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Conserved domains on  [gi|1575802319|ref|WP_130084363|]
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MULTISPECIES: exodeoxyribonuclease III [unclassified Akkermansia]

Protein Classification

exodeoxyribonuclease III( domain architecture ID 10173395)

exodeoxyribonuclease III is a Mg-dependent 3' to 5' exonuclease acting on dsDNA, which releases 5' phosphomononucleotides as degradation products; similar to bacterial exodeoxyribonuclease III and eukaryotic DNA-(apurinic or apyrimidinic site) endonuclease

CATH:  3.60.10.10
EC:  3.1.11.2
Gene Ontology:  GO:0003677|GO:0046872|GO:0004519|GO:0004527|GO:0006281|GO:0008311
PubMed:  7885481|10838565

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 1-251 2.02e-150

Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This subfamily includes human Ape1 (also known as Apex, Hap1, or Ref-1) and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Ape1 and Ape2 in humans. Ape1 is found in this subfamily, it exhibits strong AP-endonuclease activity but shows weak 3'-5' exonuclease and 3'-phosphodiesterase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


:

Pssm-ID: 197321 [Multi-domain]  Cd Length: 253  Bit Score: 419.26  E-value: 2.02e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQVDD--LWLSSWPYQLWNPAEKAGYSGVLVLSRVKPLST 78
Cdd:cd09087     1 LKIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKelKELLKGYHQYWNAAEKKGYSGTAILSKKKPLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  79 SMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYRQQWDQAFRNYVAGLAAVKPVIFCGDLNVAHQEIDIAR 158
Cdd:cd09087    81 TYGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 159 PKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHMD 238
Cdd:cd09087   161 PKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSD 240

                         250
                  ....*....|...
gi 1575802319 239 VMGSDHCPVSLEI 251
Cdd:cd09087   241 IMGSDHCPIGLEL 253
 
Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 1-251 2.02e-150

Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This subfamily includes human Ape1 (also known as Apex, Hap1, or Ref-1) and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Ape1 and Ape2 in humans. Ape1 is found in this subfamily, it exhibits strong AP-endonuclease activity but shows weak 3'-5' exonuclease and 3'-phosphodiesterase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197321 [Multi-domain]  Cd Length: 253  Bit Score: 419.26  E-value: 2.02e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQVDD--LWLSSWPYQLWNPAEKAGYSGVLVLSRVKPLST 78
Cdd:cd09087     1 LKIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKelKELLKGYHQYWNAAEKKGYSGTAILSKKKPLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  79 SMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYRQQWDQAFRNYVAGLAAVKPVIFCGDLNVAHQEIDIAR 158
Cdd:cd09087    81 TYGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 159 PKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHMD 238
Cdd:cd09087   161 PKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSD 240

                         250
                  ....*....|...
gi 1575802319 239 VMGSDHCPVSLEI 251
Cdd:cd09087   241 IMGSDHCPIGLEL 253
XthA COG0708
Exonuclease III [Replication, recombination and repair];
1-252 8.25e-120

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 342.06  E-value: 8.25e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKgLGEAADALDADILCLQEIKARPEQVDDLWLSSWPYQL-WNPaeKAGYSGVLVLSRVKPLSTS 79
Cdd:COG0708     1 MKIASWNVNGIRARLPK-LLDWLAEEDPDVLCLQETKAQDEQFPLEAFEAAGYHVyFHG--QKGYNGVAILSRLPPEDVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  80 MGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQS-ELARLPYRQQWDQAFRNYVAGL-AAVKPVIFCGDLNVAHQEIDIA 157
Cdd:COG0708    78 RGLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSvGSEKFDYKLRFLDALRAYLAELlAPGRPLILCGDFNIAPTEIDVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 158 RPKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIH- 236
Cdd:COG0708   158 NPKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDr 237

                         250
                  ....*....|....*....
gi 1575802319 237 ---MDVMGSDHCPVSLEID 252
Cdd:COG0708   238 eprGDERPSDHAPVVVELD 256
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 1-252 2.44e-112

exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are 5' AP endonucleases that funciton in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273186 [Multi-domain]  Cd Length: 254  Bit Score: 323.08  E-value: 2.44e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQvddlwlssWPYQL---------WNPAeKAGYSGVLVLS 71
Cdd:TIGR00633   1 MKIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQ--------FPAELfeelgyhvfFHGA-KKGYSGVAILS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  72 RVKPLSTSMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSE-LARLPYRQQ-WDQAFRNYVAGLAAVKPVIFCGDLNV 149
Cdd:TIGR00633  72 KVEPLDVRYGFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGSRdLERLEYKLQfWDALFQYLEKELDAGKPVVICGDMNV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 150 AHQEIDIARPKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPR 229
Cdd:TIGR00633 152 AHTEIDLGNPKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAER 231

