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Conserved domains on  [gi|1622913602|ref|XP_014980905|]
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deoxyribonuclease-1 [Macaca mulatta]

Protein Classification

DNase I family protein( domain architecture ID 11270576)

deoxyribonuclease I (DNase I) family protein similar to Homo sapiens deoxyribonuclease-1 that catalyzes endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

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
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
22-288 4.69e-175

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: 484.25  E-value: 4.69e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602   22 SLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKER 101
Cdd:smart00476  17 SLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYKEQ 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  102 YLFVYRPDQVSVVDSYYYDDGCEpCGNDTFSREPAIVRFSCPFTgsgrctEVREFAIVPLHAAPEDAVAEIDALYDVYLD 181
Cdd:smart00476  97 YLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPST------AVKEFVIVPLHTTPEAAVAEIDALYDVYLD 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  182 VQDKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLRTSPTFQWLIPDTADTTATSTHCAYDRIVVAGTLLQDAVVPDSALPF 261
Cdd:smart00476 170 VRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVF 249
                          250       260
                   ....*....|....*....|....*..
gi 1622913602  262 NFQAAYGLSDQLAQAISDHYPVEVMLK 288
Cdd:smart00476 250 DFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
22-288 4.69e-175

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: 484.25  E-value: 4.69e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602   22 SLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKER 101
Cdd:smart00476  17 SLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYKEQ 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  102 YLFVYRPDQVSVVDSYYYDDGCEpCGNDTFSREPAIVRFSCPFTgsgrctEVREFAIVPLHAAPEDAVAEIDALYDVYLD 181
Cdd:smart00476  97 YLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPST------AVKEFVIVPLHTTPEAAVAEIDALYDVYLD 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  182 VQDKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLRTSPTFQWLIPDTADTTATSTHCAYDRIVVAGTLLQDAVVPDSALPF 261
Cdd:smart00476 170 VRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVF 249
                          250       260
                   ....*....|....*....|....*..
gi 1622913602  262 NFQAAYGLSDQLAQAISDHYPVEVMLK 288
Cdd:smart00476 250 DFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
24-287 1.55e-142

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: 401.23  E-value: 1.55e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  24 KIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYL 103
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 104 FVYRPDQVSVVDSYYYDDGCEPcgNDTFSREPAIVRFSCPFTGsgrcteVREFAIVPLHAAPEDAVAEIDALYDVYLDVQ 183
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDEG--TDVFSREPFVVRFSSPSTA------VKDFVLVPIHTSPDDAVAEIDALYDVYDDVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 184 DKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLRTSPTFQWLIPDTADTTATSTHCAYDRIVVAGTLLQDAVVPDSALPFNF 263
Cdd:cd10282   153 QRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQSAVVPGSAGVFDF 232
                         250       260
                  ....*....|....*....|....
gi 1622913602 264 QAAYGLSDQLAQAISDHYPVEVML 287
Cdd:cd10282   233 DKEFGLTEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
26-199 3.13e-12

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: 63.78  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  26 AAFNIQTFGETKMSNATLVSYIVQILSRY--DIALVQEVRDSHLTAVGKLLDNLnqdapdtYHYVVSEPLGRNSYKERYL 103
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-------GGFLSYGGPGGGGGGGGVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 104 FVYRPDQVSVVDSYYYDDGCEPCGNDTFSREPAIVRFSCPFtgsgrctevrefaiVPLHAAPEDAVAEIDALYDVYLDVQ 183
Cdd:pfam03372  74 ILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLT--------------LAPHASPRLARDEQRADLLLLLLAL 139
                         170
                  ....*....|....*.
gi 1622913602 184 DKWGLEDVMLMGDFNA 199
Cdd:pfam03372 140 LAPRSEPVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
21-200 1.38e-08

