NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|677494755|gb|KFQ84160|]
View 

Deoxyribonuclease gamma, partial [Phoenicopterus ruber ruber]

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 10178909)

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 Danio rerio deoxyribonuclease-1-like 1

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
27-287 1.53e-166

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: 462.86  E-value: 1.53e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  27 KICSFNVRSFGETKIARPEVVDAVVKIISRCDIMLLMEIKENKNRVCPLLLEKLTSqqkGLKEEYSCVVSERLGRKSYKE 106
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNS---ASSNTYSYVVSERLGRSSYKE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 107 QYAFIYRHHLVSVKQTYQYPDTEPgDEDAFSREPFAVWFQSPKTAVKEFAIIPLHTTPETAVREIDELYDVYLDVKQRWK 186
Cdd:cd10282   78 QYAFIYRSDKVSVLESYQYDDGDE-GTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 187 TENFIFMGDFNAGCSYVPRKQWKNIRLRTYSEFVWLIGDKNDTTVKsSTSCPYDRIVVSGQKLVHAVVPHSANIFDFQKD 266
Cdd:cd10282  157 EDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKE 235
                        250       260
                 ....*....|....*....|.
gi 677494755 267 FQMTEEQALGVSDHFPVEFEL 287
Cdd:cd10282  236 FGLTEEEALAVSDHYPVEVEL 256
 
Name Accession Description Interval E-value
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
27-287 1.53e-166

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: 462.86  E-value: 1.53e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  27 KICSFNVRSFGETKIARPEVVDAVVKIISRCDIMLLMEIKENKNRVCPLLLEKLTSqqkGLKEEYSCVVSERLGRKSYKE 106
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNS---ASSNTYSYVVSERLGRSSYKE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 107 QYAFIYRHHLVSVKQTYQYPDTEPgDEDAFSREPFAVWFQSPKTAVKEFAIIPLHTTPETAVREIDELYDVYLDVKQRWK 186
Cdd:cd10282   78 QYAFIYRSDKVSVLESYQYDDGDE-GTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 187 TENFIFMGDFNAGCSYVPRKQWKNIRLRTYSEFVWLIGDKNDTTVKsSTSCPYDRIVVSGQKLVHAVVPHSANIFDFQKD 266
Cdd:cd10282  157 EDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKE 235
                        250       260
                 ....*....|....*....|.
gi 677494755 267 FQMTEEQALGVSDHFPVEFEL 287
Cdd:cd10282  236 FGLTEEEALAVSDHYPVEVEL 256
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
9-288 5.10e-162

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: 452.28  E-value: 5.10e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755     9 MLLFVLLslfnFNPSLSLKICSFNVRSFGETKIARPEVVDAVVKIISRCDIMLLMEIKENKNRVCPLLLEKLTSQQKGlk 88
Cdd:smart00476   5 LLLFLLL----LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPN-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755    89 eEYSCVVSERLGRKSYKEQYAFIYRHHLVSVKQTYQYPDTEPGDEDAFSREPFAVWFQSPKTAVKEFAIIPLHTTPETAV 168
Cdd:smart00476  79 -TYSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755   169 REIDELYDVYLDVKQRWKTENFIFMGDFNAGCSYVPRKQWKNIRLRTYSEFVWLIGDKNDTTVKsSTSCPYDRIVVSGQK 248
Cdd:smart00476 158 AEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGER 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 677494755   249 LVHAVVPHSANIFDFQKDFQMTEEQALGVSDHFPVEFELK 288
Cdd:smart00476 237 LRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
29-198 1.05e-14

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: 71.10  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755   29 CSFNVRSFGETKIARPEVVDAVVKIISRC--DIMLLMEIKENKNRVCPLLLEKLTSqqkglkeeYSCVVSERLGRKSYKe 106
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGG--------FLSYGGPGGGGGGGG- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  107 qYAFIYRHHLVSVKQTYQYPDTEPGDEDAFSREPFAVWFqspktavKEFAIIPLHTTPETAVREIDELYDVYLDVKQRWK 186
Cdd:pfam03372  72 -VAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVV-------PLVLTLAPHASPRLARDEQRADLLLLLLALLAPR 143
                         170
                  ....*....|..
gi 677494755  187 TENFIFMGDFNA 198
Cdd:pfam03372 144 SEPVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
25-289 1.07e-11

