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Conserved domains on  [gi|375151549|ref|NP_001243489|]
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deoxyribonuclease gamma isoform 2 precursor [Homo sapiens]

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 ...
15-252 1.30e-144

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: 406.44  E-value: 1.30e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549    15 IHSALAMRICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLN------------------ 76
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsseplgrn 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549    77 ----------REKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVK 146
Cdd:smart00476  92 sykeqylflyRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVR 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549   147 HRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFD 226
Cdd:smart00476 172 QKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAVFD 250
                          250       260
                   ....*....|....*....|....*.
gi 375151549   227 FQKAYKLTEEEALDVSDHFPVEFKLQ 252
Cdd:smart00476 251 FQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
15-252 1.30e-144

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: 406.44  E-value: 1.30e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549    15 IHSALAMRICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLN------------------ 76
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsseplgrn 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549    77 ----------REKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVK 146
Cdd:smart00476  92 sykeqylflyRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVR 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549   147 HRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFD 226
Cdd:smart00476 172 QKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAVFD 250
                          250       260
                   ....*....|....*....|....*.
gi 375151549   227 FQKAYKLTEEEALDVSDHFPVEFKLQ 252
Cdd:smart00476 251 FQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
22-251 1.60e-135

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: 382.74  E-value: 1.60e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  22 RICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLN------------------------- 76
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNsassntysyvvserlgrssykeqya 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  77 ---REKLVSVKRSYHYHDYQDGDaDVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRWKAEN 153
Cdd:cd10282   81 fiyRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549 154 FIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAYKL 233
Cdd:cd10282  160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238
                        250
                 ....*....|....*...
gi 375151549 234 TEEEALDVSDHFPVEFKL 251
Cdd:cd10282  239 TEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
24-162 3.93e-11

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: 60.70  E-value: 3.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549   24 CSFNVRSFGESKQEDKNAMDVIVKVIKRC--DIILVMEIKDSNNRICPILMEKLNReklVSVKRSYHYHDYQDGDAdVFS 101
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGG---FLSYGGPGGGGGGGGVA-ILS 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375151549  102 REPFVVWFQ---------SPHTAVKDFVI---------IPLHTTPETSVKEIDELVEVYTDVKHRWKAENFIFMGDFNA 162
Cdd:pfam03372  77 RYPLSSVILvdlgefgdpALRGAIAPFAGvlvvplvltLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
21-162 3.21e-05

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 44.60  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  21 MRICSFNVRsfGESKQEDKnamdvIVKVIKR--CDIILVMEikdsnnricpilMEKLNREKLVSVKRSY--HYHDYQDGD 96
Cdd:COG3021   95 LRVLTANVL--FGNADAEA-----LAALVREedPDVLVLQE------------TTPAWEEALAALEADYpyRVLCPLDNA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  97 AD--VFSREPFV---------VWFQSPHTAVK----DFVIIPLHTTP--ETSVKEIDELVEVYTDVKHRwkAENFIFMGD 159
Cdd:COG3021  156 YGmaLLSRLPLTeaevvylvgDDIPSIRATVElpggPVRLVAVHPAPpvGGSAERDAELAALAKAVAAL--DGPVIVAGD 233

                 ...
gi 375151549 160 FNA 162
Cdd:COG3021  234 FNA 236
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
15-252 1.30e-144

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: 406.44  E-value: 1.30e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549    15 IHSALAMRICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLN------------------ 76
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsseplgrn 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549    77 ----------REKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVK 146
Cdd:smart00476  92 sykeqylflyRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVR 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549   147 HRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFD 226
Cdd:smart00476 172 QKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAVFD 250
                          250       260
                   ....*....|....*....|....*.
gi 375151549   227 FQKAYKLTEEEALDVSDHFPVEFKLQ 252
Cdd:smart00476 251 FQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
22-251 1.60e-135

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: 382.74  E-value: 1.60e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  22 RICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLN------------------------- 76
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNsassntysyvvserlgrssykeqya 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  77 ---REKLVSVKRSYHYHDYQDGDaDVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRWKAEN 153
Cdd:cd10282   81 fiyRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549 154 FIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAYKL 233
Cdd:cd10282  160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238
                        250
                 ....*....|....*...
gi 375151549 234 TEEEALDVSDHFPVEFKL 251
Cdd:cd10282  239 TEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
22-251 3.48e-57

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: 183.75  E-value: 3.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  22 RICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLN------------------------- 76
Cdd:cd09075    1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNqddpntyhyvvseplgrnsykeryl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  77 ---REKLVSVKRSYHYHDyQDGDA--DVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRWKA 151
Cdd:cd09075   81 flfRPNKVSVLDTYQYDD-GCKSCgnDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549 152 ENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTvKKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAY 231
Cdd:cd09075  160 NDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTT-ATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAY 238
                        250       260
                 ....*....|....*....|
gi 375151549 232 KLTEEEALDVSDHFPVEFKL 251
Cdd:cd09075  239 GLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
22-251 7.08e-21

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: 88.99  E-value: 7.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  22 RICSFNVRSFGESKQEDKNamDVIVKVIKR--CDIILVMEIKDSNNRICPI--LMEKLN--------------------- 76
Cdd:cd10283    2 RIASWNILNFGNSKGKEKN--PAIAEIISAfdLDLIALQEVMDNGGGLDALakLVNELNkpggtwkyivsdktggssgdk 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  77 --------REKLVSVKRSYHYHDYQDgdaDVFSREPFVVWFQSPHTAvKDFVIIPLH-TTPETS--------VKEIDELV 139
Cdd:cd10283   80 eryaflykSSKVRKVGKAVLEKDSNT---DGFARPPYAAKFKSGGTG-FDFTLVNVHlKSGGSSksgqgakrVAEAQALA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549 140 EVYTDVKHRWKAENFIFMGDFNAgcsYVPKKAWKNIrlrTDPRFVWLIGDQEDTT--VKKSTNCaYDRIVLRG----QEI 213
Cdd:cd10283  156 EYLKELADEDPDDDVILLGDFNI---PADEDAFKAL---TKAGFKSLLPDSTNLStsFKGYANS-YDNIFVSGnlkeKFS 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 375151549 214 VSSVVPKSNSVFDFQKAYKLTEEEALDVSDHFPVEFKL 251
Cdd:cd10283  229 NSGVFDFNILVDEAGEEDLDYSKWRKQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
23-251 1.30e-15

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: 74.05  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  23 ICSFNVRSFGESKQEDKnamdvIVKVIKRC--DIILVMEIKDSNNRICPILMEKLNREKLVSVKRSYHY----------- 89
Cdd:cd08372    1 VASYNVNGLNAATRASG-----IARWVRELdpDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSRKEgyegvailskt 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  90 --------HDYQDGDADVFSREPFVVWFQSphtAVKDFVIIPLHTTPETS-----VKEIDELVEVYTDVKhRWKAENFIF 156
Cdd:cd08372   76 pkfkivekHQYKFGEGDSGERRAVVVKFDV---HDKELCVVNAHLQAGGTradvrDAQLKEVLEFLKRLR-QPNSAPVVI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549 157 MGDFNAGCSYVPKKAWKN-IRLRTDPRFVWLI--GDQEDT--TVKKSTNCAYDRIVLRGQEIVSsvvPKSNSVFDFQKay 231
Cdd:cd08372  152 CGDFNVRPSEVDSENPSSmLRLFVALNLVDSFetLPHAYTfdTYMHNVKSRLDYIFVSKSLLPS---VKSSKILSDAA-- 226
                        250       260
                 ....*....|....*....|
gi 375151549 232 klteeEALDVSDHFPVEFKL 251
Cdd:cd08372  227 -----RARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
24-162 3.93e-11

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: 60.70  E-value: 3.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549   24 CSFNVRSFGESKQEDKNAMDVIVKVIKRC--DIILVMEIKDSNNRICPILMEKLNReklVSVKRSYHYHDYQDGDAdVFS 101
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGG---FLSYGGPGGGGGGGGVA-ILS 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375151549  102 REPFVVWFQ---------SPHTAVKDFVI---------IPLHTTPETSVKEIDELVEVYTDVKHRWKAENFIFMGDFNA 162
Cdd:pfam03372  77 RYPLSSVILvdlgefgdpALRGAIAPFAGvlvvplvltLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
21-162 3.21e-05

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 44.60  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  21 MRICSFNVRsfGESKQEDKnamdvIVKVIKR--CDIILVMEikdsnnricpilMEKLNREKLVSVKRSY--HYHDYQDGD 96
Cdd:COG3021   95 LRVLTANVL--FGNADAEA-----LAALVREedPDVLVLQE------------TTPAWEEALAALEADYpyRVLCPLDNA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  97 AD--VFSREPFV---------VWFQSPHTAVK----DFVIIPLHTTP--ETSVKEIDELVEVYTDVKHRwkAENFIFMGD 159
Cdd:COG3021  156 YGmaLLSRLPLTeaevvylvgDDIPSIRATVElpggPVRLVAVHPAPpvGGSAERDAELAALAKAVAAL--DGPVIVAGD 233

                 ...
gi 375151549 160 FNA 162
Cdd:COG3021  234 FNA 236
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
20-251 9.45e-05

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 41.82  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  20 AMRICSFNVRS-FGeskQEDKNAMDVIVKVIKR--CDIILVMEIkdsnnricPILmeklNREKLVSVKRsyhyHDYQDGD 96
Cdd:COG3568    7 TLRVMTYNIRYgLG---TDGRADLERIARVIRAldPDVVALQEN--------AIL----SRYPIVSSGT----FDLPDPG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549  97 ADvfSREPFVVWFQSPHtavKDFVIIPLH---TTPETSVKEIDELVEVytdVKHRWKAENFIFMGDFNagcsyvpkkawk 173
Cdd:COG3568   68 GE--PRGALWADVDVPG---KPLRVVNTHldlRSAAARRRQARALAEL---LAELPAGAPVILAGDFN------------ 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549 174 nirlrtdprfvwligdqedttvkkstncAYDRIVLRGQ-EIVSSVVpksnsvfdfqkaykLTEEEALDVSDHFPV--EFK 250
Cdd:COG3568  128 ----------------------------DIDYILVSPGlRVLSAEV--------------LDSPLGRAASDHLPVvaDLE 165

                 .
gi 375151549 251 L 251
Cdd:COG3568  166 L 166
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
146-245 2.06e-03

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


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 38.86  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375151549 146 KHRWKAENFIFMGDFNAGCSYVP--------KKAWKNIRLRTDPRFVWligDQEDTTVKKSTN----CAYDRIVLRGQEI 213
Cdd:cd09080  140 KKPPGAANVILGGDFNLRDKEDDtgglpngfVDAWEELGPPGEPGYTW---DTQKNPMLRKGEagprKRFDRVLLRGSDL 216
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 375151549 214 VssvvpksnsvfdfQKAYKLTEEEALD-------VSDHF 245
Cdd:cd09080  217 K-------------PKSIELIGTEPIPgdeeglfPSDHF 242
 
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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