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Conserved domains on  [gi|518484724|ref|WP_019654931|]
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MULTISPECIES: thermonuclease family protein [Variovorax]

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];
17-166 3.30e-39

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


:

Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 131.34  E-value: 3.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724  17 AFPHLSQAAPRNCLVVGISDGDTLTARCGRigayERVKVRIAAIDAPE------KAQPYGQRSRQALSGICFGEQA-LIT 89
Cdd:COG1525   14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDG----KGERVRLAGIDAPElgqpcgPEQPCGEEARQALRALLAGKTVtLEP 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484724  90 EVDTDRYGRTVADVSCNGEDAGSRMVSEGWAWVYdYNHLATRRGGGLFKLQERAQARRAGLWADPQPTPPwEWRKHQ 166
Cdd:COG1525   90 DEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAY-RRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPP-EWRRRK 164
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
17-166 3.30e-39

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 131.34  E-value: 3.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724  17 AFPHLSQAAPRNCLVVGISDGDTLTARCGRigayERVKVRIAAIDAPE------KAQPYGQRSRQALSGICFGEQA-LIT 89
Cdd:COG1525   14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDG----KGERVRLAGIDAPElgqpcgPEQPCGEEARQALRALLAGKTVtLEP 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484724  90 EVDTDRYGRTVADVSCNGEDAGSRMVSEGWAWVYdYNHLATRRGGGLFKLQERAQARRAGLWADPQPTPPwEWRKHQ 166
Cdd:COG1525   90 DEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAY-RRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPP-EWRRRK 164
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
54-153 1.11e-25

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: 95.08  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724   54 KVRIAAIDAPEKA------QPYGQRSRQALSGICFGEQALITEVDTDRYGRTVADVSCNGEDAGSRMVSEGWAWVYDYNH 127
Cdd:pfam00565   1 RVRLVGIDAPETAkpntpvQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVYKAYP 80
                          90       100
                  ....*....|....*....|....*.
gi 518484724  128 LATRRGGGLFKLQERAQARRAGLWAD 153
Cdd:pfam00565  81 PNFKHYDELLAAEEEAKKKKKGLWSD 106
SNc smart00318
Staphylococcal nuclease homologues;
25-153 2.45e-25

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 95.02  E-value: 2.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724    25 APRNCLVVGISDGDTLTARCGRigaYERVKVRIAAIDAPEKA----------QPYGQRSRQALSGICFGEQALITEVDTD 94
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPK---GPLITIRLSGIDAPETArpnkgdgtpdEPFGEEAKEFLKKLLLGKKVQVEVDSKD 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724    95 RYGRTVADVSCNGEDAGSR-MVSEGWAWVYDYNHLATRRGGGLFKLQERAQARRAGLWAD 153
Cdd:smart00318  78 RYGRFLGTVYLNGGNNIAEeLVKEGLAKVYRYADKDEYVYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
34-153 1.48e-23

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: 90.03  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724  34 ISDGDTLTARCGRiGAYerVKVRIAAIDAPEKA----------QPYGQRSRQALSGICFGEQALITEVDTDRYGRTVADV 103
Cdd:cd00175    2 VIDGDTIRVRLPP-GPL--ITVRLSGIDAPETArpnkgksetdEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518484724 104 SCNG-EDAGSRMVSEGWAWVYDYNHLATRRGGGLFKLQERAQARRAGLWAD 153
Cdd:cd00175   79 YLNGgENIAEELVKEGLARVYRYYPDDSEYYDELLEAEEAAKKARKGLWSD 129
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
17-166 3.30e-39

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 131.34  E-value: 3.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724  17 AFPHLSQAAPRNCLVVGISDGDTLTARCGRigayERVKVRIAAIDAPE------KAQPYGQRSRQALSGICFGEQA-LIT 89
Cdd:COG1525   14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDG----KGERVRLAGIDAPElgqpcgPEQPCGEEARQALRALLAGKTVtLEP 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484724  90 EVDTDRYGRTVADVSCNGEDAGSRMVSEGWAWVYdYNHLATRRGGGLFKLQERAQARRAGLWADPQPTPPwEWRKHQ 166
Cdd:COG1525   90 DEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAY-RRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPP-EWRRRK 164
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
54-153 1.11e-25

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: 95.08  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724   54 KVRIAAIDAPEKA------QPYGQRSRQALSGICFGEQALITEVDTDRYGRTVADVSCNGEDAGSRMVSEGWAWVYDYNH 127
Cdd:pfam00565   1 RVRLVGIDAPETAkpntpvQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVYKAYP 80
                          90       100
                  ....*....|....*....|....*.
gi 518484724  128 LATRRGGGLFKLQERAQARRAGLWAD 153
Cdd:pfam00565  81 PNFKHYDELLAAEEEAKKKKKGLWSD 106
SNc smart00318
Staphylococcal nuclease homologues;
25-153 2.45e-25

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 95.02  E-value: 2.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724    25 APRNCLVVGISDGDTLTARCGRigaYERVKVRIAAIDAPEKA----------QPYGQRSRQALSGICFGEQALITEVDTD 94
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPK---GPLITIRLSGIDAPETArpnkgdgtpdEPFGEEAKEFLKKLLLGKKVQVEVDSKD 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724    95 RYGRTVADVSCNGEDAGSR-MVSEGWAWVYDYNHLATRRGGGLFKLQERAQARRAGLWAD 153
Cdd:smart00318  78 RYGRFLGTVYLNGGNNIAEeLVKEGLAKVYRYADKDEYVYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
34-153 1.48e-23

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: 90.03  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484724  34 ISDGDTLTARCGRiGAYerVKVRIAAIDAPEKA----------QPYGQRSRQALSGICFGEQALITEVDTDRYGRTVADV 103
Cdd:cd00175    2 VIDGDTIRVRLPP-GPL--ITVRLSGIDAPETArpnkgksetdEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518484724 104 SCNG-EDAGSRMVSEGWAWVYDYNHLATRRGGGLFKLQERAQARRAGLWAD 153
Cdd:cd00175   79 YLNGgENIAEELVKEGLARVYRYYPDDSEYYDELLEAEEAAKKARKGLWSD 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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