                         250       260
                  ....*....|....*....|...
gi 1575802319 230 VKSAAIHMDVMGSDHCPVSLEID 252
Cdd:TIGR00633 232 VVDSYIDSEIRGSDHCPIVLELD 254
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
 1-251 5.37e-101

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 294.29  E-value: 5.37e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQvdDLWLSSWPYQLWNPAEKAGYSGVLVLSRVKPLSTSM 80
Cdd:PRK13911    1 MKLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQ--NTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  81 GMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYRQQWDQAFRNYVAGLAAVKPVIFCGDLNVAHQEIDIARPK 160
Cdd:PRK13911   79 GINIEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENPK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 161 DNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHMDVM 240
Cdd:PRK13911  159 TNRKNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDIL 238

                         250
                  ....*....|.
gi 1575802319 241 GSDHCPVSLEI 251
Cdd:PRK13911  239 GSDHCPVGLEL 249
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 4-149 9.73e-18

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: 78.42  E-value: 9.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   4 VSWNVNGLRA------ILGKGLGEAADALDADILCLQEIKARPEQVDDLWLSS--WPYQLWNPAEKAGYSGVLVLSRVKP 75
Cdd:pfam03372   1 LTWNVNGGNAdaagddRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAygGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1575802319  76 LSTSMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYR-QQWDQAFRNYVAGLAAVKPVIFCGDLNV 149
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDeQRADLLLLLLALLAPRSEPVILAGDFNA 155
 
Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 1-251 2.02e-150

Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This subfamily includes human Ape1 (also known as Apex, Hap1, or Ref-1) and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Ape1 and Ape2 in humans. Ape1 is found in this subfamily, it exhibits strong AP-endonuclease activity but shows weak 3'-5' exonuclease and 3'-phosphodiesterase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197321 [Multi-domain]  Cd Length: 253  Bit Score: 419.26  E-value: 2.02e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQVDD--LWLSSWPYQLWNPAEKAGYSGVLVLSRVKPLST 78
Cdd:cd09087     1 LKIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKelKELLKGYHQYWNAAEKKGYSGTAILSKKKPLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  79 SMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYRQQWDQAFRNYVAGLAAVKPVIFCGDLNVAHQEIDIAR 158
Cdd:cd09087    81 TYGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 159 PKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHMD 238
Cdd:cd09087   161 PKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSD 240

                         250
                  ....*....|...
gi 1575802319 239 VMGSDHCPVSLEI 251
Cdd:cd09087   241 IMGSDHCPIGLEL 253
XthA COG0708
Exonuclease III [Replication, recombination and repair];
1-252 8.25e-120

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 342.06  E-value: 8.25e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKgLGEAADALDADILCLQEIKARPEQVDDLWLSSWPYQL-WNPaeKAGYSGVLVLSRVKPLSTS 79
Cdd:COG0708     1 MKIASWNVNGIRARLPK-LLDWLAEEDPDVLCLQETKAQDEQFPLEAFEAAGYHVyFHG--QKGYNGVAILSRLPPEDVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  80 MGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQS-ELARLPYRQQWDQAFRNYVAGL-AAVKPVIFCGDLNVAHQEIDIA 157
Cdd:COG0708    78 RGLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSvGSEKFDYKLRFLDALRAYLAELlAPGRPLILCGDFNIAPTEIDVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 158 RPKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIH- 236
Cdd:COG0708   158 NPKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDr 237

                         250
                  ....*....|....*....
gi 1575802319 237 ---MDVMGSDHCPVSLEID 252
Cdd:COG0708   238 eprGDERPSDHAPVVVELD 256
ExoIII_AP-endo cd09073
Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ...
 2-251 7.19e-119

Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ExoIII family AP endonucleases belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, which is then followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, which have both mutagenic and cytotoxic effects. AP endonucleases can carry out a wide range of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two functional AP endonucleases, for example, APE1/Ref-1 and Ape2 in humans, Apn1 and Apn2 in bakers yeast, Nape and NExo in Neisseria meningitides, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. Usually, one of the two is the dominant AP endonuclease, the other has weak AP endonuclease activity, but exhibits strong 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, and 3'-phosphatase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes. This family contains the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197307 [Multi-domain]  Cd Length: 251  Bit Score: 339.65  E-value: 7.19e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   2 KLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQVDDLWLSSWPY-QLWNPAEKAGYSGVLVLSRVKPLSTSM 80
Cdd:cd09073     1 KIISWNVNGLRARLKKGVLKWLKEEKPDILCLQETKADEDKLPEELQHVEGYhSYWSPARKKGYSGVATLSKEEPLDVSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  81 GMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYRQQWDQAFRNYVAGLAAV-KPVIFCGDLNVAHQEIDIARP 159
Cdd:cd09073    81 GIGGEEFDSEGRVITAEFDDFYLINVYFPNGGRGLERLDYKLRFYEAFLEFLEKLRKRgKPVVICGDFNVAHEEIDLARP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 160 KDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSwYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHMDV 239
Cdd:cd09073   161 KKNEKNAGFTPEERAWFDKLLSLGYVDTFRHFHPEPGA-YTWWSYRGNARERNVGWRIDYFLVSEELAEKVKDSGILSKV 239

