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Conserved domains on  [gi|1958807883|ref|XP_038955855|]
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deoxyribonuclease-1-like 1 isoform X3 [Rattus norvegicus]

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 ...
24-250 2.05e-104

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: 304.75  E-value: 2.05e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883   24 VASLL--ILLVGGTDAFRICAFNAHRLTLTK------------ILARCDIMVLQEVVDSSQNTVLFLLQKLQ-------- 81
Cdd:smart00476   2 VPSLLlfLLLLHGAASLRICAFNIQSFGDSKmsnatlmsiivkILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntys 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883   82 --------------------RSDKTQVLNFYQYNDT----EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELN 137
Cdd:smart00476  82 yvsseplgrnsykeqylflyRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEID 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  138 ALYDVFLDVSQRWQNENVILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQGCQKL 217
Cdd:smart00476 162 ALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSS 240
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958807883  218 LK--AAATFDFPRRFQLTEEEALRVSDHYPVEVEL 250
Cdd:smart00476 241 VVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTL 275
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
24-250 2.05e-104

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: 304.75  E-value: 2.05e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883   24 VASLL--ILLVGGTDAFRICAFNAHRLTLTK------------ILARCDIMVLQEVVDSSQNTVLFLLQKLQ-------- 81
Cdd:smart00476   2 VPSLLlfLLLLHGAASLRICAFNIQSFGDSKmsnatlmsiivkILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntys 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883   82 --------------------RSDKTQVLNFYQYNDT----EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELN 137
Cdd:smart00476  82 yvsseplgrnsykeqylflyRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEID 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  138 ALYDVFLDVSQRWQNENVILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQGCQKL 217
Cdd:smart00476 162 ALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSS 240
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958807883  218 LK--AAATFDFPRRFQLTEEEALRVSDHYPVEVEL 250
Cdd:smart00476 241 VVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTL 275
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
39-250 1.52e-99

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: 291.45  E-value: 1.52e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  39 RICAFNAHRL------------TLTKILARCDIMVLQEVVDSSQNTVLFLLQKL-----------------------Q-- 81
Cdd:cd10282     1 RIAAFNIQVFgeskmskpevmdVLVKILSRYDIVLIQEIRDSSGTAIPELLDELnsassntysyvvserlgrssykeQya 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  82 ---RSDKTQVLNFYQYNDT---EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENV 155
Cdd:cd10282    81 fiyRSDKVSVLESYQYDDGdegTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883 156 ILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQG--CQKLLKAAATFDFPRRFQLT 233
Cdd:cd10282   161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKEFGLT 239
                         250
                  ....*....|....*..
gi 1958807883 234 EEEALRVSDHYPVEVEL 250
Cdd:cd10282   240 EEEALAVSDHYPVEVEL 256
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
42-164 7.46e-09

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: 54.15  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  42 AFNAHRLTLTKILARC--DIMVLQEVVDSSQNTVLFLLQKLQRSD------------------KTQVLNFYQYNDTEDIF 101
Cdd:pfam03372  14 GDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGGFLsyggpggggggggvailsRYPLSSVILVDLGEFGD 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807883 102 AREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENVILLGDFNAD 164
Cdd:pfam03372  94 PALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNAD 156
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
58-250 3.99e-03

Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 38.05  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  58 DIMVLQEVVDSSQNTVLFLLQKLQrsdktqvlnfYQYNDTED------IFAREPF----------------VAQFTLPSK 115
Cdd:COG3021   122 DVLVLQETTPAWEEALAALEADYP----------YRVLCPLDnaygmaLLSRLPLteaevvylvgddipsiRATVELPGG 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883 116 ilpSVVLVPLHTTP-----KDVEKELNALYDVFldvsqRWQNENVILLGDFNADCASLAKKRL--NSLLLRTKAGFHWVi 188
Cdd:COG3021   192 ---PVRLVAVHPAPpvggsAERDAELAALAKAV-----AALDGPVIVAGDFNATPWSPTLRRLlrASGLRDARAGRGLG- 262
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807883 189 pdgedttvrastnCTYDRivmhgqgcqKLLKAAATFD---FPRRFQLTEEEALRV--SDHYPVEVEL 250
Cdd:COG3021   263 -------------PTWPA---------NLPFLRLPIDhvlVSRGLTVVDVRVLPVigSDHRPLLAEL 307
 
