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Conserved domains on  [gi|1743207534|ref|XP_030666027|]
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deoxyribonuclease gamma isoform X2 [Nomascus leucogenys]

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 ...
 14-251 3.09e-146

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: 410.68  E-value: 3.09e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534   14 IHSALALRICSFNVRSFGESKQEDQNAMDVIVKIIKRCDIILVMEIKDSNNRICPILMEKLN------------------ 75
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsseplgrn 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534   76 ----------REKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYMDVK 145
Cdd:smart00476  92 sykeqylflyRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVR 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  146 HRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFD 225
Cdd:smart00476 172 QKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAVFD 250

                          250       260
                   ....*....|....*....|....*.
gi 1743207534  226 FQKAYKLTEEEALDVSDHFPVEFKLQ 251
Cdd:smart00476 251 FQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 14-251 3.09e-146

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: 410.68  E-value: 3.09e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534   14 IHSALALRICSFNVRSFGESKQEDQNAMDVIVKIIKRCDIILVMEIKDSNNRICPILMEKLN------------------ 75
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsseplgrn 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534   76 ----------REKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYMDVK 145
Cdd:smart00476  92 sykeqylflyRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVR 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  146 HRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFD 225
Cdd:smart00476 172 QKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAVFD 250

                          250       260
                   ....*....|....*....|....*.
gi 1743207534  226 FQKAYKLTEEEALDVSDHFPVEFKLQ 251
Cdd:smart00476 251 FQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 21-250 1.55e-136

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: 385.44  E-value: 1.55e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  21 RICSFNVRSFGESKQEDQNAMDVIVKIIKRCDIILVMEIKDSNNRICPILMEKLN------------------------- 75
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNsassntysyvvserlgrssykeqya 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  76 ---REKLVSVKRSYHYHDYQDGDaDVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYMDVKHRWKAEN 152
Cdd:cd10282    81 fiyRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534 153 FIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAYKL 232
Cdd:cd10282   160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238

                         250
                  ....*....|....*...
gi 1743207534 233 TEEEALDVSDHFPVEFKL 250
Cdd:cd10282   239 TEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 23-161 1.67e-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: 58.78  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  23 CSFNVRSFGESKQEDQNAMDVIVKIIKRC--DIILVMEIKDSNNRICPILMEKLNReklVSVKRSYHYHDYQDGDAdVFS 100
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGG---FLSYGGPGGGGGGGGVA-ILS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743207534 101 REPFVVWFQ---------SPHTAVKDFVI---------IPLHTTPETSVKEIDELVEVYMDVKHRWKAENFIFMGDFNA 161
Cdd:pfam03372  77 RYPLSSVILvdlgefgdpALRGAIAPFAGvlvvplvltLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
 20-161 1.60e-05

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 45.37  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  20 LRICSFNVRsfGESKQEDQnamdvIVKIIKR--CDIILVMEikdsnnricpilMEKLNREKLVSVKRSY--HYHDYQDGD 95
Cdd:COG3021    95 LRVLTANVL--FGNADAEA-----LAALVREedPDVLVLQE------------TTPAWEEALAALEADYpyRVLCPLDNA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  96 AD--VFSREPFV---------VWFQSPHTAVK----DFVIIPLHTTP--ETSVKEIDELVEVYMDVKHRwkAENFIFMGD 158
Cdd:COG3021   156 YGmaLLSRLPLTeaevvylvgDDIPSIRATVElpggPVRLVAVHPAPpvGGSAERDAELAALAKAVAAL--DGPVIVAGD 233


                  ...
gi 1743207534 159 FNA 161
Cdd:COG3021   234 FNA 236
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 14-251 3.09e-146

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: 410.68  E-value: 3.09e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534   14 IHSALALRICSFNVRSFGESKQEDQNAMDVIVKIIKRCDIILVMEIKDSNNRICPILMEKLN------------------ 75
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntysyvsseplgrn 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534   76 ----------REKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYMDVK 145
Cdd:smart00476  92 sykeqylflyRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVR 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  146 HRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFD 225
Cdd:smart00476 172 QKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAVFD 250

                          250       260
                   ....*....|....*....|....*.
gi 1743207534  226 FQKAYKLTEEEALDVSDHFPVEFKLQ 251
Cdd:smart00476 251 FQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 21-250 1.55e-136

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: 385.44  E-value: 1.55e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  21 RICSFNVRSFGESKQEDQNAMDVIVKIIKRCDIILVMEIKDSNNRICPILMEKLN------------------------- 75
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNsassntysyvvserlgrssykeqya 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  76 ---REKLVSVKRSYHYHDYQDGDaDVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYMDVKHRWKAEN 152
Cdd:cd10282    81 fiyRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534 153 FIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAYKL 232
Cdd:cd10282   160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238

                         250
                  ....*....|....*...
gi 1743207534 233 TEEEALDVSDHFPVEFKL 250
Cdd:cd10282   239 TEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 21-250 3.92e-58

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: 186.07  E-value: 3.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  21 RICSFNVRSFGESKQEDQNAMDVIVKIIKRCDIILVMEIKDSNNRICPILMEKLN------------------------- 75
Cdd:cd09075     1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNqddpntyhyvvseplgrnsykeryl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  76 ---REKLVSVKRSYHYHDyQDGDA--DVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYMDVKHRWKA 150
Cdd:cd09075    81 flfRPNKVSVLDTYQYDD-GCKSCgnDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534 151 ENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTvKKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAY 230
Cdd:cd09075   160 NDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTT-ATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAY 238

                         250       260
                  ....*....|....*....|
gi 1743207534 231 KLTEEEALDVSDHFPVEFKL 250
Cdd:cd09075   239 GLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 20-250 9.81e-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: 88.61  E-value: 9.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  20 LRICSFNVRSFGESKQEDQNamDVIVKIIKR--CDIILVMEIKDSNNRICPI--LMEKLN-------------------- 75
Cdd:cd10283     1 LRIASWNILNFGNSKGKEKN--PAIAEIISAfdLDLIALQEVMDNGGGLDALakLVNELNkpggtwkyivsdktggssgd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  76 ---------REKLVSVKRSYHYHDYQDgdaDVFSREPFVVWFQSPHTAvKDFVIIPLH-TTPETS--------VKEIDEL 137
Cdd:cd10283    79 keryaflykSSKVRKVGKAVLEKDSNT---DGFARPPYAAKFKSGGTG-FDFTLVNVHlKSGGSSksgqgakrVAEAQAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534 138 VEVYMDVKHRWKAENFIFMGDFNAgcsYVPKKAWKNIrlrTDPRFVWLIGDQEDTT--VKKSTNCaYDRIVLRG----QE 211
Cdd:cd10283   155 AEYLKELADEDPDDDVILLGDFNI---PADEDAFKAL---TKAGFKSLLPDSTNLStsFKGYANS-YDNIFVSGnlkeKF 227

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1743207534 212 IVSSVVPKSNSVFDFQKAYKLTEEEALDVSDHFPVEFKL 250
Cdd:cd10283   228 SNSGVFDFNILVDEAGEEDLDYSKWRKQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 22-250 4.57e-16

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: 75.60  E-value: 4.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  22 ICSFNVRSFGESKQEDqnamdVIVKIIKRC--DIILVMEIKDSNNRICPILMEKLNREKLVSVKRSYHY----------- 88
Cdd:cd08372     1 VASYNVNGLNAATRAS-----GIARWVRELdpDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSRKEgyegvailskt 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  89 --------HDYQDGDADVFSREPFVVWFQSphtAVKDFVIIPLHTTPETS-----VKEIDELVEVYMDVKhRWKAENFIF 155
Cdd:cd08372    76 pkfkivekHQYKFGEGDSGERRAVVVKFDV---HDKELCVVNAHLQAGGTradvrDAQLKEVLEFLKRLR-QPNSAPVVI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534 156 MGDFNAGCSYVPKKAWKN-IRLRTDPRFVWLI--GDQEDT--TVKKSTNCAYDRIVLRGQEIVSsvvPKSNSVFDFQKay 230
Cdd:cd08372   152 CGDFNVRPSEVDSENPSSmLRLFVALNLVDSFetLPHAYTfdTYMHNVKSRLDYIFVSKSLLPS---VKSSKILSDAA-- 226

                         250       260
                  ....*....|....*....|
gi 1743207534 231 klteeEALDVSDHFPVEFKL 250
Cdd:cd08372   227 -----RARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 23-161 1.67e-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: 58.78  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  23 CSFNVRSFGESKQEDQNAMDVIVKIIKRC--DIILVMEIKDSNNRICPILMEKLNReklVSVKRSYHYHDYQDGDAdVFS 100
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGG---FLSYGGPGGGGGGGGVA-ILS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743207534 101 REPFVVWFQ---------SPHTAVKDFVI---------IPLHTTPETSVKEIDELVEVYMDVKHRWKAENFIFMGDFNA 161
Cdd:pfam03372  77 RYPLSSVILvdlgefgdpALRGAIAPFAGvlvvplvltLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
 20-161 1.60e-05

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 45.37  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  20 LRICSFNVRsfGESKQEDQnamdvIVKIIKR--CDIILVMEikdsnnricpilMEKLNREKLVSVKRSY--HYHDYQDGD 95
Cdd:COG3021    95 LRVLTANVL--FGNADAEA-----LAALVREedPDVLVLQE------------TTPAWEEALAALEADYpyRVLCPLDNA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  96 AD--VFSREPFV---------VWFQSPHTAVK----DFVIIPLHTTP--ETSVKEIDELVEVYMDVKHRwkAENFIFMGD 158
Cdd:COG3021   156 YGmaLLSRLPLTeaevvylvgDDIPSIRATVElpggPVRLVAVHPAPpvGGSAERDAELAALAKAVAAL--DGPVIVAGD 233


                  ...
gi 1743207534 159 FNA 161
Cdd:COG3021   234 FNA 236
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 19-250 4.20e-04

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 39.89  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  19 ALRICSFNVRS-FGESKQEDqnaMDVIVKIIKR--CDIILVMEIkdsnnricPILmeklNREKLVSVKRsyhyHDYQDGD 95
Cdd:COG3568     7 TLRVMTYNIRYgLGTDGRAD---LERIARVIRAldPDVVALQEN--------AIL----SRYPIVSSGT----FDLPDPG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534  96 ADvfSREPFVVWFQSPHtavKDFVIIPLH---TTPETSVKEIDELVEVymdVKHRWKAENFIFMGDFNagcsyvpkkawk 172
Cdd:COG3568    68 GE--PRGALWADVDVPG---KPLRVVNTHldlRSAAARRRQARALAEL---LAELPAGAPVILAGDFN------------ 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534 173 nirlrtdprfvwligdqedttvkkstncAYDRIVLRGQ-EIVSSVVpksnsvfdfqkaykLTEEEALDVSDHFPV--EFK 249
Cdd:COG3568   128 ----------------------------DIDYILVSPGlRVLSAEV--------------LDSPLGRAASDHLPVvaDLE 165


                  .
gi 1743207534 250 L 250
Cdd:COG3568   166 L 166
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 145-244 2.18e-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: 38.48  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743207534 145 KHRWKAENFIFMGDFNAGCSYVP--------KKAWKNIRLRTDPRFVWligDQEDTTVKKSTN----CAYDRIVLRGQEI 212
Cdd:cd09080   140 KKPPGAANVILGGDFNLRDKEDDtgglpngfVDAWEELGPPGEPGYTW---DTQKNPMLRKGEagprKRFDRVLLRGSDL 216

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1743207534 213 VssvvpksnsvfdfQKAYKLTEEEALD-------VSDHF 244
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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