                         250
                  ....*....|..
gi 1575802319 240 MGSDHCPVSLEI 251
Cdd:cd09073   240 KGSDHAPVTLEL 251
Mth212-like_AP-endo cd09085
Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic ...
 1-251 5.56e-118

Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes the thermophilic archaeon Methanothermobacter thermautotrophicus Mth212and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Mth212 is an AP endonuclease, and a DNA uridine endonuclease (U-endo) that nicks double-stranded DNA at the 5'-side of a 2'-d-uridine residue. After incision at the 5'-side of a 2'-d-uridine residue by Mth212, DNA polymerase B takes over the 3'-OH terminus and carries out repair synthesis, generating a 5'-flap structure that is resolved by a 5'-flap endonuclease. Finally, DNA ligase seals the resulting nick. This U-endo activity shares the same catalytic center as its AP-endo activity, and is absent from other AP endonuclease homologues.


Pssm-ID: 197319 [Multi-domain]  Cd Length: 252  Bit Score: 337.33  E-value: 5.56e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQV-DDLWLSSWPYQLWNPAEKAGYSGVLVLSRVKPLSTS 79
Cdd:cd09085     1 MKIISWNVNGLRAVHKKGFLDWFKEEKPDILCLQETKAQPEQLpEDLRNIEGYHSYFNSAERKGYSGVALYSKIEPDSVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  80 MGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYRQQWDQAFRNYVAGL-AAVKPVIFCGDLNVAHQEIDIAR 158
Cdd:cd09085    81 EGLGVEEFDNEGRILIADFDDFTLFNIYFPNGQMSEERLDYKLEFYDAFLEYLNELrDSGKNVIICGDFNTAHKEIDLAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 159 PKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEePSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHMD 238
Cdd:cd09085   161 PKENEKVSGFLPEERAWMDKFIENGYVDTFRMFNKE-PGQYTWWSYRTRARERNVGWRIDYFFVNEEFKPKVKDAGILPD 239

                         250
                  ....*....|...
gi 1575802319 239 VMGSDHCPVSLEI 251
Cdd:cd09085   240 VMGSDHCPVSLEL 252
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 1-252 2.44e-112

exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are 5' AP endonucleases that funciton in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273186 [Multi-domain]  Cd Length: 254  Bit Score: 323.08  E-value: 2.44e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQvddlwlssWPYQL---------WNPAeKAGYSGVLVLS 71
Cdd:TIGR00633   1 MKIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQ--------FPAELfeelgyhvfFHGA-KKGYSGVAILS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  72 RVKPLSTSMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSE-LARLPYRQQ-WDQAFRNYVAGLAAVKPVIFCGDLNV 149
Cdd:TIGR00633  72 KVEPLDVRYGFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGSRdLERLEYKLQfWDALFQYLEKELDAGKPVVICGDMNV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 150 AHQEIDIARPKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPR 229
Cdd:TIGR00633 152 AHTEIDLGNPKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAER 231

                         250       260
                  ....*....|....*....|...
gi 1575802319 230 VKSAAIHMDVMGSDHCPVSLEID 252
Cdd:TIGR00633 232 VVDSYIDSEIRGSDHCPIVLELD 254
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
 1-251 5.37e-101

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 294.29  E-value: 5.37e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQvdDLWLSSWPYQLWNPAEKAGYSGVLVLSRVKPLSTSM 80
Cdd:PRK13911    1 MKLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQ--NTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  81 GMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYRQQWDQAFRNYVAGLAAVKPVIFCGDLNVAHQEIDIARPK 160
Cdd:PRK13911   79 GINIEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENPK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 161 DNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHMDVM 240
Cdd:PRK13911  159 TNRKNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDIL 238

