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Conserved domains on  [gi|161016801|ref|NP_034191|]
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deoxyribonuclease-1 precursor [Mus musculus]

Protein Classification

DNase1 domain-containing protein( domain architecture ID 11270576)

DNase1 domain-containing protein

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 ...
20-282 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: 508.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801    20 AGTLRIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRDKPDTYRYVVSEPLGRKSYK 99
Cdd:smart00476  15 AASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYK 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801   100 EQYLFVYRPDQVSILDSYQYDDGCEpCGNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPTEAVSEIDALYDVYLDVWQK 179
Cdd:smart00476  95 EQYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQK 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801   180 WGLEDIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAGALLQAAVVPNSAVPFDFQA 259
Cdd:smart00476 174 WGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQT 253
                          250       260
                   ....*....|....*....|...
gi 161016801   260 EYGLSNQLAEAISDHYPVEVTLR 282
Cdd:smart00476 254 AYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
20-282 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: 508.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801    20 AGTLRIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRDKPDTYRYVVSEPLGRKSYK 99
Cdd:smart00476  15 AASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYK 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801   100 EQYLFVYRPDQVSILDSYQYDDGCEpCGNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPTEAVSEIDALYDVYLDVWQK 179
Cdd:smart00476  95 EQYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQK 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801   180 WGLEDIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAGALLQAAVVPNSAVPFDFQA 259
Cdd:smart00476 174 WGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQT 253
                          250       260
                   ....*....|....*....|...
gi 161016801   260 EYGLSNQLAEAISDHYPVEVTLR 282
Cdd:smart00476 254 AYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
24-281 1.21e-151

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: 423.96  E-value: 1.21e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  24 RIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRDKPDTYRYVVSEPLGRKSYKEQYL 103
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 104 FVYRPDQVSILDSYQYDDGCEPcgNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPTEAVSEIDALYDVYLDVWQKWGLE 183
Cdd:cd10282   81 FIYRSDKVSVLESYQYDDGDEG--TDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 184 DIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAGALLQAAVVPNSAVPFDFQAEYGL 263
Cdd:cd10282  159 DVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238
                        250
                 ....*....|....*...
gi 161016801 264 SNQLAEAISDHYPVEVTL 281
Cdd:cd10282  239 TEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
26-193 7.30e-11

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: 59.93  E-value: 7.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801   26 AAFNIRTFGETKMSNATLSVYFVKILSRY--DIAVIQEVRDSHLVAVGKLLDELnrdkpdtYRYVVSEPLGRKSYKEQYL 103
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-------GGFLSYGGPGGGGGGGGVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  104 FVYRPDQVSILDSYQYDDGCEPCGNDTFSREPAIVKFFspytevqeFAIVPLHAAPTEAVSEIDALYDVYLDVWQKWGLE 183
Cdd:pfam03372  74 ILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPL--------VLTLAPHASPRLARDEQRADLLLLLLALLAPRSE 145
                         170
                  ....*....|
gi 161016801  184 DIMFMGDFNA 193
Cdd:pfam03372 146 PVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
20-283 2.59e-08

