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Conserved domains on  [gi|58430944|ref|NP_001009933|]
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deoxyribonuclease-1-like 1 precursor [Homo sapiens]

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 662)

exonuclease/endonuclease/phosphatase (EEP) family protein may cleave phosphodiester bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 2-273 9.66e-160

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


The actual alignment was detected with superfamily member smart00476:

Pssm-ID: 469791  Cd Length: 276  Bit Score: 446.12  E-value: 9.66e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944      2 HYPTALLFLILANGAQAFRICAFNAQRLTLAKVAREQVMDTLVRILARCDIMVLQEVVDSSGSAIPLLLRELNRfDGSGP 81
Cdd:smart00476   1 LVPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNS-DSPNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944     82 YSTLSSPQLGRSTYMETYVYFYRSHKTQVLSSYVYND----EDDVFAREPFVAQFSLPSNVLPSLVLVPLHTTPKAVEKE 157
Cdd:smart00476  80 YSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944    158 LNALYDVFLEVSQHWQSKDVILLGDFNADCASLTKKRLDKLELRTEPGFHWVIADGEDTTVRaSTHCTYDRVVLHGERCR 237
Cdd:smart00476 160 IDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLR 238

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 58430944    238 SLLH--TAAAFDFPTSFQLTEEEALNISDHYPVEVELK 273
Cdd:smart00476 239 SSVVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 2-273 9.66e-160

deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of double-stranded DNA. The enzyme is secreted outside the cell and also involved in apoptosis in the nucleus.


Pssm-ID: 128752  Cd Length: 276  Bit Score: 446.12  E-value: 9.66e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944      2 HYPTALLFLILANGAQAFRICAFNAQRLTLAKVAREQVMDTLVRILARCDIMVLQEVVDSSGSAIPLLLRELNRfDGSGP 81
Cdd:smart00476   1 LVPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNS-DSPNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944     82 YSTLSSPQLGRSTYMETYVYFYRSHKTQVLSSYVYND----EDDVFAREPFVAQFSLPSNVLPSLVLVPLHTTPKAVEKE 157
Cdd:smart00476  80 YSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944    158 LNALYDVFLEVSQHWQSKDVILLGDFNADCASLTKKRLDKLELRTEPGFHWVIADGEDTTVRaSTHCTYDRVVLHGERCR 237
Cdd:smart00476 160 IDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLR 238

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 58430944    238 SLLH--TAAAFDFPTSFQLTEEEALNISDHYPVEVELK 273
Cdd:smart00476 239 SSVVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 20-272 8.63e-127

Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a Ca2+, Mg2+/Mn2+-dependent secretory endonuclease, first isolated from bovine pancreas extracts. It cleaves DNA preferentially at phosphodiester linkages next to a pyrimidine nucleotide, producing 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. It generally produces tetranucleotides. DNase1 substrates include single-stranded DNA, double-stranded DNA, and chromatin. This enzyme may be responsible for apoptotic DNA fragmentation. Other deoxyribonucleases in this subfamily include human DNL1L (human DNase I lysosomal-like, also known as DNASE1L1, Xib, and DNase X ), human DNASE1L2 (also known as DNAS1L2), and DNASE1L3 (also known as DNAS1L3, nhDNase, LS-DNase, DNase Y, and DNase gamma) . DNASE1L3 is implicated in apoptotic DNA fragmentation. DNase I is also a cytoskeletal protein which binds actin. A recombinant form of human DNase1 is used as a mucoactive therapy in patients with cystic fibrosis; it hydrolyzes the extracellular DNA in sputum and reduces its viscosity. Mutations in the gene encoding DNase1 have been associated with Systemic Lupus Erythematosus, a multifactorial autoimmune disease. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197337 [Multi-domain]  Cd Length: 256  Bit Score: 361.94  E-value: 8.63e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944  20 RICAFNAQRLTLAKVAREQVMDTLVRILARCDIMVLQEVVDSSGSAIPLLLRELNRFDgSGPYSTLSSPQLGRSTYMETY 99
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSAS-SNTYSYVVSERLGRSSYKEQY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 100 VYFYRSHKTQVLSSYVYNDED---DVFAREPFVAQFSLPSNVLPSLVLVPLHTTPKAVEKELNALYDVFLEVSQHWQSKD 176
Cdd:cd10282  80 AFIYRSDKVSVLESYQYDDGDegtDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 177 VILLGDFNADCASLTKKRLDKLELRTEPGFHWVIADGEDTTVRaSTHCTYDRVVLHGERCRS--LLHTAAAFDFPTSFQL 254
Cdd:cd10282 160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLLQSavVPGSAGVFDFDKEFGL 238