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 64.66  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  25 SLKICSFNVRSF------------GETKIARPEV-VDAVVKIISR--CDIMLLMEIkENKNRVcpllLEKLTSQqkglke 89
Cdd:COG2374   68 DLRVATFNVENLfdtddddddfgrGADTPEEYERkLAKIAAAIAAldADIVGLQEV-ENNGSA----LQDLVAA------ 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  90 eyscvVSERLGRKSYKEQY----------AFIYRHHLVSVKQTYQYPDTE--PGDEDAFSREPFAVWFQSPKTavKEFAI 157
Cdd:COG2374  137 -----LNLAGGTYAFVHPPdgpdgdgirvALLYRPDRVTLVGSATIADLPdsPGNPDRFSRPPLAVTFELANG--EPFTV 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 158 IPLH----TTPETA----------VREIDELYDVYLDVKQRWKTENFIFMGDFNAGCSYVP------RKQWKNIRLRTYS 217
Cdd:COG2374  210 IVNHfkskGSDDPGdgqgaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDYPFEDPlrallgAGGLTNLAEKLPA 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 218 EFVWligdkndTTVKSSTSCPYDRIVVSG---QKLVHAVVPH-SANIF--DFQKDFQMTEEQALGVSDHFPV--EFELKP 289
Cdd:COG2374  290 AERY-------SYVYDGNSGLLDHILVSPalaARVTGADIWHiNADIYndDFKPDFRTYADDPGRASDHDPVvvGLRLPP 362
 
Name Accession Description Interval E-value
DNase1 cd10282
Deoxyribonuclease 1; Deoxyribonuclease 1 (DNase1, EC 3.1.21.1), also known as DNase I, is a ...
27-287 1.53e-166

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: 462.86  E-value: 1.53e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  27 KICSFNVRSFGETKIARPEVVDAVVKIISRCDIMLLMEIKENKNRVCPLLLEKLTSqqkGLKEEYSCVVSERLGRKSYKE 106
Cdd:cd10282    1 RIAAFNIQVFGESKMSKPEVMDVLVKILSRYDIVLIQEIRDSSGTAIPELLDELNS---ASSNTYSYVVSERLGRSSYKE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 107 QYAFIYRHHLVSVKQTYQYPDTEPgDEDAFSREPFAVWFQSPKTAVKEFAIIPLHTTPETAVREIDELYDVYLDVKQRWK 186
Cdd:cd10282   78 QYAFIYRSDKVSVLESYQYDDGDE-GTDVFSREPFVVRFSSPSTAVKDFVLVPIHTSPDDAVAEIDALYDVYDDVKQRWR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 187 TENFIFMGDFNAGCSYVPRKQWKNIRLRTYSEFVWLIGDKNDTTVKsSTSCPYDRIVVSGQKLVHAVVPHSANIFDFQKD 266
Cdd:cd10282  157 EDDVILLGDFNADCSYVTSKGWKSIRLRTDSRFHWLIGDDADTTVR-STNCAYDRIVVAGSLLQSAVVPGSAGVFDFDKE 235
                        250       260
                 ....*....|....*....|.
gi 677494755 267 FQMTEEQALGVSDHFPVEFEL 287
Cdd:cd10282  236 FGLTEEEALAVSDHYPVEVEL 256
DNaseIc smart00476
deoxyribonuclease I; Deoxyribonuclease I catalyzes the endonucleolytic cleavage of ...
9-288 5.10e-162

