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Conserved domains on  [gi|490821596|ref|WP_004683693|]
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MULTISPECIES: exodeoxyribonuclease III [Brucella]

Protein Classification

exodeoxyribonuclease III( domain architecture ID 10173387)

exodeoxyribonuclease III is a Mg-dependent 3' to 5' exonuclease acting on dsDNA, which releases 5' phosphomononucleotides as degradation products

CATH:  3.60.10.10
EC:  3.1.11.2
Gene Ontology:  GO:0046872|GO:0006281|GO:0008311|GO:0004519|GO:0003677
PubMed:  7885481|10838565
SCOP:  4002213

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
 1-258 1.83e-142

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: 399.58  E-value: 1.83e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:cd09086    1 MKIATWNVNSIRARLEQVLDWLKEEDPDVLCLQETKVEDDQFPADAFEALGYHVAVHGQKAYNGVAILSRLPLEDVRTGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  81 PGDDSDEQARFIEGIYSTdtgvVRVVSLYLPNGNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVDA 160
Cdd:cd09086   81 PGDPDDDQARLIAARVGG----VRVINLYVPNGGDIGSPKFAYKLDWLDRLIRYLQKLLKPDDPLVLVGDFNIAPEDIDV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 161 RNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRASTDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANIEK 240
Cdd:cd09086  157 WDPKQLLGKVLFTPEEREALRALLDLGFVDAFRALHPDEKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGIDR 236

                        250
                 ....*....|....*...
gi 490821596 241 HVRAWEKPSDHVPVTVTL 258
Cdd:cd09086  237 EPRGWEKPSDHAPVVAEL 254
 
Name Accession Description Interval E-value
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
 1-258 1.83e-142

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: 399.58  E-value: 1.83e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:cd09086    1 MKIATWNVNSIRARLEQVLDWLKEEDPDVLCLQETKVEDDQFPADAFEALGYHVAVHGQKAYNGVAILSRLPLEDVRTGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  81 PGDDSDEQARFIEGIYSTdtgvVRVVSLYLPNGNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVDA 160
Cdd:cd09086   81 PGDPDDDQARLIAARVGG----VRVINLYVPNGGDIGSPKFAYKLDWLDRLIRYLQKLLKPDDPLVLVGDFNIAPEDIDV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 161 RNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRASTDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANIEK 240
Cdd:cd09086  157 WDPKQLLGKVLFTPEEREALRALLDLGFVDAFRALHPDEKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGIDR 236

                        250
                 ....*....|....*...
gi 490821596 241 HVRAWEKPSDHVPVTVTL 258
Cdd:cd09086  237 EPRGWEKPSDHAPVVAEL 254
XthA COG0708
Exonuclease III [Replication, recombination and repair];
1-259 3.59e-139

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 391.36  E-value: 3.59e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:COG0708    1 MKIASWNVNGIRARLPKLLDWLAEEDPDVLCLQETKAQDEQFPLEAFEAAGYHVYFHGQKGYNGVAILSRLPPEDVRRGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  81 PGDDSDEQARFIEGiystDTGVVRVVSLYLPNGNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVDA 160
Cdd:COG0708   81 GGDEFDAEGRYIEA----DFGGVRVVSLYVPNGGSVGSEKFDYKLRFLDALRAYLAELLAPGRPLILCGDFNIAPTEIDV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 161 RNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRAST-DESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANIE 239
Cdd:COG0708  157 KNPKANLKNAGFLPEERAWFDRLLELGLVDAFRALHpDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGID 236

                        250       260
                 ....*....|....*....|
gi 490821596 240 KHVRAWEKPSDHVPVTVTLA 259
Cdd:COG0708  237 REPRGDERPSDHAPVVVELD 256
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
 1-258 2.36e-87

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: 260.01  E-value: 2.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596    1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:TIGR00195   1 MKIISWNVNGLRARPHKGLAWLKENQPDVLCLQETKVQDEQFPLEPFHKEGYHVFFSGQKGYSGVAIFSKEEPISVRRGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   81 PGDDSDEQARFIEGIYSTdtgvVRVVSLYLPNGNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVDA 160
Cdd:TIGR00195  81 GVEEEDAEGRIIMAEFDS----FLVINGYFPNGSRDDSEKLPYKLQWLEALQNYLEKLVDKDKPVLICGDMNIAPTEIDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  161 RNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRASTDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANIEK 240
Cdd:TIGR00195 157 HIPDENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNPDEGAYSWWDYRTKARDRNRGWRIDYFLVSEPLKERCVDCGIDY 236

