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Conserved domains on  [gi|569001367|ref|XP_006524861|]
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deoxyribonuclease-1-like 2 isoform X1 [Mus musculus]

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 ...
7-303 3.01e-155

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: 434.95  E-value: 3.01e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367     7 PLTAVWALGVMGATALRIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGF 86
Cdd:smart00476   3 PSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367    87 VSSKPLGRDQYKEMYLFVYRKDVASVVSTYQYPD----PEDAFSREPFVVKFSVPScgelilpsprqaylfqasldphip 162
Cdd:smart00476  83 VSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPS------------------------ 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367   163 ppsTATKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDS 242
Cdd:smart00476 139 ---TAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDS 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569001367   243 ADTTVGNSDCAYDRIVVSGAHLRRSLKPHSASVHNFQEEFDLDQTQALAISDHFPVEVTFK 303
Cdd:smart00476 216 ADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
7-303 3.01e-155

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: 434.95  E-value: 3.01e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367     7 PLTAVWALGVMGATALRIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGF 86
Cdd:smart00476   3 PSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367    87 VSSKPLGRDQYKEMYLFVYRKDVASVVSTYQYPD----PEDAFSREPFVVKFSVPScgelilpsprqaylfqasldphip 162
Cdd:smart00476  83 VSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPS------------------------ 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367   163 ppsTATKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDS 242
Cdd:smart00476 139 ---TAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDS 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569001367   243 ADTTVGNSDCAYDRIVVSGAHLRRSLKPHSASVHNFQEEFDLDQTQALAISDHFPVEVTFK 303
Cdd:smart00476 216 ADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
23-302 9.33e-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: 384.67  E-value: 9.33e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  23 RIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGFVSSKPLGRDQYKEMYL 102
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 103 FVYRKDVASVVSTYQYPD---PEDAFSREPFVVKFSVPScgelilpsprqaylfqasldphipppsTATKELVLIPLHAA 179
Cdd:cd10282   81 FIYRSDKVSVLESYQYDDgdeGTDVFSREPFVVRFSSPS---------------------------TAVKDFVLVPIHTS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 180 PHQAVAEIDALYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVV 259
Cdd:cd10282  134 PDDAVAEIDALYDVYDDVKQRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVV 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 569001367 260 SGAHLRRSLKPHSASVHNFQEEFDLDQTQALAISDHFPVEVTF 302
Cdd:cd10282  214 AGSLLQSAVVPGSAGVFDFDKEFGLTEEEALAVSDHYPVEVEL 256
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
19-303 3.22e-09

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 57.34  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  19 ATALRIGAFNVQSFGDNKVSDPDCGS-----------------VIAQILAgyDIALVQEVRDpDLSAVSLLMEQINrVSK 81
Cdd:COG2374   66 GGDLRVATFNVENLFDTDDDDDDFGRgadtpeeyerklakiaaAIAALDA--DIVGLQEVEN-NGSALQDLVAALN-LAG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  82 HEYGFVSSKPlGRDQYKEMYLFVYRKDVASVVSTYQY------PDPEDAFSREPFVVKFSVPScGELI------LPSPR- 148
Cdd:COG2374  142 GTYAFVHPPD-GPDGDGIRVALLYRPDRVTLVGSATIadlpdsPGNPDRFSRPPLAVTFELAN-GEPFtvivnhFKSKGs 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 149 -QAYLFQASldphipppSTATKelvliplhaaphqaVAEIDALYDVYLDVIDKWNTDDMLFLGDFNADckyvkAHDwPSI 227
Cdd:COG2374  220 dDPGDGQGA--------SEAKR--------------TAQAEALRAFVDSLLAADPDAPVIVLGDFNDY-----PFE-DPL 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 228 R-LRSSE----VFKWLIPDSADTTV--GNSdCAYDRIVVSGAHLRRSLKPH----SASVHN--FQEEFDLDQTQALAISD 294
Cdd:COG2374  272 RaLLGAGgltnLAEKLPAAERYSYVydGNS-GLLDHILVSPALAARVTGADiwhiNADIYNddFKPDFRTYADDPGRASD 350

                 ....*....
gi 569001367 295 HFPVEVTFK 303
Cdd:COG2374  351 HDPVVVGLR 359
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
27-215 2.11e-08