                         250
                  ....*....|.
gi 1575802319 241 GSDHCPVSLEI 251
Cdd:PRK13911  239 GSDHCPVGLEL 249
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
 1-251 1.04e-97

exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model also contains eukaryotic apurinic/apyrimidinic endonucleases which group in the same family [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 272954 [Multi-domain]  Cd Length: 254  Bit Score: 285.82  E-value: 1.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLgEAADALDADILCLQEIKARPEQVD-DLWLSSWPYQLWNPAEkaGYSGVLVLSRVKPLSTS 79
Cdd:TIGR00195   1 MKIISWNVNGLRARPHKGL-AWLKENQPDVLCLQETKVQDEQFPlEPFHKEGYHVFFSGQK--GYSGVAIFSKEEPISVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  80 MGMGWQEHDREGRVCTMEFEQFYLVNCYTPN-SQSELARLPYRQQWDQAFRNYVAGLA-AVKPVIFCGDLNVAHQEIDIA 157
Cdd:TIGR00195  78 RGFGVEEEDAEGRIIMAEFDSFLVINGYFPNgSRDDSEKLPYKLQWLEALQNYLEKLVdKDKPVLICGDMNIAPTEIDLH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 158 RPKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPeEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHM 237
Cdd:TIGR00195 158 IPDENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNP-DEGAYSWWDYRTKARDRNRGWRIDYFLVSEPLKERCVDCGIDY 236

                         250
                  ....*....|....*...
gi 1575802319 238 DVMG----SDHCPVSLEI 251
Cdd:TIGR00195 237 DIRGsekpSDHCPVVLEF 254
Nape_like_AP-endo cd10281
Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) ...
 1-251 5.48e-85

Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes Neisseria meningitides Nape and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Neisseria meningitides Nape and NExo. Nape, found in this subfamily, is the dominant AP endonuclease. It exhibits strong AP endonuclease activity, and also exhibits 3'-5'exonuclease and 3'-deoxyribose phosphodiesterase activities.


Pssm-ID: 197336 [Multi-domain]  Cd Length: 253  Bit Score: 253.69  E-value: 5.48e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKGLGEAADALDADILCLQEIKARPEQVDD--LWLSSWPYQLWnPAEKAGYSGVLVLSRVKPLST 78
Cdd:cd10281     1 MRVISVNVNGIRAAAKKGFLEWLAAQDADVVCLQEVRAQEEQLDDdfFEPEGYNAYFF-DAEKKGYAGVAIYSRTQPKAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  79 SMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYRQQWDQAFRNYVAGLAAVKP-VIFCGDLNVAHQEIDIA 157
Cdd:cd10281    80 IYGLGFEEFDDEGRYIEADFDNVSVASLYVPSGSSGDERQEAKMAFLDAFLEHLKELRRKRReFIVCGDFNIAHTEIDIK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 158 RPKDNRFSAGFTDEERSGFTQLL-KAGFTDTFRLLHPEEPSwYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIH 236
Cdd:cd10281   160 NWKANQKNSGFLPEERAWLDQVFgELGYVDAFRELNPDEGQ-YTWWSNRGQARANNVGWRIDYQIATPGLASKVVSAWIY 238

                         250
                  ....*....|....*
gi 1575802319 237 MDVMGSDHCPVSLEI 251
Cdd:cd10281   239 REERFSDHAPLIVDY 253
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
 1-251 3.03e-69

Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes Escherichia coli ExoIII, Neisseria meningitides NExo,and related proteins. These are ExoIII family AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiencies. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For example, Neisseria meningitides Nape and NExo, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. NExo and ExoIII are found in this subfamily. NExo is the non-dominant AP endonuclease. It exhibits strong 3'-5' exonuclease and 3'-deoxyribose phosphodiesterase activities. Escherichia coli ExoIII is an active AP endonuclease, and in addition, it exhibits double strand (ds)-specific 3'-5' exonuclease, exonucleolytic RNase H, 3'-phosphomonoesterase and 3'-phosphodiesterase activities, all catalyzed by a single active site. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes ExoIII and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197320 [Multi-domain]  Cd Length: 254  Bit Score: 213.53  E-value: 3.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKgLGEAADALDADILCLQEIKARPEQ--VDDLwLSSWPYQLWNpAEKAgYSGVLVLSRVKPLST 78
Cdd:cd09086     1 MKIATWNVNSIRARLEQ-VLDWLKEEDPDVLCLQETKVEDDQfpADAF-EALGYHVAVH-GQKA-YNGVAILSRLPLEDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  79 SMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSE-LARLPYRQQWDQAFRNYVAGLAAV-KPVIFCGDLNVAHQEIDI 156
Cdd:cd09086    77 RTGFPGDPDDDQARLIAARVGGVRVINLYVPNGGDIgSPKFAYKLDWLDRLIRYLQKLLKPdDPLVLVGDFNIAPEDIDV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 157 ARPKDNRFSAGFTDEERSGFTQLLKAGFTDTFRLLHPEEPSwYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIH 236
Cdd:cd09086   157 WDPKQLLGKVLFTPEEREALRALLDLGFVDAFRALHPDEKL-FTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGID 235