                       250
                ....*....|....*...
gi 58430944 255 TEEEALNISDHYPVEVEL 272
Cdd:cd10282 239 TEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 24-186 9.83e-14

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 68.40  E-value: 9.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944    24 FNAQRLTLAKVAREQVMDTLVRILARC--DIMVLQEVVDSSGSAIPLLLRELNRFDGSGPYstlsspqlGRSTYMETYVY 101
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGGFLSYGGP--------GGGGGGGGVAI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944   102 FYRSHKTQVLSSYVYNDEDDVFAREPFVAqfsLPSNVLPSLVLVPLHTTPKAVEKELNALYDVFLEVSQHWQSKDVILLG 181
Cdd:pfam03372  75 LSRYPLSSVILVDLGEFGDPALRGAIAPF---AGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAG 151


                  ....*
gi 58430944   182 DFNAD 186
Cdd:pfam03372 152 DFNAD 156
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 2-273 9.66e-160

deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of double-stranded DNA. The enzyme is secreted outside the cell and also involved in apoptosis in the nucleus.


Pssm-ID: 128752  Cd Length: 276  Bit Score: 446.12  E-value: 9.66e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944      2 HYPTALLFLILANGAQAFRICAFNAQRLTLAKVAREQVMDTLVRILARCDIMVLQEVVDSSGSAIPLLLRELNRfDGSGP 81
Cdd:smart00476   1 LVPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNS-DSPNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944     82 YSTLSSPQLGRSTYMETYVYFYRSHKTQVLSSYVYND----EDDVFAREPFVAQFSLPSNVLPSLVLVPLHTTPKAVEKE 157
Cdd:smart00476  80 YSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944    158 LNALYDVFLEVSQHWQSKDVILLGDFNADCASLTKKRLDKLELRTEPGFHWVIADGEDTTVRaSTHCTYDRVVLHGERCR 237
Cdd:smart00476 160 IDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLR 238

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 58430944    238 SLLH--TAAAFDFPTSFQLTEEEALNISDHYPVEVELK 273
Cdd:smart00476 239 SSVVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 20-272 8.63e-127

Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a Ca2+, Mg2+/Mn2+-dependent secretory endonuclease, first isolated from bovine pancreas extracts. It cleaves DNA preferentially at phosphodiester linkages next to a pyrimidine nucleotide, producing 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. It generally produces tetranucleotides. DNase1 substrates include single-stranded DNA, double-stranded DNA, and chromatin. This enzyme may be responsible for apoptotic DNA fragmentation. Other deoxyribonucleases in this subfamily include human DNL1L (human DNase I lysosomal-like, also known as DNASE1L1, Xib, and DNase X ), human DNASE1L2 (also known as DNAS1L2), and DNASE1L3 (also known as DNAS1L3, nhDNase, LS-DNase, DNase Y, and DNase gamma) . DNASE1L3 is implicated in apoptotic DNA fragmentation. DNase I is also a cytoskeletal protein which binds actin. A recombinant form of human DNase1 is used as a mucoactive therapy in patients with cystic fibrosis; it hydrolyzes the extracellular DNA in sputum and reduces its viscosity. Mutations in the gene encoding DNase1 have been associated with Systemic Lupus Erythematosus, a multifactorial autoimmune disease. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197337 [Multi-domain]  Cd Length: 256  Bit Score: 361.94  E-value: 8.63e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944  20 RICAFNAQRLTLAKVAREQVMDTLVRILARCDIMVLQEVVDSSGSAIPLLLRELNRFDgSGPYSTLSSPQLGRSTYMETY 99
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSAS-SNTYSYVVSERLGRSSYKEQY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 100 VYFYRSHKTQVLSSYVYNDED---DVFAREPFVAQFSLPSNVLPSLVLVPLHTTPKAVEKELNALYDVFLEVSQHWQSKD 176
Cdd:cd10282  80 AFIYRSDKVSVLESYQYDDGDegtDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 177 VILLGDFNADCASLTKKRLDKLELRTEPGFHWVIADGEDTTVRaSTHCTYDRVVLHGERCRS--LLHTAAAFDFPTSFQL 254
Cdd:cd10282 160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLLQSavVPGSAGVFDFDKEFGL 238