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: 452.28  E-value: 5.10e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755     9 MLLFVLLslfnFNPSLSLKICSFNVRSFGETKIARPEVVDAVVKIISRCDIMLLMEIKENKNRVCPLLLEKLTSQQKGlk 88
Cdd:smart00476   5 LLLFLLL----LHGAASLRICAFNIQSFGDSKMSNATLMSIIVKILSRYDIALVQEVRDSDLSAVPKLMDQLNSDSPN-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755    89 eEYSCVVSERLGRKSYKEQYAFIYRHHLVSVKQTYQYPDTEPGDEDAFSREPFAVWFQSPKTAVKEFAIIPLHTTPETAV 168
Cdd:smart00476  79 -TYSYVSSEPLGRNSYKEQYLFLYRSDLVSVLDSYLYDDGCECGNDVFSREPFVVKFSSPSTAVKEFVIVPLHTTPEAAV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755   169 REIDELYDVYLDVKQRWKTENFIFMGDFNAGCSYVPRKQWKNIRLRTYSEFVWLIGDKNDTTVKsSTSCPYDRIVVSGQK 248
Cdd:smart00476 158 AEIDALYDVYLDVRQKWGTEDVIFMGDFNAGCSYVTKKQWSSIRLRTSPTFHWLIPDSADTTVT-STHCAYDRIVVAGER 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 677494755   249 LVHAVVPHSANIFDFQKDFQMTEEQALGVSDHFPVEFELK 288
Cdd:smart00476 237 LRSSVVPGSAAVFDFQTAYGLTEEEALAISDHFPVEVTLK 276
DNase1-like cd09075
Deoxyribonuclease 1 and related proteins; This family includes Deoxyribonuclease 1 (DNase1, EC ...
27-287 1.24e-73

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: 227.28  E-value: 1.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  27 KICSFNVRSFGETKIARPEVVDAVVKIISRCDIMLLMEIKENKNRVCPLLLEKLtsqQKGLKEEYSCVVSERLGRKSYKE 106
Cdd:cd09075    1 KIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYL---NQDDPNTYHYVVSEPLGRNSYKE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 107 QYAFIYRHHLVSVKQTYQYPDTEPG-DEDAFSREPFAVWFQSPKTAVKEFAIIPLHTTPETAVREIDELYDVYLDVKQRW 185
Cdd:cd09075   78 RYLFLFRPNKVSVLDTYQYDDGCKScGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 186 KTENFIFMGDFNAGCSYVPRKQWKNIRLRTYSEFVWLIGDKNDTTvKSSTSCPYDRIVVSGQKLVHAVVPHSANIFDFQK 265
Cdd:cd09075  158 HLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTT-ATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQA 236
                        250       260
                 ....*....|....*....|..
gi 677494755 266 DFQMTEEQALGVSDHFPVEFEL 287
Cdd:cd09075  237 AYGLSNEMALAISDHYPVEVTL 258
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
26-287 1.76e-29

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: 113.26  E-value: 1.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  26 LKICSFNVRSFGETKiaRPEVVDAVVKIISR--CDIMLLMEIKENKNRVcpLLLEKLTSQQKGLKEEYSCVVSERLGRKS 103
Cdd:cd10283    1 LRIASWNILNFGNSK--GKEKNPAIAEIISAfdLDLIALQEVMDNGGGL--DALAKLVNELNKPGGTWKYIVSDKTGGSS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 104 -YKEQYAFIYR-HHLVSVKQTYQYPDTEPgdeDAFSREPFAVWFQSPKTAvKEFAIIPLH-------TTPETA--VREID 172
Cdd:cd10283   77 gDKERYAFLYKsSKVRKVGKAVLEKDSNT---DGFARPPYAAKFKSGGTG-FDFTLVNVHlksggssKSGQGAkrVAEAQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 173 ELYDVYLDVKQRWKTENFIFMGDFNAgcsYVPRKQWKNIRLRTyseFVWLIGDKNDTTVKSST-SCPYDRIVVSG---QK 248
Cdd:cd10283  153 ALAEYLKELADEDPDDDVILLGDFNI---PADEDAFKALTKAG---FKSLLPDSTNLSTSFKGyANSYDNIFVSGnlkEK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 677494755 249 LVHAVVPHSANIFDFQKDFQMTEEQ-ALGVSDHFPVEFEL 287
Cdd:cd10283  227 FSNSGVFDFNILVDEAGEEDLDYSKwRKQISDHDPVWVEF 266
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
28-287 1.24e-22