                         250
                  ....*....|....*....
gi 1575802319 237 MDVMG----SDHCPVSLEI 251
Cdd:cd09086   236 REPRGwekpSDHAPVVAEL 254
Ape2-like_AP-endo cd09088
Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This ...
 2-251 4.61e-45

Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes human APE2, Saccharomyces cerevisiae Apn2/Eth1, and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For examples, Ape1 and Ape2 in humans, and Apn1 and Apn2 in bakers yeast. Ape2 and Apn2/Eth1 are both found in this subfamily, and have the weaker AP endonuclease activity. Ape2 shows strong 3'-5' exonuclease and 3'-phosphodiesterase activities; it can reduce the mutagenic consequences of attack by reactive oxygen species by removing 3'-end adenine opposite from 8-oxoG, in addition to repairing 3'-damaged termini. Apn2/Eth1 exhibits AP endonuclease activity, but has 30-40 fold more active 3'-phosphodiesterase and 3'-5' exonuclease activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197322 [Multi-domain]  Cd Length: 309  Bit Score: 153.24  E-value: 4.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   2 KLVSWNVNGLRAILG-------KGLGEAADALDADILCLQEIKARPEQVDDlwlsswPYQL---WN-----PAEKAGYSG 66
Cdd:cd09088     1 RIVTWNVNGIRTRLQyqpwnkeNSLKSFLDSLDADIICLQETKLTRDELDE------PSAIvegYDsffsfSRGRKGYSG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  67 VLVLSR---VKPLSTSMGMGWQ-----------EHDR---------------------EGRVCTMEFEQFYLVNCYTPNS 111
Cdd:cd09088    75 VATYCRdsaATPVAAEEGLTGVlsspnqknelsENDDigcygemleftdskelleldsEGRCVLTDHGTFVLINVYCPRA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 112 QSE-LARLPYRQQWDQAFRNYVAGL-AAVKPVIFCGDLNVAHQEIDIARPKDNRFSAGFTDEE---RSGFTQLLKAG--- 183
Cdd:cd09088   155 DPEkEERLEFKLDFYRLLEERVEALlKAGRRVILVGDVNVSHRPIDHCDPDDSEDFGGESFEDnpsRQWLDQLLGDSgeg 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1575802319 184 -------FTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDSLAPRVKSAAIHMDVMGSDHCPVSLEI 251
Cdd:cd09088   235 ggspgglLIDSFRYFHPTRKGAYTCWNTLTGARPTNYGTRIDYILADRGLLPWVKAADILPEVEGSDHCPVYADL 309
PRK11756 PRK11756
exonuclease III; Provisional
 1-252 2.96e-40

exonuclease III; Provisional


Pssm-ID: 236970 [Multi-domain]  Cd Length: 268  Bit Score: 139.64  E-value: 2.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKgLGEAADALDADILCLQEIKARPEQ--VDDLwlSSWPYQLWNPAEKAGYsGVLVLSRVKPLST 78
Cdd:PRK11756    1 MKFVSFNINGLRARPHQ-LEAIIEKHQPDVIGLQETKVHDEMfpLEEV--EALGYHVFYHGQKGHY-GVALLSKQTPIAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  79 SMGMGWQEHDREGRVCTMEFE----QFYLVNCYTPN--SQSELARLPYRQQWDQAFRNYVAG-LAAVKPVIFCGDLNVAH 151
Cdd:PRK11756   77 RKGFPTDDEEAQRRIIMATIPtpngNLTVINGYFPQgeSRDHPTKFPAKRQFYQDLQNYLETeLSPDNPLLIMGDMNISP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 152 QEIDIARPKDNR---FSAG---FTDEERSGFTQLLKAGFTDTFRLLHPEEPSWYSWWSYRGGARARNIGWRIDYFCVSDS 225
Cdd:PRK11756  157 TDLDIGIGEENRkrwLRTGkcsFLPEEREWLDRLMDWGLVDTFRQLNPDVNDRFSWFDYRSKGFDDNRGLRIDLILATQP 236

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1575802319 226 LAPRVKSAAIHMDVMG----SDHCPVSLEID 252
Cdd:PRK11756  237 LAERCVETGIDYDIRGmekpSDHAPIWATFK 267
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 5-251 7.61e-33

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: 119.51  E-value: 7.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   5 SWNVNGLRA-ILGKGLGEAADALDADILCLQEIKARPEQVDDLWLSS--WPYQLWNPAE-KAGYSGVLVLSR---VKPLS 77
Cdd:cd08372     3 SYNVNGLNAaTRASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLpeGYHQYQSGPSrKEGYEGVAILSKtpkFKIVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  78 TSMGMGWQEHDREGRVCTMEFE----QFYLVNCYTPNSQSelaRLPYRQQWDQAFRNYVAGLAAVK--PVIFCGDLNVAH 151
Cdd:cd08372    83 KHQYKFGEGDSGERRAVVVKFDvhdkELCVVNAHLQAGGT---RADVRDAQLKEVLEFLKRLRQPNsaPVVICGDFNVRP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 152 QEIDIARPKdnrfsagftdEERSGFTQLlkaGFTDTFRLLHPEepswYSWWSYRggaraRNIGWRIDYFCVSDSLAPRVK 231
Cdd:cd08372   160 SEVDSENPS----------SMLRLFVAL---NLVDSFETLPHA----YTFDTYM-----HNVKSRLDYIFVSKSLLPSVK 217

                         250       260
                  ....*....|....*....|....
gi 1575802319 232 SAAIHMDV----MGSDHCPVSLEI 251
Cdd:cd08372   218 SSKILSDAararIPSDHYPIEVTL 241
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
 3-251 7.27e-21

Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-clade. 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: 197310 [Multi-domain]  Cd Length: 236  Bit Score: 87.79  E-value: 7.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   3 LVSWNVNGLRAIlGKgLGEAADAL---DADILCLQEIKARPEQVDDLWLSSWPYqLWNPAEKAGYSGVLVLsrVKPLSTS 79
Cdd:cd09076     1 IGTLNVRGLRSP-GK-RAQLLEELkrkKLDILGLQETHWTGEGELKKKREGGTI-LYSGSDSGKSRGVAIL--LSKTAAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  80 MGMGWqEHDREGRVCTMEFE----QFYLVNCYTPNSQSELARLPYRQQwdqaFRNYVAGLAAVKPVIFCGDLNVahqeid 155
Cdd:cd09076    76 KLLEY-TKVVSGRIIMVRFKikgkRLTIINVYAPTARDEEEKEEFYDQ----LQDVLDKVPRHDTLIIGGDFNA------ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 156 IARPKDN-RFSAGFTDE--ERSGFTQLLKAGFTDTFRLLHPEEPsWYSWWSYRGGARARnigwrIDYFCVSDSLAPRVKS 232
Cdd:cd09076   145 VLGPKDDgRKGLDKRNEngERALSALIEEHDLVDVWRENNPKTR-EYTWRSPDHGSRSR-----IDRILVSKRLRVKVKK 218

                         250
                  ....*....|....*....
gi 1575802319 233 AAIhMDVMGSDHCPVSLEI 251
Cdd:cd09076   219 TKI-TPGAGSDHRLVTLKL 236
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 4-149 9.73e-18

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: 78.42  E-value: 9.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   4 VSWNVNGLRA------ILGKGLGEAADALDADILCLQEIKARPEQVDDLWLSS--WPYQLWNPAEKAGYSGVLVLSRVKP 75
Cdd:pfam03372   1 LTWNVNGGNAdaagddRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAygGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1575802319  76 LSTSMGMGWQEHDREGRVCTMEFEQFYLVNCYTPNSQSELARLPYR-QQWDQAFRNYVAGLAAVKPVIFCGDLNV 149
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDeQRADLLLLLLALLAPRSEPVILAGDFNA 155
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
 1-247 1.68e-09

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 56.93  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILGKgLGEAADALDADILCLQEIKARPEQVDDLWLSSWPYQLWNPAEKAGysGVLVLSRVkPLSTSM 80
Cdd:COG3021    95 LRVLTANVLFGNADAEA-LAALVREEDPDVLVLQETTPAWEEALAALEADYPYRVLCPLDNAY--GMALLSRL-PLTEAE 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  81 GMGWQEHDREGRVCTMEFE----QFYLVNCYTPNSQSElarlpyrqQWDQAFRN---YVAGLAavKPVIFCGDLNVAhqe 153
Cdd:COG3021   171 VVYLVGDDIPSIRATVELPggpvRLVAVHPAPPVGGSA--------ERDAELAAlakAVAALD--GPVIVAGDFNAT--- 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 154 idiarpkdnRFSAGFTD-EERSGFT-QLLKAGFTDTFrllhpeePSWYSWwsyrggararnIGWRIDYFCVSDSLAPRvk 231
Cdd:COG3021   238 ---------PWSPTLRRlLRASGLRdARAGRGLGPTW-------PANLPF-----------LRLPIDHVLVSRGLTVV-- 288

