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Conserved domains on  [gi|1908122207|ref|NP_001374070|]
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deoxyribonuclease-1 isoform 4 [Homo sapiens]

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 ...
 8-213 8.09e-145

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: 404.52  E-value: 8.09e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207    8 LCRDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEpCGNDTFNREPAIVRFFSRFTEVREFAIVPLH 87
Cdd:smart00476  72 LNSDSPNTYSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLH 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207   88 AAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRI 167
Cdd:smart00476 151 TTPEAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRI 230

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1908122207  168 VVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK 213
Cdd:smart00476 231 VVAGERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 8-213 8.09e-145

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: 404.52  E-value: 8.09e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207    8 LCRDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEpCGNDTFNREPAIVRFFSRFTEVREFAIVPLH 87
Cdd:smart00476  72 LNSDSPNTYSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLH 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207   88 AAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRI 167
Cdd:smart00476 151 TTPEAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRI 230

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1908122207  168 VVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK 213
Cdd:smart00476 231 VVAGERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 14-212 1.11e-114

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: 327.27  E-value: 1.11e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  14 DTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPcgNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDA 93
Cdd:cd10282    60 NTYSYVVSERLGRSSYKEQYAFIYRSDKVSVLESYQYDDGDEG--TDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  94 VAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGML 173
Cdd:cd10282   138 VAEIDALYDVYDDVKQRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSL 217

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1908122207 174 LRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVML 212
Cdd:cd10282   218 LQSAVVPGSAGVFDFDKEFGLTEEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 16-124 4.58e-05

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: 42.60  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  16 YHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFsrftevreFAIVPLHAAPGDAVA 95
Cdd:pfam03372  55 GGFLSYGGPGGGGGGGGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPL--------VLTLAPHASPRLARD 126

                          90       100
                  ....*....|....*....|....*....
gi 1908122207  96 EIDALYDVYLDVQEKWGLEDVMLMGDFNA 124
Cdd:pfam03372 127 EQRADLLLLLLALLAPRSEPVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
35-125 1.01e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 42.32  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  35 FVYRPDQVSAVDS-YYYDDGCEPCGNDTFNREPAIVRFfsRFTEVREFAIVPLH------AAPGDA--------VAEIDA 99
Cdd:COG2374   162 LLYRPDRVTLVGSaTIADLPDSPGNPDRFSRPPLAVTF--ELANGEPFTVIVNHfkskgsDDPGDGqgaseakrTAQAEA 239

                          90       100
                  ....*....|....*....|....*.
gi 1908122207 100 LYDVYLDVQEKWGLEDVMLMGDFNAG 125
Cdd:COG2374   240 LRAFVDSLLAADPDAPVIVLGDFNDY 265
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
 8-213 8.09e-145

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: 404.52  E-value: 8.09e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207    8 LCRDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEpCGNDTFNREPAIVRFFSRFTEVREFAIVPLH 87
Cdd:smart00476  72 LNSDSPNTYSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCE-CGNDVFSREPFVVKFSSPSTAVKEFVIVPLH 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207   88 AAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRI 167
Cdd:smart00476 151 TTPEAAVAEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVTSTHCAYDRI 230

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1908122207  168 VVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK 213
Cdd:smart00476 231 VVAGERLRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
 14-212 1.11e-114

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: 327.27  E-value: 1.11e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  14 DTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPcgNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDA 93
Cdd:cd10282    60 NTYSYVVSERLGRSSYKEQYAFIYRSDKVSVLESYQYDDGDEG--TDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  94 VAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGML 173
Cdd:cd10282   138 VAEIDALYDVYDDVKQRWREDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVRSTNCAYDRIVVAGSL 217

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1908122207 174 LRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVML 212
Cdd:cd10282   218 LQSAVVPGSAGVFDFDKEFGLTEEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
 8-212 2.83e-101

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: 293.54  E-value: 2.83e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207   8 LCRDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLH 87
Cdd:cd09075    54 LNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCKSCGNDSFSREPAVVKFSSHSTKVKEFAIVALH 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  88 AAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRI 167
Cdd:cd09075   134 SAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRI 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1908122207 168 VVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVML 212
Cdd:cd09075   214 VVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTL 258
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 1-212 1.34e-27

