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Conserved domains on  [gi|1677501223|ref|NP_001357716|]
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deoxyribonuclease-1-like 1 isoform 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

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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 ...
9-245 2.25e-113

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: 327.09  E-value: 2.25e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223    9 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK------------- 75
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsse 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223   76 ---------------RSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 136
Cdd:smart00476  87 plgrnsykeqylflyRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  137 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQGCQMLLK--A 214
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSSVVpgS 245
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1677501223  215 AATFDFPKRFQLTEEEALRISDHYPVEVELS 245
Cdd:smart00476 246 AAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
9-245 2.25e-113

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: 327.09  E-value: 2.25e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223    9 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK------------- 75
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsse 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223   76 ---------------RSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 136
Cdd:smart00476  87 plgrnsykeqylflyRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  137 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQGCQMLLK--A 214
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSSVVpgS 245
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1677501223  215 AATFDFPKRFQLTEEEALRISDHYPVEVELS 245
Cdd:smart00476 246 AAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
21-244 4.31e-110

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: 318.03  E-value: 4.31e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  21 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK------------------------- 75
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNsassntysyvvserlgrssykeqya 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  76 ---RSDKTQVLNFYQYNDTD---DIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENV 149
Cdd:cd10282    81 fiyRSDKVSVLESYQYDDGDegtDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223 150 ILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQG--CQMLLKAAATFDFPKRFQLT 227
Cdd:cd10282   161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKEFGLT 239
                         250
                  ....*....|....*..
gi 1677501223 228 EEEALRISDHYPVEVEL 244
Cdd:cd10282   240 EEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
25-158 9.90e-10

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: 56.46  E-value: 9.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  25 FNAHRLTLAKLTKESVMDTLVQILARC--DIMVLQEVVDSSQNTVPFLLQKLKRSD------------------KTQVLN 84
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGGFLsyggpggggggggvailsRYPLSS 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677501223  85 FYQYNDTDDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENVILLGDFNAD 158
Cdd:pfam03372  83 VILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNAD 156
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
52-245 1.75e-03

Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 39.21  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  52 DIMVLQEVVDSSQNTVPFLLQKLKrsdktqvlnfYQYNDTDD------IFAREPF----------------VAHFTLPSK 109
Cdd:COG3021   122 DVLVLQETTPAWEEALAALEADYP----------YRVLCPLDnaygmaLLSRLPLteaevvylvgddipsiRATVELPGG 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223 110 TlpsVVLVPLHTTP-----KDVEKELNALYDvfldvYQRWQNENVILLGDFNADCASLTKKRLKSL--LLRTKAGFHWVi 182
Cdd:COG3021   192 P---VRLVAVHPAPpvggsAERDAELAALAK-----AVAALDGPVIVAGDFNATPWSPTLRRLLRAsgLRDARAGRGLG- 262
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677501223 183 pdgedttvrastnCTYDRivvhgqgcqMLLKAAATFD---FPKRFQLTEEEALRI--SDHYPVEVELS 245
Cdd:COG3021   263 -------------PTWPA---------NLPFLRLPIDhvlVSRGLTVVDVRVLPVigSDHRPLLAELA 308
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
9-245 2.25e-113

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: 327.09  E-value: 2.25e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223    9 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK------------- 75
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsse 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223   76 ---------------RSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 136
Cdd:smart00476  87 plgrnsykeqylflyRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  137 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQGCQMLLK--A 214
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSSVVpgS 245
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1677501223  215 AATFDFPKRFQLTEEEALRISDHYPVEVELS 245
Cdd:smart00476 246 AAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
21-244 4.31e-110

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: 318.03  E-value: 4.31e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  21 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK------------------------- 75
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNsassntysyvvserlgrssykeqya 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  76 ---RSDKTQVLNFYQYNDTD---DIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENV 149
Cdd:cd10282    81 fiyRSDKVSVLESYQYDDGDegtDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223 150 ILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVVHGQG--CQMLLKAAATFDFPKRFQLT 227
Cdd:cd10282   161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKEFGLT 239
                         250
                  ....*....|....*..
gi 1677501223 228 EEEALRISDHYPVEVEL 244
Cdd:cd10282   240 EEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
21-244 1.15e-50

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: 166.81  E-value: 1.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  21 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLKRSD---------------------- 78
Cdd:cd09075     1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDpntyhyvvseplgrnsykeryl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  79 ------KTQVLNFYQYNDT-----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNE 147
Cdd:cd09075    81 flfrpnKVSVLDTYQYDDGckscgNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223 148 NVILLGDFNADCASLTKKRLKSLLLRTKAGFHWVIPDGEDTTVrASTNCTYDRIVVHGQGCQ--MLLKAAATFDFPKRFQ 225
Cdd:cd09075   161 DVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTA-TSTNCAYDRIVVAGSLLQssVVPGSAAPFDFQAAYG 239
                         250
                  ....*....|....*....
gi 1677501223 226 LTEEEALRISDHYPVEVEL 244
Cdd:cd09075   240 LSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
20-244 4.42e-17