                         250
                  ....*....|....*.
gi 1575802319 232 sAAIHMDVMGSDHCPV 247
Cdd:COG3021   289 -DVRVLPVIGSDHRPL 303
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 3-251 2.37e-09

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, 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: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 56.15  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   3 LVSWNVNGLRAILGKGLGEAA----DALDADILCLQE----IKARPEQVDDLwLSSWPYQLWNPAEKAGYSGVLVLSR-- 72
Cdd:cd09084     1 VMSYNVRSFNRYKWKDDPDKIldfiKKQDPDILCLQEyygsEGDKDDDLRLL-LKGYPYYYVVYKSDSGGTGLAIFSKyp 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  73 ---VKPL---STSMGMGWQEHDREG---RVCTMEFEQFYL-----VNCYTPNSQSELARLPYRQ----QWDQAfrNYVAG 134
Cdd:cd09084    80 ilnSGSIdfpNTNNNAIFADIRVGGdtiRVYNVHLESFRItpsdkELYKEEKKAKELSRNLLRKlaeaFKRRA--AQADL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 135 LAAVK-----PVIFCGDLNvahqeidiarpkdnrfsagftDEERSGFTQLLKAGFTDTFRLlhpeepSWYSW-WSYRGGA 208
Cdd:cd09084   158 LAADIaaspyPVIVCGDFN---------------------DTPASYVYRTLKKGLTDAFVE------AGSGFgYTFNGLF 210

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1575802319 209 rarnIGWRIDYFCVSDSLapRVKSAAIHMDVMgSDHCPVSLEI 251
Cdd:cd09084   211 ----FPLRIDYILTSKGF--KVLRYRVDPGKY-SDHYPIVATL 246
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 1-155 4.42e-09

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 54.14  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNV-NGL----RAILgKGLGEAADALDADILCLQEikarpeqvddlwlsswpyqlwnpaekagysgVLVLSRVKP 75
Cdd:COG3568     8 LRVMTYNIrYGLgtdgRADL-ERIARVIRALDPDVVALQE-------------------------------NAILSRYPI 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  76 LStsmgmgWQEHD-----REGRVCT-----MEFEQFYLVNCYTpNSQSELARlpyRQQWdQAFRNYVAGLAAVKPVIFCG 145
Cdd:COG3568    56 VS------SGTFDlpdpgGEPRGALwadvdVPGKPLRVVNTHL-DLRSAAAR---RRQA-RALAELLAELPAGAPVILAG 124

                         170
                  ....*....|
gi 1575802319 146 DLNvahqEID 155
Cdd:COG3568   125 DFN----DID 130
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 27-251 1.20e-07

Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, 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: 197317 [Multi-domain]  Cd Length: 252  Bit Score: 51.06  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  27 DADILCLQEikARPEQVDDLwLSSWPYQLW------NPAEKAGYSGVLVL-SRVKPLStsMGMGW--QEHDREG------ 91
Cdd:cd09083    34 DPDIIGTQE--ALPHQLADL-EELLPEYDWigvgrdDGKEKGEFSAIFYRkDRFELLD--SGTFWlsETPDVVGskgwda 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  92 ---RVCTM-EFEQ------FYLVNCYTPNsQSELARlpyrQQWDQAFRNYVAGLAAVKPVIFCGDLNvahqeidiARPKD 161
Cdd:cd09083   109 alpRICTWaRFKDkktgkeFYVFNTHLDH-VGEEAR----EESAKLILERIKEIAGDLPVILTGDFN--------AEPDS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 162 NRFSAgftdeersgftqLLKAGFTDTFRLL-HPEEPSWYSWWSYRGGARARnigwRIDYFCVSDSLapRVKSAAIHMDVM 240
Cdd:cd09083   176 EPYKT------------LTSGGLKDARDTAaTTDGGPEGTFHGFKGPPGGS----RIDYIFVSPGV--KVLSYEILTDRY 237

                         250
                  ....*....|....*
gi 1575802319 241 G----SDHCPVSLEI 251
Cdd:cd09083   238 DgrypSDHFPVVADL 252
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 1-251 3.54e-07

