NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|148539953|ref|NP_079994|]
View 

deoxyribonuclease-1-like 2 precursor [Mus musculus]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
7-276 9.63e-160

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


The actual alignment was detected with superfamily member smart00476:

Pssm-ID: 469791  Cd Length: 276  Bit Score: 444.96  E-value: 9.63e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953     7 PLTAVWALGVMGATALRIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGF 86
Cdd:smart00476   3 PSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953    87 VSSKPLGRDQYKEMYLFVYRKDVASVVSTYQYPD----PEDAFSREPFVVKFSVPSCATKELVLIPLHAAPHQAVAEIDA 162
Cdd:smart00476  83 VSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953   163 LYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVVSGAHLRRSLK 242
Cdd:smart00476 163 LYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVV 242
                          250       260       270
                   ....*....|....*....|....*....|....
gi 148539953   243 PHSASVHNFQEEFDLDQTQALAISDHFPVEVTFK 276
Cdd:smart00476 243 PGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
7-276 9.63e-160

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


Pssm-ID: 128752  Cd Length: 276  Bit Score: 444.96  E-value: 9.63e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953     7 PLTAVWALGVMGATALRIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGF 86
Cdd:smart00476   3 PSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953    87 VSSKPLGRDQYKEMYLFVYRKDVASVVSTYQYPD----PEDAFSREPFVVKFSVPSCATKELVLIPLHAAPHQAVAEIDA 162
Cdd:smart00476  83 VSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953   163 LYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVVSGAHLRRSLK 242
Cdd:smart00476 163 LYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVV 242
                          250       260       270
                   ....*....|....*....|....*....|....
gi 148539953   243 PHSASVHNFQEEFDLDQTQALAISDHFPVEVTFK 276
Cdd:smart00476 243 PGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
23-275 2.96e-140

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: 394.68  E-value: 2.96e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  23 RIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGFVSSKPLGRDQYKEMYL 102
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 103 FVYRKDVASVVSTYQYPD---PEDAFSREPFVVKFSVPSCATKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTDDM 179
Cdd:cd10282   81 FIYRSDKVSVLESYQYDDgdeGTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 180 LFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVVSGAHLRRSLKPHSASVHNFQEEFDLDQ 259
Cdd:cd10282  161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGLTE 240
                        250
                 ....*....|....*.
gi 148539953 260 TQALAISDHFPVEVTF 275
Cdd:cd10282  241 EEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
27-188 1.69e-12

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: 64.55  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953   27 FNVQSFGDNKVSDPDCGSVIAQILAGY--DIALVQEVRDPDLSAVSLLMeqinrvsKHEYGFVSSKPLGRDQYKEMYLFV 104
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLAL-------LAYGGFLSYGGPGGGGGGGGVAIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  105 YRKDVASVVstyQYPDPEDAFSREPFVVKFSVPSCATKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTDDMLFLGD 184
Cdd:pfam03372  76 SRYPLSSVI---LVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGD 152

                  ....
gi 148539953  185 FNAD 188
Cdd:pfam03372 153 FNAD 156
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
19-276 2.02e-11

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 63.50  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  19 ATALRIGAFNVQSFGDNKVSDPDCGS-----------------VIAQILAgyDIALVQEVRDpDLSAVSLLMEQINrVSK 81
Cdd:COG2374   66 GGDLRVATFNVENLFDTDDDDDDFGRgadtpeeyerklakiaaAIAALDA--DIVGLQEVEN-NGSALQDLVAALN-LAG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  82 HEYGFVSSKPlGRDQYKEMYLFVYRKDVASVVSTYQY------PDPEDAFSREPFVVKFSVPScaTKELVLIPLH----- 150
Cdd:COG2374  142 GTYAFVHPPD-GPDGDGIRVALLYRPDRVTLVGSATIadlpdsPGNPDRFSRPPLAVTFELAN--GEPFTVIVNHfkskg 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 151 ---AAPHQA------VAEIDALYDVYLDVIDKWNTDDMLFLGDFNADckyvkAHDwPSIR-LRSSE----VFKWLIPDSA 216
Cdd:COG2374  219 sddPGDGQGaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDY-----PFE-DPLRaLLGAGgltnLAEKLPAAER 292
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539953 217 DTTV--GNSdCAYDRIVVSGAHLRRSLKPH----SASVHN--FQEEFDLDQTQALAISDHFPVEVTFK 276
Cdd:COG2374  293 YSYVydGNS-GLLDHILVSPALAARVTGADiwhiNADIYNddFKPDFRTYADDPGRASDHDPVVVGLR 359
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
7-276 9.63e-160

