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Conserved domains on  [gi|1677498123|ref|NP_081385|]
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deoxyribonuclease-1-like 1 isoform 1 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

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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 ...
9-271 4.95e-131

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: 372.93  E-value: 4.95e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123    9 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK--SSRSYSFLNSS 86
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdSPNTYSYVSSE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123   87 LLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 162
Cdd:smart00476  87 PLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  163 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQGCQMLLK--A 240
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSSVVpgS 245
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1677498123  241 AATFDFPKRFQLTEEEALRISDHYPVEVELS 271
Cdd:smart00476 246 AAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
9-271 4.95e-131

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: 372.93  E-value: 4.95e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123    9 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK--SSRSYSFLNSS 86
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdSPNTYSYVSSE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123   87 LLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 162
Cdd:smart00476  87 PLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  163 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQGCQMLLK--A 240
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSSVVpgS 245
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1677498123  241 AATFDFPKRFQLTEEEALRISDHYPVEVELS 271
Cdd:smart00476 246 AAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
21-270 3.42e-130

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: 370.03  E-value: 3.42e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  21 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKL--KSSRSYSFLNSSLLGRSTYKEKYV 98
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELnsASSNTYSYVVSERLGRSSYKEQYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  99 YIYRSDKTQVLNFYQYNDTD---DIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENV 175
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDegtDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 176 ILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQG--CQMLLKAAATFDFPKRFQLT 253
Cdd:cd10282   161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKEFGLT 239
                         250
                  ....*....|....*..
gi 1677498123 254 EEEALRISDHYPVEVEL 270
Cdd:cd10282   240 EEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
25-184 5.73e-13

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: 66.09  E-value: 5.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  25 FNAHRLTLAKLTKESVMDTLVQILARC--DIMVLQEVVDSSQNTVPFLLQKLkssrsYSFLNSSLLGRSTYKEKYVYIYR 102
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-----GGFLSYGGPGGGGGGGGVAILSR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 103 SDKTQVLNFYQYNDTDDIFAREPFVAHFTLPsktLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENVILLGDFN 182
Cdd:pfam03372  78 YPLSSVILVDLGEFGDPALRGAIAPFAGVLV---VPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFN 154

                  ..
gi 1677498123 183 AD 184
Cdd:pfam03372 155 AD 156
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
98-270 8.33e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 40.39  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  98 VYIYRSDK------TQVLNFYQYNDTDDIFAREPFVAHFTLPSKtlPSVVLVPLH---------------TTPKDVE--K 154
Cdd:COG2374   161 ALLYRPDRvtlvgsATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskgsddpgdgqgaSEAKRTAqaE 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 155 ELNALYDvflDVYQRWQNENVILLGDFNADCASltkkrlKSLLLRTKAGFHWVIPDGEDTTVRASTN-----CTYDRIVV 229
Cdd:COG2374   239 ALRAFVD---SLLAADPDAPVIVLGDFNDYPFE------DPLRALLGAGGLTNLAEKLPAAERYSYVydgnsGLLDHILV 309
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1677498123 230 ------HGQGCQMLLKAAATF--DFPKRFQLTEEEALRISDHYPVEVEL 270
Cdd:COG2374   310 spalaaRVTGADIWHINADIYndDFKPDFRTYADDPGRASDHDPVVVGL 358
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
9-271 4.95e-131

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: 372.93  E-value: 4.95e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123    9 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK--SSRSYSFLNSS 86
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdSPNTYSYVSSE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123   87 LLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 162
Cdd:smart00476  87 PLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  163 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQGCQMLLK--A 240
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSSVVpgS 245
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1677498123  241 AATFDFPKRFQLTEEEALRISDHYPVEVELS 271
Cdd:smart00476 246 AAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
21-270 3.42e-130

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: 370.03  E-value: 3.42e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  21 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKL--KSSRSYSFLNSSLLGRSTYKEKYV 98
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELnsASSNTYSYVVSERLGRSSYKEQYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  99 YIYRSDKTQVLNFYQYNDTD---DIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENV 175
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDegtDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 176 ILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQG--CQMLLKAAATFDFPKRFQLT 253
Cdd:cd10282   161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKEFGLT 239
                         250
                  ....*....|....*..
gi 1677498123 254 EEEALRISDHYPVEVEL 270
Cdd:cd10282   240 EEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
21-270 4.64e-62

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: 197.24  E-value: 4.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  21 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK--SSRSYSFLNSSLLGRSTYKEKYV 98
Cdd:cd09075     1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNqdDPNTYHYVVSEPLGRNSYKERYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  99 YIYRSDKTQVLNFYQYNDT-----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNE 173
Cdd:cd09075    81 FLFRPNKVSVLDTYQYDDGckscgNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 174 NVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVrASTNCTYDRIVVHGQGCQ--MLLKAAATFDFPKRFQ 251
Cdd:cd09075   161 DVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTA-TSTNCAYDRIVVAGSLLQssVVPGSAAPFDFQAAYG 239
                         250
                  ....*....|....*....
gi 1677498123 252 LTEEEALRISDHYPVEVEL 270
Cdd:cd09075   240 LSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
20-270 4.14e-26