                         250
                  ....*....|....*...
gi 490821596  241 HVRAWEKPSDHVPVTVTL 258
Cdd:TIGR00195 237 DIRGSEKPSDHCPVVLEF 254
PRK11756 PRK11756
exonuclease III; Provisional
 1-260 1.26e-77

exonuclease III; Provisional


Pssm-ID: 236970 [Multi-domain]  Cd Length: 268  Bit Score: 235.56  E-value: 1.26e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:PRK11756   1 MKFVSFNINGLRARPHQLEAIIEKHQPDVIGLQETKVHDEMFPLEEVEALGYHVFYHGQKGHYGVALLSKQTPIAVRKGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  81 PGDDSDEQARFIEGIYSTDTGVVRVVSLYLPNGNPIDTE-KFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVD 159
Cdd:PRK11756  81 PTDDEEAQRRIIMATIPTPNGNLTVINGYFPQGESRDHPtKFPAKRQFYQDLQNYLETELSPDNPLLIMGDMNISPTDLD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 160 ----ARNPQAWL--GDALFQPQSRQAFRRLENLGFTDAIRAST-DESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNR 232
Cdd:PRK11756 161 igigEENRKRWLrtGKCSFLPEEREWLDRLMDWGLVDTFRQLNpDVNDRFSWFDYRSKGFDDNRGLRIDLILATQPLAER 240

                        250       260
                 ....*....|....*....|....*...
gi 490821596 233 FISANIEKHVRAWEKPSDHVPVTVTLAV 260
Cdd:PRK11756 241 CVETGIDYDIRGMEKPSDHAPIWATFKL 268
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 4-153 4.90e-21

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: 87.28  E-value: 4.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596    4 ATWNING-------VKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGY---HVETHGQKGFNGVALLSKKSP 73
Cdd:pfam03372   1 LTWNVNGgnadaagDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGflsYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   74 DEINKGLPGDDSDEQARFIEGIYSTDTGVVRVVSLylpngNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNV 153
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTL-----APHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
 
Name Accession Description Interval E-value
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
 1-258 1.83e-142

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: 399.58  E-value: 1.83e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:cd09086    1 MKIATWNVNSIRARLEQVLDWLKEEDPDVLCLQETKVEDDQFPADAFEALGYHVAVHGQKAYNGVAILSRLPLEDVRTGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  81 PGDDSDEQARFIEGIYSTdtgvVRVVSLYLPNGNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVDA 160
Cdd:cd09086   81 PGDPDDDQARLIAARVGG----VRVINLYVPNGGDIGSPKFAYKLDWLDRLIRYLQKLLKPDDPLVLVGDFNIAPEDIDV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 161 RNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRASTDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANIEK 240
Cdd:cd09086  157 WDPKQLLGKVLFTPEEREALRALLDLGFVDAFRALHPDEKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGIDR 236

                        250
                 ....*....|....*...
gi 490821596 241 HVRAWEKPSDHVPVTVTL 258
Cdd:cd09086  237 EPRGWEKPSDHAPVVAEL 254
XthA COG0708
Exonuclease III [Replication, recombination and repair];
1-259 3.59e-139

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 391.36  E-value: 3.59e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:COG0708    1 MKIASWNVNGIRARLPKLLDWLAEEDPDVLCLQETKAQDEQFPLEAFEAAGYHVYFHGQKGYNGVAILSRLPPEDVRRGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  81 PGDDSDEQARFIEGiystDTGVVRVVSLYLPNGNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVDA 160
Cdd:COG0708   81 GGDEFDAEGRYIEA----DFGGVRVVSLYVPNGGSVGSEKFDYKLRFLDALRAYLAELLAPGRPLILCGDFNIAPTEIDV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 161 RNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRAST-DESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANIE 239
Cdd:COG0708  157 KNPKANLKNAGFLPEERAWFDRLLELGLVDAFRALHpDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGID 236

                        250       260
                 ....*....|....*....|
gi 490821596 240 KHVRAWEKPSDHVPVTVTLA 259
Cdd:COG0708  237 REPRGDERPSDHAPVVVELD 256
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
 1-258 2.36e-87

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: 260.01  E-value: 2.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596    1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:TIGR00195   1 MKIISWNVNGLRARPHKGLAWLKENQPDVLCLQETKVQDEQFPLEPFHKEGYHVFFSGQKGYSGVAIFSKEEPISVRRGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   81 PGDDSDEQARFIEGIYSTdtgvVRVVSLYLPNGNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVDA 160
Cdd:TIGR00195  81 GVEEEDAEGRIIMAEFDS----FLVINGYFPNGSRDDSEKLPYKLQWLEALQNYLEKLVDKDKPVLICGDMNIAPTEIDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  161 RNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRASTDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANIEK 240
Cdd:TIGR00195 157 HIPDENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNPDEGAYSWWDYRTKARDRNRGWRIDYFLVSEPLKERCVDCGIDY 236

                         250
                  ....*....|....*...
gi 490821596  241 HVRAWEKPSDHVPVTVTL 258
Cdd:TIGR00195 237 DIRGSEKPSDHCPVVLEF 254
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 1-259 6.57e-82

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: 246.04  E-value: 6.57e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596    1 MKIATWNINGVKARI--DNLQhWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQK-GFNGVALLSKKSPDEIN 77
Cdd:TIGR00633   1 MKIISWNVNGLRARLhkLFLD-WLKEEQPDVLCLQETKVADEQFPAELFEELGYHVFFHGAKkGYSGVAILSKVEPLDVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   78 KGLPGDDSDEQARFIEGIYstdtGVVRVVSLYLPNGNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEP 157
Cdd:TIGR00633  80 YGFGGEPHDEEGRVITAEF----DGFTVVNVYVPNGGSRDLERLEYKLQFWDALFQYLEKELDAGKPVVICGDMNVAHTE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  158 VDARNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRAST-DESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISA 236
Cdd:TIGR00633 156 IDLGNPKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNpDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDS 235

                         250       260
                  ....*....|....*....|...
gi 490821596  237 NIEKHVRAwekpSDHVPVTVTLA 259
Cdd:TIGR00633 236 YIDSEIRG----SDHCPIVLELD 254
PRK11756 PRK11756
exonuclease III; Provisional
 1-260 1.26e-77

exonuclease III; Provisional


Pssm-ID: 236970 [Multi-domain]  Cd Length: 268  Bit Score: 235.56  E-value: 1.26e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKGL 80
Cdd:PRK11756   1 MKFVSFNINGLRARPHQLEAIIEKHQPDVIGLQETKVHDEMFPLEEVEALGYHVFYHGQKGHYGVALLSKQTPIAVRKGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  81 PGDDSDEQARFIEGIYSTDTGVVRVVSLYLPNGNPIDTE-KFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVD 159
Cdd:PRK11756  81 PTDDEEAQRRIIMATIPTPNGNLTVINGYFPQGESRDHPtKFPAKRQFYQDLQNYLETELSPDNPLLIMGDMNISPTDLD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 160 ----ARNPQAWL--GDALFQPQSRQAFRRLENLGFTDAIRAST-DESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNR 232
Cdd:PRK11756 161 igigEENRKRWLrtGKCSFLPEEREWLDRLMDWGLVDTFRQLNpDVNDRFSWFDYRSKGFDDNRGLRIDLILATQPLAER 240

                        250       260
                 ....*....|....*....|....*...
gi 490821596 233 FISANIEKHVRAWEKPSDHVPVTVTLAV 260
Cdd:PRK11756 241 CVETGIDYDIRGMEKPSDHAPIWATFKL 268
ExoIII_AP-endo cd09073
Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ...
 2-258 2.22e-74

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: 226.79  E-value: 2.22e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   2 KIATWNINGVKARIDN-LQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETHGQ--KGFNGVALLSKKSPDEINK 78
Cdd:cd09073    1 KIISWNVNGLRARLKKgVLKWLKEEKPDILCLQETKADEDKLPEELQHVEGYHSYWSPArkKGYSGVATLSKEEPLDVSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  79 GLPGDDSDEQARFIegiySTDTGVVRVVSLYLPNGNPiDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPV 158
Cdd:cd09073   81 GIGGEEFDSEGRVI----TAEFDDFYLINVYFPNGGR-GLERLDYKLRFYEAFLEFLEKLRKRGKPVVICGDFNVAHEEI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 159 DARNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRASTDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANI 238
Cdd:cd09073  156 DLARPKKNEKNAGFTPEERAWFDKLLSLGYVDTFRHFHPEPGAYTWWSYRGNARERNVGWRIDYFLVSEELAEKVKDSGI 235