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 55.03  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  21 MSLKIAAFNIQTFGETK-------MSNATLVSY------IVQILSRY--DIALVQEVrDSHLTAVGKLLDNLNQDAPdTY 85
Cdd:COG2374    67 GDLRVATFNVENLFDTDdddddfgRGADTPEEYerklakIAAAIAALdaDIVGLQEV-ENNGSALQDLVAALNLAGG-TY 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  86 HYVVSEplgrNSYKERYL---FVYRPDQVSVVDS-YYYDDGCEPCGNDTFSREPAIVRFScpfTGSGRctevrEFAIVPL 161
Cdd:COG2374   145 AFVHPP----DGPDGDGIrvaLLYRPDRVTLVGSaTIADLPDSPGNPDRFSRPPLAVTFE---LANGE-----PFTVIVN 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622913602 162 HA---APEDA-----------VAEIDALYDVYLDVQDKWGLEDVMLMGDFNAG 200
Cdd:COG2374   213 HFkskGSDDPgdgqgaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDY 265
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
22-288 4.69e-175

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: 484.25  E-value: 4.69e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602   22 SLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKER 101
Cdd:smart00476  17 SLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYKEQ 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  102 YLFVYRPDQVSVVDSYYYDDGCEpCGNDTFSREPAIVRFSCPFTgsgrctEVREFAIVPLHAAPEDAVAEIDALYDVYLD 181
Cdd:smart00476  97 YLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPST------AVKEFVIVPLHTTPEAAVAEIDALYDVYLD 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  182 VQDKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLRTSPTFQWLIPDTADTTATSTHCAYDRIVVAGTLLQDAVVPDSALPF 261
Cdd:smart00476 170 VRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVF 249
                          250       260
                   ....*....|....*....|....*..
gi 1622913602  262 NFQAAYGLSDQLAQAISDHYPVEVMLK 288
Cdd:smart00476 250 DFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
24-287 1.55e-142

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: 401.23  E-value: 1.55e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  24 KIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYL 103
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 104 FVYRPDQVSVVDSYYYDDGCEPcgNDTFSREPAIVRFSCPFTGsgrcteVREFAIVPLHAAPEDAVAEIDALYDVYLDVQ 183
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDEG--TDVFSREPFVVRFSSPSTA------VKDFVLVPIHTSPDDAVAEIDALYDVYDDVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 184 DKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLRTSPTFQWLIPDTADTTATSTHCAYDRIVVAGTLLQDAVVPDSALPFNF 263
Cdd:cd10282   153 QRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQSAVVPGSAGVFDF 232
                         250       260
                  ....*....|....*....|....
gi 1622913602 264 QAAYGLSDQLAQAISDHYPVEVML 287
Cdd:cd10282   233 DKEFGLTEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
24-287 3.35e-125

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: 357.48  E-value: 3.35e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  24 KIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYL 103
Cdd:cd09075     1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 104 FVYRPDQVSVVDSYYYDDGCEPCGNDTFSREPAIVRFScpftgsGRCTEVREFAIVPLHAAPEDAVAEIDALYDVYLDVQ 183
Cdd:cd09075    81 FLFRPNKVSVLDTYQYDDGCKSCGNDSFSREPAVVKFS------SHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 184 DKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLRTSPTFQWLIPDTADTTATSTHCAYDRIVVAGTLLQDAVVPDSALPFNF 263
Cdd:cd09075   155 QKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDF 234
                         250       260
                  ....*....|....*....|....
gi 1622913602 264 QAAYGLSDQLAQAISDHYPVEVML 287
Cdd:cd09075   235 QAAYGLSNEMALAISDHYPVEVTL 258
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
25-287 5.53e-35

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: 126.44  E-value: 5.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  25 IAAFNIQTFGEtkmsnATLVSYIVQILSR--YDIALVQEVRDSHLTAVGklldnLNQDAPDTYHYVVSEPLGRnSYKERY 102
Cdd:cd08372     1 VASYNVNGLNA-----ATRASGIARWVREldPDIVCLQEVKDSQYSAVA-----LNQLLPEGYHQYQSGPSRK-EGYEGV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 103 LFVYRPDQVSVVDSYYYDDGCEpcgnDTFSREPAIVRFSCpftgsgrctEVREFAIVPLHAAP-----EDAVAEIDALYD 177
Cdd:cd08372    70 AILSKTPKFKIVEKHQYKFGEG----DSGERRAVVVKFDV---------HDKELCVVNAHLQAggtraDVRDAQLKEVLE 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 178 VYLDVQDkWGLEDVMLMGDFNAGCSYVRPSQWSS-IRLRTSPTFQWLIPDTADT-----TATSTHCAYDRIVVAGTLLqd 251
Cdd:cd08372   137 FLKRLRQ-PNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFETLPHAytfdtYMHNVKSRLDYIFVSKSLL-- 213
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622913602 252 aVVPDSALPFNFQaayglsdQLAQAISDHYPVEVML 287
Cdd:cd08372   214 -PSVKSSKILSDA-------ARARIPSDHYPIEVTL 241
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
23-287 7.47e-31