Name Accession Description Interval E-value
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
24-250 2.05e-104

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: 304.75  E-value: 2.05e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883   24 VASLL--ILLVGGTDAFRICAFNAHRLTLTK------------ILARCDIMVLQEVVDSSQNTVLFLLQKLQ-------- 81
Cdd:smart00476   2 VPSLLlfLLLLHGAASLRICAFNIQSFGDSKmsnatlmsiivkILSRYDIALVQEVRDSDLSAVPKLMDQLNsdspntys 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883   82 --------------------RSDKTQVLNFYQYNDT----EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELN 137
Cdd:smart00476  82 yvsseplgrnsykeqylflyRSDLVSVLDSYLYDDGcecgNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAVAEID 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  138 ALYDVFLDVSQRWQNENVILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQGCQKL 217
Cdd:smart00476 162 ALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGERLRSS 240
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958807883  218 LK--AAATFDFPRRFQLTEEEALRVSDHYPVEVEL 250
Cdd:smart00476 241 VVpgSAAVFDFQTAYGLTEEEALAISDHFPVEVTL 275
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
39-250 1.52e-99

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: 291.45  E-value: 1.52e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  39 RICAFNAHRL------------TLTKILARCDIMVLQEVVDSSQNTVLFLLQKL-----------------------Q-- 81
Cdd:cd10282     1 RIAAFNIQVFgeskmskpevmdVLVKILSRYDIVLIQEIRDSSGTAIPELLDELnsassntysyvvserlgrssykeQya 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  82 ---RSDKTQVLNFYQYNDT---EDIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENV 155
Cdd:cd10282    81 fiyRSDKVSVLESYQYDDGdegTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWREDDV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883 156 ILLGDFNADCASLAKKRLNSLLLRTKAGFHWVIPDGEDTTVRaSTNCTYDRIVMHGQG--CQKLLKAAATFDFPRRFQLT 233
Cdd:cd10282   161 ILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLlqSAVVPGSAGVFDFDKEFGLT 239
                         250
                  ....*....|....*..
gi 1958807883 234 EEEALRVSDHYPVEVEL 250
Cdd:cd10282   240 EEEALAVSDHYPVEVEL 256
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
50-250 2.71e-47

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: 158.33  E-value: 2.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  50 LTKILARCDIMVLQEVVDSSQNTVLFLLQKLQRSD----------------------------KTQVLNFYQYNDTE--- 98
Cdd:cd09075    24 IVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDpntyhyvvseplgrnsykerylflfrpnKVSVLDTYQYDDGCksc 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  99 --DIFAREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENVILLGDFNADCASLAKKRLNSL 176
Cdd:cd09075   104 gnDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSI 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807883 177 LLRTKAGFHWVIPDGEDTTVrASTNCTYDRIVMHGQGCQ--KLLKAAATFDFPRRFQLTEEEALRVSDHYPVEVEL 250
Cdd:cd09075   184 RLRTSSTFQWLIPDSADTTA-TSTNCAYDRIVVAGSLLQssVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
38-250 1.09e-15