                        250       260
                 ....*....|....*....|
gi 490821596 239 EKHVraweKPSDHVPVTVTL 258
Cdd:cd09073  236 LSKV----KGSDHAPVTLEL 251
Nape_like_AP-endo cd10281
Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) ...
 1-257 1.30e-58

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: 186.66  E-value: 1.30e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDN-LQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYHVETH--GQKGFNGVALLSKKSPDEIN 77
Cdd:cd10281    1 MRVISVNVNGIRAAAKKgFLEWLAAQDADVVCLQEVRAQEEQLDDDFFEPEGYNAYFFdaEKKGYAGVAIYSRTQPKAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  78 KGLPGDDSDEQARFIEgiysTDTGVVRVVSLYLPNGNpIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEP 157
Cdd:cd10281   81 YGLGFEEFDDEGRYIE----ADFDNVSVASLYVPSGS-SGDERQEAKMAFLDAFLEHLKELRRKRREFIVCGDFNIAHTE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 158 VDARNPQAWLGDALFQPQSRQAF-RRLENLGFTDAIRASTDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISA 236
Cdd:cd10281  156 IDIKNWKANQKNSGFLPEERAWLdQVFGELGYVDAFRELNPDEGQYTWWSNRGQARANNVGWRIDYQIATPGLASKVVSA 235

                        250       260
                 ....*....|....*....|.
gi 490821596 237 NIEKHVRaWekpSDHVPVTVT 257
Cdd:cd10281  236 WIYREER-F---SDHAPLIVD 252
Mth212-like_AP-endo cd09085
Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic ...
 1-258 5.46e-52

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: 169.76  E-value: 5.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARID-NLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYH--VETHGQKGFNGVALLSKKSPDEIN 77
Cdd:cd09085    1 MKIISWNVNGLRAVHKkGFLDWFKEEKPDILCLQETKAQPEQLPEDLRNIEGYHsyFNSAERKGYSGVALYSKIEPDSVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  78 KGLPGDDSDEQARFIEGIYSTDTgvvrVVSLYLPNGNpIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEP 157
Cdd:cd09085   81 EGLGVEEFDNEGRILIADFDDFT----LFNIYFPNGQ-MSEERLDYKLEFYDAFLEYLNELRDSGKNVIICGDFNTAHKE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 158 VDARNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRASTDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISAN 237
Cdd:cd09085  156 IDLARPKENEKVSGFLPEERAWMDKFIENGYVDTFRMFNKEPGQYTWWSYRTRARERNVGWRIDYFFVNEEFKPKVKDAG 235

                        250       260
                 ....*....|....*....|.
gi 490821596 238 IEKHVRAwekpSDHVPVTVTL 258
Cdd:cd09085  236 ILPDVMG----SDHCPVSLEL 252
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 1-258 1.49e-51

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: 168.50  E-value: 1.49e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDN-LQHWLRESSPDIVCLQEIKSVDEQFP-RLEIEALGYHVETHG--QKGFNGVALLSKKSPDEI 76
Cdd:cd09087    1 LKIISWNVNGLRALLKKgLLDYVKKEDPDILCLQETKLQEGDVPkELKELLKGYHQYWNAaeKKGYSGTAILSKKKPLSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  77 NKGLPGDDSDEQARFIEGIYSTdtgvVRVVSLYLPN-GNpiDTEKFPYKLSWMQRLENWAKKrLTLEEPLVLAGDYNVIP 155
Cdd:cd09087   81 TYGIGIEEHDQEGRVITAEFEN----FYLVNTYVPNsGR--GLERLDRRKEWDVDFRAYLKK-LDSKKPVIWCGDLNVAH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 156 EPVDARNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRAST-DESGVYSFWDYQAGAWQKNNGIRIDHLMLSpeatNRFI 234
Cdd:cd09087  154 EEIDLANPKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHpDKEGAYTFWSYRGNARAKNVGWRLDYFLVS----ERLK 229