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: 103.63  E-value: 4.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  20 FRICAFNAHRLTLAKlTKESVmDTLVQILAR--CDIMVLQEVVDSSQ--NTVPFLLQKLKSSRS-YSFLNSS-LLGRSTY 93
Cdd:cd10283     1 LRIASWNILNFGNSK-GKEKN-PAIAEIISAfdLDLIALQEVMDNGGglDALAKLVNELNKPGGtWKYIVSDkTGGSSGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  94 KEKYVYIYRSDKTQ-VLNFYQYNDT-DDIFAREPFVAHF-TLPSKTlpSVVLVPLHTTPKDV---------EKELNALYD 161
Cdd:cd10283    79 KERYAFLYKSSKVRkVGKAVLEKDSnTDGFARPPYAAKFkSGGTGF--DFTLVNVHLKSGGSsksgqgakrVAEAQALAE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 162 VFLDVYQRWQNENVILLGDFNADCASLTKKRLkslllrTKAGFHWVIPDGEDTTvrASTNC---TYDRIVVHGQGCQMlL 238
Cdd:cd10283   157 YLKELADEDPDDDVILLGDFNIPADEDAFKAL------TKAGFKSLLPDSTNLS--TSFKGyanSYDNIFVSGNLKEK-F 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1677498123 239 KAAATFDFPKRFQLTEEEAL-------RISDHYPVEVEL 270
Cdd:cd10283   228 SNSGVFDFNILVDEAGEEDLdyskwrkQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
22-270 2.06e-21

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: 90.62  E-value: 2.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  22 ICAFNAHRLTLAKLTKEsvmdtLVQILARC--DIMVLQEVVDSsQNTVPFLLQKLKSsrsYSFLNSSLLGRSTYKEKYVY 99
Cdd:cd08372     1 VASYNVNGLNAATRASG-----IARWVRELdpDIVCLQEVKDS-QYSAVALNQLLPE---GYHQYQSGPSRKEGYEGVAI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 100 IYRSDKTQVLNFYQYND-TDDIFAREPFVAHFTLPSKtlpSVVLVPLH-----TTPKDVEKELNALYDVFLDVyQRWQNE 173
Cdd:cd08372    72 LSKTPKFKIVEKHQYKFgEGDSGERRAVVVKFDVHDK---ELCVVNAHlqaggTRADVRDAQLKEVLEFLKRL-RQPNSA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 174 NVILLGDFNADCASLTKKRLKSLL-LRTKAGFHWVIPDGEDT----TVRASTNCTYDRIVVHGqgcQMLLKaaatfdfPK 248
Cdd:cd08372   148 PVVICGDFNVRPSEVDSENPSSMLrLFVALNLVDSFETLPHAytfdTYMHNVKSRLDYIFVSK---SLLPS-------VK 217
                         250       260
                  ....*....|....*....|....
gi 1677498123 249 RFQLT--EEEALRISDHYPVEVEL 270
Cdd:cd08372   218 SSKILsdAARARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
25-184 5.73e-13

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: 66.09  E-value: 5.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  25 FNAHRLTLAKLTKESVMDTLVQILARC--DIMVLQEVVDSSQNTVPFLLQKLkssrsYSFLNSSLLGRSTYKEKYVYIYR 102
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-----GGFLSYGGPGGGGGGGGVAILSR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 103 SDKTQVLNFYQYNDTDDIFAREPFVAHFTLPsktLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENVILLGDFN 182
Cdd:pfam03372  78 YPLSSVILVDLGEFGDPALRGAIAPFAGVLV---VPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFN 154

                  ..
gi 1677498123 183 AD 184
Cdd:pfam03372 155 AD 156
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
98-270 8.33e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 40.39  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123  98 VYIYRSDK------TQVLNFYQYNDTDDIFAREPFVAHFTLPSKtlPSVVLVPLH---------------TTPKDVE--K 154
Cdd:COG2374   161 ALLYRPDRvtlvgsATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskgsddpgdgqgaSEAKRTAqaE 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677498123 155 ELNALYDvflDVYQRWQNENVILLGDFNADCASltkkrlKSLLLRTKAGFHWVIPDGEDTTVRASTN-----CTYDRIVV 229
Cdd:COG2374   239 ALRAFVD---SLLAADPDAPVIVLGDFNDYPFE------DPLRALLGAGGLTNLAEKLPAAERYSYVydgnsGLLDHILV 309
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1677498123 230 ------HGQGCQMLLKAAATF--DFPKRFQLTEEEALRISDHYPVEVEL 270
Cdd:COG2374   310 spalaaRVTGADIWHINADIYndDFKPDFRTYADDPGRASDHDPVVVGL 358
 
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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