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: 53.00  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367   27 FNVQSFGDNKVSDPDCGSVIAQILAGY--DIALVQEVRDPDLSAVSLLMeqinrvsKHEYGFVSSKPLGRDQYKEMYLFV 104
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLAL-------LAYGGFLSYGGPGGGGGGGGVAIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  105 YRKDVASVVSTYQYPDPEDAFSREPFVVKFSVPscgelilpsprqaylfqasldphipppstaTKELVLIPLHAAPHQAV 184
Cdd:pfam03372  76 SRYPLSSVILVDLGEFGDPALRGAIAPFAGVLV------------------------------VPLVLTLAPHASPRLAR 125
                         170       180       190
                  ....*....|....*....|....*....|.
gi 569001367  185 AEIDALYDVYLDVIDKWNTDDMLFLGDFNAD 215
Cdd:pfam03372 126 DEQRADLLLLLLALLAPRSEPVILAGDFNAD 156
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
7-303 3.01e-155

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: 434.95  E-value: 3.01e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367     7 PLTAVWALGVMGATALRIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGF 86
Cdd:smart00476   3 PSLLLFLLLLHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367    87 VSSKPLGRDQYKEMYLFVYRKDVASVVSTYQYPD----PEDAFSREPFVVKFSVPScgelilpsprqaylfqasldphip 162
Cdd:smart00476  83 VSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDgcecGNDVFSREPFVVKFSSPS------------------------ 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367   163 ppsTATKELVLIPLHAAPHQAVAEIDALYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDS 242
Cdd:smart00476 139 ---TAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDS 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569001367   243 ADTTVGNSDCAYDRIVVSGAHLRRSLKPHSASVHNFQEEFDLDQTQALAISDHFPVEVTFK 303
Cdd:smart00476 216 ADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
23-302 9.33e-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: 384.67  E-value: 9.33e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  23 RIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGFVSSKPLGRDQYKEMYL 102
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 103 FVYRKDVASVVSTYQYPD---PEDAFSREPFVVKFSVPScgelilpsprqaylfqasldphipppsTATKELVLIPLHAA 179
Cdd:cd10282   81 FIYRSDKVSVLESYQYDDgdeGTDVFSREPFVVRFSSPS---------------------------TAVKDFVLVPIHTS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 180 PHQAVAEIDALYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVV 259
Cdd:cd10282  134 PDDAVAEIDALYDVYDDVKQRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVV 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 569001367 260 SGAHLRRSLKPHSASVHNFQEEFDLDQTQALAISDHFPVEVTF 302
Cdd:cd10282  214 AGSLLQSAVVPGSAGVFDFDKEFGLTEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
23-302 1.92e-78

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: 239.22  E-value: 1.92e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  23 RIGAFNVQSFGDNKVSDPDCGSVIAQILAGYDIALVQEVRDPDLSAVSLLMEQINRVSKHEYGFVSSKPLGRDQYKEMYL 102
Cdd:cd09075    1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 103 FVYRKDVASVVSTYQYPDPE-----DAFSREPFVVKFSVPScgelilpsprqaylfqasldphipppsTATKELVLIPLH 177
Cdd:cd09075   81 FLFRPNKVSVLDTYQYDDGCkscgnDSFSREPAVVKFSSHS---------------------------TKVKEFAIVALH 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 178 AAPHQAVAEIDALYDVYLDVIDKWNTDDMLFLGDFNADCKYVKAHDWPSIRLRSSEVFKWLIPDSADTTVGNSDCAYDRI 257
Cdd:cd09075  134 SAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRI 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 569001367 258 VVSGAHLRRSLKPHSASVHNFQEEFDLDQTQALAISDHFPVEVTF 302
Cdd:cd09075  214 VVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
22-302 2.63e-22

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: 93.62  E-value: 2.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  22 LRIGAFNVQSFGDNK-VSDPDCgsvIAQILAGYDIALV--QEVRD--PDLSAVSLLMEQINRVSKHeYGFV-SSKPLGRD 95
Cdd:cd10283    1 LRIASWNILNFGNSKgKEKNPA---IAEIISAFDLDLIalQEVMDngGGLDALAKLVNELNKPGGT-WKYIvSDKTGGSS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  96 QYKEMYLFVYRKD-VASVVSTYQYPD-PEDAFSREPFVVKFSVPSCG-ELILpsprqaylfqASLdpHIPPPSTATKElv 172
Cdd:cd10283   77 GDKERYAFLYKSSkVRKVGKAVLEKDsNTDGFARPPYAAKFKSGGTGfDFTL----------VNV--HLKSGGSSKSG-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 173 liplhaAPHQAVAEIDALYDVYLDVIDKWNTDDMLFLGDFNAdckYVKAHDWPSIRlrsSEVFKWLIPDSADTT--VGNS 250
Cdd:cd10283  143 ------QGAKRVAEAQALAEYLKELADEDPDDDVILLGDFNI---PADEDAFKALT---KAGFKSLLPDSTNLStsFKGY 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569001367 251 DCAYDRIVVSGAHL----RRSLKPHSASVHNFQEEFDLDQTQALAISDHFPVEVTF 302
Cdd:cd10283  211 ANSYDNIFVSGNLKekfsNSGVFDFNILVDEAGEEDLDYSKWRKQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
24-301 4.96e-22