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 54.26  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  20 AGTLRIAAFNIRTFGETK-------MSNATLSVY------FVKILSRY--DIAVIQEVrDSHLVAVGKLLDELNRDKPdT 84
Cdd:COG2374   66 GGDLRVATFNVENLFDTDdddddfgRGADTPEEYerklakIAAAIAALdaDIVGLQEV-ENNGSALQDLVAALNLAGG-T 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  85 YRYVVSEP--------LGrksykeqylFVYRPDQVSILDSYQYDDGCEPCGN-DTFSREPAIVKFFSPYTEvqEFAIVPL 155
Cdd:COG2374  144 YAFVHPPDgpdgdgirVA---------LLYRPDRVTLVGSATIADLPDSPGNpDRFSRPPLAVTFELANGE--PFTVIVN 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 156 H--------AAPTEAVSEID------ALYDVYLDVWQKWGLEDIMFMGDFNAgcsYVTSSqwsSIR-LRTSPIF----QW 216
Cdd:COG2374  213 HfkskgsddPGDGQGASEAKrtaqaeALRAFVDSLLAADPDAPVIVLGDFND---YPFED---PLRaLLGAGGLtnlaEK 286
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161016801 217 LIPDSADTTVTS-THCAYDRIVVAGALLQ----AAVVPNSAVPF--DFQAEYGLSNQLAEAISDHYPVEVTLRK 283
Cdd:COG2374  287 LPAAERYSYVYDgNSGLLDHILVSPALAArvtgADIWHINADIYndDFKPDFRTYADDPGRASDHDPVVVGLRL 360
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
20-282 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: 508.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801    20 AGTLRIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRDKPDTYRYVVSEPLGRKSYK 99
Cdd:smart00476  15 AASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYK 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801   100 EQYLFVYRPDQVSILDSYQYDDGCEpCGNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPTEAVSEIDALYDVYLDVWQK 179
Cdd:smart00476  95 EQYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQK 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801   180 WGLEDIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAGALLQAAVVPNSAVPFDFQA 259
Cdd:smart00476 174 WGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQT 253
                          250       260
                   ....*....|....*....|...
gi 161016801   260 EYGLSNQLAEAISDHYPVEVTLR 282
Cdd:smart00476 254 AYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
24-281 1.21e-151

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: 423.96  E-value: 1.21e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  24 RIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRDKPDTYRYVVSEPLGRKSYKEQYL 103
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 104 FVYRPDQVSILDSYQYDDGCEPcgNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPTEAVSEIDALYDVYLDVWQKWGLE 183
Cdd:cd10282   81 FIYRSDKVSVLESYQYDDGDEG--TDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 184 DIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAGALLQAAVVPNSAVPFDFQAEYGL 263
Cdd:cd10282  159 DVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238
                        250
                 ....*....|....*...
gi 161016801 264 SNQLAEAISDHYPVEVTL 281
Cdd:cd10282  239 TEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
24-281 2.20e-132

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: 375.58  E-value: 2.20e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  24 RIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRDKPDTYRYVVSEPLGRKSYKEQYL 103
Cdd:cd09075    1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 104 FVYRPDQVSILDSYQYDDGCEPCGNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPTEAVSEIDALYDVYLDVWQKWGLE 183
Cdd:cd09075   81 FLFRPNKVSVLDTYQYDDGCKSCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 184 DIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAGALLQAAVVPNSAVPFDFQAEYGL 263
Cdd:cd09075  161 DVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGL 240
                        250
                 ....*....|....*...
gi 161016801 264 SNQLAEAISDHYPVEVTL 281
Cdd:cd09075  241 SNEMALAISDHYPVEVTL 258
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
25-281 1.48e-36

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: 130.29  E-value: 1.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  25 IAAFNIRTFGETKMSNATLSvyFVKILSrYDIAVIQEVRDSHLVAVGklldeLNRDKPDTYRYVVSEPlGRKSYKEQYLF 104
Cdd:cd08372    1 VASYNVNGLNAATRASGIAR--WVRELD-PDIVCLQEVKDSQYSAVA-----LNQLLPEGYHQYQSGP-SRKEGYEGVAI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 105 VYRPDQVSILDSYQYDDGCEpcgnDTFSREPAIVKFFSpytEVQEFAIVPLHAAPT-----EAVSEIDALYDVYLDVwQK 179
Cdd:cd08372   72 LSKTPKFKIVEKHQYKFGEG----DSGERRAVVVKFDV---HDKELCVVNAHLQAGgtradVRDAQLKEVLEFLKRL-RQ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 180 WGLEDIMFMGDFNAGCSYVTSSQWSS-IRLRTSPIFQWLIPD--SADTTVTSTH---CAYDRIVVAGALLqaaVVPNSAV 253
Cdd:cd08372  144 PNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFETlpHAYTFDTYMHnvkSRLDYIFVSKSLL---PSVKSSK 220
                        250       260
                 ....*....|....*....|....*...
gi 161016801 254 PFDFQaeyglsnQLAEAISDHYPVEVTL 281
Cdd:cd08372  221 ILSDA-------ARARIPSDHYPIEVTL 241
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
23-281 3.43e-31