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


Pssm-ID: 128752  Cd Length: 276  Bit Score: 444.96  E-value: 9.63e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953     7 PLTAVWALGVMGATALRIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGF 86
Cdd:smart00476   3 PSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953    87 VSSKPLGRDQYKEMYLFVYRKDVASVVSTYQYPD----PEDAFSREPFVVKFSVPSCATKELVLIPLHAAPHQAVAEIDA 162
Cdd:smart00476  83 VSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953   163 LYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVVSGAHLRRSLK 242
Cdd:smart00476 163 LYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVV 242
                          250       260       270
                   ....*....|....*....|....*....|....
gi 148539953   243 PHSASVHNFQEEFDLDQTQALAISDHFPVEVTFK 276
Cdd:smart00476 243 PGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
23-275 2.96e-140

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: 394.68  E-value: 2.96e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  23 RIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGFVSSKPLGRDQYKEMYL 102
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 103 FVYRKDVASVVSTYQYPD---PEDAFSREPFVVKFSVPSCATKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTDDM 179
Cdd:cd10282   81 FIYRSDKVSVLESYQYDDgdeGTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 180 LFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVVSGAHLRRSLKPHSASVHNFQEEFDLDQ 259
Cdd:cd10282  161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGLTE 240
                        250
                 ....*....|....*.
gi 148539953 260 TQALAISDHFPVEVTF 275
Cdd:cd10282  241 EEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
23-275 7.35e-83

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: 249.62  E-value: 7.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  23 RIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGFVSSKPLGRDQYKEMYL 102
Cdd:cd09075    1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 103 FVYRKDVASVVSTYQYPDPE-----DAFSREPFVVKFSVPSCATKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTD 177
Cdd:cd09075   81 FLFRPNKVSVLDTYQYDDGCkscgnDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 178 DMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVVSGAHLRRSLKPHSASVHNFQEEFDL 257
Cdd:cd09075  161 DVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGL 240
                        250
                 ....*....|....*...
gi 148539953 258 DQTQALAISDHFPVEVTF 275
Cdd:cd09075  241 SNEMALAISDHYPVEVTL 258
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
24-274 4.16e-26

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: 102.56  E-value: 4.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  24 IGAFNVQSFGDNKVSdpdcgSVIAQIL--AGYDIALVQEVRDPDLSAVSLLMEQINRVskheYGFVSskPLGRDQYKEMY 101
Cdd:cd08372    1 VASYNVNGLNAATRA-----SGIARWVreLDPDIVCLQEVKDSQYSAVALNQLLPEGY----HQYQS--GPSRKEGYEGV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 102 LFVYRKDVASVVSTYQY-PDPEDAFSREPFVVKFSvpsCATKELVLIPLHAAPHQ-----AVAEIDALYDVYLDVIDkWN 175
Cdd:cd08372   70 AILSKTPKFKIVEKHQYkFGEGDSGERRAVVVKFD---VHDKELCVVNAHLQAGGtradvRDAQLKEVLEFLKRLRQ-PN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 176 TDDMLFLGDFNADCKYVKAHDWPS-IRLRSSEVFKWLIPDSA-----DTTVGNSDCAYDRIVVSGAHLrrsLKPHSASVH 249
Cdd:cd08372  146 SAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFETLPhaytfDTYMHNVKSRLDYIFVSKSLL---PSVKSSKIL 222
                        250       260
                 ....*....|....*....|....*
gi 148539953 250 NfqeefdlDQTQALAISDHFPVEVT 274
Cdd:cd08372  223 S-------DAARARIPSDHYPIEVT 240
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
22-275 4.72e-25

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: 100.55  E-value: 4.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  22 LRIGAFNVQSFGDNK-VSDPDCgsvIAQILAGYDIALV--QEVRD--PDLSAVSLLMEQINRVSKHeYGFV-SSKPLGRD 95
Cdd:cd10283    1 LRIASWNILNFGNSKgKEKNPA---IAEIISAFDLDLIalQEVMDngGGLDALAKLVNELNKPGGT-WKYIvSDKTGGSS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  96 QYKEMYLFVYRKD-VASVVSTYQYPD-PEDAFSREPFVVKFSVPScATKELVLIPLHAAPHQA---------VAEIDALY 164
Cdd:cd10283   77 GDKERYAFLYKSSkVRKVGKAVLEKDsNTDGFARPPYAAKFKSGG-TGFDFTLVNVHLKSGGSsksgqgakrVAEAQALA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 165 DVYLDVIDKWNTDDMLFLGDFNAdckYVKAHDWPSIRlrsSEVFKWLIPDSADTT--VGNSDCAYDRIVVSGAHL----R 238
Cdd:cd10283  156 EYLKELADEDPDDDVILLGDFNI---PADEDAFKALT---KAGFKSLLPDSTNLStsFKGYANSYDNIFVSGNLKekfsN 229
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148539953 239 RSLKPHSASVHNFQEEFDLDQTQALAISDHFPVEVTF 275
Cdd:cd10283  230 SGVFDFNILVDEAGEEDLDYSKWRKQISDHDPVWVEF 266
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
27-188 1.69e-12