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: 74.74  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  38 FRICAFNAHRLTLTK----------ILAR--CDIMVLQEVVDSSQ--NTVLFLLQKLQR---------SDKTQ------- 87
Cdd:cd10283     1 LRIASWNILNFGNSKgkeknpaiaeIISAfdLDLIALQEVMDNGGglDALAKLVNELNKpggtwkyivSDKTGgssgdke 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  88 -------------VLNFYQYNDT-EDIFAREPFVAQFtlpsKILPS---VVLVPLHTTPKDV---------EKELNALYD 141
Cdd:cd10283    81 ryaflyksskvrkVGKAVLEKDSnTDGFARPPYAAKF----KSGGTgfdFTLVNVHLKSGGSsksgqgakrVAEAQALAE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883 142 VFLDVSQRWQNENVILLGDFNADCASLAKKRLnslllrTKAGFHWVIPDGEDTTvrASTNC---TYDRIVMHGQGCQKlL 218
Cdd:cd10283   157 YLKELADEDPDDDVILLGDFNIPADEDAFKAL------TKAGFKSLLPDSTNLS--TSFKGyanSYDNIFVSGNLKEK-F 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807883 219 KAAATFDFPRRFQLTEEEAL-------RVSDHYPVEVEL 250
Cdd:cd10283   228 SNSGVFDFNILVDEAGEEDLdyskwrkQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
58-250 7.18e-15

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: 72.13  E-value: 7.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  58 DIMVLQEVVDSSQNTVLFLLQKLQRSDKTQ----------------------VLNFYQYNDTE-DIFAREPFVAQFTLPS 114
Cdd:cd08372    28 DIVCLQEVKDSQYSAVALNQLLPEGYHQYQsgpsrkegyegvailsktpkfkIVEKHQYKFGEgDSGERRAVVVKFDVHD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883 115 KILpsvVLVPLH-----TTPKDVEKELNALYDVFLDVsQRWQNENVILLGDFNADCASLAKKRLNSLL-LRTKAGFHWVI 188
Cdd:cd08372   108 KEL---CVVNAHlqaggTRADVRDAQLKEVLEFLKRL-RQPNSAPVVICGDFNVRPSEVDSENPSSMLrLFVALNLVDSF 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807883 189 PDGEDT----TVRASTNCTYDRIVMHGQGCQKLLKAAATFDFPRrfqlteeeALRVSDHYPVEVEL 250
Cdd:cd08372   184 ETLPHAytfdTYMHNVKSRLDYIFVSKSLLPSVKSSKILSDAAR--------ARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
42-164 7.46e-09

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: 54.15  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  42 AFNAHRLTLTKILARC--DIMVLQEVVDSSQNTVLFLLQKLQRSD------------------KTQVLNFYQYNDTEDIF 101
Cdd:pfam03372  14 GDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGGFLsyggpggggggggvailsRYPLSSVILVDLGEFGD 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807883 102 AREPFVAQFTLPSKILPSVVLVPLHTTPKDVEKELNALYDVFLDVSQRWQNENVILLGDFNAD 164
Cdd:pfam03372  94 PALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNAD 156
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
58-250 3.99e-03

Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 38.05  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883  58 DIMVLQEVVDSSQNTVLFLLQKLQrsdktqvlnfYQYNDTED------IFAREPF----------------VAQFTLPSK 115
Cdd:COG3021   122 DVLVLQETTPAWEEALAALEADYP----------YRVLCPLDnaygmaLLSRLPLteaevvylvgddipsiRATVELPGG 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807883 116 ilpSVVLVPLHTTP-----KDVEKELNALYDVFldvsqRWQNENVILLGDFNADCASLAKKRL--NSLLLRTKAGFHWVi 188
Cdd:COG3021   192 ---PVRLVAVHPAPpvggsAERDAELAALAKAV-----AALDGPVIVAGDFNATPWSPTLRRLlrASGLRDARAGRGLG- 262
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807883 189 pdgedttvrastnCTYDRivmhgqgcqKLLKAAATFD---FPRRFQLTEEEALRV--SDHYPVEVEL 250
Cdd:COG3021   263 -------------PTWPA---------NLPFLRLPIDhvlVSRGLTVVDVRVLPVigSDHRPLLAEL 307
 
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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