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Conserved domains on  [gi|2052144882|gb|KAG6939400|]
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deoxyribonuclease 1 like 3 [Chelydra serpentina]

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 10178909)

endonuclease/exonuclease/phosphatase (EEP) family protein is among a diverse set of enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins; similar to Danio rerio deoxyribonuclease-1-like 1

CATH:  3.60.10.10
EC:  3.1.21.-
PubMed:  10838565
SCOP:  4002213

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
19-276 1.28e-169

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: 469.41  E-value: 1.28e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  19 KICSFNVRSFGEAKRARPEVLDVIVKVISRCDIMLLMEIKDNSNKICPLLIEKLNGQSQEEYDYVISKRLGRKSYKEQYA 98
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  99 FIYRSNLVSVKQTYQYPDTQPGDvDAFSREPFVVWFKSPKTVVKEFVIIPQHTTPETAVREIDELYDVYLDVKQRWKSKN 178
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882 179 FIFMGDFNADCGYVPKKHWKNIRLRTQSEFVWLIGDKNDTTVRnSTNCAYDRIVIHGEKLINAVVPNSADIIDFQKAFGM 258
Cdd:cd10282   160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238
                         250
                  ....*....|....*...
gi 2052144882 259 TEEQALEVSDHFPIEFEL 276
Cdd:cd10282   239 TEEEALAVSDHYPVEVEL 256
 
Name Accession Description Interval E-value
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
19-276 1.28e-169

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: 469.41  E-value: 1.28e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  19 KICSFNVRSFGEAKRARPEVLDVIVKVISRCDIMLLMEIKDNSNKICPLLIEKLNGQSQEEYDYVISKRLGRKSYKEQYA 98
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  99 FIYRSNLVSVKQTYQYPDTQPGDvDAFSREPFVVWFKSPKTVVKEFVIIPQHTTPETAVREIDELYDVYLDVKQRWKSKN 178
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882 179 FIFMGDFNADCGYVPKKHWKNIRLRTQSEFVWLIGDKNDTTVRnSTNCAYDRIVIHGEKLINAVVPNSADIIDFQKAFGM 258
Cdd:cd10282   160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238
                         250
                  ....*....|....*...
gi 2052144882 259 TEEQALEVSDHFPIEFEL 276
Cdd:cd10282   239 TEEEALAVSDHYPVEVEL 256
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
1-277 3.48e-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: 464.22  E-value: 3.48e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882    1 MFCISLFLLFFFNATLSIKICSFNVRSFGEAKRARPEVLDVIVKVISRCDIMLLMEIKDNSNKICPLLIEKLNGQSQEEY 80
Cdd:smart00476   1 LVPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882   81 DYVISKRLGRKSYKEQYAFIYRSNLVSVKQTYQYPDTQPGDVDAFSREPFVVWFKSPKTVVKEFVIIPQHTTPETAVREI 160
Cdd:smart00476  81 SYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  161 DELYDVYLDVKQRWKSKNFIFMGDFNADCGYVPKKHWKNIRLRTQSEFVWLIGDKNDTTVRnSTNCAYDRIVIHGEKLIN 240
Cdd:smart00476 161 DALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRS 239
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2052144882  241 AVVPNSADIIDFQKAFGMTEEQALEVSDHFPIEFELK 277
Cdd:smart00476 240 SVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
21-213 1.03e-18

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: 81.50  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  21 CSFNVRSFGEAKRARPEVLDVIVKVISRC--DIMLLMEIKDNSNKICPLLIEKLNGqsqeeydYVISKRLGRKSYKEQYA 98
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGG-------FLSYGGPGGGGGGGGVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  99 FIYRSNLVSVKQTYQYPDTQPGDVDAFSREPFVVwfkspktVVKEFVIIPQHTTPETAVREIDELYDVYLDVKQRWKSKN 178
Cdd:pfam03372  74 ILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVL-------VVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEP 146
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2052144882 179 FIFMGDFNADcgYV-PKKHWKNIRLRTQSEFVWLIG 213
Cdd:pfam03372 147 VILAGDFNAD--YIlVSGGLTVLSVGVLPDLGPRTG 180
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
17-278 2.64e-08

