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Conserved domains on  [gi|915089299|ref|WP_050755296|]
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endonuclease/exonuclease/phosphatase family protein [Fusobacterium periodonticum]

Protein Classification

endonuclease/exonuclease/phosphatase family protein( domain architecture ID 10178918)

endonuclease/exonuclease/phosphatase (EEP) family protein is among a diverse set of enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins; similar to Metamycoplasma arthritidis membrane nuclease A-like protein, which might be a membrane-associated nuclease related to deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
17-258 1.55e-54

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: 176.82  E-value: 1.55e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  17 IASFNILRLGA--AEKDMVQTAKLLQGF--DLVGLVEVINK----EGIEDLVDELNRQSPnTWDYHISPFGVGSSKYKEY 88
Cdd:cd10283    3 IASWNILNFGNskGKEKNPAIAEIISAFdlDLIALQEVMDNggglDALAKLVNELNKPGG-TWKYIVSDKTGGSSGDKER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  89 FGYVYKKDKVKFVKSEGFYKDGKSSLL-REPYGATFKI--DNFDFTLVLVHTIYG-----NNESQRKAENFKMVEVYDYF 160
Cdd:cd10283   82 YAFLYKSSKVRKVGKAVLEKDSNTDGFaRPPYAAKFKSggTGFDFTLVNVHLKSGgssksGQGAKRVAEAQALAEYLKEL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299 161 QDKDrKENDILIAGDFNLYALDESFRPMYKHkdKITYAIDPAIKTTIGTKGRANSYDNFFFSQKyTTEFTGSSGALDFSE 240
Cdd:cd10283  162 ADED-PDDDVILLGDFNIPADEDAFKALTKA--GFKSLLPDSTNLSTSFKGYANSYDNIFVSGN-LKEKFSNSGVFDFNI 237
                        250       260
                 ....*....|....*....|....*..
gi 915089299 241 KDPQLM---------RKIISDHIPVFI 258
Cdd:cd10283  238 LVDEAGeedldyskwRKQISDHDPVWV 264
 
Name Accession Description Interval E-value
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
17-258 1.55e-54

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: 176.82  E-value: 1.55e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  17 IASFNILRLGA--AEKDMVQTAKLLQGF--DLVGLVEVINK----EGIEDLVDELNRQSPnTWDYHISPFGVGSSKYKEY 88
Cdd:cd10283    3 IASWNILNFGNskGKEKNPAIAEIISAFdlDLIALQEVMDNggglDALAKLVNELNKPGG-TWKYIVSDKTGGSSGDKER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  89 FGYVYKKDKVKFVKSEGFYKDGKSSLL-REPYGATFKI--DNFDFTLVLVHTIYG-----NNESQRKAENFKMVEVYDYF 160
Cdd:cd10283   82 YAFLYKSSKVRKVGKAVLEKDSNTDGFaRPPYAAKFKSggTGFDFTLVNVHLKSGgssksGQGAKRVAEAQALAEYLKEL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299 161 QDKDrKENDILIAGDFNLYALDESFRPMYKHkdKITYAIDPAIKTTIGTKGRANSYDNFFFSQKyTTEFTGSSGALDFSE 240
Cdd:cd10283  162 ADED-PDDDVILLGDFNIPADEDAFKALTKA--GFKSLLPDSTNLSTSFKGYANSYDNIFVSGN-LKEKFSNSGVFDFNI 237
                        250       260
                 ....*....|....*....|....*..
gi 915089299 241 KDPQLM---------RKIISDHIPVFI 258
Cdd:cd10283  238 LVDEAGeedldyskwRKQISDHDPVWV 264
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
17-177 2.45e-19