                        250       260
                 ....*....|....*....|....
gi 490821596 235 SANIEKHVRAWEKPSDHVPVTVTL 258
Cdd:cd09087  230 DRVVDSFIRSDIMGSDHCPIGLEL 253
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
 1-258 2.16e-29

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 111.32  E-value: 2.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKA-RIDNLQHWLRESSPDIVCLQEIKSVDEQfPRLEIEALGYHVETHGQKGFNGVALLSKKSPDEINKG 79
Cdd:PRK13911   1 MKLISWNVNGLRAcMTKGFMDFFNSVDADVFCIQESKMQQEQ-NTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  80 LPGDDSDEQARFIEGIYSTdtgvVRVVSLYLPNGNPIdTEKFPYKLSWMQRLENWAKKrLTLEEPLVLAGDYNVIPEPVD 159
Cdd:PRK13911  80 INIEEHDKEGRVITCEFES----FYLVNVYTPNSQQA-LSRLSYRMSWEVEFKKFLKA-LELKKPVIVCGDLNVAHNEID 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 160 ARNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRA-STDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANI 238
Cdd:PRK13911 154 LENPKTNRKNAGFSDEERGKFSELLNAGFIDTFRYfYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALI 233

                        250       260
                 ....*....|....*....|
gi 490821596 239 EKHVRAwekpSDHVPVTVTL 258
Cdd:PRK13911 234 YKDILG----SDHCPVGLEL 249
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 3-258 6.29e-24

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: 96.40  E-value: 6.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   3 IATWNINGVKA--RIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGYH----VETHGQKGFNGVALLSKK---SP 73
Cdd:cd08372    1 VASYNVNGLNAatRASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYhqyqSGPSRKEGYEGVAILSKTpkfKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  74 DEINKGLPGDDSDEQARFIEGIYSTDTGVVRVVSLYLPNGNPIDTEKFPYklsWMQRLENWAKKRLTLEEPLVLAGDYNV 153
Cdd:cd08372   81 VEKHQYKFGEGDSGERRAVVVKFDVHDKELCVVNAHLQAGGTRADVRDAQ---LKEVLEFLKRLRQPNSAPVVICGDFNV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 154 IPEPVDARNPQAWLgdALFQPqsrqafrrlenLGFTDAIRASTDEsgvYSFWDYqagawQKNNGIRIDHLMLSPEATNRF 233
Cdd:cd08372  158 RPSEVDSENPSSML--RLFVA-----------LNLVDSFETLPHA---YTFDTY-----MHNVKSRLDYIFVSKSLLPSV 216

                        250       260
                 ....*....|....*....|....*
gi 490821596 234 ISANIEKHVRAWEKPSDHVPVTVTL 258
Cdd:cd08372  217 KSSKILSDAARARIPSDHYPIEVTL 241
Ape2-like_AP-endo cd09088
Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This ...
 2-258 3.57e-22

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: 93.15  E-value: 3.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   2 KIATWNINGVKARIdNLQHWLRESS---------PDIVCLQEIKSVDEQFPRLEIEALGYHVE---THGQKGFNGVALLS 69
Cdd:cd09088    1 RIVTWNVNGIRTRL-QYQPWNKENSlksfldsldADIICLQETKLTRDELDEPSAIVEGYDSFfsfSRGRKGYSGVATYC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  70 KKS------------------------PDEINKGLPGDDSDEQARFI------EG---IysTDTGVVRVVSLYLPNGNPI 116
Cdd:cd09088   80 RDSaatpvaaeegltgvlsspnqknelSENDDIGCYGEMLEFTDSKElleldsEGrcvL--TDHGTFVLINVYCPRADPE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 117 DTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNVIPEPVD---ARNPQAWLGDALFQPQSRQAFRR-LENLGFTDAI 192
Cdd:cd09088  158 KEERLEFKLDFYRLLEERVEALLKAGRRVILVGDVNVSHRPIDhcdPDDSEDFGGESFEDNPSRQWLDQlLGDSGEGGGS 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490821596 193 RAS----------TDESGVYSFWDYQAGAWQKNNGIRIDHLMLSPEATNRFISANIEKHVraweKPSDHVPVTVTL 258
Cdd:cd09088  238 PGGllidsfryfhPTRKGAYTCWNTLTGARPTNYGTRIDYILADRGLLPWVKAADILPEV----EGSDHCPVYADL 309
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 4-153 4.90e-21