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 94.09  E-value: 1.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  28 ICSFNVRSFGETKIARpevvdAVVKIISRC--DIMLLMEIKENKNRVCPLLLEKltsqqkglKEEYSCVVSERlGRKSYK 105
Cdd:cd08372    1 VASYNVNGLNAATRAS-----GIARWVRELdpDIVCLQEVKDSQYSAVALNQLL--------PEGYHQYQSGP-SRKEGY 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 106 EQYAFIYRHHLVSVKQTYQYpdtEPGDEDAFSREPFAVWFqspKTAVKEFAIIPLH-----TTPETAVREIDELYDVYLD 180
Cdd:cd08372   67 EGVAILSKTPKFKIVEKHQY---KFGEGDSGERRAVVVKF---DVHDKELCVVNAHlqaggTRADVRDAQLKEVLEFLKR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 181 vKQRWKTENFIFMGDFNAGCSYVPRKQWKN-IRLRTYSEFVWLI--GDKNDT--TVKSSTSCPYDRIVVSGQklvHAVVP 255
Cdd:cd08372  141 -LRQPNSAPVVICGDFNVRPSEVDSENPSSmLRLFVALNLVDSFetLPHAYTfdTYMHNVKSRLDYIFVSKS---LLPSV 216
                        250       260       270
                 ....*....|....*....|....*....|..
gi 677494755 256 HSANIFDFQKDFQMteeqalgVSDHFPVEFEL 287
Cdd:cd08372  217 KSSKILSDAARARI-------PSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
29-198 1.05e-14

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: 71.10  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755   29 CSFNVRSFGETKIARPEVVDAVVKIISRC--DIMLLMEIKENKNRVCPLLLEKLTSqqkglkeeYSCVVSERLGRKSYKe 106
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYdpDVVALQETDDDDASRLLLALLAYGG--------FLSYGGPGGGGGGGG- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  107 qYAFIYRHHLVSVKQTYQYPDTEPGDEDAFSREPFAVWFqspktavKEFAIIPLHTTPETAVREIDELYDVYLDVKQRWK 186
Cdd:pfam03372  72 -VAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVV-------PLVLTLAPHASPRLARDEQRADLLLLLLALLAPR 143
                         170
                  ....*....|..
gi 677494755  187 TENFIFMGDFNA 198
Cdd:pfam03372 144 SEPVILAGDFNA 155
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
25-289 1.07e-11

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 64.66  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  25 SLKICSFNVRSF------------GETKIARPEV-VDAVVKIISR--CDIMLLMEIkENKNRVcpllLEKLTSQqkglke 89
Cdd:COG2374   68 DLRVATFNVENLfdtddddddfgrGADTPEEYERkLAKIAAAIAAldADIVGLQEV-ENNGSA----LQDLVAA------ 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755  90 eyscvVSERLGRKSYKEQY----------AFIYRHHLVSVKQTYQYPDTE--PGDEDAFSREPFAVWFQSPKTavKEFAI 157
Cdd:COG2374  137 -----LNLAGGTYAFVHPPdgpdgdgirvALLYRPDRVTLVGSATIADLPdsPGNPDRFSRPPLAVTFELANG--EPFTV 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 158 IPLH----TTPETA----------VREIDELYDVYLDVKQRWKTENFIFMGDFNAGCSYVP------RKQWKNIRLRTYS 217
Cdd:COG2374  210 IVNHfkskGSDDPGdgqgaseakrTAQAEALRAFVDSLLAADPDAPVIVLGDFNDYPFEDPlrallgAGGLTNLAEKLPA 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677494755 218 EFVWligdkndTTVKSSTSCPYDRIVVSG---QKLVHAVVPH-SANIF--DFQKDFQMTEEQALGVSDHFPV--EFELKP 289
Cdd:COG2374  290 AERY-------SYVYDGNSGLLDHILVSPalaARVTGADIWHiNADIYndDFKPDFRTYADDPGRASDHDPVvvGLRLPP 362
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH