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Conserved domains on  [gi|16758784|ref|NP_446359|]
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deoxyribonuclease gamma precursor [Rattus norvegicus]

Protein Classification

DNase I family protein( domain architecture ID 11270576)

deoxyribonuclease I (DNase I) family protein similar to Homo sapiens deoxyribonuclease-1 that catalyzes endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

CATH:  3.60.10.10
EC:  3.1.21.-
Gene Ontology:  GO:0046872|GO:0003677|GO:0004530|GO:0006259
PubMed:  10838565
SCOP:  4002213

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 9-287 0e+00

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: 504.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784      9 YLASLLLFILALHGALSLRLCSFNVRSFGESKKENHNAMDIIVKIIKRCDLILLMEIKDSNNNICPMLMEKLNGNSrrST 88
Cdd:smart00476   1 LVPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDS--PN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784     89 TYNYVISSRLGRNTYKEQYAFLYKEKLVSVKAKYLYHDYQDGDTDVFSREPFVVWFQAPFTAAKDFVIVPLHTTPETSVK 168
Cdd:smart00476  79 TYSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784    169 EIDELADVYTDVRRRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPNFVWLIGDQEDTTVkKSTSCAYDRIVLRGQEI 248
Cdd:smart00476 159 EIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERL 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 16758784    249 VNSVVPRSSGVFDFQKAYELSEEEALDVSDHFPVEFKLQ 287
Cdd:smart00476 238 RSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 9-287 0e+00

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: 504.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784      9 YLASLLLFILALHGALSLRLCSFNVRSFGESKKENHNAMDIIVKIIKRCDLILLMEIKDSNNNICPMLMEKLNGNSrrST 88
Cdd:smart00476   1 LVPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDS--PN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784     89 TYNYVISSRLGRNTYKEQYAFLYKEKLVSVKAKYLYHDYQDGDTDVFSREPFVVWFQAPFTAAKDFVIVPLHTTPETSVK 168
Cdd:smart00476  79 TYSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784    169 EIDELADVYTDVRRRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPNFVWLIGDQEDTTVkKSTSCAYDRIVLRGQEI 248
Cdd:smart00476 159 EIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERL 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 16758784    249 VNSVVPRSSGVFDFQKAYELSEEEALDVSDHFPVEFKLQ 287
Cdd:smart00476 238 RSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 27-286 2.60e-158

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: 442.06  E-value: 2.60e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784  27 RLCSFNVRSFGESKKENHNAMDIIVKIIKRCDLILLMEIKDSNNNICPMLMEKLNGNSRRstTYNYVISSRLGRNTYKEQ 106
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSN--TYSYVVSERLGRSSYKEQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 107 YAFLYKEKLVSVKAKYLYHDYQDgDTDVFSREPFVVWFQAPFTAAKDFVIVPLHTTPETSVKEIDELADVYTDVRRRWKA 186
Cdd:cd10282  79 YAFIYRSDKVSVLESYQYDDGDE-GTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 187 ENFIFMGDFNAGCSYVPKKAWKNIRLRTDPNFVWLIGDQEDTTVkKSTSCAYDRIVLRGQEIVNSVVPRSSGVFDFQKAY 266
Cdd:cd10282 158 DDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEF 236

                       250       260
                ....*....|....*....|
gi 16758784 267 ELSEEEALDVSDHFPVEFKL 286
Cdd:cd10282 237 GLTEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 29-197 8.22e-15

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: 71.49  E-value: 8.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784    29 CSFNVRSFGESKKENHNAMDIIVKIIKRC--DLILLMEIKDSNNNICPMLMEKLngnsrrsttYNYVISSRLGRNTYKEQ 106
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY---------GGFLSYGGPGGGGGGGG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784   107 YAFLYKEKLVSVKAKYLYHDYQDGDTDVFSREPFVVWFqapftaaKDFVIVPLHTTPETSVKEIDELADVYTDVRRRWKA 186
Cdd:pfam03372  72 VAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVV-------PLVLTLAPHASPRLARDEQRADLLLLLLALLAPRS 144

                         170
                  ....*....|.
gi 16758784   187 ENFIFMGDFNA 197
Cdd:pfam03372 145 EPVILAGDFNA 155
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 9-287 0e+00

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: 504.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784      9 YLASLLLFILALHGALSLRLCSFNVRSFGESKKENHNAMDIIVKIIKRCDLILLMEIKDSNNNICPMLMEKLNGNSrrST 88
Cdd:smart00476   1 LVPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDS--PN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784     89 TYNYVISSRLGRNTYKEQYAFLYKEKLVSVKAKYLYHDYQDGDTDVFSREPFVVWFQAPFTAAKDFVIVPLHTTPETSVK 168
Cdd:smart00476  79 TYSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784    169 EIDELADVYTDVRRRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPNFVWLIGDQEDTTVkKSTSCAYDRIVLRGQEI 248
Cdd:smart00476 159 EIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERL 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 16758784    249 VNSVVPRSSGVFDFQKAYELSEEEALDVSDHFPVEFKLQ 287
Cdd:smart00476 238 RSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 27-286 2.60e-158

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: 442.06  E-value: 2.60e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784  27 RLCSFNVRSFGESKKENHNAMDIIVKIIKRCDLILLMEIKDSNNNICPMLMEKLNGNSRRstTYNYVISSRLGRNTYKEQ 106
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSN--TYSYVVSERLGRSSYKEQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 107 YAFLYKEKLVSVKAKYLYHDYQDgDTDVFSREPFVVWFQAPFTAAKDFVIVPLHTTPETSVKEIDELADVYTDVRRRWKA 186
Cdd:cd10282  79 YAFIYRSDKVSVLESYQYDDGDE-GTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 187 ENFIFMGDFNAGCSYVPKKAWKNIRLRTDPNFVWLIGDQEDTTVkKSTSCAYDRIVLRGQEIVNSVVPRSSGVFDFQKAY 266
Cdd:cd10282 158 DDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEF 236

                       250       260
                ....*....|....*....|
gi 16758784 267 ELSEEEALDVSDHFPVEFKL 286
Cdd:cd10282 237 GLTEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 27-286 1.15e-75

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: 232.29  E-value: 1.15e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784  27 RLCSFNVRSFGESKKENHNAMDIIVKIIKRCDLILLMEIKDSNNNICPMLMEKLNGNSrrSTTYNYVISSRLGRNTYKEQ 106
Cdd:cd09075   1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDD--PNTYHYVVSEPLGRNSYKER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 107 YAFLYKEKLVSVKAKYLYHDyQDGD--TDVFSREPFVVWFQAPFTAAKDFVIVPLHTTPETSVKEIDELADVYTDVRRRW 184
Cdd:cd09075  79 YLFLFRPNKVSVLDTYQYDD-GCKScgNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKW 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 185 KAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPNFVWLIGDQEDTTvKKSTSCAYDRIVLRGQEIVNSVVPRSSGVFDFQK 264
Cdd:cd09075 158 HLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTT-ATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQA 236

                       250       260
                ....*....|....*....|..
gi 16758784 265 AYELSEEEALDVSDHFPVEFKL 286
Cdd:cd09075 237 AYGLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 26-286 1.90e-34

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: 126.36  E-value: 1.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784  26 LRLCSFNVRSFGESKKENHNAMdiIVKIIKR--CDLILLMEIKDSNNNICPM--LMEKLNGnsrRSTTYNYVISS-RLGR 100
Cdd:cd10283   1 LRIASWNILNFGNSKGKEKNPA--IAEIISAfdLDLIALQEVMDNGGGLDALakLVNELNK---PGGTWKYIVSDkTGGS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 101 NTYKEQYAFLYKEKLVSVKAKYLYhdYQDGDTDVFSREPFVVWFQAPFTAaKDFVIVPLHTTPETS---------VKEID 171
Cdd:cd10283  76 SGDKERYAFLYKSSKVRKVGKAVL--EKDSNTDGFARPPYAAKFKSGGTG-FDFTLVNVHLKSGGSsksgqgakrVAEAQ 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 172 ELADVYTDVRRRWKAENFIFMGDFNAgcsYVPKKAWKNIrlrTDPNFVWLIGDQED-TTVKKSTSCAYDRIVLRGQEIVN 250
Cdd:cd10283 153 ALAEYLKELADEDPDDDVILLGDFNI---PADEDAFKAL---TKAGFKSLLPDSTNlSTSFKGYANSYDNIFVSGNLKEK 226

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 16758784 251 svvPRSSGVFDFQKAYELSEEEALD-------VSDHFPVEFKL 286
Cdd:cd10283 227 ---FSNSGVFDFNILVDEAGEEDLDyskwrkqISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 28-286 2.77e-19

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: 84.84  E-value: 2.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784  28 LCSFNVRSFGESKKEnhnamDIIVKIIKRC--DLILLMEIKDSNNNICPMLMEKLNGnsrrsttYNYVISSRLGRNtYKE 105
Cdd:cd08372   1 VASYNVNGLNAATRA-----SGIARWVRELdpDIVCLQEVKDSQYSAVALNQLLPEG-------YHQYQSGPSRKE-GYE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 106 QYAFLYKEKLVSVKAKylyHDYQDGDTDVFSREPFVVWFQApftAAKDFVIVPLHTTPETS-----VKEIDELADVYTDv 180
Cdd:cd08372  68 GVAILSKTPKFKIVEK---HQYKFGEGDSGERRAVVVKFDV---HDKELCVVNAHLQAGGTradvrDAQLKEVLEFLKR- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 181 RRRWKAENFIFMGDFNAGCSYVPKKAWKN-IRLRTDPNFVWLI--GDQEDT--TVKKSTSCAYDRIVLRGQeivNSVVPR 255
Cdd:cd08372 141 LRQPNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFetLPHAYTfdTYMHNVKSRLDYIFVSKS---LLPSVK 217

                       250       260       270
                ....*....|....*....|....*....|.
gi 16758784 256 SSGVFDFQKayelseeEALDVSDHFPVEFKL 286
Cdd:cd08372 218 SSKILSDAA-------RARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 29-197 8.22e-15

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: 71.49  E-value: 8.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784    29 CSFNVRSFGESKKENHNAMDIIVKIIKRC--DLILLMEIKDSNNNICPMLMEKLngnsrrsttYNYVISSRLGRNTYKEQ 106
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY---------GGFLSYGGPGGGGGGGG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784   107 YAFLYKEKLVSVKAKYLYHDYQDGDTDVFSREPFVVWFqapftaaKDFVIVPLHTTPETSVKEIDELADVYTDVRRRWKA 186
Cdd:pfam03372  72 VAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVV-------PLVLTLAPHASPRLARDEQRADLLLLLLALLAPRS 144

                         170
                  ....*....|.
gi 16758784   187 ENFIFMGDFNA 197
Cdd:pfam03372 145 EPVILAGDFNA 155
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 132-280 7.26e-04

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: 40.40  E-value: 7.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 132 TDVFSREPFVVWfQAPFTAA---KDFVIVPLHT---------------TPETSVKEIDELADVYTDVRRRWKAENFIFMG 193
Cdd:cd09080  74 VLILSKKSLVVR-RVPFTSTrmgRNLLAAEINLgsgeplrlatthlesLKSHSSERTAQLEEIAKKLKKPPGAANVILGG 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758784 194 DFNAGCSYVP--------KKAWKNIRLRTDPNFVWligDQEDTTVKKST----SCAYDRIVLRGQ-------EIV--NSV 252
Cdd:cd09080 153 DFNLRDKEDDtgglpngfVDAWEELGPPGEPGYTW---DTQKNPMLRKGeagpRKRFDRVLLRGSdlkpksiELIgtEPI 229

                       170       180
                ....*....|....*....|....*...
gi 16758784 253 VPRSSGVFdfqkayelseeealdVSDHF 280
Cdd:cd09080 230 PGDEEGLF---------------PSDHF 242
 
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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