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Conserved domains on  [gi|431315389|gb|ELG03301|]
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endonuclease [Escherichia coli KTE48]

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];
1-153 1.96e-53

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


:

Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 166.39  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389   1 MRKYIPLVLFIFSWPVLSA---DIHGRVIRVLDGDTIEVMDSRKAERIRLVNIDAPEKK------QDYGRWSTDMMKSLV 71
Cdd:COG1525    1 MRKLLLALLLALAALAAAAaaaTLTAGVVRVIDGDTLRVRDDGKGERVRLAGIDAPELGqpcgpeQPCGEEARQALRALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389  72 AGKTVTVTYFQ-RDRYGRILGQVYApDGMNVNQFMVRAGAAWVYEQYNTDPV---LSALQNEARQQKRGLWSDADPVPPW 147
Cdd:COG1525   81 AGKTVTLEPDEgRDRYGRLLAYVYV-DGRDLNEELVREGLAWAYRRYSPDKYadrYLAAEAEARAARRGLWSDAFPVPPE 159

                 ....*.
gi 431315389 148 iWRHRK 153
Cdd:COG1525  160 -WRRRK 164
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
1-153 1.96e-53

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 166.39  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389   1 MRKYIPLVLFIFSWPVLSA---DIHGRVIRVLDGDTIEVMDSRKAERIRLVNIDAPEKK------QDYGRWSTDMMKSLV 71
Cdd:COG1525    1 MRKLLLALLLALAALAAAAaaaTLTAGVVRVIDGDTLRVRDDGKGERVRLAGIDAPELGqpcgpeQPCGEEARQALRALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389  72 AGKTVTVTYFQ-RDRYGRILGQVYApDGMNVNQFMVRAGAAWVYEQYNTDPV---LSALQNEARQQKRGLWSDADPVPPW 147
Cdd:COG1525   81 AGKTVTLEPDEgRDRYGRLLAYVYV-DGRDLNEELVREGLAWAYRRYSPDKYadrYLAAEAEARAARRGLWSDAFPVPPE 159

                 ....*.
gi 431315389 148 iWRHRK 153
Cdd:COG1525  160 -WRRRK 164
SNc smart00318
Staphylococcal nuclease homologues;
19-140 6.04e-46

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 146.25  E-value: 6.04e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389    19 ADIHGRVIRVLDGDTIEVMDSRKAE-RIRLVNIDAPEKK----------QDYGRWSTDMMKSLVAGKTVTVTYFQRDRYG 87
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLiTIRLSGIDAPETArpnkgdgtpdEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 431315389    88 RILGQVYAPDGMNVNQFMVRAGAAWVYEQYNTDPV----LSALQNEARQQKRGLWSD 140
Cdd:smart00318  81 RFLGTVYLNGGNNIAEELVKEGLAKVYRYADKDEYvydeLLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
27-140 4.56e-43

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: 138.95  E-value: 4.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389  27 RVLDGDTIEVMDSRKAE-RIRLVNIDAPEKK----------QDYGRWSTDMMKSLVAGKTVTVTYFQRDRYGRILGQVYA 95
Cdd:cd00175    1 RVIDGDTIRVRLPPGPLiTVRLSGIDAPETArpnkgksetdEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 431315389  96 PDGMNVNQFMVRAGAAWVYEQYN----TDPVLSALQNEARQQKRGLWSD 140
Cdd:cd00175   81 NGGENIAEELVKEGLARVYRYYPddseYYDELLEAEEAAKKARKGLWSD 129
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
44-140 1.07e-38

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: 127.05  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389   44 RIRLVNIDAPEKK------QDYGRWSTDMMKSLVAGKTVTVTYFQRDRYGRILGQVYApDGMNVNQFMVRAGAAWVYEQY 117
Cdd:pfam00565   1 RVRLVGIDAPETAkpntpvQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYL-NGKNINEELVKEGLAWVYKAY 79
                          90       100
                  ....*....|....*....|....*..
gi 431315389  118 N----TDPVLSALQNEARQQKRGLWSD 140
Cdd:pfam00565  80 PpnfkHYDELLAAEEEAKKKKKGLWSD 106
PRK06518 PRK06518
hypothetical protein; Provisional
22-150 4.70e-06

hypothetical protein; Provisional


Pssm-ID: 235818  Cd Length: 177  Bit Score: 44.07  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389  22 HGRViRVLDGDTIE----VMDSRKAERIRLVNIDAPE-------KKQDY--GRWSTDMMKSLVAGKTVTVTYFqRDRYGR 88
Cdd:PRK06518  25 HGRA-QVTSGVTFKliadGWRKEITRDIRLYGVDTCAprqkarlGDQEWpcGAVATAWLVTKTLNKWLSCRQA-RMENGV 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431315389  89 ILGQVYApDGMNVNQFMVRAGAAWVYEQYNTDPVL---SALQNEARQQKRGLWSdADPVPPWIWR 150
Cdd:PRK06518 103 HYAQCFV-DGVDIAALGLAEGMAVLSKDDHEDPGPaqyASLEEKARKAYRGLWS-STFQMPWDWR 165
 
