Cdd:cd00175   58 GKKVQVEVDSKDRYGRTLGTVYL------NGG--ENIAEELVKEGLARVYRYYPDDSEYYDE----LLEAEEAAKKARKG 125

                 ....
gi 334350969 279 LWKD 282
Cdd:cd00175  126 LWSD 129
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
115-282 7.18e-28

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 106.69  E-value: 7.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 115 RSLLGRVTSVGDGDNFRIfhtpggrlvgwgwlpwmkvptarkELKDKTVHIRLAGVDAPELAHFGRPAQPYAYEAHMWLT 194
Cdd:COG1525   22 ATLTAGVVRVIDGDTLRV------------------------RDDGKGERVRLAGIDAPELGQPCGPEQPCGEEARQALR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 195 SYLMNRRVR-AYVHRPDQYKRVIATVYVrrwldfpplRRRDVSYEMLRRGLATVYeaksgVEFGGTENERKYREAEMLAK 273
Cdd:COG1525   78 ALLAGKTVTlEPDEGRDRYGRLLAYVYV---------DGRDLNEELVREGLAWAY-----RRYSPDKYADRYLAAEAEAR 143

                 ....*....
gi 334350969 274 NRRQGLWKD 282
Cdd:COG1525  144 AARRGLWSD 152
SNc smart00318
Staphylococcal nuclease homologues;
119-282 3.42e-23

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 93.48  E-value: 3.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969   119 GRVTSVGDGDNFRIFHTPGgrlvgwgwlpwmkvptarkelkdKTVHIRLAGVDAPELAHFG----RPAQPYAYEAHMWLT 194
Cdd:smart00318   5 GVVERVIDGDTIRVRLPKG-----------------------PLITIRLSGIDAPETARPNkgdgTPDEPFGEEAKEFLK 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969   195 SYLMNRRVRAYVHRPDQYKRVIATVYVRRWldfpplrrRDVSYEMLRRGLATVYEAKSGVEFGGTEnerkYREAEMLAKN 274
Cdd:smart00318  62 KLLLGKKVQVEVDSKDRYGRFLGTVYLNGG--------NNIAEELVKEGLAKVYRYADKDEYVYDE----LLEAEEAAKK 129

                   ....*...
gi 334350969   275 RRQGLWKD 282
Cdd:smart00318 130 ARKGLWSD 137
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
165-282 2.20e-21

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 87.38  E-value: 2.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969  165 IRLAGVDAPELAHFGRPAQPYAYEAHMWLTSYLMNRRVRAYVHRPDQYKRVIATVYVrrwldfpplRRRDVSYEMLRRGL 244
Cdd:pfam00565   2 VRLVGIDAPETAKPNTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYL---------NGKNINEELVKEGL 72
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 334350969  245 ATVYEAKSGveFGGTENErkYREAEMLAKNRRQGLWKD 282
Cdd:pfam00565  73 AWVYKAYPP--NFKHYDE--LLAAEEEAKKKKKGLWSD 106
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
123-282 3.77e-18

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 79.24  E-value: 3.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 123 SVGDGDNFRIFHTPGgrlvgwgwlpwmkvptarkelkdKTVHIRLAGVDAPELAH----FGRPAQPYAYEAHMWLTSYLM 198
Cdd:cd00175    1 RVIDGDTIRVRLPPG-----------------------PLITVRLSGIDAPETARpnkgKSETDEPFGEEAKEFLKKLLL 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334350969 199 NRRVRAYVHRPDQYKRVIATVYVrrwldfPPLrrRDVSYEMLRRGLATVYEAKSGVEFGGTEnerkYREAEMLAKNRRQG 278
Cdd:cd00175   58 GKKVQVEVDSKDRYGRTLGTVYL------NGG--ENIAEELVKEGLARVYRYYPDDSEYYDE----LLEAEEAAKKARKG 125

                 ....
gi 334350969 279 LWKD 282
Cdd:cd00175  126 LWSD 129
 
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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