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Conserved domains on  [gi|1370468004|ref|XP_024305938|]
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deoxyribonuclease-1 isoform X2 [Homo sapiens]

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.-
Gene Ontology:  GO:0046872|GO:0003677|GO:0004530|GO:0006259
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 ...
 21-267 2.55e-173

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: 479.25  E-value: 2.55e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004   21 VSLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKE 100
Cdd:smart00476  16 ASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYKE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  101 RYLFVYRPDQVSAVDSYYYDDGCEpCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKW 180
Cdd:smart00476  96 QYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQKW 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  181 GLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAA 260
Cdd:smart00476 175 GTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQTA 254


                   ....*..
gi 1370468004  261 YGLSDQL 267
Cdd:smart00476 255 YGLTEEE 261
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 21-267 2.55e-173

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: 479.25  E-value: 2.55e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004   21 VSLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKE 100
Cdd:smart00476  16 ASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYKE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  101 RYLFVYRPDQVSAVDSYYYDDGCEpCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKW 180
Cdd:smart00476  96 QYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQKW 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  181 GLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAA 260
Cdd:smart00476 175 GTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQTA 254


                   ....*..
gi 1370468004  261 YGLSDQL 267
Cdd:smart00476 255 YGLTEEE 261
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 24-265 1.11e-138

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: 390.83  E-value: 1.11e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  24 KIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYL 103
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 104 FVYRPDQVSAVDSYYYDDGCEPcgNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLE 183
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDEG--TDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRED 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 184 DVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGL 263
Cdd:cd10282   159 DVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238


                  ..
gi 1370468004 264 SD 265
Cdd:cd10282   239 TE 240
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 26-193 1.08e-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: 64.94  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  26 AAFNIQTFGETKMSNATLVSYIVQILSRY--DIALVQEVRDSHLTAVGKLLDNLnqdapdtYHYVVSEPLGRNSYKERYL 103
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-------GGFLSYGGPGGGGGGGGVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 104 FVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFsrftevreFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLE 183
Cdd:pfam03372  74 ILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPL--------VLTLAPHASPRLARDEQRADLLLLLLALLAPRSE 145

                         170
                  ....*....|
gi 1370468004 184 DVMLMGDFNA 193
Cdd:pfam03372 146 PVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
22-194 3.17e-09

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 56.95  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  22 SLKIAAFNIQTFGETKMSN-------------ATLVSYIVQILSRY--DIALVQEVrDSHLTAVGKLLDNLNQDAPdTYH 86
Cdd:COG2374    68 DLRVATFNVENLFDTDDDDddfgrgadtpeeyERKLAKIAAAIAALdaDIVGLQEV-ENNGSALQDLVAALNLAGG-TYA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  87 YVVSEplgrNSYKERYL---FVYRPDQVSAVDS-YYYDDGCEPCGNDTFNREPAIVRFfsRFTEVREFAIVPLH------ 156
Cdd:COG2374   146 FVHPP----DGPDGDGIrvaLLYRPDRVTLVGSaTIADLPDSPGNPDRFSRPPLAVTF--ELANGEPFTVIVNHfkskgs 219

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370468004 157 AAPGDA--------VAEIDALYDVYLDVQEKWGLEDVMLMGDFNAG 194
Cdd:COG2374   220 DDPGDGqgaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDY 265
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 21-267 2.55e-173

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: 479.25  E-value: 2.55e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004   21 VSLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKE 100
Cdd:smart00476  16 ASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPNTYSYVSSEPLGRNSYKE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  101 RYLFVYRPDQVSAVDSYYYDDGCEpCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKW 180
Cdd:smart00476  96 QYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEIDALYDVYLDVRQKW 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  181 GLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAA 260
Cdd:smart00476 175 GTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRIVVAGERLRSSVVPGSAAVFDFQTA 254


                   ....*..
gi 1370468004  261 YGLSDQL 267
Cdd:smart00476 255 YGLTEEE 261
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 24-265 1.11e-138

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: 390.83  E-value: 1.11e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  24 KIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYL 103
Cdd:cd10282     1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNSASSNTYSYVVSERLGRSSYKEQYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 104 FVYRPDQVSAVDSYYYDDGCEPcgNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLE 183
Cdd:cd10282    81 FIYRSDKVSVLESYQYDDGDEG--TDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWRED 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 184 DVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGL 263
Cdd:cd10282   159 DVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKEFGL 238


                  ..
gi 1370468004 264 SD 265
Cdd:cd10282   239 TE 240
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 24-267 8.10e-122

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: 348.23  E-value: 8.10e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  24 KIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYL 103
Cdd:cd09075     1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 104 FVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLE 183
Cdd:cd09075    81 FLFRPNKVSVLDTYQYDDGCKSCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 184 DVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGL 263
Cdd:cd09075   161 DVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGL 240


                  ....
gi 1370468004 264 SDQL 267
Cdd:cd09075   241 SNEM 244
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 25-265 4.64e-32