Name Accession Description Interval E-value
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
1-153 1.96e-53

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 166.39  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389   1 MRKYIPLVLFIFSWPVLSA---DIHGRVIRVLDGDTIEVMDSRKAERIRLVNIDAPEKK------QDYGRWSTDMMKSLV 71
Cdd:COG1525    1 MRKLLLALLLALAALAAAAaaaTLTAGVVRVIDGDTLRVRDDGKGERVRLAGIDAPELGqpcgpeQPCGEEARQALRALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389  72 AGKTVTVTYFQ-RDRYGRILGQVYApDGMNVNQFMVRAGAAWVYEQYNTDPV---LSALQNEARQQKRGLWSDADPVPPW 147
Cdd:COG1525   81 AGKTVTLEPDEgRDRYGRLLAYVYV-DGRDLNEELVREGLAWAYRRYSPDKYadrYLAAEAEARAARRGLWSDAFPVPPE 159

                 ....*.
gi 431315389 148 iWRHRK 153
Cdd:COG1525  160 -WRRRK 164
SNc smart00318
Staphylococcal nuclease homologues;
19-140 6.04e-46

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 146.25  E-value: 6.04e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389    19 ADIHGRVIRVLDGDTIEVMDSRKAE-RIRLVNIDAPEKK----------QDYGRWSTDMMKSLVAGKTVTVTYFQRDRYG 87
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLiTIRLSGIDAPETArpnkgdgtpdEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 431315389    88 RILGQVYAPDGMNVNQFMVRAGAAWVYEQYNTDPV----LSALQNEARQQKRGLWSD 140
Cdd:smart00318  81 RFLGTVYLNGGNNIAEELVKEGLAKVYRYADKDEYvydeLLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
27-140 4.56e-43

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: 138.95  E-value: 4.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389  27 RVLDGDTIEVMDSRKAE-RIRLVNIDAPEKK----------QDYGRWSTDMMKSLVAGKTVTVTYFQRDRYGRILGQVYA 95
Cdd:cd00175    1 RVIDGDTIRVRLPPGPLiTVRLSGIDAPETArpnkgksetdEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 431315389  96 PDGMNVNQFMVRAGAAWVYEQYN----TDPVLSALQNEARQQKRGLWSD 140
Cdd:cd00175   81 NGGENIAEELVKEGLARVYRYYPddseYYDELLEAEEAAKKARKGLWSD 129
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
44-140 1.07e-38

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: 127.05  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389   44 RIRLVNIDAPEKK------QDYGRWSTDMMKSLVAGKTVTVTYFQRDRYGRILGQVYApDGMNVNQFMVRAGAAWVYEQY 117
Cdd:pfam00565   1 RVRLVGIDAPETAkpntpvQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYL-NGKNINEELVKEGLAWVYKAY 79
                          90       100
                  ....*....|....*....|....*..
gi 431315389  118 N----TDPVLSALQNEARQQKRGLWSD 140
Cdd:pfam00565  80 PpnfkHYDELLAAEEEAKKKKKGLWSD 106
PRK06518 PRK06518
hypothetical protein; Provisional
22-150 4.70e-06

hypothetical protein; Provisional


Pssm-ID: 235818  Cd Length: 177  Bit Score: 44.07  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431315389  22 HGRViRVLDGDTIE----VMDSRKAERIRLVNIDAPE-------KKQDY--GRWSTDMMKSLVAGKTVTVTYFqRDRYGR 88
Cdd:PRK06518  25 HGRA-QVTSGVTFKliadGWRKEITRDIRLYGVDTCAprqkarlGDQEWpcGAVATAWLVTKTLNKWLSCRQA-RMENGV 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431315389  89 ILGQVYApDGMNVNQFMVRAGAAWVYEQYNTDPVL---SALQNEARQQKRGLWSdADPVPPWIWR 150
Cdd:PRK06518 103 HYAQCFV-DGVDIAALGLAEGMAVLSKDDHEDPGPaqyASLEEKARKAYRGLWS-STFQMPWDWR 165
 
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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