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: 115.96  E-value: 7.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  23 LKIAAFNIQTFGETKMSNATlvSYIVQILSRYDIALV--QEVRDS--HLTAVGKLLDNLNQdAPDTYHYVVSEPLGRNS- 97
Cdd:cd10283     1 LRIASWNILNFGNSKGKEKN--PAIAEIISAFDLDLIalQEVMDNggGLDALAKLVNELNK-PGGTWKYIVSDKTGGSSg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  98 YKERYLFVYRPDQVSVVD-SYYYDDGcepcGNDTFSREPAIVRFSCPFTGSgrctevrEFAIVPLHA---------APED 167
Cdd:cd10283    78 DKERYAFLYKSSKVRKVGkAVLEKDS----NTDGFARPPYAAKFKSGGTGF-------DFTLVNVHLksggssksgQGAK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 168 AVAEIDALYDVYLDVQDKWGLEDVMLMGDFNAgcsYVRPSQWSSIrlrTSPTFQWLIPDTADTTATSTHCA--YDRIVVA 245
Cdd:cd10283   147 RVAEAQALAEYLKELADEDPDDDVILLGDFNI---PADEDAFKAL---TKAGFKSLLPDSTNLSTSFKGYAnsYDNIFVS 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622913602 246 GTLLQDAVVPDSalpFNFQAAYGLSDQLAQ-------AISDHYPVEVML 287
Cdd:cd10283   221 GNLKEKFSNSGV---FDFNILVDEAGEEDLdyskwrkQISDHDPVWVEF 266
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
26-199 3.13e-12

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: 63.78  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  26 AAFNIQTFGETKMSNATLVSYIVQILSRY--DIALVQEVRDSHLTAVGKLLDNLnqdapdtYHYVVSEPLGRNSYKERYL 103
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-------GGFLSYGGPGGGGGGGGVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602 104 FVYRPDQVSVVDSYYYDDGCEPCGNDTFSREPAIVRFSCPFtgsgrctevrefaiVPLHAAPEDAVAEIDALYDVYLDVQ 183
Cdd:pfam03372  74 ILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLT--------------LAPHASPRLARDEQRADLLLLLLAL 139
                         170
                  ....*....|....*.
gi 1622913602 184 DKWGLEDVMLMGDFNA 199
Cdd:pfam03372 140 LAPRSEPVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
21-200 1.38e-08

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 55.03  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  21 MSLKIAAFNIQTFGETK-------MSNATLVSY------IVQILSRY--DIALVQEVrDSHLTAVGKLLDNLNQDAPdTY 85
Cdd:COG2374    67 GDLRVATFNVENLFDTDdddddfgRGADTPEEYerklakIAAAIAALdaDIVGLQEV-ENNGSALQDLVAALNLAGG-TY 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622913602  86 HYVVSEplgrNSYKERYL---FVYRPDQVSVVDS-YYYDDGCEPCGNDTFSREPAIVRFScpfTGSGRctevrEFAIVPL 161
Cdd:COG2374   145 AFVHPP----DGPDGDGIrvaLLYRPDRVTLVGSaTIADLPDSPGNPDRFSRPPLAVTFE---LANGE-----PFTVIVN 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622913602 162 HA---APEDA-----------VAEIDALYDVYLDVQDKWGLEDVMLMGDFNAG 200
Cdd:COG2374   213 HFkskGSDDPgdgqgaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDY 265
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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