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: 104.87  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207   1 MPPSSATLCRDAPDTYHYVVSEPLGRnSYKERYLFVYRPDQVSAVDSYYYDDGCEpcgnDTFNREPAIVRFFSrftEVRE 80
Cdd:cd08372    38 SQYSAVALNQLLPEGYHQYQSGPSRK-EGYEGVAILSKTPKFKIVEKHQYKFGEG----DSGERRAVVVKFDV---HDKE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  81 FAIVPLHAAPG-----DAVAEIDALYDVYLDVQEkWGLEDVMLMGDFNAGCSYVRPSQWSS-IRLWTSPTFQWLIPD--S 152
Cdd:cd08372   110 LCVVNAHLQAGgtradVRDAQLKEVLEFLKRLRQ-PNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFETlpH 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1908122207 153 ADTTATPTH---CAYDRIVVAGMLLrgaVVPDSALPFNFQaayglsdQLAQAISDHYPVEVML 212
Cdd:cd08372   189 AYTFDTYMHnvkSRLDYIFVSKSLL---PSVKSSKILSDA-------ARARIPSDHYPIEVTL 241
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 11-212 5.58e-21

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: 87.84  E-value: 5.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  11 DAPDTYHYVVSEPLGRNS-YKERYLFVYRPDQVSAVD-SYYYDDGcepcGNDTFNREPAIVRFFSRFTEVrEFAIVPLHA 88
Cdd:cd10283    59 KPGGTWKYIVSDKTGGSSgDKERYAFLYKSSKVRKVGkAVLEKDS----NTDGFARPPYAAKFKSGGTGF-DFTLVNVHL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  89 APGDA---------VAEIDALYDVYLDVQEKWGLEDVMLMGDFNAgcsyvrPSQWSSIRLWTSPTFQWLIPDSADTTATP 159
Cdd:cd10283   134 KSGGSsksgqgakrVAEAQALAEYLKELADEDPDDDVILLGDFNI------PADEDAFKALTKAGFKSLLPDSTNLSTSF 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1908122207 160 THCA--YDRIVVAGMLLRGAVVPDSalpFNFQAAYGLSDQLAQ-------AISDHYPVEVML 212
Cdd:cd10283   208 KGYAnsYDNIFVSGNLKEKFSNSGV---FDFNILVDEAGEEDLdyskwrkQISDHDPVWVEF 266
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 16-124 4.58e-05

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: 42.60  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  16 YHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFsrftevreFAIVPLHAAPGDAVA 95
Cdd:pfam03372  55 GGFLSYGGPGGGGGGGGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPL--------VLTLAPHASPRLARD 126

                          90       100
                  ....*....|....*....|....*....
gi 1908122207  96 EIDALYDVYLDVQEKWGLEDVMLMGDFNA 124
Cdd:pfam03372 127 EQRADLLLLLLALLAPRSEPVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
35-125 1.01e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 42.32  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908122207  35 FVYRPDQVSAVDS-YYYDDGCEPCGNDTFNREPAIVRFfsRFTEVREFAIVPLH------AAPGDA--------VAEIDA 99
Cdd:COG2374   162 LLYRPDRVTLVGSaTIADLPDSPGNPDRFSRPPLAVTF--ELANGEPFTVIVNHfkskgsDDPGDGqgaseakrTAQAEA 239

                          90       100
                  ....*....|....*....|....*.
gi 1908122207 100 LYDVYLDVQEKWGLEDVMLMGDFNAG 125
Cdd:COG2374   240 LRAFVDSLLAADPDAPVIVLGDFNDY 265
CdiI_Ykris-like cd20687
inhibitor (or immunity protein) of the contact-dependent growth inhibition (CDI) system of ...
 93-140 5.27e-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: 34.82  E-value: 5.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1908122207  93 AVAEIDALYDVYLDVQEkwgLEDVMLmgdFNAGCSYVRPSQWSSIRLW 140
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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