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 54.26  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  17 SIKICSFNVRSF------------GEAKRARPEV-LDVIVKVISR--CDIMLLMEIKDNSNkicplLIEKLNGQSQEE-- 79
Cdd:COG2374    68 DLRVATFNVENLfdtddddddfgrGADTPEEYERkLAKIAAAIAAldADIVGLQEVENNGS-----ALQDLVAALNLAgg 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  80 -YDYVISKRlGRKSYKEQYAFIYRSNLVSVKQTYQYPDT--QPGDVDAFSREPFVVWFKSPKTvvKEFVIIPQH----TT 152
Cdd:COG2374   143 tYAFVHPPD-GPDGDGIRVALLYRPDRVTLVGSATIADLpdSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskGS 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882 153 PETA----------VREIDELYDVYLDVKQRWKSKNFIFMGDFNADCGYVPKKHwknirLRTQSEFV----WLIGDKNDT 218
Cdd:COG2374   220 DDPGdgqgaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDYPFEDPLRA-----LLGAGGLTnlaeKLPAAERYS 294
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2052144882 219 TVRNSTNCAYDRIVIHGEkLINAVVP-----NSADI--IDFQKAFGMTEEQALEVSDHFP--IEFELKT 278
Cdd:COG2374   295 YVYDGNSGLLDHILVSPA-LAARVTGadiwhINADIynDDFKPDFRTYADDPGRASDHDPvvVGLRLPP 362
 
Name Accession Description Interval E-value
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
19-276 1.28e-169

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: 469.41  E-value: 1.28e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  19 KICSFNVRSFGEAKRARPEVLDVIVKVISRCDIMLLMEIKDNSNKICPLLIEKLNGQSQEEYDYVISKRLGRKSYKEQYA 98
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  99 FIYRSNLVSVKQTYQYPDTQPGDvDAFSREPFVVWFKSPKTVVKEFVIIPQHTTPETAVREIDELYDVYLDVKQRWKSKN 178
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDEGT-DVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882 179 FIFMGDFNADCGYVPKKHWKNIRLRTQSEFVWLIGDKNDTTVRnSTNCAYDRIVIHGEKLINAVVPNSADIIDFQKAFGM 258
Cdd:cd10282   160 VILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238
                         250
                  ....*....|....*...
gi 2052144882 259 TEEQALEVSDHFPIEFEL 276
Cdd:cd10282   239 TEEEALAVSDHYPVEVEL 256
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
1-277 3.48e-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: 464.22  E-value: 3.48e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882    1 MFCISLFLLFFFNATLSIKICSFNVRSFGEAKRARPEVLDVIVKVISRCDIMLLMEIKDNSNKICPLLIEKLNGQSQEEY 80
Cdd:smart00476   1 LVPSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882   81 DYVISKRLGRKSYKEQYAFIYRSNLVSVKQTYQYPDTQPGDVDAFSREPFVVWFKSPKTVVKEFVIIPQHTTPETAVREI 160
Cdd:smart00476  81 SYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  161 DELYDVYLDVKQRWKSKNFIFMGDFNADCGYVPKKHWKNIRLRTQSEFVWLIGDKNDTTVRnSTNCAYDRIVIHGEKLIN 240
Cdd:smart00476 161 DALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRS 239
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2052144882  241 AVVPNSADIIDFQKAFGMTEEQALEVSDHFPIEFELK 277
Cdd:smart00476 240 SVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
19-276 3.31e-79

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: 240.38  E-value: 3.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  19 KICSFNVRSFGEAKRARPEVLDVIVKVISRCDIMLLMEIKDNSNKICPLLIEKLNGQSQEEYDYVISKRLGRKSYKEQYA 98
Cdd:cd09075     1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  99 FIYRSNLVSVKQTYQYpDTQPGDV--DAFSREPFVVWFKSPKTVVKEFVIIPQHTTPETAVREIDELYDVYLDVKQRWKS 176
Cdd:cd09075    81 FLFRPNKVSVLDTYQY-DDGCKSCgnDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882 177 KNFIFMGDFNADCGYVPKKHWKNIRLRTQSEFVWLIGDKNDTTVrNSTNCAYDRIVIHGEKLINAVVPNSADIIDFQKAF 256
Cdd:cd09075   160 NDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTA-TSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAY 238
                         250       260
                  ....*....|....*....|
gi 2052144882 257 GMTEEQALEVSDHFPIEFEL 276
Cdd:cd09075   239 GLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
18-276 1.48e-29

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: 112.49  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  18 IKICSFNVRSFGEAKRArpEVLDVIVKVISR--CDIMLLMEIKDNSNKICPL--LIEKLNGQSqEEYDYVIS-KRLGRKS 92
Cdd:cd10283     1 LRIASWNILNFGNSKGK--EKNPAIAEIISAfdLDLIALQEVMDNGGGLDALakLVNELNKPG-GTWKYIVSdKTGGSSG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  93 YKEQYAFIYRSNLVS-VKQTYQYPDTQPgdvDAFSREPFVVWFKSpKTVVKEFVIIPQH-------TTPETA--VREIDE 162
Cdd:cd10283    78 DKERYAFLYKSSKVRkVGKAVLEKDSNT---DGFARPPYAAKFKS-GGTGFDFTLVNVHlksggssKSGQGAkrVAEAQA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882 163 LYDVYLDVKQRWKSKNFIFMGDFNAdcgYVPKKHWKNIrlrTQSEFVWLIGDKNDTTvrNSTNC---AYDRIVIHGEKLI 239
Cdd:cd10283   154 LAEYLKELADEDPDDDVILLGDFNI---PADEDAFKAL---TKAGFKSLLPDSTNLS--TSFKGyanSYDNIFVSGNLKE 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2052144882 240 NavvPNSADIIDFQKAFGMTEEQALE-------VSDHFPIEFEL 276
Cdd:cd10283   226 K---FSNSGVFDFNILVDEAGEEDLDyskwrkqISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
20-276 3.73e-25

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: 100.25  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  20 ICSFNVRSFGEAKRARpevldVIVKVISRC--DIMLLMEIKDNSNKICPLLIEKLNGqsqeeYDYVISKRlGRKSYKEQY 97
Cdd:cd08372     1 VASYNVNGLNAATRAS-----GIARWVRELdpDIVCLQEVKDSQYSAVALNQLLPEG-----YHQYQSGP-SRKEGYEGV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  98 AFIYRSNLVSVKQTYQYpdtQPGDVDAFSREPFVVWFKSPKtvvKEFVIIPQH-----TTPETAVREIDELYDVYLDvKQ 172
Cdd:cd08372    70 AILSKTPKFKIVEKHQY---KFGEGDSGERRAVVVKFDVHD---KELCVVNAHlqaggTRADVRDAQLKEVLEFLKR-LR 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882 173 RWKSKNFIFMGDFNADCGYVPKKHWKN-IRLRTQSEFVWLI-----GDKNDTTVRNsTNCAYDRIVIHGEKLInavVPNS 246
Cdd:cd08372   143 QPNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFetlphAYTFDTYMHN-VKSRLDYIFVSKSLLP---SVKS 218
                         250       260       270
                  ....*....|....*....|....*....|
gi 2052144882 247 ADIIDFQKAfgmteeqALEVSDHFPIEFEL 276
Cdd:cd08372   219 SKILSDAAR-------ARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
21-213 1.03e-18

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: 81.50  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  21 CSFNVRSFGEAKRARPEVLDVIVKVISRC--DIMLLMEIKDNSNKICPLLIEKLNGqsqeeydYVISKRLGRKSYKEQYA 98
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGG-------FLSYGGPGGGGGGGGVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  99 FIYRSNLVSVKQTYQYPDTQPGDVDAFSREPFVVwfkspktVVKEFVIIPQHTTPETAVREIDELYDVYLDVKQRWKSKN 178
Cdd:pfam03372  74 ILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVL-------VVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEP 146
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2052144882 179 FIFMGDFNADcgYV-PKKHWKNIRLRTQSEFVWLIG 213
Cdd:pfam03372 147 VILAGDFNAD--YIlVSGGLTVLSVGVLPDLGPRTG 180
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
17-278 2.64e-08

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 54.26  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  17 SIKICSFNVRSF------------GEAKRARPEV-LDVIVKVISR--CDIMLLMEIKDNSNkicplLIEKLNGQSQEE-- 79
Cdd:COG2374    68 DLRVATFNVENLfdtddddddfgrGADTPEEYERkLAKIAAAIAAldADIVGLQEVENNGS-----ALQDLVAALNLAgg 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882  80 -YDYVISKRlGRKSYKEQYAFIYRSNLVSVKQTYQYPDT--QPGDVDAFSREPFVVWFKSPKTvvKEFVIIPQH----TT 152
Cdd:COG2374   143 tYAFVHPPD-GPDGDGIRVALLYRPDRVTLVGSATIADLpdSPGNPDRFSRPPLAVTFELANG--EPFTVIVNHfkskGS 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052144882 153 PETA----------VREIDELYDVYLDVKQRWKSKNFIFMGDFNADCGYVPKKHwknirLRTQSEFV----WLIGDKNDT 218
Cdd:COG2374   220 DDPGdgqgaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDYPFEDPLRA-----LLGAGGLTnlaeKLPAAERYS 294
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2052144882 219 TVRNSTNCAYDRIVIHGEkLINAVVP-----NSADI--IDFQKAFGMTEEQALEVSDHFP--IEFELKT 278
Cdd:COG2374   295 YVYDGNSGLLDHILVSPA-LAARVTGadiwhINADIynDDFKPDFRTYADDPGRASDHDPvvVGLRLPP 362
 
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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