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: 84.80  E-value: 2.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299    17 IASFNILRLGAAEKD----MVQTAKLLQGFDLVGLVEVINKEG--IEDLVDELNRQSPNTWDYHISPfGVGSSKYKEYFG 90
Cdd:smart00476  20 ICAFNIQSFGDSKMSnatlMSIIVKILSRYDIALVQEVRDSDLsaVPKLMDQLNSDSPNTYSYVSSE-PLGRNSYKEQYL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299    91 YVYKKDKVKfVKSEGFYKDGKS----SLLREPYGATFKIDNF---DFTLVLVHTiygnNESQRKAEnfkMVEVYDYFQDK 163
Cdd:smart00476  99 FLYRSDLVS-VLDSYLYDDGCEcgndVFSREPFVVKFSSPSTavkEFVIVPLHT----TPEAAVAE---IDALYDVYLDV 170
                          170
                   ....*....|....*.
gi 915089299   164 DRK--ENDILIAGDFN 177
Cdd:smart00476 171 RQKwgTEDVIFMGDFN 186
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
17-261 4.28e-17

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 79.68  E-value: 4.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  17 IASFNILRL------------GA--AEKDMVQTAKLLQGF-----DLVGLVEVINKEG-IEDLVDELNRQSPnTWDYHIS 76
Cdd:COG2374   71 VATFNVENLfdtddddddfgrGAdtPEEYERKLAKIAAAIaaldaDIVGLQEVENNGSaLQDLVAALNLAGG-TYAFVHP 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  77 PFGVGSSKYKeyFGYVYKKDKVKFVKSEGFYKDGKSSLL-----REPYGATFKI-DNFDFTLVLVH----------TIYG 140
Cdd:COG2374  150 PDGPDGDGIR--VALLYRPDRVTLVGSATIADLPDSPGNpdrfsRPPLAVTFELaNGEPFTVIVNHfkskgsddpgDGQG 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299 141 NNESQRKAENFKMVEVYDYFQDKDRKENdILIAGDFNLYALDESFRPMYKHKDkITYAIDPAIKTTIGT---KGRANSYD 217
Cdd:COG2374  228 ASEAKRTAQAEALRAFVDSLLAADPDAP-VIVLGDFNDYPFEDPLRALLGAGG-LTNLAEKLPAAERYSyvyDGNSGLLD 305
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 915089299 218 NFFFSQKYTTEFTGSSG--------ALDFSEKDPQLMRKII--SDHIPVFIVVE 261
Cdd:COG2374  306 HILVSPALAARVTGADIwhinadiyNDDFKPDFRTYADDPGraSDHDPVVVGLR 359
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
18-177 1.68e-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: 44.52  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299   18 ASFNILRLGAAEKDMVQTAKLL------QGFDLVGLVEVINkegiEDLVDELNRQSPNTWDYHISPFGVGSSKYKeyFGY 91
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALaaliraYDPDVVALQETDD----DDASRLLLALLAYGGFLSYGGPGGGGGGGG--VAI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299   92 VYKKDKVKFVKSEGFYKDGKSSLLREPYGATFKIDNFDFTLVLVHTIYGNNESQRKAENFKmvevydYFQDKDRKENDIL 171
Cdd:pfam03372  75 LSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLL------LLALLAPRSEPVI 148

                  ....*.
gi 915089299  172 IAGDFN 177
Cdd:pfam03372 149 LAGDFN 154
 
Name Accession Description Interval E-value
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
17-258 1.55e-54

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: 176.82  E-value: 1.55e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  17 IASFNILRLGA--AEKDMVQTAKLLQGF--DLVGLVEVINK----EGIEDLVDELNRQSPnTWDYHISPFGVGSSKYKEY 88
Cdd:cd10283    3 IASWNILNFGNskGKEKNPAIAEIISAFdlDLIALQEVMDNggglDALAKLVNELNKPGG-TWKYIVSDKTGGSSGDKER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  89 FGYVYKKDKVKFVKSEGFYKDGKSSLL-REPYGATFKI--DNFDFTLVLVHTIYG-----NNESQRKAENFKMVEVYDYF 160
Cdd:cd10283   82 YAFLYKSSKVRKVGKAVLEKDSNTDGFaRPPYAAKFKSggTGFDFTLVNVHLKSGgssksGQGAKRVAEAQALAEYLKEL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299 161 QDKDrKENDILIAGDFNLYALDESFRPMYKHkdKITYAIDPAIKTTIGTKGRANSYDNFFFSQKyTTEFTGSSGALDFSE 240
Cdd:cd10283  162 ADED-PDDDVILLGDFNIPADEDAFKALTKA--GFKSLLPDSTNLSTSFKGYANSYDNIFVSGN-LKEKFSNSGVFDFNI 237
                        250       260
                 ....*....|....*....|....*..
gi 915089299 241 KDPQLM---------RKIISDHIPVFI 258
Cdd:cd10283  238 LVDEAGeedldyskwRKQISDHDPVWV 264
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
17-256 1.01e-29

