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Conserved domains on  [gi|2494173|sp|Q13609|]
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RecName: Full=Deoxyribonuclease gamma; Short=DNase gamma; AltName: Full=DNase I homolog protein DHP2; AltName: Full=Deoxyribonuclease I-like 3; Short=DNase I-like 3; AltName: Full=Liver and spleen DNase; Short=LS-DNase; Short=LSD; Flags: Precursor

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 11270576)

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
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 15-282 2.56e-167

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: 465.38  E-value: 2.56e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173      15 IHSALAMRICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLNRNSRRgiTYNYVISSRLG 94
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPN--TYSYVSSEPLG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173      95 RNTYKEQYAFLYKEKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTD 174
Cdd:smart00476  90 RNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLD 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173     175 VKHRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSV 254
Cdd:smart00476 170 VRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAV 248

                          250       260
                   ....*....|....*....|....*...
gi 2494173     255 FDFQKAYKLTEEEALDVSDHFPVEFKLQ 282
Cdd:smart00476 249 FDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 15-282 2.56e-167

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: 465.38  E-value: 2.56e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173      15 IHSALAMRICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLNRNSRRgiTYNYVISSRLG 94
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPN--TYSYVSSEPLG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173      95 RNTYKEQYAFLYKEKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTD 174
Cdd:smart00476  90 RNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLD 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173     175 VKHRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSV 254
Cdd:smart00476 170 VRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAV 248

                          250       260
                   ....*....|....*....|....*...
gi 2494173     255 FDFQKAYKLTEEEALDVSDHFPVEFKLQ 282
Cdd:smart00476 249 FDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 22-281 1.70e-158

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: 442.06  E-value: 1.70e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   22 RICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLNRNSRRgiTYNYVISSRLGRNTYKEQ 101
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSN--TYSYVVSERLGRSSYKEQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  102 YAFLYKEKLVSVKRSYHYHDYQDGDaDVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRWKA 181
Cdd:cd10282  79 YAFIYRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  182 ENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAY 261
Cdd:cd10282 158 DDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEF 236

                       250       260
                ....*....|....*....|
gi 2494173  262 KLTEEEALDVSDHFPVEFKL 281
Cdd:cd10282 237 GLTEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 24-192 6.49e-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: 6.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173     24 CSFNVRSFGESKQEDKNAMDVIVKVIKRC--DIILVMEIKDSNNRICPILMEKLnrnsrrgitYNYVISSRLGRNTYKEQ 101
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY---------GGFLSYGGPGGGGGGGG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173    102 YAFLYKEKLVSVKRSYHYHDYQDGDADVFSREPFVVWFqsphtavKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRWKA 181
Cdd:pfam03372  72 VAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVV-------PLVLTLAPHASPRLARDEQRADLLLLLLALLAPRS 144

                         170
                  ....*....|.
gi 2494173    182 ENFIFMGDFNA 192
Cdd:pfam03372 145 EPVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
21-193 7.32e-10

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 59.26  E-value: 7.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   21 MRICSFNVRSF-------------GESKQEDKNAMDVIVKVIKR--CDIILVMEIKDSNNricpiLMEKL-NRNSRRGIT 84
Cdd:COG2374  69 LRVATFNVENLfdtddddddfgrgADTPEEYERKLAKIAAAIAAldADIVGLQEVENNGS-----ALQDLvAALNLAGGT 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   85 YNYV--ISSRLGRN--TykeqyAFLYKEKLVSVK--RSYHYHDYQDGDADVFSREPFVVWFQSPHTavKDFVIIPLH--- 155
Cdd:COG2374 144 YAFVhpPDGPDGDGirV-----ALLYRPDRVTLVgsATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfks 216

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 2494173  156 --------TTPETSVKEIDE---LVEVYTDVKHRWKAENFIFMGDFNAG 193
Cdd:COG2374 217 kgsddpgdGQGASEAKRTAQaeaLRAFVDSLLAADPDAPVIVLGDFNDY 265
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 15-282 2.56e-167

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: 465.38  E-value: 2.56e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173      15 IHSALAMRICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLNRNSRRgiTYNYVISSRLG 94
Cdd:smart00476  12 LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPN--TYSYVSSEPLG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173      95 RNTYKEQYAFLYKEKLVSVKRSYHYHDYQDGDADVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTD 174
Cdd:smart00476  90 RNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLD 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173     175 VKHRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSV 254
Cdd:smart00476 170 VRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTV-TSTHCAYDRIVVAGERLRSSVVPGSAAV 248

                          250       260
                   ....*....|....*....|....*...
gi 2494173     255 FDFQKAYKLTEEEALDVSDHFPVEFKLQ 282
Cdd:smart00476 249 FDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 22-281 1.70e-158

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: 442.06  E-value: 1.70e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   22 RICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLNRNSRRgiTYNYVISSRLGRNTYKEQ 101
Cdd:cd10282   1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSN--TYSYVVSERLGRSSYKEQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  102 YAFLYKEKLVSVKRSYHYHDYQDGDaDVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRWKA 181
Cdd:cd10282  79 YAFIYRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  182 ENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTVkKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQKAY 261
Cdd:cd10282 158 DDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTV-RSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEF 236

                       250       260
                ....*....|....*....|
gi 2494173  262 KLTEEEALDVSDHFPVEFKL 281
Cdd:cd10282 237 GLTEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 22-281 1.33e-73

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: 226.90  E-value: 1.33e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   22 RICSFNVRSFGESKQEDKNAMDVIVKVIKRCDIILVMEIKDSNNRICPILMEKLNRNSRRgiTYNYVISSRLGRNTYKEQ 101
Cdd:cd09075   1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPN--TYHYVVSEPLGRNSYKER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  102 YAFLYKEKLVSVKRSYHYHDyQDGDA--DVFSREPFVVWFQSPHTAVKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRW 179
Cdd:cd09075  79 YLFLFRPNKVSVLDTYQYDD-GCKSCgnDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKW 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  180 KAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPRFVWLIGDQEDTTvKKSTNCAYDRIVLRGQEIVSSVVPKSNSVFDFQK 259
Cdd:cd09075 158 HLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTT-ATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQA 236

                       250       260
                ....*....|....*....|..
gi 2494173  260 AYKLTEEEALDVSDHFPVEFKL 281
Cdd:cd09075 237 AYGLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 22-281 1.12e-33

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: 124.05  E-value: 1.12e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   22 RICSFNVRSFGESKQEDKNamDVIVKVIKR--CDIILVMEIKDSNNRICPiLMEKLNRNSRRGITYNYVISS-RLGRNTY 98
Cdd:cd10283   2 RIASWNILNFGNSKGKEKN--PAIAEIISAfdLDLIALQEVMDNGGGLDA-LAKLVNELNKPGGTWKYIVSDkTGGSSGD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   99 KEQYAFLYKEKLVSVKRSYHYhdYQDGDADVFSREPFVVWFQSPHTAvKDFVIIPLHTTPETS---------VKEIDELV 169
Cdd:cd10283  79 KERYAFLYKSSKVRKVGKAVL--EKDSNTDGFARPPYAAKFKSGGTG-FDFTLVNVHLKSGGSsksgqgakrVAEAQALA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  170 EVYTDVKHRWKAENFIFMGDFNAgcsYVPKKAWKNIrlrTDPRFVWLIGDQEDTT--VKKSTNCaYDRIVLRG----QEI 243
Cdd:cd10283 156 EYLKELADEDPDDDVILLGDFNI---PADEDAFKAL---TKAGFKSLLPDSTNLStsFKGYANS-YDNIFVSGnlkeKFS 228

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 2494173  244 VSSVVPKSNSVFDFQKAYKLTEEEALDVSDHFPVEFKL 281
Cdd:cd10283 229 NSGVFDFNILVDEAGEEDLDYSKWRKQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 23-281 7.76e-18

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: 80.99  E-value: 7.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   23 ICSFNVRSFGESKQEDKnamdvIVKVIKRC--DIILVMEIKDSNNRICPILMEKLNRnsrrgitYNYVISSRLGRNtYKE 100
Cdd:cd08372   1 VASYNVNGLNAATRASG-----IARWVRELdpDIVCLQEVKDSQYSAVALNQLLPEG-------YHQYQSGPSRKE-GYE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  101 QYAFLYKEKLVSVKRSyhyHDYQDGDADVFSREPFVVWFQSphtAVKDFVIIPLHTTPETS-----VKEIDELVEVYTDV 175
Cdd:cd08372  68 GVAILSKTPKFKIVEK---HQYKFGEGDSGERRAVVVKFDV---HDKELCVVNAHLQAGGTradvrDAQLKEVLEFLKRL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  176 KhRWKAENFIFMGDFNAGCSYVPKKAWKN-IRLRTDPRFVWLI--GDQEDT--TVKKSTNCAYDRIVLRGQEIVSsvvPK 250
Cdd:cd08372 142 R-QPNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFetLPHAYTfdTYMHNVKSRLDYIFVSKSLLPS---VK 217

