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Conserved domains on  [gi|291561139|emb|CBL39938|]
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exodeoxyribonuclease III [butyrate-producing bacterium SS3/4]

Protein Classification

exodeoxyribonuclease III( domain architecture ID 10173395)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
36-283 1.38e-176

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: 487.06  E-value: 1.38e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQVDLE----LPGYHQYWNYAEKKGYSGTAMFTKEEPIAVT 111
Cdd:cd09087    2 KIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 112 YGLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNP 191
Cdd:cd09087   82 YGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLANP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 192 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 271
Cdd:cd09087  162 KTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSDI 241
                        250
                 ....*....|..
gi 291561139 272 MGSDHCPVELDI 283
Cdd:cd09087  242 MGSDHCPIGLEL 253
 
Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
36-283 1.38e-176

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: 487.06  E-value: 1.38e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQVDLE----LPGYHQYWNYAEKKGYSGTAMFTKEEPIAVT 111
Cdd:cd09087    2 KIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 112 YGLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNP 191
Cdd:cd09087   82 YGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLANP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 192 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 271
Cdd:cd09087  162 KTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSDI 241
                        250
                 ....*....|..
gi 291561139 272 MGSDHCPVELDI 283
Cdd:cd09087  242 MGSDHCPIGLEL 253
XthA COG0708
Exonuclease III [Replication, recombination and repair];
36-283 8.37e-142

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 399.07  E-value: 8.37e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKgFLEYLKESDADIFCIQESKLQEGQVDLEL---PGYHQYWNYaeKKGYSGTAMFTKEEPIAVTY 112
Cdd:COG0708    2 KIASWNVNGIRARLPK-LLDWLAEEDPDVLCLQETKAQDEQFPLEAfeaAGYHVYFHG--QKGYNGVAILSRLPPEDVRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQD-GLKRLDYRMQWEDAFRAYLKEL-ETKKPVIFCGDLNVAHQEIDLKN 190
Cdd:COG0708   79 GLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSvGSEKFDYKLRFLDALRAYLAELlAPGRPLILCGDFNIAPTEIDVKN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 191 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 270
Cdd:COG0708  159 PKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDRE 238
                        250
                 ....*....|....*..
gi 291561139 271 ----VMGSDHCPVELDI 283
Cdd:COG0708  239 prgdERPSDHAPVVVEL 255
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
36-283 1.43e-137

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: 388.18  E-value: 1.43e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139   36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQ---VDLELPGYHQYWNYAeKKGYSGTAMFTKEEPIAVTY 112
Cdd:TIGR00633   2 KIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQfpaELFEELGYHVFFHGA-KKGYSGVAILSKVEPLDVRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQ-DGLKRLDYRMQ-WEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKN 190
Cdd:TIGR00633  81 GFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGsRDLERLEYKLQfWDALFQYLEKELDAGKPVVICGDMNVAHTEIDLGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  191 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 270
Cdd:TIGR00633 161 PKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYIDSE 240
                         250
                  ....*....|...
gi 291561139  271 VMGSDHCPVELDI 283
Cdd:TIGR00633 241 IRGSDHCPIVLEL 253
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
36-283 4.69e-124

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 354.00  E-value: 4.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQVDLELPGYHQYWNYAEKKGYSGTAMFTKEEPIAVTYGLG 115
Cdd:PRK13911   2 KLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQNTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSYGIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 116 IEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNPKTNR 195
Cdd:PRK13911  82 IEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENPKTNR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 196 KNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEVMGSD 275
Cdd:PRK13911 162 KNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDILGSD 241

                 ....*...
gi 291561139 276 HCPVELDI 283
Cdd:PRK13911 242 HCPVGLEL 249
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
38-181 3.40e-19

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: 83.04  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139   38 ISWNVNGLRA------CLGKGFLEYLKESDADIFCIQESKLQEGQVD----LELPGYHQYWNYAEKKGYSGTAMFTKEEP 107
Cdd:pfam03372   1 LTWNVNGGNAdaagddRKLDALAALIRAYDPDVVALQETDDDDASRLllalLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291561139  108 IAVTYGLGIEEHDHEGRVITAEFPEYYVV-TCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNV 181
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVpLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
 
Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
36-283 1.38e-176

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: 487.06  E-value: 1.38e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQVDLE----LPGYHQYWNYAEKKGYSGTAMFTKEEPIAVT 111
Cdd:cd09087    2 KIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 112 YGLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNP 191
Cdd:cd09087   82 YGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLANP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 192 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 271
Cdd:cd09087  162 KTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSDI 241
                        250
                 ....*....|..
gi 291561139 272 MGSDHCPVELDI 283
Cdd:cd09087  242 MGSDHCPIGLEL 253
XthA COG0708
Exonuclease III [Replication, recombination and repair];
36-283 8.37e-142

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 399.07  E-value: 8.37e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKgFLEYLKESDADIFCIQESKLQEGQVDLEL---PGYHQYWNYaeKKGYSGTAMFTKEEPIAVTY 112
Cdd:COG0708    2 KIASWNVNGIRARLPK-LLDWLAEEDPDVLCLQETKAQDEQFPLEAfeaAGYHVYFHG--QKGYNGVAILSRLPPEDVRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQD-GLKRLDYRMQWEDAFRAYLKEL-ETKKPVIFCGDLNVAHQEIDLKN 190
Cdd:COG0708   79 GLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSvGSEKFDYKLRFLDALRAYLAELlAPGRPLILCGDFNIAPTEIDVKN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 191 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 270
Cdd:COG0708  159 PKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDRE 238
                        250
                 ....*....|....*..
gi 291561139 271 ----VMGSDHCPVELDI 283
Cdd:COG0708  239 prgdERPSDHAPVVVEL 255
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
36-283 1.43e-137

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: 388.18  E-value: 1.43e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139   36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQ---VDLELPGYHQYWNYAeKKGYSGTAMFTKEEPIAVTY 112
Cdd:TIGR00633   2 KIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQfpaELFEELGYHVFFHGA-KKGYSGVAILSKVEPLDVRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQ-DGLKRLDYRMQ-WEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKN 190
Cdd:TIGR00633  81 GFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGsRDLERLEYKLQfWDALFQYLEKELDAGKPVVICGDMNVAHTEIDLGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  191 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 270
Cdd:TIGR00633 161 PKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYIDSE 240
                         250
                  ....*....|...
gi 291561139  271 VMGSDHCPVELDI 283
Cdd:TIGR00633 241 IRGSDHCPIVLEL 253
Mth212-like_AP-endo cd09085
Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic ...
36-283 2.75e-134

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: 379.70  E-value: 2.75e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQVDLEL---PGYHQYWNYAEKKGYSGTAMFTKEEPIAVTY 112
Cdd:cd09085    2 KIISWNVNGLRAVHKKGFLDWFKEEKPDILCLQETKAQPEQLPEDLrniEGYHSYFNSAERKGYSGVALYSKIEPDSVRE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETK-KPVIFCGDLNVAHQEIDLKNP 191
Cdd:cd09085   82 GLGVEEFDNEGRILIADFDDFTLFNIYFPNGQMSEERLDYKLEFYDAFLEYLNELRDSgKNVIICGDFNTAHKEIDLARP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 192 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDqEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 271
Cdd:cd09085  162 KENEKVSGFLPEERAWMDKFIENGYVDTFRMFNKE-PGQYTWWSYRTRARERNVGWRIDYFFVNEEFKPKVKDAGILPDV 240
                        250
                 ....*....|..
gi 291561139 272 MGSDHCPVELDI 283
Cdd:cd09085  241 MGSDHCPVSLEL 252
ExoIII_AP-endo cd09073
Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ...
36-281 5.55e-134

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: 378.94  E-value: 5.55e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQVDLEL---PGYHQYWNYAEKKGYSGTAMFTKEEPIAVTY 112
Cdd:cd09073    1 KIISWNVNGLRARLKKGVLKWLKEEKPDILCLQETKADEDKLPEELqhvEGYHSYWSPARKKGYSGVATLSKEEPLDVSY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETK-KPVIFCGDLNVAHQEIDLKNP 191
Cdd:cd09073   81 GIGGEEFDSEGRVITAEFDDFYLINVYFPNGGRGLERLDYKLRFYEAFLEFLEKLRKRgKPVVICGDFNVAHEEIDLARP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 192 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDqEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 271
Cdd:cd09073  161 KKNEKNAGFTPEERAWFDKLLSLGYVDTFRHFHPE-PGAYTWWSYRGNARERNVGWRIDYFLVSEELAEKVKDSGILSKV 239
                        250
                 ....*....|
gi 291561139 272 MGSDHCPVEL 281
Cdd:cd09073  240 KGSDHAPVTL 249
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
36-283 4.69e-124

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 354.00  E-value: 4.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQVDLELPGYHQYWNYAEKKGYSGTAMFTKEEPIAVTYGLG 115
Cdd:PRK13911   2 KLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQNTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSYGIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 116 IEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNPKTNR 195
Cdd:PRK13911  82 IEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENPKTNR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 196 KNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEVMGSD 275
Cdd:PRK13911 162 KNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDILGSD 241

                 ....*...
gi 291561139 276 HCPVELDI 283
Cdd:PRK13911 242 HCPVGLEL 249
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
36-283 9.49e-124

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: 353.23  E-value: 9.49e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139   36 KMISWNVNGLRACLGKGfLEYLKESDADIFCIQESKLQEGQVDLELP---GYHQYWNYAekKGYSGTAMFTKEEPIAVTY 112
Cdd:TIGR00195   2 KIISWNVNGLRARPHKG-LAWLKENQPDVLCLQETKVQDEQFPLEPFhkeGYHVFFSGQ--KGYSGVAIFSKEEPISVRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPN-SQDGLKRLDYRMQWEDAFRAYLKELETK-KPVIFCGDLNVAHQEIDLKN 190
Cdd:TIGR00195  79 GFGVEEEDAEGRIIMAEFDSFLVINGYFPNgSRDDSEKLPYKLQWLEALQNYLEKLVDKdKPVLICGDMNIAPTEIDLHI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  191 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDqEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 270
Cdd:TIGR00195 159 PDENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNPD-EGAYSWWDYRTKARDRNRGWRIDYFLVSEPLKERCVDCGIDYD 237
                         250
                  ....*....|....*..
gi 291561139  271 VMG----SDHCPVELDI 283
Cdd:TIGR00195 238 IRGsekpSDHCPVVLEF 254
Nape_like_AP-endo cd10281
Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) ...
36-283 1.80e-105

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: 306.85  E-value: 1.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKGFLEYLKESDADIFCIQESKLQEGQVD---LELPGYHQYWNYAEKKGYSGTAMFTKEEPIAVTY 112
Cdd:cd10281    2 RVISVNVNGIRAAAKKGFLEWLAAQDADVVCLQEVRAQEEQLDddfFEPEGYNAYFFDAEKKGYAGVAIYSRTQPKAVIY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKP-VIFCGDLNVAHQEIDLKNP 191
Cdd:cd10281   82 GLGFEEFDDEGRYIEADFDNVSVASLYVPSGSSGDERQEAKMAFLDAFLEHLKELRRKRReFIVCGDFNIAHTEIDIKNW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 192 KTNRKNAGFSDEERAKFTELL-EAGFVDTFRYFYPDQeGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 270
Cdd:cd10281  162 KANQKNSGFLPEERAWLDQVFgELGYVDAFRELNPDE-GQYTWWSNRGQARANNVGWRIDYQIATPGLASKVVSAWIYRE 240
                        250
                 ....*....|...
gi 291561139 271 VMGSDHCPVELDI 283
Cdd:cd10281  241 ERFSDHAPLIVDY 253
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
36-279 1.85e-79

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: 240.88  E-value: 1.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKgFLEYLKESDADIFCIQESKLQEGQ---VDLELPGYHQYWNyaEKKGYSGTAMFTKEEPIAVTY 112
Cdd:cd09086    2 KIATWNVNSIRARLEQ-VLDWLKEEDPDVLCLQETKVEDDQfpaDAFEALGYHVAVH--GQKAYNGVAILSRLPLEDVRT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 113 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQD-GLKRLDYRMQWEDAFRAYL-KELETKKPVIFCGDLNVAHQEIDLKN 190
Cdd:cd09086   79 GFPGDPDDDQARLIAARVGGVRVINLYVPNGGDiGSPKFAYKLDWLDRLIRYLqKLLKPDDPLVLVGDFNIAPEDIDVWD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 191 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDqEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 270
Cdd:cd09086  159 PKQLLGKVLFTPEEREALRALLDLGFVDAFRALHPD-EKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGIDRE 237
                        250
                 ....*....|...
gi 291561139 271 VMG----SDHCPV 279
Cdd:cd09086  238 PRGwekpSDHAPV 250
Ape2-like_AP-endo cd09088
Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This ...
36-283 1.64e-55