                       250
                ....*....|....*...
gi 58430944 255 TEEEALNISDHYPVEVEL 272
Cdd:cd10282 239 TEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 20-272 8.34e-58

Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC 3.1.21.1) and related proteins. DNase1, also known as DNase I, is a Ca2+, Mg2+/Mn2+-dependent secretory endonuclease, first isolated from bovine pancreas extracts. It cleaves DNA preferentially at phosphodiester linkages next to a pyrimidine nucleotide, producing 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. It generally produces tetranucleotides. DNase1 substrates include single-stranded DNA, double-stranded DNA, and chromatin. This enzyme may be responsible for apoptotic DNA fragmentation. Other deoxyribonucleases in this subfamily include human DNL1L (human DNase I lysosomal-like, also known as DNASE1L1, Xib and DNase X ), human DNASE1L2 (also known as DNAS1L2), and DNASE1L3 (also known as DNAS1L3, nhDNase, LS-DNase, DNase Y, and DNase gamma). DNASE1L3 is also implicated in apoptotic DNA fragmentation. DNase1 is also a cytoskeletal protein which binds actin. A recombinant form of human DNase1 is used as a mucoactive therapy in patients with cystic fibrosis; it hydrolyzes the extracellular DNA in sputum and reduces its viscosity. Mutations in the gene encoding DNase1 have been associated with Systemic Lupus Erythematosus, a multifactorial autoimmune disease. This family also includes a subfamily of mostly uncharacterized proteins, which includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease. The in vivo role of MnuA is as yet undetermined. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197309 [Multi-domain]  Cd Length: 258  Bit Score: 186.45  E-value: 8.34e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944  20 RICAFNAQRLTLAKVAREQVMDTLVRILARCDIMVLQEVVDSSGSAIPLLLRELNRfDGSGPYSTLSSPQLGRSTYMETY 99
Cdd:cd09075   1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQ-DDPNTYHYVVSEPLGRNSYKERY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 100 VYFYRSHKTQVLSSYVYNDE-----DDVFAREPFVAQFSLPSNVLPSLVLVPLHTTPKAVEKELNALYDVFLEVSQHWQS 174
Cdd:cd09075  80 LFLFRPNKVSVLDTYQYDDGckscgNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 175 KDVILLGDFNADCASLTKKRLDKLELRTEPGFHWVIADGEDTTVrASTHCTYDRVVLHGERCRS--LLHTAAAFDFPTSF 252
Cdd:cd09075 160 NDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTA-TSTNCAYDRIVVAGSLLQSsvVPGSAAPFDFQAAY 238

                       250       260
                ....*....|....*....|
gi 58430944 253 QLTEEEALNISDHYPVEVEL 272
Cdd:cd09075 239 GLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 19-272 1.78e-26

Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197338 [Multi-domain]  Cd Length: 266  Bit Score: 104.79  E-value: 1.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944  19 FRICAFNAQRL--TLAKVAREQVMDTLVRILArcDIMVLQEVVDSSGSAIPL--LLRELNRFDGSgpYSTLSSPQL-GRS 93
Cdd:cd10283   1 LRIASWNILNFgnSKGKEKNPAIAEIISAFDL--DLIALQEVMDNGGGLDALakLVNELNKPGGT--WKYIVSDKTgGSS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944  94 TYMETYVYFYRSHKTQ-VLSSYVYNDE-DDVFAREPFVAQF-SLPSNVlpSLVLVPLHTTPKAV---------EKELNAL 161
Cdd:cd10283  77 GDKERYAFLYKSSKVRkVGKAVLEKDSnTDGFARPPYAAKFkSGGTGF--DFTLVNVHLKSGGSsksgqgakrVAEAQAL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 162 YDVFLEVSQHWQSKDVILLGDFNADCASLTKKRLdklelrTEPGFHWVIADGEDTTVRASTHC-TYDRVVLHGERCRSLL 240
Cdd:cd10283 155 AEYLKELADEDPDDDVILLGDFNIPADEDAFKAL------TKAGFKSLLPDSTNLSTSFKGYAnSYDNIFVSGNLKEKFS 228

