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Conserved domains on  [gi|84490435|ref|NP_031896|]
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deoxyribonuclease gamma precursor [Mus musculus]

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.-
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 ...
10-287 2.67e-177

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: 490.80  E-value: 2.67e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435     10 LASLLLFILALHDTLALRLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSrrSTT 89
Cdd:smart00476   2 VPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDS--PNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435     90 YNYVISSRLGRNTYKEQYAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKE 169
Cdd:smart00476  80 YSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435    170 IDELVDVYTDVRSQWKTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVkKSTSCAYDRIVLCGQEIV 249
Cdd:smart00476 160 IDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLR 238
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 84490435    250 NSVVPRSSGVFDFQKAYDLSEEEALDVSDHFPVEFKLQ 287
Cdd:smart00476 239 SSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
10-287 2.67e-177

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: 490.80  E-value: 2.67e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435     10 LASLLLFILALHDTLALRLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSrrSTT 89
Cdd:smart00476   2 VPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDS--PNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435     90 YNYVISSRLGRNTYKEQYAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKE 169
Cdd:smart00476  80 YSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435    170 IDELVDVYTDVRSQWKTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVkKSTSCAYDRIVLCGQEIV 249
Cdd:smart00476 160 IDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLR 238
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 84490435    250 NSVVPRSSGVFDFQKAYDLSEEEALDVSDHFPVEFKLQ 287
Cdd:smart00476 239 SSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
27-286 1.17e-160

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: 447.84  E-value: 1.17e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435  27 RLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSRRstTYNYVISSRLGRNTYKEQ 106
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSN--TYSYVVSERLGRSSYKEQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 107 YAFVYKEKLVSVKTKYHYHDYQDgDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKT 186
Cdd:cd10282  79 YAFIYRSDKVSVLESYQYDDGDE-GTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 187 ENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVkKSTSCAYDRIVLCGQEIVNSVVPRSSGVFDFQKAY 266
Cdd:cd10282 158 DDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEF 236
                       250       260
                ....*....|....*....|
gi 84490435 267 DLSEEEALDVSDHFPVEFKL 286
Cdd:cd10282 237 GLTEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
29-197 1.27e-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: 70.72  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435    29 CSFNVRSFGASKKENHEAMDIIVKIIKRC--DLILLMEIKDSSNNICPMLMEKLngnsrrsttYNYVISSRLGRNTYKEQ 106
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY---------GGFLSYGGPGGGGGGGG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435   107 YAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSpftavkdFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKT 186
Cdd:pfam03372  72 VAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPL-------VLTLAPHASPRLARDEQRADLLLLLLALLAPRS 144
                         170
                  ....*....|.
gi 84490435   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 ...
10-287 2.67e-177

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: 490.80  E-value: 2.67e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435     10 LASLLLFILALHDTLALRLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSrrSTT 89
Cdd:smart00476   2 VPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDS--PNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435     90 YNYVISSRLGRNTYKEQYAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKE 169
Cdd:smart00476  80 YSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435    170 IDELVDVYTDVRSQWKTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVkKSTSCAYDRIVLCGQEIV 249
Cdd:smart00476 160 IDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLR 238
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 84490435    250 NSVVPRSSGVFDFQKAYDLSEEEALDVSDHFPVEFKLQ 287
Cdd:smart00476 239 SSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
27-286 1.17e-160

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: 447.84  E-value: 1.17e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435  27 RLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSRRstTYNYVISSRLGRNTYKEQ 106
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSN--TYSYVVSERLGRSSYKEQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 107 YAFVYKEKLVSVKTKYHYHDYQDgDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKT 186
Cdd:cd10282  79 YAFIYRSDKVSVLESYQYDDGDE-GTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 187 ENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVkKSTSCAYDRIVLCGQEIVNSVVPRSSGVFDFQKAY 266
Cdd:cd10282 158 DDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEF 236
                       250       260
                ....*....|....*....|
gi 84490435 267 DLSEEEALDVSDHFPVEFKL 286
Cdd:cd10282 237 GLTEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
27-286 6.38e-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: 230.36  E-value: 6.38e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435  27 RLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSrrSTTYNYVISSRLGRNTYKEQ 106
Cdd:cd09075   1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDD--PNTYHYVVSEPLGRNSYKER 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 107 YAFVYKEKLVSVKTKYHYHDyQDGD--TDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKEIDELVDVYTDVRSQW 184
Cdd:cd09075  79 YLFLFRPNKVSVLDTYQYDD-GCKScgNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKW 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 185 KTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTvKKSTSCAYDRIVLCGQEIVNSVVPRSSGVFDFQK 264
Cdd:cd09075 158 HLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTT-ATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQA 236
                       250       260
                ....*....|....*....|..
gi 84490435 265 AYDLSEEEALDVSDHFPVEFKL 286
Cdd:cd09075 237 AYGLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
26-286 1.99e-32

