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Conserved domains on  [gi|4503347|ref|NP_001365|]
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deoxyribonuclease-1-like 2 precursor [Homo sapiens]

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 ...
18-296 9.29e-169

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: 468.84  E-value: 9.29e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347      18 GTAALRIGAFNIQSFGDSKVSDPACGSIIAKILAGYDLALVQEVRDPDLSAVSALMEQINSVSEHEYSFVSSQPLGRDQY 97
Cdd:smart00476  14 GAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347      98 KEMYLFVYRKDAVSVVDTYLYPD----PEDVFSREPFVVKFSAPGTgerapplpsrraltppplpaAAQNLVLIPLHAAP 173
Cdd:smart00476  94 KEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPST--------------------AVKEFVIVPLHTTP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347     174 HQAVAEIDALYDVYLDVIDKWGTDDMLFLGDFNADCSYVRAQDWAAIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVAC 253
Cdd:smart00476 154 EAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVA 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 4503347     254 GARLRRSLKPQSATVHDFQEEFGLDQTQALAISDHFPVEVTLK 296
Cdd:smart00476 234 GERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
18-296 9.29e-169

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: 468.84  E-value: 9.29e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347      18 GTAALRIGAFNIQSFGDSKVSDPACGSIIAKILAGYDLALVQEVRDPDLSAVSALMEQINSVSEHEYSFVSSQPLGRDQY 97
Cdd:smart00476  14 GAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347      98 KEMYLFVYRKDAVSVVDTYLYPD----PEDVFSREPFVVKFSAPGTgerapplpsrraltppplpaAAQNLVLIPLHAAP 173
Cdd:smart00476  94 KEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPST--------------------AVKEFVIVPLHTTP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347     174 HQAVAEIDALYDVYLDVIDKWGTDDMLFLGDFNADCSYVRAQDWAAIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVAC 253
Cdd:smart00476 154 EAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVA 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 4503347     254 GARLRRSLKPQSATVHDFQEEFGLDQTQALAISDHFPVEVTLK 296
Cdd:smart00476 234 GERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
23-295 1.94e-137

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: 388.52  E-value: 1.94e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   23 RIGAFNIQSFGDSKVSDPACGSIIAKILAGYDLALVQEVRDPDLSAVSALMEQINSVSEHEYSFVSSQPLGRDQYKEMYL 102
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  103 FVYRKDAVSVVDTYLYPD---PEDVFSREPFVVKFSAPGTgerapplpsrraltppplpaAAQNLVLIPLHAAPHQAVAE 179
Cdd:cd10282  81 FIYRSDKVSVLESYQYDDgdeGTDVFSREPFVVRFSSPST--------------------AVKDFVLVPIHTSPDDAVAE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  180 IDALYDVYLDVIDKWGTDDMLFLGDFNADCSYVRAQDWAAIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVACGARLRR 259
Cdd:cd10282 141 IDALYDVYDDVKQRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQS 220
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 4503347  260 SLKPQSATVHDFQEEFGLDQTQALAISDHFPVEVTL 295
Cdd:cd10282 221 AVVPGSAGVFDFDKEFGLTEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
27-208 2.17e-08

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: 53.00  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347     27 FNIQSFGDSKVSDPACGSIIAKILAGY--DLALVQEVRDPDLSAVSALMEqinsvseHEYSFVSSQPLGRDQYKEMYLFV 104
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALL-------AYGGFLSYGGPGGGGGGGGVAIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347    105 YRKDAVSVVDTYLYPDPEDVFSREPFVVKFSAPGTGERAPPLpsrraltppplpaaaqnlvliplHAAPHQAVAEIDALY 184
Cdd:pfam03372  76 SRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAP-----------------------HASPRLARDEQRADL 132
                         170       180
                  ....*....|....*....|....
gi 4503347    185 DVYLDVIDKWGTDDMLFLGDFNAD 208
Cdd:pfam03372 133 LLLLLALLAPRSEPVILAGDFNAD 156
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
22-297 2.03e-07