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: 78.59  E-value: 4.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  20 FRICAFNAHRLTLAKlTKESVmDTLVQILAR--CDIMVLQEVVDSSQ--NTVPFLLQKLKR---------SDKTQ----- 81
Cdd:cd10283     1 LRIASWNILNFGNSK-GKEKN-PAIAEIISAfdLDLIALQEVMDNGGglDALAKLVNELNKpggtwkyivSDKTGgssgd 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  82 ---------------VLNFYQYNDT-DDIFAREPFVAHF-TLPSKTlpSVVLVPLHTTPKDV---------EKELNALYD 135
Cdd:cd10283    79 keryaflyksskvrkVGKAVLEKDSnTDGFARPPYAAKFkSGGTGF--DFTLVNVHLKSGGSsksgqgakrVAEAQALAE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223 136 VFLDVYQRWQNENVILLGDFNADCASLTKKRLkslllrTKAGFHWVIPDGEDTTvrASTNC---TYDRIVVHGQGCQMlL 212
Cdd:cd10283   157 YLKELADEDPDDDVILLGDFNIPADEDAFKAL------TKAGFKSLLPDSTNLS--TSFKGyanSYDNIFVSGNLKEK-F 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1677501223 213 KAAATFDFPKRFQLTEEEAL-------RISDHYPVEVEL 244
Cdd:cd10283   228 SNSGVFDFNILVDEAGEEDLdyskwrkQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
22-244 4.89e-17

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: 77.91  E-value: 4.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  22 ICAFNAHRLTLAKLTKEsvmdtLVQILARC--DIMVLQEVVDSsQNTVPFLLQKLK-----------------------R 76
Cdd:cd08372     1 VASYNVNGLNAATRASG-----IARWVRELdpDIVCLQEVKDS-QYSAVALNQLLPegyhqyqsgpsrkegyegvailsK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  77 SDKTQVLNFYQYND-TDDIFAREPFVAHFTLPSKtlpSVVLVPLH-----TTPKDVEKELNALYDVFLDVyQRWQNENVI 150
Cdd:cd08372    75 TPKFKIVEKHQYKFgEGDSGERRAVVVKFDVHDK---ELCVVNAHlqaggTRADVRDAQLKEVLEFLKRL-RQPNSAPVV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223 151 LLGDFNADCASLTKKRLKSLL-LRTKAGFHWVIPDGEDT----TVRASTNCTYDRIVVHGqgcQMLLKaaatfdfPKRFQ 225
Cdd:cd08372   151 ICGDFNVRPSEVDSENPSSMLrLFVALNLVDSFETLPHAytfdTYMHNVKSRLDYIFVSK---SLLPS-------VKSSK 220
                         250       260
                  ....*....|....*....|.
gi 1677501223 226 LT--EEEALRISDHYPVEVEL 244
Cdd:cd08372   221 ILsdAARARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
25-158 9.90e-10

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: 56.46  E-value: 9.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  25 FNAHRLTLAKLTKESVMDTLVQILARC--DIMVLQEVVDSSQNTVPFLLQKLKRSD------------------KTQVLN 84
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGGFLsyggpggggggggvailsRYPLSS 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677501223  85 FYQYNDTDDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENVILLGDFNAD 158
Cdd:pfam03372  83 VILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNAD 156
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
52-245 1.75e-03

Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 39.21  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  52 DIMVLQEVVDSSQNTVPFLLQKLKrsdktqvlnfYQYNDTDD------IFAREPF----------------VAHFTLPSK 109
Cdd:COG3021   122 DVLVLQETTPAWEEALAALEADYP----------YRVLCPLDnaygmaLLSRLPLteaevvylvgddipsiRATVELPGG 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223 110 TlpsVVLVPLHTTP-----KDVEKELNALYDvfldvYQRWQNENVILLGDFNADCASLTKKRLKSL--LLRTKAGFHWVi 182
Cdd:COG3021   192 P---VRLVAVHPAPpvggsAERDAELAALAK-----AVAALDGPVIVAGDFNATPWSPTLRRLLRAsgLRDARAGRGLG- 262
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677501223 183 pdgedttvrastnCTYDRivvhgqgcqMLLKAAATFD---FPKRFQLTEEEALRI--SDHYPVEVELS 245
Cdd:COG3021   263 -------------PTWPA---------NLPFLRLPIDhvlVSRGLTVVDVRVLPVigSDHRPLLAELA 308
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
72-244 7.99e-03

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 37.31  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223  72 QKLKRSDKTQVLNFYQYNDTDDIFAREPFVAHFTLPSKtlPSVVLVPLH---------------TTPKDVE--KELNALY 134
Cdd:COG2374   167 DRVTLVGSATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskgsddpgdgqgaSEAKRTAqaEALRAFV 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501223 135 DvflDVYQRWQNENVILLGDFNADCASltkkrlKSLLLRTKAGFHWVIPDGEDTTVRASTN-----CTYDRIVV------ 203
Cdd:COG2374   245 D---SLLAADPDAPVIVLGDFNDYPFE------DPLRALLGAGGLTNLAEKLPAAERYSYVydgnsGLLDHILVspalaa 315
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1677501223 204 HGQGCQMLLKAAATF--DFPKRFQLTEEEALRISDHYPVEVEL 244
Cdd:COG2374   316 RVTGADIWHINADIYndDFKPDFRTYADDPGRASDHDPVVVGL 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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