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: 92.54  E-value: 4.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  24 IGAFNVQSFGDNKVSdpdcgSVIAQIL--AGYDIALVQEVRDPDLSAVSLLMEQINRVskheYGFVSskPLGRDQYKEMY 101
Cdd:cd08372    1 VASYNVNGLNAATRA-----SGIARWVreLDPDIVCLQEVKDSQYSAVALNQLLPEGY----HQYQS--GPSRKEGYEGV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 102 LFVYRKDVASVVSTYQY-PDPEDAFSREPFVVKFSVpscgelilpsprqaylfqasldphipppstATKELVLIPLHAAP 180
Cdd:cd08372   70 AILSKTPKFKIVEKHQYkFGEGDSGERRAVVVKFDV------------------------------HDKELCVVNAHLQA 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 181 HQ-----AVAEIDALYDVYLDVIDkWNTDDMLFLGDFNADCKYVKAHDWPS-IRLRSSEVFKWLIPDSA-----DTTVGN 249
Cdd:cd08372  120 GGtradvRDAQLKEVLEFLKRLRQ-PNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFETLPhaytfDTYMHN 198
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569001367 250 SDCAYDRIVVSGAHLrrsLKPHSASVHNfqeefdlDQTQALAISDHFPVEVT 301
Cdd:cd08372  199 VKSRLDYIFVSKSLL---PSVKSSKILS-------DAARARIPSDHYPIEVT 240
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
19-303 3.22e-09

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 57.34  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  19 ATALRIGAFNVQSFGDNKVSDPDCGS-----------------VIAQILAgyDIALVQEVRDpDLSAVSLLMEQINrVSK 81
Cdd:COG2374   66 GGDLRVATFNVENLFDTDDDDDDFGRgadtpeeyerklakiaaAIAALDA--DIVGLQEVEN-NGSALQDLVAALN-LAG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  82 HEYGFVSSKPlGRDQYKEMYLFVYRKDVASVVSTYQY------PDPEDAFSREPFVVKFSVPScGELI------LPSPR- 148
Cdd:COG2374  142 GTYAFVHPPD-GPDGDGIRVALLYRPDRVTLVGSATIadlpdsPGNPDRFSRPPLAVTFELAN-GEPFtvivnhFKSKGs 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 149 -QAYLFQASldphipppSTATKelvliplhaaphqaVAEIDALYDVYLDVIDKWNTDDMLFLGDFNADckyvkAHDwPSI 227
Cdd:COG2374  220 dDPGDGQGA--------SEAKR--------------TAQAEALRAFVDSLLAADPDAPVIVLGDFNDY-----PFE-DPL 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367 228 R-LRSSE----VFKWLIPDSADTTV--GNSdCAYDRIVVSGAHLRRSLKPH----SASVHN--FQEEFDLDQTQALAISD 294
Cdd:COG2374  272 RaLLGAGgltnLAEKLPAAERYSYVydGNS-GLLDHILVSPALAARVTGADiwhiNADIYNddFKPDFRTYADDPGRASD 350

                 ....*....
gi 569001367 295 HFPVEVTFK 303
Cdd:COG2374  351 HDPVVVGLR 359
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
27-215 2.11e-08

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: 53.00  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367   27 FNVQSFGDNKVSDPDCGSVIAQILAGY--DIALVQEVRDPDLSAVSLLMeqinrvsKHEYGFVSSKPLGRDQYKEMYLFV 104
Cdd:pfam03372   3 WNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLAL-------LAYGGFLSYGGPGGGGGGGGVAIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001367  105 YRKDVASVVSTYQYPDPEDAFSREPFVVKFSVPscgelilpsprqaylfqasldphipppstaTKELVLIPLHAAPHQAV 184
Cdd:pfam03372  76 SRYPLSSVILVDLGEFGDPALRGAIAPFAGVLV------------------------------VPLVLTLAPHASPRLAR 125
                         170       180       190
                  ....*....|....*....|....*....|.
gi 569001367  185 AEIDALYDVYLDVIDKWNTDDMLFLGDFNAD 215
Cdd:pfam03372 126 DEQRADLLLLLLALLAPRSEPVILAGDFNAD 156
 
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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