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: 116.73  E-value: 3.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  23 LRIAAFNIRTFGETKMSNATLsvYFVKILSRYDIAVI--QEVRDS--HLVAVGKLLDELNRdKPDTYRYVVSEPLGRKS- 97
Cdd:cd10283    1 LRIASWNILNFGNSKGKEKNP--AIAEIISAFDLDLIalQEVMDNggGLDALAKLVNELNK-PGGTWKYIVSDKTGGSSg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  98 YKEQYLFVYRPDQVSILD-SYQYDDGcepcGNDTFSREPAIVKFFSPYTEvQEFAIVPLHAAPTEA---------VSEID 167
Cdd:cd10283   78 DKERYAFLYKSSKVRKVGkAVLEKDS----NTDGFARPPYAAKFKSGGTG-FDFTLVNVHLKSGGSsksgqgakrVAEAQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 168 ALYDVYLDVWQKWGLEDIMFMGDFNAgcsYVTSSQWSSIRLRTspiFQWLIPDSADTTvTSTHC---AYDRIVVAGALLQ 244
Cdd:cd10283  153 ALAEYLKELADEDPDDDVILLGDFNI---PADEDAFKALTKAG---FKSLLPDSTNLS-TSFKGyanSYDNIFVSGNLKE 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 161016801 245 AAV---VPNSAVPFDFQAEYGLSN-QLAEAISDHYPVEVTL 281
Cdd:cd10283  226 KFSnsgVFDFNILVDEAGEEDLDYsKWRKQISDHDPVWVEF 266
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
26-193 7.30e-11

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: 59.93  E-value: 7.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801   26 AAFNIRTFGETKMSNATLSVYFVKILSRY--DIAVIQEVRDSHLVAVGKLLDELnrdkpdtYRYVVSEPLGRKSYKEQYL 103
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-------GGFLSYGGPGGGGGGGGVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  104 FVYRPDQVSILDSYQYDDGCEPCGNDTFSREPAIVKFFspytevqeFAIVPLHAAPTEAVSEIDALYDVYLDVWQKWGLE 183
Cdd:pfam03372  74 ILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPL--------VLTLAPHASPRLARDEQRADLLLLLLALLAPRSE 145
                         170
                  ....*....|
gi 161016801  184 DIMFMGDFNA 193
Cdd:pfam03372 146 PVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
20-283 2.59e-08

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 54.26  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  20 AGTLRIAAFNIRTFGETK-------MSNATLSVY------FVKILSRY--DIAVIQEVrDSHLVAVGKLLDELNRDKPdT 84
Cdd:COG2374   66 GGDLRVATFNVENLFDTDdddddfgRGADTPEEYerklakIAAAIAALdaDIVGLQEV-ENNGSALQDLVAALNLAGG-T 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801  85 YRYVVSEP--------LGrksykeqylFVYRPDQVSILDSYQYDDGCEPCGN-DTFSREPAIVKFFSPYTEvqEFAIVPL 155
Cdd:COG2374  144 YAFVHPPDgpdgdgirVA---------LLYRPDRVTLVGSATIADLPDSPGNpDRFSRPPLAVTFELANGE--PFTVIVN 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016801 156 H--------AAPTEAVSEID------ALYDVYLDVWQKWGLEDIMFMGDFNAgcsYVTSSqwsSIR-LRTSPIF----QW 216
Cdd:COG2374  213 HfkskgsddPGDGQGASEAKrtaqaeALRAFVDSLLAADPDAPVIVLGDFND---YPFED---PLRaLLGAGGLtnlaEK 286
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161016801 217 LIPDSADTTVTS-THCAYDRIVVAGALLQ----AAVVPNSAVPF--DFQAEYGLSNQLAEAISDHYPVEVTLRK 283
Cdd:COG2374  287 LPAAERYSYVYDgNSGLLDHILVSPALAArvtgADIWHINADIYndDFKPDFRTYADDPGRASDHDPVVVGLRL 360
 
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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