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: 120.97  E-value: 1.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435  26 LRLCSFNVRSFGASKKEnhEAMDIIVKIIKR--CDLILLMEIKDSSNNICPM--LMEKLNGnsrRSTTYNYVISS-RLGR 100
Cdd:cd10283   1 LRIASWNILNFGNSKGK--EKNPAIAEIISAfdLDLIALQEVMDNGGGLDALakLVNELNK---PGGTWKYIVSDkTGGS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 101 NTYKEQYAFVYKEKLVSVKTKYHYhdYQDGDTDVFSREPFVVWFHSPFTAvKDFVIVPLH-TTPETS--------VKEID 171
Cdd:cd10283  76 SGDKERYAFLYKSSKVRKVGKAVL--EKDSNTDGFARPPYAAKFKSGGTG-FDFTLVNVHlKSGGSSksgqgakrVAEAQ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 172 ELVDVYTDVRSQWKTENFIFMGDFNAgcsYVPKKAWQNIrlrTDPKFVWLIGDQED-TTVKKSTSCAYDRIVLCGQEIVN 250
Cdd:cd10283 153 ALAEYLKELADEDPDDDVILLGDFNI---PADEDAFKAL---TKAGFKSLLPDSTNlSTSFKGYANSYDNIFVSGNLKEK 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 84490435 251 svvPRSSGVFDFQKAYDLSEEEALD-------VSDHFPVEFKL 286
Cdd:cd10283 227 ---FSNSGVFDFNILVDEAGEEDLDyskwrkqISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
28-286 4.76e-18

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: 81.37  E-value: 4.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435  28 LCSFNVRSFGASKKEnheamDIIVKIIKRC--DLILLMEIKDSSNNICPMLMEKLNGnsrrsttYNYVISSRLGRNtYKE 105
Cdd:cd08372   1 VASYNVNGLNAATRA-----SGIARWVRELdpDIVCLQEVKDSQYSAVALNQLLPEG-------YHQYQSGPSRKE-GYE 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 106 QYAFVYKEKLVSVKTKyhyHDYQDGDTDVFSREPFVVWFHSpftAVKDFVIVPLHTTPETS-----VKEIDELVDVYTDV 180
Cdd:cd08372  68 GVAILSKTPKFKIVEK---HQYKFGEGDSGERRAVVVKFDV---HDKELCVVNAHLQAGGTradvrDAQLKEVLEFLKRL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435 181 RsQWKTENFIFMGDFNAGCSYVPKKAWQN-IRLRTDPKFVWLI--GDQEDT--TVKKSTSCAYDRIVLCGQeivNSVVPR 255
Cdd:cd08372 142 R-QPNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFetLPHAYTfdTYMHNVKSRLDYIFVSKS---LLPSVK 217
                       250       260       270
                ....*....|....*....|....*....|.
gi 84490435 256 SSGVFDFQKaydlseeEALDVSDHFPVEFKL 286
Cdd:cd08372 218 SSKILSDAA-------RARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
29-197 1.27e-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: 70.72  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435    29 CSFNVRSFGASKKENHEAMDIIVKIIKRC--DLILLMEIKDSSNNICPMLMEKLngnsrrsttYNYVISSRLGRNTYKEQ 106
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY---------GGFLSYGGPGGGGGGGG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84490435   107 YAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSpftavkdFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKT 186
Cdd:pfam03372  72 VAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPL-------VLTLAPHASPRLARDEQRADLLLLLLALLAPRS 144
                         170
                  ....*....|.
gi 84490435   187 ENFIFMGDFNA 197
Cdd:pfam03372 145 EPVILAGDFNA 155
 
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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