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Conserved domains on  [gi|2033823601|dbj|GIR64457|]
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MAG: exodeoxyribonuclease III [Ectothiorhodospiraceae bacterium]

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 ...
 1-259 1.94e-120

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: 343.73  E-value: 1.94e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKTYNGVAILSKGKCLDVELN- 79
Cdd:cd09086     1 MKIATWNVNSIRARLEQVLDWLKEEDPDVLCLQETKVEDDQFPADAFEALGYHVAVHGQKAYNGVAILSRLPLEDVRTGf 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFDIE 159
Cdd:cd09086    81 PGDPDDDQARLIAARVGGVRVINLYVPNGGDIGSPKFAYKLDWLDRLIRYLQKLLKPDDPLVLVGDFNIAPEDIDVWDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 160 STKDQILCSVDERKSFNNLLKLGLYDLFEKFDFSPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTIDKETRH 239
Cdd:cd09086   161 QLLGKVLFTPEEREALRALLDLGFVDAFRALHPDEKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGIDREPRG 240

                         250       260
                  ....*....|....*....|
gi 2033823601 240 KswckkePRTSDHAPVRVEL 259
Cdd:cd09086   241 W------EKPSDHAPVVAEL 254
 
Name Accession Description Interval E-value
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
 1-259 1.94e-120

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: 343.73  E-value: 1.94e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKTYNGVAILSKGKCLDVELN- 79
Cdd:cd09086     1 MKIATWNVNSIRARLEQVLDWLKEEDPDVLCLQETKVEDDQFPADAFEALGYHVAVHGQKAYNGVAILSRLPLEDVRTGf 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFDIE 159
Cdd:cd09086    81 PGDPDDDQARLIAARVGGVRVINLYVPNGGDIGSPKFAYKLDWLDRLIRYLQKLLKPDDPLVLVGDFNIAPEDIDVWDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 160 STKDQILCSVDERKSFNNLLKLGLYDLFEKFDFSPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTIDKETRH 239
Cdd:cd09086   161 QLLGKVLFTPEEREALRALLDLGFVDAFRALHPDEKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGIDREPRG 240

                         250       260
                  ....*....|....*....|
gi 2033823601 240 KswckkePRTSDHAPVRVEL 259
Cdd:cd09086   241 W------EKPSDHAPVVAEL 254
XthA COG0708
Exonuclease III [Replication, recombination and repair];
1-259 5.68e-107

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 309.70  E-value: 5.68e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKTYNGVAILSKGKCLDVELN- 79
Cdd:COG0708     1 MKIASWNVNGIRARLPKLLDWLAEEDPDVLCLQETKAQDEQFPLEAFEAAGYHVYFHGQKGYNGVAILSRLPPEDVRRGl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFDIE 159
Cdd:COG0708    81 GGDEFDAEGRYIEADFGGVRVVSLYVPNGGSVGSEKFDYKLRFLDALRAYLAELLAPGRPLILCGDFNIAPTEIDVKNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 160 STKDQILCSVDERKSFNNLLKLGLYDLFEKFDF-SPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTIDKETR 238
Cdd:COG0708   161 ANLKNAGFLPEERAWFDRLLELGLVDAFRALHPdVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDREPR 240

                         250       260
                  ....*....|....*....|.
gi 2033823601 239 hkswckKEPRTSDHAPVRVEL 259
Cdd:COG0708   241 ------GDERPSDHAPVVVEL 255
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 1-259 1.41e-78

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: 237.56  E-value: 1.41e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPNV-LQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKT-YNGVAILSKGKCLDVEL 78
Cdd:TIGR00633   1 MKIISWNVNGLRARLHKLfLDWLKEEQPDVLCLQETKVADEQFPAELFEELGYHVFFHGAKKgYSGVAILSKVEPLDVRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  79 N-PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFD 157
Cdd:TIGR00633  81 GfGGEPHDEEGRVITAEFDGFTVVNVYVPNGGSRDLERLEYKLQFWDALFQYLEKELDAGKPVVICGDMNVAHTEIDLGN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 158 IESTKDQILCSVDERKSFNNLLKLGLYDLFEKfdFSPQT---FTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTID 234
Cdd:TIGR00633 161 PKENKGNAGFTPEEREWFDELLEAGFVDTFRH--FNPDTgdaYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYID 238