                       250       260       270
                ....*....|....*....|....*....|.
gi 2494173  251 SNSVFDFQKayklteeEALDVSDHFPVEFKL 281
Cdd:cd08372 218 SSKILSDAA-------RARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 24-192 6.49e-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: 6.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173     24 CSFNVRSFGESKQEDKNAMDVIVKVIKRC--DIILVMEIKDSNNRICPILMEKLnrnsrrgitYNYVISSRLGRNTYKEQ 101
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY---------GGFLSYGGPGGGGGGGG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173    102 YAFLYKEKLVSVKRSYHYHDYQDGDADVFSREPFVVWFqsphtavKDFVIIPLHTTPETSVKEIDELVEVYTDVKHRWKA 181
Cdd:pfam03372  72 VAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVV-------PLVLTLAPHASPRLARDEQRADLLLLLLALLAPRS 144

                         170
                  ....*....|.
gi 2494173    182 ENFIFMGDFNA 192
Cdd:pfam03372 145 EPVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
21-193 7.32e-10

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 59.26  E-value: 7.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   21 MRICSFNVRSF-------------GESKQEDKNAMDVIVKVIKR--CDIILVMEIKDSNNricpiLMEKL-NRNSRRGIT 84
Cdd:COG2374  69 LRVATFNVENLfdtddddddfgrgADTPEEYERKLAKIAAAIAAldADIVGLQEVENNGS-----ALQDLvAALNLAGGT 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   85 YNYV--ISSRLGRN--TykeqyAFLYKEKLVSVK--RSYHYHDYQDGDADVFSREPFVVWFQSPHTavKDFVIIPLH--- 155
Cdd:COG2374 144 YAFVhpPDGPDGDGirV-----ALLYRPDRVTLVgsATIADLPDSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfks 216

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 2494173  156 --------TTPETSVKEIDE---LVEVYTDVKHRWKAENFIFMGDFNAG 193
Cdd:COG2374 217 kgsddpgdGQGASEAKRTAQaeaLRAFVDSLLAADPDAPVIVLGDFNDY 265
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 176-275 2.20e-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: 2.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  176 KHRWKAENFIFMGDFNAGCSYVP--------KKAWKNIRLRTDPRFVWligDQEDTTVKKSTN----CAYDRIVLRGQEI 243
Cdd:cd09080 140 KKPPGAANVILGGDFNLRDKEDDtgglpngfVDAWEELGPPGEPGYTW---DTQKNPMLRKGEagprKRFDRVLLRGSDL 216

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2494173  244 VssvvpksnsvfdfQKAYKLTEEEALD-------VSDHF 275
Cdd:cd09080 217 K-------------PKSIELIGTEPIPgdeeglfPSDHF 242
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
 117-192 4.14e-03

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 38.44  E-value: 4.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173  117 YHYHDYQDGDAD--VFSREPFV---------VWFQSPHTAVK----DFVIIPLHTTP--ETSVKEIDELVEVYTDVKHRw 179
Cdd:COG3021 146 YRVLCPLDNAYGmaLLSRLPLTeaevvylvgDDIPSIRATVElpggPVRLVAVHPAPpvGGSAERDAELAALAKAVAAL- 224

                        90
                ....*....|...
gi 2494173  180 kAENFIFMGDFNA 192
Cdd:COG3021 225 -DGPVIVAGDFNA 236
RgfB-like cd09079
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, ...
 25-191 4.14e-03

Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, and related proteins; This family includes Streptococcus agalactiae RgfB (for regulator of fibrinogen binding) and related proteins. The function of RgfB is unknown. It is part of a putative two component signal transduction system designated rgfBDAC (the rgf locus was identified in a screen for mutants of Streptococcus agalactiae with altered binding to fibrinogen). RgfA,-C,and -D do not belong to this superfamily: rgfA encodes a putative response regulator, and rgfC, a putative histidine kinase. All four genes are co-transcribed, and may be involved in regulating expression of bacterial cell surface components. 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: 197313 [Multi-domain]  Cd Length: 259  Bit Score: 38.01  E-value: 4.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   25 SFNVRSFGESKQEDKnaMDVIVKVIKR--CDIILVMEI---KDSNNRICPI--------LMEKLNRNsrrGITYNYV-IS 90
Cdd:cd09079   3 TLNTHSWLEENQKEK--LERLAKIIAEedYDVIALQEVnqsIDAPVSQVPIkednfallLYEKLREL---GATYYWTwIL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494173   91 SRLGRNTYKEQYAFLYKEKLVSVK-----RSYHYHDYQdgdadvfSR---------EPFVVWFQSPHtavkdfviIPLHT 156
Cdd:cd09079  78 SHIGYDKYDEGLAILSKRPIAEVEdfyvsKSQDYTDYK-------SRkilgatieiNGQPIDVYSCH--------LGWWY 142

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 2494173  157 TPETSVK-EIDELVEVYTDVKHRwkaenFIFMGDFN 191
Cdd:cd09079 143 DEEEPFAyEWSKLEKALAEAGRP-----VLLMGDFN 173
 
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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