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 51.56  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   22 LRIGAFNIQSFGDSKVSDPACGSI-------------IAKILAGY--DLALVQEVRDpDLSAVSALMEQINsVSEHEYSF 86
Cdd:COG2374  69 LRVATFNVENLFDTDDDDDDFGRGadtpeeyerklakIAAAIAALdaDIVGLQEVEN-NGSALQDLVAALN-LAGGTYAF 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   87 VSSQPlGRDQYKEMYLFVYRKDAVSVVDT------YLYPDPEDVFSREPFVVKFSAPGtGER----APPLPSRRaltpPP 156
Cdd:COG2374 147 VHPPD-GPDGDGIRVALLYRPDRVTLVGSatiadlPDSPGNPDRFSRPPLAVTFELAN-GEPftviVNHFKSKG----SD 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  157 LPAAAQNLVLIplhaaphQAVAEIDALYDVYLDVIDKWGTDDMLFLGDFNAdcsYVRAQDWAAIRLRSS--EVFKWLIPD 234
Cdd:COG2374 221 DPGDGQGASEA-------KRTAQAEALRAFVDSLLAADPDAPVIVLGDFND---YPFEDPLRALLGAGGltNLAEKLPAA 290
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503347  235 SADTTV--GNSdCAYDRIVACGARLRRSlkPQSATVH--------DFQEEFGLDQTQALAISDHFPVEVTLKF 297
Cdd:COG2374 291 ERYSYVydGNS-GLLDHILVSPALAARV--TGADIWHinadiyndDFKPDFRTYADDPGRASDHDPVVVGLRL 360
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
18-296 9.29e-169

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: 468.84  E-value: 9.29e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347      18 GTAALRIGAFNIQSFGDSKVSDPACGSIIAKILAGYDLALVQEVRDPDLSAVSALMEQINSVSEHEYSFVSSQPLGRDQY 97
Cdd:smart00476  14 GAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347      98 KEMYLFVYRKDAVSVVDTYLYPD----PEDVFSREPFVVKFSAPGTgerapplpsrraltppplpaAAQNLVLIPLHAAP 173
Cdd:smart00476  94 KEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPST--------------------AVKEFVIVPLHTTP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347     174 HQAVAEIDALYDVYLDVIDKWGTDDMLFLGDFNADCSYVRAQDWAAIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVAC 253
Cdd:smart00476 154 EAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVA 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 4503347     254 GARLRRSLKPQSATVHDFQEEFGLDQTQALAISDHFPVEVTLK 296
Cdd:smart00476 234 GERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
23-295 1.94e-137

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: 388.52  E-value: 1.94e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   23 RIGAFNIQSFGDSKVSDPACGSIIAKILAGYDLALVQEVRDPDLSAVSALMEQINSVSEHEYSFVSSQPLGRDQYKEMYL 102
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  103 FVYRKDAVSVVDTYLYPD---PEDVFSREPFVVKFSAPGTgerapplpsrraltppplpaAAQNLVLIPLHAAPHQAVAE 179
Cdd:cd10282  81 FIYRSDKVSVLESYQYDDgdeGTDVFSREPFVVRFSSPST--------------------AVKDFVLVPIHTSPDDAVAE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  180 IDALYDVYLDVIDKWGTDDMLFLGDFNADCSYVRAQDWAAIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVACGARLRR 259
Cdd:cd10282 141 IDALYDVYDDVKQRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQS 220
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 4503347  260 SLKPQSATVHDFQEEFGLDQTQALAISDHFPVEVTL 295
Cdd:cd10282 221 AVVPGSAGVFDFDKEFGLTEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
23-295 2.04e-82

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: 249.24  E-value: 2.04e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   23 RIGAFNIQSFGDSKVSDPACGSIIAKILAGYDLALVQEVRDPDLSAVSALMEQINSVSEHEYSFVSSQPLGRDQYKEMYL 102
Cdd:cd09075   1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  103 FVYRKDAVSVVDTYLYPDPE-----DVFSREPFVVKFSAPGTgerapplpsrraltppplpaAAQNLVLIPLHAAPHQAV 177
Cdd:cd09075  81 FLFRPNKVSVLDTYQYDDGCkscgnDSFSREPAVVKFSSHST--------------------KVKEFAIVALHSAPSDAV 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  178 AEIDALYDVYLDVIDKWGTDDMLFLGDFNADCSYVRAQDWAAIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVACGARL 257
Cdd:cd09075 141 AEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLL 220
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 4503347  258 RRSLKPQSATVHDFQEEFGLDQTQALAISDHFPVEVTL 295
Cdd:cd09075 221 QSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
22-295 3.95e-28