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: 87.28  E-value: 4.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596    4 ATWNING-------VKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEALGY---HVETHGQKGFNGVALLSKKSP 73
Cdd:pfam03372   1 LTWNVNGgnadaagDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGflsYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   74 DEINKGLPGDDSDEQARFIEGIYSTDTGVVRVVSLylpngNPIDTEKFPYKLSWMQRLENWAKKRLTLEEPLVLAGDYNV 153
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTL-----APHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
 1-260 2.34e-16

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 76.96  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNINGVKARIDNLQHWLRESSPDIVCLQEI-KSVDEQFPRLEiEALGYHVeTHGQKGFNGVALLSKK--SPDEIN 77
Cdd:COG3021   95 LRVLTANVLFGNADAEALAALVREEDPDVLVLQETtPAWEEALAALE-ADYPYRV-LCPLDNAYGMALLSRLplTEAEVV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  78 kglpgDDSDEQARFIEGIYSTDTGVVRVVSLYLPngNPIDTEKFpyklsWMQRLENWAKKRLTLEEPLVLAGDYNvipep 157
Cdd:COG3021  173 -----YLVGDDIPSIRATVELPGGPVRLVAVHPA--PPVGGSAE-----RDAELAALAKAVAALDGPVIVAGDFN----- 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 158 vdarnpqawlgDALFQPqsrqAFRRLENL-GFTDAIRAstdeSGVYSFWDyqagAWQKNNGIRIDHLMLSPEATNRfisa 236
Cdd:COG3021  236 -----------ATPWSP----TLRRLLRAsGLRDARAG----RGLGPTWP----ANLPFLRLPIDHVLVSRGLTVV---- 288

                        250       260
                 ....*....|....*....|....*
gi 490821596 237 niekHVRAWEKP-SDHVPVTVTLAV 260
Cdd:COG3021  289 ----DVRVLPVIgSDHRPLLAELAL 309
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 3-258 5.38e-11

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: 60.77  E-value: 5.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   3 IATWNING-----VKARIDNLQHWLRESSPDIVCLQEIKSVDEQFPRLEIEAL----GYHVETHGQKGFNGVALLSkKSP 73
Cdd:cd09084    1 VMSYNVRSfnrykWKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLkgypYYYVVYKSDSGGTGLAIFS-KYP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  74 dEINKG-LPGDDSDEQARFIEGIYSTDTgvVRVVSLYLP----NGNPIDTEKFPYKLSW-----MQRLENWAKKR----- 138
Cdd:cd09084   80 -ILNSGsIDFPNTNNNAIFADIRVGGDT--IRVYNVHLEsfriTPSDKELYKEEKKAKElsrnlLRKLAEAFKRRaaqad 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 139 ------LTLEEPLVLAGDYNvipepvdarNPqawlgdalfqPQSRqAFRRLENlGFTDAIRASTDESGvYSFWDYqaGAW 212
Cdd:cd09084  157 llaadiAASPYPVIVCGDFN---------DT----------PASY-VYRTLKK-GLTDAFVEAGSGFG-YTFNGL--FFP 212

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 490821596 213 qknngIRIDHLMLSPEAtnRFISANIEKhvrawEKPSDHVPVTVTL 258
Cdd:cd09084  213 -----LRIDYILTSKGF--KVLRYRVDP-----GKYSDHYPIVATL 246
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
 3-258 1.71e-10

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: 59.29  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   3 IATWNINGV--KARIDNLQHWLRESSPDIVCLQEIKSVDE---QFPRLEIEALgYHveTHGQKGFNGVALLSKKS--PDE 75
Cdd:cd09076    1 IGTLNVRGLrsPGKRAQLLEELKRKKLDILGLQETHWTGEgelKKKREGGTIL-YS--GSDSGKSRGVAILLSKTaaNKL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  76 INKGLPGDDSDEQARF-IEGIystdtgVVRVVSLYLPN-GNPIDTEKFpYklswmQRLENWAKKRlTLEEPLVLAGDYNV 153
Cdd:cd09076   78 LEYTKVVSGRIIMVRFkIKGK------RLTIINVYAPTaRDEEEKEEF-Y-----DQLQDVLDKV-PRHDTLIIGGDFNA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 154 IpepVDARNPQAWLGDALFQPQSRQAFRRLENLGFTDAIRASTDESGVYSF--WDYQAGAwqknngiRIDHLMlspeaTN 231
Cdd:cd09076  145 V---LGPKDDGRKGLDKRNENGERALSALIEEHDLVDVWRENNPKTREYTWrsPDHGSRS-------RIDRIL-----VS 209

