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Conserved domains on  [gi|84662732|ref|NP_001014245|]
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deoxyribonuclease-1-like 1 precursor [Rattus norvegicus]

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 ...
 24-288 6.96e-130

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: 371.00  E-value: 6.96e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732     24 VASLL--ILLVGGTDAFRICAFNAHRLTLTKVIKESVMDTLVQILARCDIMVLQEVVDSSQNTVLFLLQKL--QSSKSYS 99
Cdd:smart00476   2 VPSLLlfLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLnsDSPNTYS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732    100 FLNSSLLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELN 175
Cdd:smart00476  82 YVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEID 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732    176 ALYDVFLDVSQRWQNENVILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQGCQKL 255
Cdd:smart00476 162 ALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSS 240

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 84662732    256 LK--AAATFDFPRRFQLTEEEALRVSDHYPVEVEL 288
Cdd:smart00476 241 VVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTL 275
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 24-288 6.96e-130

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: 371.00  E-value: 6.96e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732     24 VASLL--ILLVGGTDAFRICAFNAHRLTLTKVIKESVMDTLVQILARCDIMVLQEVVDSSQNTVLFLLQKL--QSSKSYS 99
Cdd:smart00476   2 VPSLLlfLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLnsDSPNTYS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732    100 FLNSSLLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELN 175
Cdd:smart00476  82 YVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEID 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732    176 ALYDVFLDVSQRWQNENVILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQGCQKL 255
Cdd:smart00476 162 ALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSS 240

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 84662732    256 LK--AAATFDFPRRFQLTEEEALRVSDHYPVEVEL 288
Cdd:smart00476 241 VVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTL 275
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 39-288 1.72e-125

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: 358.86  E-value: 1.72e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732  39 RICAFNAHRLTLTKVIKESVMDTLVQILARCDIMVLQEVVDSSQNTVLFLLQKL--QSSKSYSFLNSSLLGRSTYKEKYV 116
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELnsASSNTYSYVVSERLGRSSYKEQYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 117 YIYRSDKTQVLNFYQYNDT---EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENV 193
Cdd:cd10282  81 FIYRSDKVSVLESYQYDDGdegTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 194 ILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQG--CQKLLKAAATFDFPRRFQLT 271
Cdd:cd10282 161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKEFGLT 239

                       250
                ....*....|....*..
gi 84662732 272 EEEALRVSDHYPVEVEL 288
Cdd:cd10282 240 EEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 43-202 1.78e-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: 67.63  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732    43 FNAHRLTLTKVIKESVMDTLVQILARC--DIMVLQEVVDSSQNTVLFLLQKLqssksYSFLNSSLLGRSTYKEKYVYIYR 120
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-----GGFLSYGGPGGGGGGGGVAILSR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732   121 SDKTQVLnfyQYNDTEDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENVILLGDFN 200
Cdd:pfam03372  78 YPLSSVI---LVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFN 154


                  ..
gi 84662732   201 AD 202
Cdd:pfam03372 155 AD 156
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
116-202 4.13e-03

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 38.46  E-value: 4.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 116 VYIYRSDK------TQVLNFYQYNDTEDIFAREPFVAQFTLPSKilPSVVLVPLH---------------TTPKDVE--K 172
Cdd:COG2374 161 ALLYRPDRvtlvgsATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskgsddpgdgqgaSEAKRTAqaE 238

                        90       100       110
                ....*....|....*....|....*....|
gi 84662732 173 ELNALYDvflDVSQRWQNENVILLGDFNAD 202
Cdd:COG2374 239 ALRAFVD---SLLAADPDAPVIVLGDFNDY 265
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 24-288 6.96e-130

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: 371.00  E-value: 6.96e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732     24 VASLL--ILLVGGTDAFRICAFNAHRLTLTKVIKESVMDTLVQILARCDIMVLQEVVDSSQNTVLFLLQKL--QSSKSYS 99
Cdd:smart00476   2 VPSLLlfLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLnsDSPNTYS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732    100 FLNSSLLGRSTYKEKYVYIYRSDKTQVLNFYQYNDT----EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELN 175
Cdd:smart00476  82 YVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEID 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732    176 ALYDVFLDVSQRWQNENVILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQGCQKL 255
Cdd:smart00476 162 ALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSS 240

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 84662732    256 LK--AAATFDFPRRFQLTEEEALRVSDHYPVEVEL 288
Cdd:smart00476 241 VVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTL 275
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 39-288 1.72e-125

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: 358.86  E-value: 1.72e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732  39 RICAFNAHRLTLTKVIKESVMDTLVQILARCDIMVLQEVVDSSQNTVLFLLQKL--QSSKSYSFLNSSLLGRSTYKEKYV 116
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELnsASSNTYSYVVSERLGRSSYKEQYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 117 YIYRSDKTQVLNFYQYNDT---EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENV 193
Cdd:cd10282  81 FIYRSDKVSVLESYQYDDGdegTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 194 ILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQG--CQKLLKAAATFDFPRRFQLT 271
Cdd:cd10282 161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKEFGLT 239