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: 109.02  E-value: 3.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   22 LRIGAFNIQSFGDSK-VSDPACgsiIAKILAGYDLALV--QEVRD--PDLSAVSALMEQINSVSEH-EYSfVSSQPLGRD 95
Cdd:cd10283   1 LRIASWNILNFGNSKgKEKNPA---IAEIISAFDLDLIalQEVMDngGGLDALAKLVNELNKPGGTwKYI-VSDKTGGSS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   96 QYKEMYLFVYRKDAVSVVD-TYLYPD-PEDVFSREPFVVKFSAPGTGerapplpsrraltppplpaaaQNLVLIPLHAAP 173
Cdd:cd10283  77 GDKERYAFLYKSSKVRKVGkAVLEKDsNTDGFARPPYAAKFKSGGTG---------------------FDFTLVNVHLKS 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  174 HQA---------VAEIDALYDVYLDVIDKWGTDDMLFLGDFNAdcsYVRAQDWAAIRlrsSEVFKWLIPDSADTT--VGN 242
Cdd:cd10283 136 GGSsksgqgakrVAEAQALAEYLKELADEDPDDDVILLGDFNI---PADEDAFKALT---KAGFKSLLPDSTNLStsFKG 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  243 SDCAYDRIvacGARLRRSLKPQSATVHDFQEEFGLDQTQAL-------AISDHFPVEVTL 295
Cdd:cd10283 210 YANSYDNI---FVSGNLKEKFSNSGVFDFNILVDEAGEEDLdyskwrkQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
24-295 7.23e-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: 83.68  E-value: 7.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   24 IGAFNIQSFGDSKVSdpacgSIIAKIL--AGYDLALVQEVRDPDLSAVsalmeqINSVSEHEYSFVSSQPLGRDQYKEMY 101
Cdd:cd08372   1 VASYNVNGLNAATRA-----SGIARWVreLDPDIVCLQEVKDSQYSAV------ALNQLLPEGYHQYQSGPSRKEGYEGV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  102 LFVYRKDAVSVVDTYLY-PDPEDVFSREPFVVKFSAPGtgerapplpsrraltppplpaaaQNLVLIPLHAAPHQ----- 175
Cdd:cd08372  70 AILSKTPKFKIVEKHQYkFGEGDSGERRAVVVKFDVHD-----------------------KELCVVNAHLQAGGtradv 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  176 AVAEIDALYDVYLDVIDkWGTDDMLFLGDFNADCSYV-RAQDWAAIRLRSSEVFKWLIPDSA-----DTTVGNSDCAYDR 249
Cdd:cd08372 127 RDAQLKEVLEFLKRLRQ-PNSAPVVICGDFNVRPSEVdSENPSSMLRLFVALNLVDSFETLPhaytfDTYMHNVKSRLDY 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 4503347  250 IVAcgarlRRSLKPqsaTVHDFQEEFglDQTQALAISDHFPVEVTL 295
Cdd:cd08372 206 IFV-----SKSLLP---SVKSSKILS--DAARARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
27-208 2.17e-08

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: 53.00  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347     27 FNIQSFGDSKVSDPACGSIIAKILAGY--DLALVQEVRDPDLSAVSALMEqinsvseHEYSFVSSQPLGRDQYKEMYLFV 104
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALL-------AYGGFLSYGGPGGGGGGGGVAIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347    105 YRKDAVSVVDTYLYPDPEDVFSREPFVVKFSAPGTGERAPPLpsrraltppplpaaaqnlvliplHAAPHQAVAEIDALY 184
Cdd:pfam03372  76 SRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAP-----------------------HASPRLARDEQRADL 132
                         170       180
                  ....*....|....*....|....
gi 4503347    185 DVYLDVIDKWGTDDMLFLGDFNAD 208
Cdd:pfam03372 133 LLLLLALLAPRSEPVILAGDFNAD 156
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
22-297 2.03e-07

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 51.56  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   22 LRIGAFNIQSFGDSKVSDPACGSI-------------IAKILAGY--DLALVQEVRDpDLSAVSALMEQINsVSEHEYSF 86
Cdd:COG2374  69 LRVATFNVENLFDTDDDDDDFGRGadtpeeyerklakIAAAIAALdaDIVGLQEVEN-NGSALQDLVAALN-LAGGTYAF 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347   87 VSSQPlGRDQYKEMYLFVYRKDAVSVVDT------YLYPDPEDVFSREPFVVKFSAPGtGER----APPLPSRRaltpPP 156
Cdd:COG2374 147 VHPPD-GPDGDGIRVALLYRPDRVTLVGSatiadlPDSPGNPDRFSRPPLAVTFELAN-GEPftviVNHFKSKG----SD 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503347  157 LPAAAQNLVLIplhaaphQAVAEIDALYDVYLDVIDKWGTDDMLFLGDFNAdcsYVRAQDWAAIRLRSS--EVFKWLIPD 234
Cdd:COG2374 221 DPGDGQGASEA-------KRTAQAEALRAFVDSLLAADPDAPVIVLGDFND---YPFEDPLRALLGAGGltNLAEKLPAA 290
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503347  235 SADTTV--GNSdCAYDRIVACGARLRRSlkPQSATVH--------DFQEEFGLDQTQALAISDHFPVEVTLKF 297
Cdd:COG2374 291 ERYSYVydGNS-GLLDHILVSPALAARV--TGADIWHinadiyndDFKPDFRTYADDPGRASDHDPVVVGLRL 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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