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Conserved domains on  [gi|1039798454|ref|XP_017174102|]
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deoxyribonuclease-1-like 1 isoform X3 [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

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 63-161 9.59e-49

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 cd10282:

Pssm-ID: 469791 [Multi-domain]  Cd Length: 256  Bit Score: 158.56  E-value: 9.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454  63 VQNVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQG--CQMLLKAAATFDFPKR 140
Cdd:cd10282   157 EDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKE 235

                          90       100
                  ....*....|....*....|.
gi 1039798454 141 FQLTEEEALRISDHYPVEVEL 161
Cdd:cd10282   236 FGLTEEEALAVSDHYPVEVEL 256
 
Name Accession Description Interval E-value
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 63-161 9.59e-49

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: 158.56  E-value: 9.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454  63 VQNVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQG--CQMLLKAAATFDFPKR 140
Cdd:cd10282   157 EDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKE 235

                          90       100
                  ....*....|....*....|.
gi 1039798454 141 FQLTEEEALRISDHYPVEVEL 161
Cdd:cd10282   236 FGLTEEEALAVSDHYPVEVEL 256
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 64-162 3.64e-48

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: 157.99  E-value: 3.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454   64 QNVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQGCQMLLK--AAATFDFPKRF 141
Cdd:smart00476 177 EDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSSVVpgSAAVFDFQTAY 255

                           90       100
                   ....*....|....*....|.
gi 1039798454  142 QLTEEEALRISDHYPVEVELS 162
Cdd:smart00476 256 GLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 63-161 9.59e-49

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: 158.56  E-value: 9.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454  63 VQNVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQG--CQMLLKAAATFDFPKR 140
Cdd:cd10282   157 EDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKE 235

                          90       100
                  ....*....|....*....|.
gi 1039798454 141 FQLTEEEALRISDHYPVEVEL 161
Cdd:cd10282   236 FGLTEEEALAVSDHYPVEVEL 256
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 64-162 3.64e-48

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: 157.99  E-value: 3.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454   64 QNVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQGCQMLLK--AAATFDFPKRF 141
Cdd:smart00476 177 EDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSSVVpgSAAVFDFQTAY 255

                           90       100
                   ....*....|....*....|.
gi 1039798454  142 QLTEEEALRISDHYPVEVELS 162
Cdd:smart00476 256 GLTEEEALAISDHFPVEVTLK 276
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 65-161 9.49e-25

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: 96.70  E-value: 9.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454  65 NVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVrASTNCTYDRIVVHGQGCQ--MLLKAAATFDFPKRFQ 142
Cdd:cd09075   161 DVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTA-TSTNCAYDRIVVAGSLLQssVVPGSAAPFDFQAAYG 239

                          90
                  ....*....|....*....
gi 1039798454 143 LTEEEALRISDHYPVEVEL 161
Cdd:cd09075   240 LSNEMALAISDHYPVEVTL 258
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 65-161 1.58e-10

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: 58.26  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454  65 NVILLGDFNADCASLTKKRLKSLL-LRTKAGFHWVIPDGEDT----TVRASTNCTYDRIVVHGqgcQMLLKaaatfdfPK 139
Cdd:cd08372   148 PVVICGDFNVRPSEVDSENPSSMLrLFVALNLVDSFETLPHAytfdTYMHNVKSRLDYIFVSK---SLLPS-------VK 217

                          90       100
                  ....*....|....*....|....
gi 1039798454 140 RFQLT--EEEALRISDHYPVEVEL 161
Cdd:cd08372   218 SSKILsdAARARIPSDHYPIEVTL 241
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 64-161 1.45e-08

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: 52.79  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454  64 QNVILLGDFNADCASLTKKRLkslllrTKAGFHWVIPDGEDTTvrASTNC---TYDRIVVHGQGCQMLLkAAATFDFPKR 140
Cdd:cd10283   168 DDVILLGDFNIPADEDAFKAL------TKAGFKSLLPDSTNLS--TSFKGyanSYDNIFVSGNLKEKFS-NSGVFDFNIL 238

                          90       100
                  ....*....|....*....|....*...
gi 1039798454 141 FQLTEEEAL-------RISDHYPVEVEL 161
Cdd:cd10283   239 VDEAGEEDLdyskwrkQISDHDPVWVEF 266
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 10-161 1.53e-03

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 38.09  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454  10 WRVPDAHIAM-RGLVMAPLLIllvGGTEAFRICafNAH---------------RLTLAKLTKESVMDtlvqNVILLGDFN 73
Cdd:cd09080    85 RRVPFTSTRMgRNLLAAEINL---GSGEPLRLA--TTHleslkshssertaqlEEIAKKLKKPPGAA----NVILGGDFN 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798454  74 ADCAS----LTKKRL----KSLLLRTKAGFHWvipDGEDTTVRASTN----CTYDRIVVHGQGCQmllkaaatfdfPKRF 141
Cdd:cd09080   156 LRDKEddtgGLPNGFvdawEELGPPGEPGYTW---DTQKNPMLRKGEagprKRFDRVLLRGSDLK-----------PKSI 221

                         170       180
                  ....*....|....*....|....*..
gi 1039798454 142 QLTEEEALRI-------SDHYPVEVEL 161
Cdd:cd09080   222 ELIGTEPIPGdeeglfpSDHFGLLAEL 248
 
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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