                       250
                ....*....|....*..
gi 84662732 272 EEEALRVSDHYPVEVEL 288
Cdd:cd10282 240 EEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 39-288 3.33e-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: 198.01  E-value: 3.33e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732  39 RICAFNAHRLTLTKVIKESVMDTLVQILARCDIMVLQEVVDSSQNTVLFLLQKLQ--SSKSYSFLNSSLLGRSTYKEKYV 116
Cdd:cd09075   1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNqdDPNTYHYVVSEPLGRNSYKERYL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 117 YIYRSDKTQVLNFYQYNDTE-----DIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNE 191
Cdd:cd09075  81 FLFRPNKVSVLDTYQYDDGCkscgnDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLN 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 192 NVILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVrASTNCTYDRIVMHGQGCQ--KLLKAAATFDFPRRFQ 269
Cdd:cd09075 161 DVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTA-TSTNCAYDRIVVAGSLLQssVVPGSAAPFDFQAAYG 239

                       250
                ....*....|....*....
gi 84662732 270 LTEEEALRVSDHYPVEVEL 288
Cdd:cd09075 240 LSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 38-288 2.61e-25

Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197338 [Multi-domain]  Cd Length: 266  Bit Score: 102.09  E-value: 2.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732  38 FRICAFNAHRLTLTKviKESVMDTLVQILAR--CDIMVLQEVVDSSQ--NTVLFLLQKL-QSSKSYSFLNSS-LLGRSTY 111
Cdd:cd10283   1 LRIASWNILNFGNSK--GKEKNPAIAEIISAfdLDLIALQEVMDNGGglDALAKLVNELnKPGGTWKYIVSDkTGGSSGD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 112 KEKYVYIYRSDKTQ-VLNFYQYNDT-EDIFAREPFVAQFtlpsKILPS---VVLVPLHTTPKDV---------EKELNAL 177
Cdd:cd10283  79 KERYAFLYKSSKVRkVGKAVLEKDSnTDGFARPPYAAKF----KSGGTgfdFTLVNVHLKSGGSsksgqgakrVAEAQAL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 178 YDVFLDVSQRWQNENVILLGDFNADCASLAKKRLnslllrTKAGFHWVIPDGEDTTvrASTNC---TYDRIVMHGQGCQK 254
Cdd:cd10283 155 AEYLKELADEDPDDDVILLGDFNIPADEDAFKAL------TKAGFKSLLPDSTNLS--TSFKGyanSYDNIFVSGNLKEK 226

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 84662732 255 lLKAAATFDFPRRFQLTEEEAL-------RVSDHYPVEVEL 288
Cdd:cd10283 227 -FSNSGVFDFNILVDEAGEEDLdyskwrkQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 40-288 4.73e-19

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: 84.46  E-value: 4.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732  40 ICAFNAHrlTLTKVIKESVMDTLVQILARcDIMVLQEVVDSsQNTVLFLLQKLqssKSYSFLNSSLLGRSTYKEKYVYIY 119
Cdd:cd08372   1 VASYNVN--GLNAATRASGIARWVRELDP-DIVCLQEVKDS-QYSAVALNQLL---PEGYHQYQSGPSRKEGYEGVAILS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 120 RSDKTQVLNFYQYNDTE-DIFAREPFVAQFTLPSKILpsvVLVPLH-----TTPKDVEKELNALYDVFLDVsQRWQNENV 193
Cdd:cd08372  74 KTPKFKIVEKHQYKFGEgDSGERRAVVVKFDVHDKEL---CVVNAHlqaggTRADVRDAQLKEVLEFLKRL-RQPNSAPV 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 194 ILLGDFNADCASLAKKRLNSLL-LRTKAGFHWVIPDGEDT----TVRASTNCTYDRIVMHGQGCQKLLKAAATFDFPRrf 268
Cdd:cd08372 150 VICGDFNVRPSEVDSENPSSMLrLFVALNLVDSFETLPHAytfdTYMHNVKSRLDYIFVSKSLLPSVKSSKILSDAAR-- 227

                       250       260
                ....*....|....*....|
gi 84662732 269 qlteeeALRVSDHYPVEVEL 288
Cdd:cd08372 228 ------ARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 43-202 1.78e-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: 67.63  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732    43 FNAHRLTLTKVIKESVMDTLVQILARC--DIMVLQEVVDSSQNTVLFLLQKLqssksYSFLNSSLLGRSTYKEKYVYIYR 120
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-----GGFLSYGGPGGGGGGGGVAILSR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732   121 SDKTQVLnfyQYNDTEDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENVILLGDFN 200
Cdd:pfam03372  78 YPLSSVI---LVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFN 154


                  ..
gi 84662732   201 AD 202
Cdd:pfam03372 155 AD 156
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
116-202 4.13e-03

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 38.46  E-value: 4.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662732 116 VYIYRSDK------TQVLNFYQYNDTEDIFAREPFVAQFTLPSKilPSVVLVPLH---------------TTPKDVE--K 172
Cdd:COG2374 161 ALLYRPDRvtlvgsATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskgsddpgdgqgaSEAKRTAqaE 238

                        90       100       110
                ....*....|....*....|....*....|
gi 84662732 173 ELNALYDvflDVSQRWQNENVILLGDFNAD 202
Cdd:COG2374 239 ALRAFVD---SLLAADPDAPVIVLGDFNDY 265
 
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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