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 58430944 241 hTAAAFDFPTSFQLTEEEALN-------ISDHYPVEVEL 272
Cdd:cd10283 229 -NSGVFDFNILVDEAGEEDLDyskwrkqISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 21-272 2.77e-14

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 70.97  E-value: 2.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944  21 ICAFNAQRLTLAKVAREqvmdtLVRILARC--DIMVLQEVVDSSGSAIPLLLRELNrfdgsGPYSTLSSPqlGRSTYMET 98
Cdd:cd08372   1 VASYNVNGLNAATRASG-----IARWVRELdpDIVCLQEVKDSQYSAVALNQLLPE-----GYHQYQSGP--SRKEGYEG 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944  99 YVYFYRSHKTQVLSSYVYND-EDDVFAREPFVAQFSLPSNVLpslVLVPLH-----TTPKAVEKELNALYDVFLEVsQHW 172
Cdd:cd08372  69 VAILSKTPKFKIVEKHQYKFgEGDSGERRAVVVKFDVHDKEL---CVVNAHlqaggTRADVRDAQLKEVLEFLKRL-RQP 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 173 QSKDVILLGDFNADCASLTKKRLDK-LELRTEPGFHWVIADGEDT----TVRASTHCTYDRVVLHGERCRSLLHTAAAFD 247
Cdd:cd08372 145 NSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFETLPHAytfdTYMHNVKSRLDYIFVSKSLLPSVKSSKILSD 224

                       250       260
                ....*....|....*....|....*
gi 58430944 248 FptsfqlteEEALNISDHYPVEVEL 272
Cdd:cd08372 225 A--------ARARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 24-186 9.83e-14

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 68.40  E-value: 9.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944    24 FNAQRLTLAKVAREQVMDTLVRILARC--DIMVLQEVVDSSGSAIPLLLRELNRFDGSGPYstlsspqlGRSTYMETYVY 101
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGGFLSYGGP--------GGGGGGGGVAI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944   102 FYRSHKTQVLSSYVYNDEDDVFAREPFVAqfsLPSNVLPSLVLVPLHTTPKAVEKELNALYDVFLEVSQHWQSKDVILLG 181
Cdd:pfam03372  75 LSRYPLSSVILVDLGEFGDPALRGAIAPF---AGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAG 151


                  ....*
gi 58430944   182 DFNAD 186
Cdd:pfam03372 152 DFNAD 156
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 43-272 1.91e-03

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 38.86  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944  43 LVRILARC--DIMVLQEVVDSS---GSAIPLLLRELNRFDGSGPYSTLSspqlgrstymetyvYFyrshkTQVLSSYvyn 117
Cdd:cd09080  23 ILKLLEELdpDVIFLQEVTPPFlayLLSQPWVRKNYYFSEGPPSPAVDP--------------YG-----VLILSKK--- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 118 deDDVFAREPFVAQFSlPSNVL---------PSLVLVPLHTT-----PKAVEKELNALYDvflEVSQHWQSKDVILLGDF 183
Cdd:cd09080  81 --SLVVRRVPFTSTRM-GRNLLaaeinlgsgEPLRLATTHLEslkshSSERTAQLEEIAK---KLKKPPGAANVILGGDF 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58430944 184 NADCASLTKKRLDK------LELR--TEPGFHWviaDGEDTTVRASTH----CTYDRVVLHGERCRsllhtaaafdfPTS 251
Cdd:cd09080 155 NLRDKEDDTGGLPNgfvdawEELGppGEPGYTW---DTQKNPMLRKGEagprKRFDRVLLRGSDLK-----------PKS 220

                       250       260
                ....*....|....*....|....*...
gi 58430944 252 FQLTEEEALNI-------SDHYPVEVEL 272
Cdd:cd09080 221 IELIGTEPIPGdeeglfpSDHFGLLAEL 248
 
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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