                        250       260
                 ....*....|....*....|....*..
gi 490821596 232 RFISANIEKHVRAWEKPSDHVPVTVTL 258
Cdd:cd09076  210 KRLRVKVKKTKITPGAGSDHRLVTLKL 236
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 1-154 3.91e-10

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 57.23  E-value: 3.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNI-NGV----KARIDNLQHWLRESSPDIVCLQEiksvdeqfprleiealgyhvethgqkgfngVALLSKKSPDE 75
Cdd:COG3568    8 LRVMTYNIrYGLgtdgRADLERIARVIRALDPDVVALQE------------------------------NAILSRYPIVS 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490821596  76 INKGLPGDDSDEQARFIEGIYSTDTGVVRVVSLYLpngnpiDTEKFPYKLSWMQRLENWAKKRLTlEEPLVLAGDYNVI 154
Cdd:COG3568   58 SGTFDLPDPGGEPRGALWADVDVPGKPLRVVNTHL------DLRSAAARRRQARALAELLAELPA-GAPVILAGDFNDI 129
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 2-258 6.40e-06

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: 46.24  E-value: 6.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   2 KIATWNI---NGVKARIDNLQ--HWLRESSPDIVCLQEIKsvDEQFPRLEIEALgyhVETHGQKG--FNGV--------- 65
Cdd:cd10283    2 RIASWNIlnfGNSKGKEKNPAiaEIISAFDLDLIALQEVM--DNGGGLDALAKL---VNELNKPGgtWKYIvsdktggss 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596  66 ------ALLSKKSPDEINKG--LPGDDSDEQ-------ARFIEGIYSTDTGVVrVVSLYLPNGNPIDTEKFPYKLSwmQR 130
Cdd:cd10283   77 gdkeryAFLYKSSKVRKVGKavLEKDSNTDGfarppyaAKFKSGGTGFDFTLV-NVHLKSGGSSKSGQGAKRVAEA--QA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 131 LENWAKKRLTL--EEPLVLAGDYNVipepvdarnpqawlgdalfqPQSRQAFRRLENLGFTDAIRASTDESgvYSFWDYQ 208
Cdd:cd10283  154 LAEYLKELADEdpDDDVILLGDFNI--------------------PADEDAFKALTKAGFKSLLPDSTNLS--TSFKGYA 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490821596 209 AgawqknngiRIDHLMLSPEATNRFISANI-EKHVRAWEKP-------------SDHVPVTVTL 258
Cdd:cd10283  212 N---------SYDNIFVSGNLKEKFSNSGVfDFNILVDEAGeedldyskwrkqiSDHDPVWVEF 266
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 1-74 3.46e-04

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: 40.79  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596   1 MKIATWNING-----VKARIDNLQHWLRESSPDIVCLQEI-----KSVDEQFPRLEIEALGYHVETHGQKGFnGVALLSK 70
Cdd:cd09080    1 LKVLTWNVDFlddvnLAERMRAILKLLEELDPDVIFLQEVtppflAYLLSQPWVRKNYYFSEGPPSPAVDPY-GVLILSK 79


                 ....
gi 490821596  71 KSPD 74
Cdd:cd09080   80 KSLV 83
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 144-258 1.29e-03

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: 39.12  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821596 144 PLVLAGDYNVIPEPvdarnpqawlgdalfqpqsrQAFRRLENLGFTDAIRAS--TDESGVYSFWDYQAgawqKNNGIRID 221
Cdd:cd09083  162 PVILTGDFNAEPDS--------------------EPYKTLTSGGLKDARDTAatTDGGPEGTFHGFKG----PPGGSRID 217

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490821596 222 HLMLSPEATnrFISANIEKHVRAWEKPSDHVPVTVTL 258
Cdd:cd09083  218 YIFVSPGVK--VLSYEILTDRYDGRYPSDHFPVVADL 252
 
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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