                         250       260
                  ....*....|....*....|....*
gi 2033823601 235 ketrhkswckKEPRTSDHAPVRVEL 259
Cdd:TIGR00633 239 ----------SEIRGSDHCPIVLEL 253
PRK11756 PRK11756
exonuclease III; Provisional
 1-261 1.61e-54

exonuclease III; Provisional


Pssm-ID: 236970 [Multi-domain]  Cd Length: 268  Bit Score: 176.62  E-value: 1.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRlPNVLQYLAE-YEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKTYNGVAILSKgkcldveLN 79
Cdd:PRK11756    1 MKFVSFNINGLRAR-PHQLEAIIEkHQPDVIGLQETKVHDEMFPLEEVEALGYHVFYHGQKGHYGVALLSK-------QT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 PVAI--------DEAEVRTISCTYN----NLRVLNVYVVNGKSVG-SDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDF 146
Cdd:PRK11756   73 PIAVrkgfptddEEAQRRIIMATIPtpngNLTVINGYFPQGESRDhPTKFPAKRQFYQDLQNYLETELSPDNPLLIMGDM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 147 NIAPTDNDVFDIESTKDQIL----CSV--DERKSFNNLLKLGLYDLFEKFDfsPQT---FTWWDYRAGAFHRNIGYRIDH 217
Cdd:PRK11756  153 NISPTDLDIGIGEENRKRWLrtgkCSFlpEEREWLDRLMDWGLVDTFRQLN--PDVndrFSWFDYRSKGFDDNRGLRIDL 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2033823601 218 ILGSKSVLDGCKSFTIDKETRhkswckKEPRTSDHAPVRVELSL 261
Cdd:PRK11756  231 ILATQPLAERCVETGIDYDIR------GMEKPSDHAPIWATFKL 268
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 5-148 5.88e-15

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 71.10  E-value: 5.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   5 TWNVNSI-------KVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYC---GQKTYNGVAILSKGKCL 74
Cdd:pfam03372   2 TWNVNGGnadaagdDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGgpgGGGGGGGVAILSRYPLS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2033823601  75 DVELNPVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNI 148
Cdd:pfam03372  82 SVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
 
Name Accession Description Interval E-value
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
 1-259 1.94e-120

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: 343.73  E-value: 1.94e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKTYNGVAILSKGKCLDVELN- 79
Cdd:cd09086     1 MKIATWNVNSIRARLEQVLDWLKEEDPDVLCLQETKVEDDQFPADAFEALGYHVAVHGQKAYNGVAILSRLPLEDVRTGf 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFDIE 159
Cdd:cd09086    81 PGDPDDDQARLIAARVGGVRVINLYVPNGGDIGSPKFAYKLDWLDRLIRYLQKLLKPDDPLVLVGDFNIAPEDIDVWDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 160 STKDQILCSVDERKSFNNLLKLGLYDLFEKFDFSPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTIDKETRH 239
Cdd:cd09086   161 QLLGKVLFTPEEREALRALLDLGFVDAFRALHPDEKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGIDREPRG 240

                         250       260
                  ....*....|....*....|
gi 2033823601 240 KswckkePRTSDHAPVRVEL 259
Cdd:cd09086   241 W------EKPSDHAPVVAEL 254
XthA COG0708
Exonuclease III [Replication, recombination and repair];
1-259 5.68e-107

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 309.70  E-value: 5.68e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKTYNGVAILSKGKCLDVELN- 79
Cdd:COG0708     1 MKIASWNVNGIRARLPKLLDWLAEEDPDVLCLQETKAQDEQFPLEAFEAAGYHVYFHGQKGYNGVAILSRLPPEDVRRGl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFDIE 159
Cdd:COG0708    81 GGDEFDAEGRYIEADFGGVRVVSLYVPNGGSVGSEKFDYKLRFLDALRAYLAELLAPGRPLILCGDFNIAPTEIDVKNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 160 STKDQILCSVDERKSFNNLLKLGLYDLFEKFDF-SPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTIDKETR 238
Cdd:COG0708   161 ANLKNAGFLPEERAWFDRLLELGLVDAFRALHPdVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDREPR 240

                         250       260
                  ....*....|....*....|.
gi 2033823601 239 hkswckKEPRTSDHAPVRVEL 259
Cdd:COG0708   241 ------GDERPSDHAPVVVEL 255
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 1-259 1.41e-78

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: 237.56  E-value: 1.41e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPNV-LQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKT-YNGVAILSKGKCLDVEL 78
Cdd:TIGR00633   1 MKIISWNVNGLRARLHKLfLDWLKEEQPDVLCLQETKVADEQFPAELFEELGYHVFFHGAKKgYSGVAILSKVEPLDVRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  79 N-PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFD 157
Cdd:TIGR00633  81 GfGGEPHDEEGRVITAEFDGFTVVNVYVPNGGSRDLERLEYKLQFWDALFQYLEKELDAGKPVVICGDMNVAHTEIDLGN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 158 IESTKDQILCSVDERKSFNNLLKLGLYDLFEKfdFSPQT---FTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTID 234
Cdd:TIGR00633 161 PKENKGNAGFTPEEREWFDELLEAGFVDTFRH--FNPDTgdaYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYID 238

                         250       260
                  ....*....|....*....|....*
gi 2033823601 235 ketrhkswckKEPRTSDHAPVRVEL 259
Cdd:TIGR00633 239 ----------SEIRGSDHCPIVLEL 253
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
 1-259 6.14e-77

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: 233.43  E-value: 6.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKTYNGVAILSKGKCLDVELN- 79
Cdd:TIGR00195   1 MKIISWNVNGLRARPHKGLAWLKENQPDVLCLQETKVQDEQFPLEPFHKEGYHVFFSGQKGYSGVAIFSKEEPISVRRGf 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFDIE 159
Cdd:TIGR00195  81 GVEEEDAEGRIIMAEFDSFLVINGYFPNGSRDDSEKLPYKLQWLEALQNYLEKLVDKDKPVLICGDMNIAPTEIDLHIPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 160 STKDQILCSVDERKSFNNLLKLGLYDLFEKFDFSPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTIDKETRh 239
Cdd:TIGR00195 161 ENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNPDEGAYSWWDYRTKARDRNRGWRIDYFLVSEPLKERCVDCGIDYDIR- 239

                         250       260
                  ....*....|....*....|
gi 2033823601 240 kSWCKkeprTSDHAPVRVEL 259
Cdd:TIGR00195 240 -GSEK----PSDHCPVVLEF 254
ExoIII_AP-endo cd09073
Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ...
 3-259 7.66e-77

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: 233.33  E-value: 7.66e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   3 ISTWNVNSIKVRLPN-VLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQ--KTYNGVAILSKGKCLDVELN 79
Cdd:cd09073     2 IISWNVNGLRARLKKgVLKWLKEEKPDILCLQETKADEDKLPEELQHVEGYHSYWSPArkKGYSGVATLSKEEPLDVSYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 -PVAIDEAEVRTISCTYNNLRVLNVYVVNGKSvGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFDI 158
Cdd:cd09073    82 iGGEEFDSEGRVITAEFDDFYLINVYFPNGGR-GLERLDYKLRFYEAFLEFLEKLRKRGKPVVICGDFNVAHEEIDLARP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 159 ESTKDQILCSVDERKSFNNLLKLGLYDLFEKFDFSPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSftidketr 238
Cdd:cd09073   161 KKNEKNAGFTPEERAWFDKLLSLGYVDTFRHFHPEPGAYTWWSYRGNARERNVGWRIDYFLVSEELAEKVKD-------- 232

                         250       260
                  ....*....|....*....|.
gi 2033823601 239 hkSWCKKEPRTSDHAPVRVEL 259
Cdd:cd09073   233 --SGILSKVKGSDHAPVTLEL 251
PRK11756 PRK11756
exonuclease III; Provisional
 1-261 1.61e-54

exonuclease III; Provisional


Pssm-ID: 236970 [Multi-domain]  Cd Length: 268  Bit Score: 176.62  E-value: 1.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRlPNVLQYLAE-YEPDILVLQETKSIDLNFPEDEIQSCGYNSYYCGQKTYNGVAILSKgkcldveLN 79
Cdd:PRK11756    1 MKFVSFNINGLRAR-PHQLEAIIEkHQPDVIGLQETKVHDEMFPLEEVEALGYHVFYHGQKGHYGVALLSK-------QT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  80 PVAI--------DEAEVRTISCTYN----NLRVLNVYVVNGKSVG-SDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDF 146
Cdd:PRK11756   73 PIAVrkgfptddEEAQRRIIMATIPtpngNLTVINGYFPQGESRDhPTKFPAKRQFYQDLQNYLETELSPDNPLLIMGDM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 147 NIAPTDNDVFDIESTKDQIL----CSV--DERKSFNNLLKLGLYDLFEKFDfsPQT---FTWWDYRAGAFHRNIGYRIDH 217
Cdd:PRK11756  153 NISPTDLDIGIGEENRKRWLrtgkCSFlpEEREWLDRLMDWGLVDTFRQLN--PDVndrFSWFDYRSKGFDDNRGLRIDL 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2033823601 218 ILGSKSVLDGCKSFTIDKETRhkswckKEPRTSDHAPVRVELSL 261
Cdd:PRK11756  231 ILATQPLAERCVETGIDYDIR------GMEKPSDHAPIWATFKL 268
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 1-259 9.71e-48

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: 158.87  E-value: 9.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPN-VLQYLAEYEPDILVLQETKsIDLNFPEDEIQS--CGYNSY--YCGQKTYNGVAILSKGKCLD 75
Cdd:cd09087     1 LKIISWNVNGLRALLKKgLLDYVKKEDPDILCLQETK-LQEGDVPKELKEllKGYHQYwnAAEKKGYSGTAILSKKKPLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  76 VELN-PVAIDEAEVRTISCTYNNLRVLNVYVVN-GKSVGSDKYqhKLKWLKKLNNYCKSsLTEFKNFVVLGDFNIAPTDN 153
Cdd:cd09087    80 VTYGiGIEEHDQEGRVITAEFENFYLVNTYVPNsGRGLERLDR--RKEWDVDFRAYLKK-LDSKKPVIWCGDLNVAHEEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 154 DVFDIESTKDQILCSVDERKSFNNLLKLGLYDLFEKF--DFSPQtFTWWDYRAGAFHRNIGYRIDHILGSKSVLDG-CKS 230
Cdd:cd09087   157 DLANPKTNKKSAGFTPEERESFTELLEAGFVDTFRHLhpDKEGA-YTFWSYRGNARAKNVGWRLDYFLVSERLKDRvVDS 235

                         250       260
                  ....*....|....*....|....*....
gi 2033823601 231 FTIDKETRhkswckkeprtSDHAPVRVEL 259
Cdd:cd09087   236 FIRSDIMG-----------SDHCPIGLEL 253
Mth212-like_AP-endo cd09085
Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic ...
 2-259 4.37e-44

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: 149.35  E-value: 4.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   2 IIStWNVNSIK-VRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYY--CGQKTYNGVAILSKGKCLDVEL 78
Cdd:cd09085     3 IIS-WNVNGLRaVHKKGFLDWFKEEKPDILCLQETKAQPEQLPEDLRNIEGYHSYFnsAERKGYSGVALYSKIEPDSVRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  79 N-PVAIDEAEVRTISCTYNNLRVLNVYVVNGKsVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFD 157
Cdd:cd09085    82 GlGVEEFDNEGRILIADFDDFTLFNIYFPNGQ-MSEERLDYKLEFYDAFLEYLNELRDSGKNVIICGDFNTAHKEIDLAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 158 IESTKDQILCSVDERKSFNNLLKLGLYDLFEKFDFSPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKsftidket 237
Cdd:cd09085   161 PKENEKVSGFLPEERAWMDKFIENGYVDTFRMFNKEPGQYTWWSYRTRARERNVGWRIDYFFVNEEFKPKVK-------- 232

                         250       260
                  ....*....|....*....|..
gi 2033823601 238 rhKSWCKKEPRTSDHAPVRVEL 259
Cdd:cd09085   233 --DAGILPDVMGSDHCPVSLEL 252
Nape_like_AP-endo cd10281
Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) ...
 1-258 4.77e-40

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: 138.90  E-value: 4.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPN-VLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYY--CGQKTYNGVAILSKGKCLDV- 76
Cdd:cd10281     1 MRVISVNVNGIRAAAKKgFLEWLAAQDADVVCLQEVRAQEEQLDDDFFEPEGYNAYFfdAEKKGYAGVAIYSRTQPKAVi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  77 -ELNPVAIDeAEVRTISCTYNNLRVLNVYVVNGkSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDV 155
Cdd:cd10281    81 yGLGFEEFD-DEGRYIEADFDNVSVASLYVPSG-SSGDERQEAKMAFLDAFLEHLKELRRKRREFIVCGDFNIAHTEIDI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 156 FDIESTKDQILCSVDERKSFNNLL-KLGLYDLFEKFDFSPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTID 234
Cdd:cd10281   159 KNWKANQKNSGFLPEERAWLDQVFgELGYVDAFRELNPDEGQYTWWSNRGQARANNVGWRIDYQIATPGLASKVVSAWIY 238

                         250       260
                  ....*....|....*....|....
gi 2033823601 235 KETRHkswckkeprtSDHAPVRVE 258
Cdd:cd10281   239 REERF----------SDHAPLIVD 252
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
 1-259 4.06e-21

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 88.98  E-value: 4.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   1 MIISTWNVNSIKVRLPN-VLQYLAEYEPDILVLQETKsidLNFPEDEIQSCGYNSYY-CG-QKTYNGVAILSKGKCLDVE 77
Cdd:PRK13911    1 MKLISWNVNGLRACMTKgFMDFFNSVDADVFCIQESK---MQQEQNTFEFKGYFDFWnCAiKKGYSGVVTFTKKEPLSVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  78 LNpVAIDE--AEVRTISCTYNNLRVLNVYVVNGKSVGSdKYQHKLKWLKKLNNYCKSsLTEFKNFVVLGDFNIAPTDNDV 155
Cdd:PRK13911   78 YG-INIEEhdKEGRVITCEFESFYLVNVYTPNSQQALS-RLSYRMSWEVEFKKFLKA-LELKKPVIVCGDLNVAHNEIDL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 156 FDIESTKDQILCSVDERKSFNNLLKLGLYDLFEKF-DFSPQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTID 234
Cdd:PRK13911  155 ENPKTNRKNAGFSDEERGKFSELLNAGFIDTFRYFyPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIY 234

                         250       260
                  ....*....|....*....|....*
gi 2033823601 235 KETrhkswckkepRTSDHAPVRVEL 259
Cdd:PRK13911  235 KDI----------LGSDHCPVGLEL 249
Ape2-like_AP-endo cd09088
Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This ...
 3-259 1.00e-20

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: 88.91  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   3 ISTWNVNSIKVRL--------PNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYC---GQKTYNGVAILSKG 71
Cdd:cd09088     2 IVTWNVNGIRTRLqyqpwnkeNSLKSFLDSLDADIICLQETKLTRDELDEPSAIVEGYDSFFSfsrGRKGYSGVATYCRD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  72 KC-------------------------------------LDVELNPVAIDeAEVRTISCTYNNLRVLNVYVVNGKSVGSD 114
Cdd:cd09088    82 SAatpvaaeegltgvlsspnqknelsenddigcygemleFTDSKELLELD-SEGRCVLTDHGTFVLINVYCPRADPEKEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 115 KYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNIAPTDNDVFDIESTKDQILCSVDE---RKSFNNLL---------KLG 182
Cdd:cd09088   161 RLEFKLDFYRLLEERVEALLKAGRRVILVGDVNVSHRPIDHCDPDDSEDFGGESFEDnpsRQWLDQLLgdsgegggsPGG 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033823601 183 -LYDLFEKFDFS-PQTFTWWDYRAGAFHRNIGYRIDHILGSKSVLDGCKSFTIDKEtrHKSwckkeprtSDHAPVRVEL 259
Cdd:cd09088   241 lLIDSFRYFHPTrKGAYTCWNTLTGARPTNYGTRIDYILADRGLLPWVKAADILPE--VEG--------SDHCPVYADL 309
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 3-259 2.44e-15

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


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 73.28  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   3 ISTWNVNSIK--VRLPNVLQYLAEYEPDILVLQETKS-----IDLNFPEDEiqscGYNSYYCG---QKTYNGVAILSKGK 72
Cdd:cd08372     1 VASYNVNGLNaaTRASGIARWVRELDPDIVCLQEVKDsqysaVALNQLLPE----GYHQYQSGpsrKEGYEGVAILSKTP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  73 CLDVELNPVAIDEAEVRT--------ISCTYNNLRVLNVYVVNGKSVGSDKyqhkLKWLKKLNNYCKSSLTEFKNFVVL- 143
Cdd:cd08372    77 KFKIVEKHQYKFGEGDSGerravvvkFDVHDKELCVVNAHLQAGGTRADVR----DAQLKEVLEFLKRLRQPNSAPVVIc 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 144 GDFNIAPtdndvFDIESTKDQilcSVDERKSFNNLLklglyDLFEKFDFSPqtfTWWdyragAFHRNIGYRIDHILGSKS 223
Cdd:cd08372   153 GDFNVRP-----SEVDSENPS---SMLRLFVALNLV-----DSFETLPHAY---TFD-----TYMHNVKSRLDYIFVSKS 211

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2033823601 224 VLDGCKSFTIDKETRhkswckKEPRTSDHAPVRVEL 259
Cdd:cd08372   212 LLPSVKSSKILSDAA------RARIPSDHYPIEVTL 241
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 5-148 5.88e-15

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 71.10  E-value: 5.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   5 TWNVNSI-------KVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYC---GQKTYNGVAILSKGKCL 74
Cdd:pfam03372   2 TWNVNGGnadaagdDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGgpgGGGGGGGVAILSRYPLS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2033823601  75 DVELNPVAIDEAEVRTISCTYNNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEFKNFVVLGDFNI 148
Cdd:pfam03372  82 SVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
 3-259 8.15e-14

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: 68.92  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   3 ISTWNVNSI--KVRLPNVLQYLAEYEPDILVLQETKS------IDLNFPEDEIQSCGynsyycGQKTYNGVAILskgkcL 74
Cdd:cd09076     1 IGTLNVRGLrsPGKRAQLLEELKRKKLDILGLQETHWtgegelKKKREGGTILYSGS------DSGKSRGVAIL-----L 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  75 DVELNPVAID---EAEVRTISCT----YNNLRVLNVYVVNGKSVgsdkyQHKLKWLKKLNNYCKSSLTEfKNFVVLGDFN 147
Cdd:cd09076    70 SKTAANKLLEytkVVSGRIIMVRfkikGKRLTIINVYAPTARDE-----EEKEEFYDQLQDVLDKVPRH-DTLIIGGDFN 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 148 iAPTDNDvfDIESTKDQILCSVDERKSFNNLLKLGLYDLFEKFDFSPQTFTWwdYRAGAFHRNigyRIDHILGSKSVLDG 227
Cdd:cd09076   144 -AVLGPK--DDGRKGLDKRNENGERALSALIEEHDLVDVWRENNPKTREYTW--RSPDHGSRS---RIDRILVSKRLRVK 215

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2033823601 228 CKSFTIDKETrhkswckkeprTSDHAPVRVEL 259
Cdd:cd09076   216 VKKTKITPGA-----------GSDHRLVTLKL 236
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
139-261 9.56e-07

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 49.25  E-value: 9.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 139 NFVVLGDFNiAPTDNDvfdiestkdqilcsvderkSFNNLLK-LGLYDLFEKFdFSPQTFTWwdyragAFHRNIGYrIDH 217
Cdd:COG2374   255 PVIVLGDFN-DYPFED-------------------PLRALLGaGGLTNLAEKL-PAAERYSY------VYDGNSGL-LDH 306

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2033823601 218 ILGSKSVLDGCKSFTI----------DKETRHKSWCKKEPRTSDHAPVRVELSL 261
Cdd:COG2374   307 ILVSPALAARVTGADIwhinadiyndDFKPDFRTYADDPGRASDHDPVVVGLRL 360
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 3-158 3.58e-06

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: 46.95  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   3 ISTWNVNS-----IKVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCgyNSYYC------GQKTYNGVAILSKg 71
Cdd:cd09080     3 VLTWNVDFlddvnLAERMRAILKLLEELDPDVIFLQEVTPPFLAYLLSQPWVR--KNYYFsegppsPAVDPYGVLILSK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  72 KCLDVELNPVA-------IDEAEVRTISCTynNLRVLNVYVvngKSvGSDKYQHKLKWLKKLNNYCKSSLTeFKNFVVLG 144
Cdd:cd09080    80 KSLVVRRVPFTstrmgrnLLAAEINLGSGE--PLRLATTHL---ES-LKSHSSERTAQLEEIAKKLKKPPG-AANVILGG 152