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. 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: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 49.65  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   1 MKLVSWNVNGLRAILG----KGLGEAADALDADILCLQEIKarPEQVDDLWLSSWPYQLW-----NPAEKAGYSGVLVLS 71
Cdd:cd09080     1 LKVLTWNVDFLDDVNLaermRAILKLLEELDPDVIFLQEVT--PPFLAYLLSQPWVRKNYyfsegPPSPAVDPYGVLILS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  72 RVKPLS-----TSMGMGWQ--------EHDREGRVCTMEFEqfylvncytpnsqSELARLPYRQQWDQAFRNYVAGLAAV 138
Cdd:cd09080    79 KKSLVVrrvpfTSTRMGRNllaaeinlGSGEPLRLATTHLE-------------SLKSHSSERTAQLEEIAKKLKKPPGA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 139 KPVIFCGDLNvahqeidiARPKDNrfsagftdeersgFTQLLKAGFTDTFRLLHPEEPSWYSW------WSYRGGARARN 212
Cdd:cd09080   146 ANVILGGDFN--------LRDKED-------------DTGGLPNGFVDAWEELGPPGEPGYTWdtqknpMLRKGEAGPRK 204

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1575802319 213 igwRID-YFCVSDSLAP----RVKSAAIHMDVMG---SDHCPVSLEI 251
Cdd:cd09080   205 ---RFDrVLLRGSDLKPksieLIGTEPIPGDEEGlfpSDHFGLLAEL 248
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
19-252 4.53e-07

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 50.02  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  19 LGEAADALDADILCLQEIKARPEQVDDL----WLSSWPYQLWNPAEKAGYSG--VLVLSR---VKPLSTS----MGMGWQ 85
Cdd:COG2374   106 IAAAIAALDADIVGLQEVENNGSALQDLvaalNLAGGTYAFVHPPDGPDGDGirVALLYRpdrVTLVGSAtiadLPDSPG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319  86 EHDREGR---VCTMEF---EQFYLVNCY----TPNSQSELAR--LPYRQQWDQAFRNYVAGLAAVKP---VIFCGDLNva 150
Cdd:COG2374   186 NPDRFSRpplAVTFELangEPFTVIVNHfkskGSDDPGDGQGasEAKRTAQAEALRAFVDSLLAADPdapVIVLGDFN-- 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 151 hqeidiarpkDNRFSAGFTDeersgftqLLKA-GFTDTFRLLHPEEPswYSWwSYRGgararNIGwRIDYFCVSDSLAPR 229
Cdd:COG2374   264 ----------DYPFEDPLRA--------LLGAgGLTNLAEKLPAAER--YSY-VYDG-----NSG-LLDHILVSPALAAR 316

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1575802319 230 VKSAA---IHMDVM-----------------GSDHCPVSLEID 252
Cdd:COG2374   317 VTGADiwhINADIYnddfkpdfrtyaddpgrASDHDPVVVGLR 359
PRK05421 PRK05421
endonuclease/exonuclease/phosphatase family protein;
2-77 1.41e-03

endonuclease/exonuclease/phosphatase family protein;


Pssm-ID: 235454 [Multi-domain]  Cd Length: 263  Bit Score: 39.15  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319   2 KLVSWNV-----NGLRAILgKGLGEaadalDADILCLQEIKARPEQVDDLWLSSWPYQLwNPA--EKAGYSGVLVLSRVK 74
Cdd:PRK05421   45 RLLVWNIykqqrAGWLSVL-KNLGK-----DADLVLLQEAQTTPELVQFATANYLAADQ-APAfvLPQHPSGVMTLSKAH 117


                  ...
gi 1575802319  75 PLS 77
Cdd:PRK05421  118 PVY 120
Exo_endo_phos_2 pfam14529
Endonuclease-reverse transcriptase; This domain represents the endonuclease region of ...
 101-247 3.24e-03

Endonuclease-reverse transcriptase; This domain represents the endonuclease region of retrotransposons from a range of bacteria, archaea and eukaryotes. These are enzymes largely from class EC:2.7.7.49.


Pssm-ID: 434019 [Multi-domain]  Cd Length: 118  Bit Score: 36.57  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 101 FYLVNCYTPNSQSELARLpyrqqwdQAFRNYVAGLAAvKPVIFCGDLNVAHQEidiarpkdnrFSAGFTDEERSgfTQLL 180
Cdd:pfam14529   1 ILIISVYCPPSDQLRNLL-------DTLEDILRSLDR-PPIIIGGDFNAHHPL----------WGSNSTDVSRG--EELI 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575802319 181 KagFTDTFRLL---HPEEPSwySWWSYRGGararNIgwrIDYFCVSDSLAPRVKSaaIHMDVMGSDHCPV 247
Cdd:pfam14529  61 E--FLNEHGLNllnLPKSGP--TFISSNGD----ST---IDLTLTSDPLAVRVLS--DLGPDSGSDHRPI 117
 
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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