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: 118.35  E-value: 4.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  25 IAAFNIQTFGEtkmsnATLVSYIVQILSR--YDIALVQEVRDSHLTAVGklldnLNQDAPDTYHYVVSEPLGRnSYKERY 102
Cdd:cd08372     1 VASYNVNGLNA-----ATRASGIARWVREldPDIVCLQEVKDSQYSAVA-----LNQLLPEGYHQYQSGPSRK-EGYEGV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 103 LFVYRPDQVSAVDSYYYDDGCEpcgnDTFNREPAIVRFFSrftEVREFAIVPLHAAPG-----DAVAEIDALYDVYLDVQ 177
Cdd:cd08372    70 AILSKTPKFKIVEKHQYKFGEG----DSGERRAVVVKFDV---HDKELCVVNAHLQAGgtradVRDAQLKEVLEFLKRLR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 178 EkWGLEDVMLMGDFNAGCSYVRPSQWSS-IRLWTSPTFQWLIPD--SADTTATPTH---CAYDRIVVAGMLLrgAVVPDS 251
Cdd:cd08372   143 Q-PNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFETlpHAYTFDTYMHnvkSRLDYIFVSKSLL--PSVKSS 219

                         250
                  ....*....|....
gi 1370468004 252 ALPFNFQAAYGLSD 265
Cdd:cd08372   220 KILSDAARARIPSD 233
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 23-265 1.34e-30

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: 115.19  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  23 LKIAAFNIQTFGETKMSNATlvSYIVQILSRYDIALV--QEVRDS--HLTAVGKLLDNLNQdAPDTYHYVVSEPLGRNS- 97
Cdd:cd10283     1 LRIASWNILNFGNSKGKEKN--PAIAEIISAFDLDLIalQEVMDNggGLDALAKLVNELNK-PGGTWKYIVSDKTGGSSg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  98 YKERYLFVYRPDQVSAVD-SYYYDDGcepcGNDTFNREPAIVRFFSRFTEVrEFAIVPLHAAPGDA---------VAEID 167
Cdd:cd10283    78 DKERYAFLYKSSKVRKVGkAVLEKDS----NTDGFARPPYAAKFKSGGTGF-DFTLVNVHLKSGGSsksgqgakrVAEAQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 168 ALYDVYLDVQEKWGLEDVMLMGDFNAgcsyvrPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCA--YDRIVVAGMLLR- 244
Cdd:cd10283   153 ALAEYLKELADEDPDDDVILLGDFNI------PADEDAFKALTKAGFKSLLPDSTNLSTSFKGYAnsYDNIFVSGNLKEk 226

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1370468004 245 -----------GAVVPDSALPFNFQAAYGLSD 265
Cdd:cd10283   227 fsnsgvfdfniLVDEAGEEDLDYSKWRKQISD 258
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 26-193 1.08e-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: 64.94  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  26 AAFNIQTFGETKMSNATLVSYIVQILSRY--DIALVQEVRDSHLTAVGKLLDNLnqdapdtYHYVVSEPLGRNSYKERYL 103
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAY-------GGFLSYGGPGGGGGGGGVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004 104 FVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFsrftevreFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLE 183
Cdd:pfam03372  74 ILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPL--------VLTLAPHASPRLARDEQRADLLLLLLALLAPRSE 145

                         170
                  ....*....|
gi 1370468004 184 DVMLMGDFNA 193
Cdd:pfam03372 146 PVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
22-194 3.17e-09

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 56.95  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  22 SLKIAAFNIQTFGETKMSN-------------ATLVSYIVQILSRY--DIALVQEVrDSHLTAVGKLLDNLNQDAPdTYH 86
Cdd:COG2374    68 DLRVATFNVENLFDTDDDDddfgrgadtpeeyERKLAKIAAAIAALdaDIVGLQEV-ENNGSALQDLVAALNLAGG-TYA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468004  87 YVVSEplgrNSYKERYL---FVYRPDQVSAVDS-YYYDDGCEPCGNDTFNREPAIVRFfsRFTEVREFAIVPLH------ 156
Cdd:COG2374   146 FVHPP----DGPDGDGIrvaLLYRPDRVTLVGSaTIADLPDSPGNPDRFSRPPLAVTF--ELANGEPFTVIVNHfkskgs 219

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370468004 157 AAPGDA--------VAEIDALYDVYLDVQEKWGLEDVMLMGDFNAG 194
Cdd:COG2374   220 DDPGDGqgaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDY 265
CdiI_Ykris-like cd20687
inhibitor (or immunity protein) of the contact-dependent growth inhibition (CDI) system of ...
 162-209 4.26e-03

inhibitor (or immunity protein) of the contact-dependent growth inhibition (CDI) system of Yersinia kristensenii, and similar proteins; CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. This model represents the inhibitor (CdiI, also called CdiI immunity protein) of the CdiA effector protein from Yersinia kristensenii (which is an RNase), and similar proteins. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered via its C-terminal domain (CdiA-CT). The CdiI immunity proteins are intracellular proteins that inactivate the toxin/effector protein. They are specific for their cognate CdiA-CT and do not protect cells from the toxins of other CDI+ bacteria. The CdiI immunity protein binds the CdiA toxin via its C-terminal domain to prevent auto-inhibition. Thus, CDI systems encode a complex network of toxin-immunity protein pairs that are deployed for intercellular competition. Y. kristensenii CdiI binds directly over the putative active site of the CdiA-CT toxin and likely neutralizes toxicity by blocking access to RNA substrates.


Pssm-ID: 412039  Cd Length: 90  Bit Score: 35.59  E-value: 4.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370468004 162 AVAEIDALYDVYLDVQEkwgLEDVMLmgdFNAGCSYVRPSQWSSIRLW 209
Cdd:cd20687    41 VRAEIDALLALDLSEEE---LRDLLL---KELGCYYYPPSEWLSGREW 82
 
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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