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: 112.33  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  17 IASFNILRLG---AAEKDMVQT-AKLLQGFDLVGLVEVINKEG--IEDLVDELNRQSPNTWDYHISPfGVGSSKYKEYFG 90
Cdd:cd10282    2 IAAFNIQVFGeskMSKPEVMDVlVKILSRYDIVLIQEIRDSSGtaIPELLDELNSASSNTYSYVVSE-RLGRSSYKEQYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  91 YVYKKDKVKfVKSEGFYKDGKS---SLLREPYGATFKIDN---FDFTLVLVHTiygnNESQRKAENFKMVEVYDYFQDKD 164
Cdd:cd10282   81 FIYRSDKVS-VLESYQYDDGDEgtdVFSREPFVVRFSSPStavKDFVLVPIHT----SPDDAVAEIDALYDVYDDVKQRW 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299 165 RkENDILIAGDFNlyaLDESFRPMyKHKDKITYAIDPAIKTTIG------TKGRANSYDNFFF--SQKYTTEFTGSSGAL 236
Cdd:cd10282  156 R-EDDVILLGDFN---ADCSYVTS-KGWKSIRLRTDSRFHWLIGddadttVRSTNCAYDRIVVagSLLQSAVVPGSAGVF 230
                        250       260
                 ....*....|....*....|...
gi 915089299 237 DFsEKDPQL---MRKIISDHIPV 256
Cdd:cd10282  231 DF-DKEFGLteeEALAVSDHYPV 252
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
17-258 3.31e-21

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: 89.77  E-value: 3.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  17 IASFNILRLGAAEKDMVQTAKLL----QGFDLVGLVEVINKE--GIEDLVDELNRQSPNTWDYHISPfGVGSSKYKEYFG 90
Cdd:cd09075    2 IAAFNIRTFGETKMSNATLASYIvrivRRYDIVLIQEVRDSHlvAVGKLLDYLNQDDPNTYHYVVSE-PLGRNSYKERYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  91 YVYKKDKVKFVKSEGF----YKDGKSSLLREPYGATFKIDNF---DFTLVLVHTiygnNESQRKAENFKMVEVYDYFQDK 163
Cdd:cd09075   81 FLFRPNKVSVLDTYQYddgcKSCGNDSFSREPAVVKFSSHSTkvkEFAIVALHS----APSDAVAEINSLYDVYLDVQQK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299 164 DRKeNDILIAGDFNL---YALDESFRPMYKHKDKITYAIDPAIKTTIGTkGRANSYDNFFF--SQKYTTEFTGSSGALDF 238
Cdd:cd09075  157 WHL-NDVMLMGDFNAdcsYVTSSQWSSIRLRTSSTFQWLIPDSADTTAT-STNCAYDRIVVagSLLQSSVVPGSAAPFDF 234
                        250       260
                 ....*....|....*....|..
gi 915089299 239 --SEKDPQLMRKIISDHIPVFI 258
Cdd:cd09075  235 qaAYGLSNEMALAISDHYPVEV 256
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
17-177 2.45e-19