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: 64.55  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953   27 FNVQSFGDNKVSDPDCGSVIAQILAGY--DIALVQEVRDPDLSAVSLLMeqinrvsKHEYGFVSSKPLGRDQYKEMYLFV 104
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLAL-------LAYGGFLSYGGPGGGGGGGGVAIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  105 YRKDVASVVstyQYPDPEDAFSREPFVVKFSVPSCATKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTDDMLFLGD 184
Cdd:pfam03372  76 SRYPLSSVI---LVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGD 152

                  ....
gi 148539953  185 FNAD 188
Cdd:pfam03372 153 FNAD 156
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
19-276 2.02e-11

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 63.50  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  19 ATALRIGAFNVQSFGDNKVSDPDCGS-----------------VIAQILAgyDIALVQEVRDpDLSAVSLLMEQINrVSK 81
Cdd:COG2374   66 GGDLRVATFNVENLFDTDDDDDDFGRgadtpeeyerklakiaaAIAALDA--DIVGLQEVEN-NGSALQDLVAALN-LAG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  82 HEYGFVSSKPlGRDQYKEMYLFVYRKDVASVVSTYQY------PDPEDAFSREPFVVKFSVPScaTKELVLIPLH----- 150
Cdd:COG2374  142 GTYAFVHPPD-GPDGDGIRVALLYRPDRVTLVGSATIadlpdsPGNPDRFSRPPLAVTFELAN--GEPFTVIVNHfkskg 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 151 ---AAPHQA------VAEIDALYDVYLDVIDKWNTDDMLFLGDFNADckyvkAHDwPSIR-LRSSE----VFKWLIPDSA 216
Cdd:COG2374  219 sddPGDGQGaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDY-----PFE-DPLRaLLGAGgltnLAEKLPAAER 292
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539953 217 DTTV--GNSdCAYDRIVVSGAHLRRSLKPH----SASVHN--FQEEFDLDQTQALAISDHFPVEVTFK 276
Cdd:COG2374  293 YSYVydGNS-GLLDHILVSPALAARVTGADiwhiNADIYNddFKPDFRTYADDPGRASDHDPVVVGLR 359
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
18-276 2.53e-03

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 37.58  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  18 GATALRIGAFNVQS-FGDNKVSDPDcgsVIAQILA--GYDIALVQEVrdpdlsavsllmeqinrvskheyGFVSSKPLGR 94
Cdd:COG3568    4 AAATLRVMTYNIRYgLGTDGRADLE---RIARVIRalDPDVVALQEN-----------------------AILSRYPIVS 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  95 dqykemylfvyrkdvasvVSTYQYPDPEDAfSREPFVVKFSVPScatKELVLIPLH---AAPHQAVAEIDALydvyLDVI 171
Cdd:COG3568   58 ------------------SGTFDLPDPGGE-PRGALWADVDVPG---KPLRVVNTHldlRSAAARRRQARAL----AELL 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 172 DKWNTDD-MLFLGDFNAdckyvkahdwpsirlrssevfkwlipdsadttvgnsdcaYDRIVVSGahlrrSLKPHSASVHn 250
Cdd:COG3568  112 AELPAGApVILAGDFND---------------------------------------IDYILVSP-----GLRVLSAEVL- 146
                        250       260
                 ....*....|....*....|....*.
gi 148539953 251 fqeefdlDQTQALAISDHFPVEVTFK 276
Cdd:COG3568  147 -------DSPLGRAASDHLPVVADLE 165
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
24-187 4.16e-03

Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-clade. 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: 197310 [Multi-domain]  Cd Length: 236  Bit Score: 37.72  E-value: 4.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953  24 IGAFNVQSFGDNKVSDpdcgSVIAQI-LAGYDIALVQEVRDPDlsavsllMEQINRVSKHEYGFVSSKPLGRdqykemyl 102
Cdd:cd09076    1 IGTLNVRGLRSPGKRA----QLLEELkRKKLDILGLQETHWTG-------EGELKKKREGGTILYSGSDSGK-------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539953 103 fvyRKDVASVVSTYQYPDPEDAFSREP---FVVKFSVPScatKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTDDM 179
Cdd:cd09076   62 ---SRGVAILLSKTAANKLLEYTKVVSgriIMVRFKIKG---KRLTIINVYAPTARDEEEKEEFYDQLQDVLDKVPRHDT 135

                 ....*....
gi 148539953 180 LFL-GDFNA 187
Cdd:cd09076  136 LIIgGDFNA 144
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH