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Conserved domains on  [gi|569010622|ref|XP_006528335|]
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deoxyribonuclease-1-like 1 isoform X1 [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 ...
 27-234 4.18e-91

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: 270.47  E-value: 4.18e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622    27 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK--SSRSYSFLNSS 104
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdSPNTYSYVSSE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622   105 LLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 180
Cdd:smart00476  87 PLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622   181 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRT------------------------------------------ 218
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTsptfhwlipdsadttvtsthcaydrivvagerlrssvvpgsa 246

                          250       260       270
                   ....*....|....*....|....*....|
gi 569010622   219 --------------KALRISDHYPVEVELS 234
Cdd:smart00476 247 avfdfqtayglteeEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 27-234 4.18e-91

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: 270.47  E-value: 4.18e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622    27 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK--SSRSYSFLNSS 104
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdSPNTYSYVSSE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622   105 LLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 180
Cdd:smart00476  87 PLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622   181 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRT------------------------------------------ 218
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTsptfhwlipdsadttvtsthcaydrivvagerlrssvvpgsa 246

                          250       260       270
                   ....*....|....*....|....*....|
gi 569010622   219 --------------KALRISDHYPVEVELS 234
Cdd:smart00476 247 avfdfqtayglteeEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 39-233 5.71e-91

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: 269.11  E-value: 5.71e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622  39 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKL--KSSRSYSFLNSSLLGRSTYKEKYV 116
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELnsASSNTYSYVVSERLGRSSYKEQYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 117 YIYRSDKTQVLNFYQYNDTD---DIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENV 193
Cdd:cd10282   81 FIYRSDKVSVLESYQYDDGDegtDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 194 ILLGDFNADCASLTKKRLKSLLLRT------------------------------------------------------- 218
Cdd:cd10282  161 ILLGDFNADCSYVTSKGWKSIRLRTdsrfhwligddadttvrstncaydrivvagsllqsavvpgsagvfdfdkefglte 240

                        250
                 ....*....|....*.
gi 569010622 219 -KALRISDHYPVEVEL 233
Cdd:cd10282  241 eEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 43-226 3.26e-14

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: 68.79  E-value: 3.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622   43 FNAHRLTLAKLTKESVMDTLVQILARC--DIMVLQEVVDSSQNTVPFLLQKLkssrsYSFLNSSLLGRSTYKEKYVYIYR 120
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-----GGFLSYGGPGGGGGGGGVAILSR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622  121 SDKTQVLNFYQYNDTDDIFAREPFVAHFTLPsktLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENVILLGDFN 200
Cdd:pfam03372  78 YPLSSVILVDLGEFGDPALRGAIAPFAGVLV---VPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFN 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 569010622  201 AD----CASLTKKRLKSLLLrTKALRISDH 226
Cdd:pfam03372 155 ADyilvSGGLTVLSVGVLPD-LGPRTGSDH 183
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
116-202 8.44e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 40.00  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 116 VYIYRSDK------TQVLNFYQYNDTDDIFAREPFVAHFTLPSKtlPSVVLVPLH---------------TTPKDVE--K 172
Cdd:COG2374  161 ALLYRPDRvtlvgsATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskgsddpgdgqgaSEAKRTAqaE 238

                         90       100       110
                 ....*....|....*....|....*....|
gi 569010622 173 ELNALYDvflDVYQRWQNENVILLGDFNAD 202
Cdd:COG2374  239 ALRAFVD---SLLAADPDAPVIVLGDFNDY 265
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 27-234 4.18e-91

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: 270.47  E-value: 4.18e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622    27 LLILLVGGTEAFRICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK--SSRSYSFLNSS 104
Cdd:smart00476   7 LFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdSPNTYSYVSSE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622   105 LLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDV 180
Cdd:smart00476  87 PLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDV 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622   181 FLDVYQRWQNENVILLGDFNADCASLTKKRLKSLLLRT------------------------------------------ 218
Cdd:smart00476 167 YLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTsptfhwlipdsadttvtsthcaydrivvagerlrssvvpgsa 246

                          250       260       270
                   ....*....|....*....|....*....|
gi 569010622   219 --------------KALRISDHYPVEVELS 234
Cdd:smart00476 247 avfdfqtayglteeEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 39-233 5.71e-91

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: 269.11  E-value: 5.71e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622  39 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKL--KSSRSYSFLNSSLLGRSTYKEKYV 116
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELnsASSNTYSYVVSERLGRSSYKEQYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 117 YIYRSDKTQVLNFYQYNDTD---DIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENV 193
Cdd:cd10282   81 FIYRSDKVSVLESYQYDDGDegtDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 194 ILLGDFNADCASLTKKRLKSLLLRT------------------------------------------------------- 218
Cdd:cd10282  161 ILLGDFNADCSYVTSKGWKSIRLRTdsrfhwligddadttvrstncaydrivvagsllqsavvpgsagvfdfdkefglte 240

                        250
                 ....*....|....*.
gi 569010622 219 -KALRISDHYPVEVEL 233
Cdd:cd10282  241 eEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 39-220 5.08e-39