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: 84.80  E-value: 2.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299    17 IASFNILRLGAAEKD----MVQTAKLLQGFDLVGLVEVINKEG--IEDLVDELNRQSPNTWDYHISPfGVGSSKYKEYFG 90
Cdd:smart00476  20 ICAFNIQSFGDSKMSnatlMSIIVKILSRYDIALVQEVRDSDLsaVPKLMDQLNSDSPNTYSYVSSE-PLGRNSYKEQYL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299    91 YVYKKDKVKfVKSEGFYKDGKS----SLLREPYGATFKIDNF---DFTLVLVHTiygnNESQRKAEnfkMVEVYDYFQDK 163
Cdd:smart00476  99 FLYRSDLVS-VLDSYLYDDGCEcgndVFSREPFVVKFSSPSTavkEFVIVPLHT----TPEAAVAE---IDALYDVYLDV 170
                          170
                   ....*....|....*.
gi 915089299   164 DRK--ENDILIAGDFN 177
Cdd:smart00476 171 RQKwgTEDVIFMGDFN 186
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
17-261 4.28e-17

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 79.68  E-value: 4.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  17 IASFNILRL------------GA--AEKDMVQTAKLLQGF-----DLVGLVEVINKEG-IEDLVDELNRQSPnTWDYHIS 76
Cdd:COG2374   71 VATFNVENLfdtddddddfgrGAdtPEEYERKLAKIAAAIaaldaDIVGLQEVENNGSaLQDLVAALNLAGG-TYAFVHP 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  77 PFGVGSSKYKeyFGYVYKKDKVKFVKSEGFYKDGKSSLL-----REPYGATFKI-DNFDFTLVLVH----------TIYG 140
Cdd:COG2374  150 PDGPDGDGIR--VALLYRPDRVTLVGSATIADLPDSPGNpdrfsRPPLAVTFELaNGEPFTVIVNHfkskgsddpgDGQG 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299 141 NNESQRKAENFKMVEVYDYFQDKDRKENdILIAGDFNLYALDESFRPMYKHKDkITYAIDPAIKTTIGT---KGRANSYD 217
Cdd:COG2374  228 ASEAKRTAQAEALRAFVDSLLAADPDAP-VIVLGDFNDYPFEDPLRALLGAGG-LTNLAEKLPAAERYSyvyDGNSGLLD 305
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 915089299 218 NFFFSQKYTTEFTGSSG--------ALDFSEKDPQLMRKII--SDHIPVFIVVE 261
Cdd:COG2374  306 HILVSPALAARVTGADIwhinadiyNDDFKPDFRTYADDPGraSDHDPVVVGLR 359
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
18-177 1.68e-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: 44.52  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299   18 ASFNILRLGAAEKDMVQTAKLL------QGFDLVGLVEVINkegiEDLVDELNRQSPNTWDYHISPFGVGSSKYKeyFGY 91
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALaaliraYDPDVVALQETDD----DDASRLLLALLAYGGFLSYGGPGGGGGGGG--VAI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299   92 VYKKDKVKFVKSEGFYKDGKSSLLREPYGATFKIDNFDFTLVLVHTIYGNNESQRKAENFKmvevydYFQDKDRKENDIL 171
Cdd:pfam03372  75 LSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLL------LLALLAPRSEPVI 148

                  ....*.
gi 915089299  172 IAGDFN 177
Cdd:pfam03372 149 LAGDFN 154
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
17-177 9.54e-04

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: 39.77  E-value: 9.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  17 IASFNILRLGAAEKdmvqtAKLL------QGFDLVGLVEVINKegIEDLVDELNRQsPNTWDYhispFGVGSSKYKEYFG 90
Cdd:cd08372    1 VASYNVNGLNAATR-----ASGIarwvreLDPDIVCLQEVKDS--QYSAVALNQLL-PEGYHQ----YQSGPSRKEGYEG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915089299  91 Y-VYKKDKVKFVKSEGFYKDGKSSLL-REPYGATFKIDNFDFTLVLVHTIYGNNESQRKAENFKMVevYDYFQDKDRKEN 168
Cdd:cd08372   69 VaILSKTPKFKIVEKHQYKFGEGDSGeRRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQLKEV--LEFLKRLRQPNS 146
                        170
                 ....*....|
gi 915089299 169 D-ILIAGDFN 177
Cdd:cd08372  147 ApVVICGDFN 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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