                         170       180
                  ....*....|....*....|.
gi 2033823601 145 DFN-------IAPTDNDVFDI 158
Cdd:cd09080   153 DFNlrdkeddTGGLPNGFVDA 173
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 141-259 7.86e-06

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: 46.06  E-value: 7.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 141 VVLGDFNiAPTDNDVFDIestkdqilcsvderksfnnLLKLGLYDLFEKFDFSPQ----TFTWWDYRAGafhrniGYRID 216
Cdd:cd09083   164 ILTGDFN-AEPDSEPYKT-------------------LTSGGLKDARDTAATTDGgpegTFHGFKGPPG------GSRID 217

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2033823601 217 HILGSKSVldGCKSFTIDKETRHKSWCkkeprtSDHAPVRVEL 259
Cdd:cd09083   218 YIFVSPGV--KVLSYEILTDRYDGRYP------SDHFPVVADL 252
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 96-259 2.62e-05

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: 44.31  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  96 NNLRVLNVYVVNGKSVGSDKYQHKLKWLKKLNNYCKSSLTEF--KNFVVLGDFNIaPTDNDVfdiestkdqilcsvderk 173
Cdd:cd10283   124 FDFTLVNVHLKSGGSSKSGQGAKRVAEAQALAEYLKELADEDpdDDVILLGDFNI-PADEDA------------------ 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 174 sFNNLLKLGLYDLFEKFDFSPQTFtwwDYRAGAFhrnigyriDHIL----------GSKSVLDGCKSFTIDKETRHKSWC 243
Cdd:cd10283   185 -FKALTKAGFKSLLPDSTNLSTSF---KGYANSY--------DNIFvsgnlkekfsNSGVFDFNILVDEAGEEDLDYSKW 252

                         170
                  ....*....|....*.
gi 2033823601 244 KKepRTSDHAPVRVEL 259
Cdd:cd10283   253 RK--QISDHDPVWVEF 266
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 3-168 1.03e-04

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 41.82  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   3 ISTWNV-----NSIKVRLPNVLQYLAEYEPDILVLQEtksidlnfpedeiqscgynsyycgqktyngVAILSKGKCLDVE 77
Cdd:COG3568    10 VMTYNIryglgTDGRADLERIARVIRALDPDVVALQE------------------------------NAILSRYPIVSSG 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  78 LNPVAIDEAEVRTisCTYNNLRV----LNVYVVNGKSVGSdkyQHKLKWLKKLNNYCKSSLTEfKNFVVLGDFNiaptdn 153
Cdd:COG3568    60 TFDLPDPGGEPRG--ALWADVDVpgkpLRVVNTHLDLRSA---AARRRQARALAELLAELPAG-APVILAGDFN------ 127

                         170
                  ....*....|....*
gi 2033823601 154 dvfDIestkDQILCS 168
Cdd:COG3568   128 ---DI----DYILVS 135
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 3-259 2.51e-03

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: 38.43  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601   3 ISTWNVNS-----IKVRLPNVLQYLAEYEPDILVLQETKSIDLNFPEDEIQSCGYNSYYC----GQKTYNGVAILSKGKC 73
Cdd:cd09084     1 VMSYNVRSfnrykWKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYvvykSDSGGTGLAIFSKYPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601  74 LDVEL------NPVAIdEAEV----RTIScTYNNLrvLNVYVVNGKSVGSDKYQHKLKWLKKL------NNYCK-----S 132
Cdd:cd09084    81 LNSGSidfpntNNNAI-FADIrvggDTIR-VYNVH--LESFRITPSDKELYKEEKKAKELSRNllrklaEAFKRraaqaD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033823601 133 SLTEFKN-----FVVLGDFNIAPTdndvfdiestkdqilcSVDERKsfnnlLKLGLYDLFEKFDFSPQtFTWWDYRagaf 207
Cdd:cd09084   157 LLAADIAaspypVIVCGDFNDTPA----------------SYVYRT-----LKKGLTDAFVEAGSGFG-YTFNGLF---- 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2033823601 208 hrnIGYRIDHILGSKSVldGCKSFTIDKEtrhkswckkepRTSDHAPVRVEL 259
Cdd:cd09084   211 ---FPLRIDYILTSKGF--KVLRYRVDPG-----------KYSDHYPIVATL 246
 
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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