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: 136.37  E-value: 5.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622  39 RICAFNAHRLTLAKLTKESVMDTLVQILARCDIMVLQEVVDSSQNTVPFLLQKLK--SSRSYSFLNSSLLGRSTYKEKYV 116
Cdd:cd09075    1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNqdDPNTYHYVVSEPLGRNSYKERYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 117 YIYRSDKTQVLNFYQYNDT-----DDIFAREPFVAHFTLPSKTLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNE 191
Cdd:cd09075   81 FLFRPNKVSVLDTYQYDDGckscgNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLN 160

                        170       180
                 ....*....|....*....|....*....
gi 569010622 192 NVILLGDFNADCASLTKKRLKSLLLRTKA 220
Cdd:cd09075  161 DVMLMGDFNADCSYVTSSQWSSIRLRTSS 189
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 38-221 4.12e-18

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: 81.29  E-value: 4.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622  38 FRICAFNAHRLTLAKlTKESVmDTLVQILAR--CDIMVLQEVVDSSQ--NTVPFLLQKLKSSRS-YSFLNSS-LLGRSTY 111
Cdd:cd10283    1 LRIASWNILNFGNSK-GKEKN-PAIAEIISAfdLDLIALQEVMDNGGglDALAKLVNELNKPGGtWKYIVSDkTGGSSGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 112 KEKYVYIYRSDKTQ-VLNFYQYNDT-DDIFAREPFVAHF-TLPSKTlpSVVLVPLHTTPKDV---------EKELNALYD 179
Cdd:cd10283   79 KERYAFLYKSSKVRkVGKAVLEKDSnTDGFARPPYAAKFkSGGTGF--DFTLVNVHLKSGGSsksgqgakrVAEAQALAE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 569010622 180 VFLDVYQRWQNENVILLGDFNADCAS-----LTKKRLKSLLLRTKAL 221
Cdd:cd10283  157 YLKELADEDPDDDVILLGDFNIPADEdafkaLTKAGFKSLLPDSTNL 203
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 40-228 1.20e-14

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: 71.36  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622  40 ICAFNAHRLTLAKLTKEsvmdtLVQILARC--DIMVLQEVVDSsQNTVPFLLQKLKSsrsYSFLNSSLLGRSTYKEKYVY 117
Cdd:cd08372    1 VASYNVNGLNAATRASG-----IARWVRELdpDIVCLQEVKDS-QYSAVALNQLLPE---GYHQYQSGPSRKEGYEGVAI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 118 IYRSDKTQVLNFYQYND-TDDIFAREPFVAHFTLPSKtlpSVVLVPLH-----TTPKDVEKELNALYDVFLDVyQRWQNE 191
Cdd:cd08372   72 LSKTPKFKIVEKHQYKFgEGDSGERRAVVVKFDVHDK---ELCVVNAHlqaggTRADVRDAQLKEVLEFLKRL-RQPNSA 147

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 569010622 192 NVILLGDFNADCASLTKKRLKSLLLRTKALRISDHYP 228
Cdd:cd08372  148 PVVICGDFNVRPSEVDSENPSSMLRLFVALNLVDSFE 184
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 43-226 3.26e-14

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: 68.79  E-value: 3.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622   43 FNAHRLTLAKLTKESVMDTLVQILARC--DIMVLQEVVDSSQNTVPFLLQKLkssrsYSFLNSSLLGRSTYKEKYVYIYR 120
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-----GGFLSYGGPGGGGGGGGVAILSR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622  121 SDKTQVLNFYQYNDTDDIFAREPFVAHFTLPsktLPSVVLVPLHTTPKDVEKELNALYDVFLDVYQRWQNENVILLGDFN 200
Cdd:pfam03372  78 YPLSSVILVDLGEFGDPALRGAIAPFAGVLV---VPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFN 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 569010622  201 AD----CASLTKKRLKSLLLrTKALRISDH 226
Cdd:pfam03372 155 ADyilvSGGLTVLSVGVLPD-LGPRTGSDH 183
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
116-202 8.44e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 40.00  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010622 116 VYIYRSDK------TQVLNFYQYNDTDDIFAREPFVAHFTLPSKtlPSVVLVPLH---------------TTPKDVE--K 172
Cdd:COG2374  161 ALLYRPDRvtlvgsATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskgsddpgdgqgaSEAKRTAqaE 238

                         90       100       110
                 ....*....|....*....|....*....|
gi 569010622 173 ELNALYDvflDVYQRWQNENVILLGDFNAD 202
Cdd:COG2374  239 ALRAFVD---SLLAADPDAPVIVLGDFNDY 265
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 190-234 4.48e-03

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 36.81  E-value: 4.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569010622 190 NENVILLGDFNA--------DCASLTKKRLKSLLLRtkalRISDHYPVEVELS 234
Cdd:COG3568  117 GAPVILAGDFNDidyilvspGLRVLSAEVLDSPLGR----AASDHLPVVADLE 165
 
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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