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: 181.36  E-value: 1.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLG-------KGFLEYLKESDADIFCIQESKLQEGQVDLE---LPGYHQYWNY-AEKKGYSGTAMFTK 104
Cdd:cd09088    1 RIVTWNVNGIRTRLQyqpwnkeNSLKSFLDSLDADIICLQETKLTRDELDEPsaiVEGYDSFFSFsRGRKGYSGVATYCR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 105 ---EEPIAVTYGL-----------GIEEH---------------------DHEGRVITAEFPEYYVVTCYTP-NSQDGLK 148
Cdd:cd09088   81 dsaATPVAAEEGLtgvlsspnqknELSENddigcygemleftdskellelDSEGRCVLTDHGTFVLINVYCPrADPEKEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 149 RLDYRMqwedAFRAYLKE-----LETKKPVIFCGDLNVAHQEIDLKNPKTNRKNAGFSDEE---RAKFTELLEAG----- 215
Cdd:cd09088  161 RLEFKL----DFYRLLEErvealLKAGRRVILVGDVNVSHRPIDHCDPDDSEDFGGESFEDnpsRQWLDQLLGDSgeggg 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291561139 216 -----FVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEVMGSDHCPVELDI 283
Cdd:cd09088  237 spgglLIDSFRYFHPTRKGAYTCWNTLTGARPTNYGTRIDYILADRGLLPWVKAADILPEVEGSDHCPVYADL 309
PRK11756 PRK11756
exonuclease III; Provisional
36-283 5.86e-43

exonuclease III; Provisional


Pssm-ID: 236970 [Multi-domain]  Cd Length: 268  Bit Score: 147.73  E-value: 5.86e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKgfLEYLKES-DADIFCIQESKLQEGQVDLELP---GYHQYwnYAEKKGYSGTAMFTKEEPIAVT 111
Cdd:PRK11756   2 KFVSFNINGLRARPHQ--LEAIIEKhQPDVIGLQETKVHDEMFPLEEVealGYHVF--YHGQKGHYGVALLSKQTPIAVR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 112 YGLGIEEHDHEGRVITAEFP----EYYVVTCYTPN--SQDGLKRLDYRMQWEDAFRAYLKELETK-KPVIFCGDLNVAHQ 184
Cdd:PRK11756  78 KGFPTDDEEAQRRIIMATIPtpngNLTVINGYFPQgeSRDHPTKFPAKRQFYQDLQNYLETELSPdNPLLIMGDMNISPT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 185 EIDLKNPKTNRK------NAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESL 258
Cdd:PRK11756 158 DLDIGIGEENRKrwlrtgKCSFLPEEREWLDRLMDWGLVDTFRQLNPDVNDRFSWFDYRSKGFDDNRGLRIDLILATQPL 237
                        250       260       270
                 ....*....|....*....|....*....|.
gi 291561139 259 KDRLVDAKIHTEVMG----SDHCPV--ELDI 283
Cdd:PRK11756 238 AERCVETGIDYDIRGmekpSDHAPIwaTFKL 268
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
38-283 2.22e-36

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: 129.91  E-value: 2.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  38 ISWNVNGLRAC-LGKGFLEYLKESDADIFCIQESKL-QEGQVDLELPGYHQYWNYA----EKKGYSGTAMFTK---EEPI 108
Cdd:cd08372    2 ASYNVNGLNAAtRASGIARWVRELDPDIVCLQEVKDsQYSAVALNQLLPEGYHQYQsgpsRKEGYEGVAILSKtpkFKIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 109 AVTYGLGIEEHDHEGRVITAEF----PEYYVVTCYTPNsqdGLKRLDYRMQWEDAFRAYLKELETKK--PVIFCGDLNVA 182
Cdd:cd08372   82 EKHQYKFGEGDSGERRAVVVKFdvhdKELCVVNAHLQA---GGTRADVRDAQLKEVLEFLKRLRQPNsaPVVICGDFNVR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 183 HQEIDLKNPKtnrknagfsdEERAKFTELleaGFVDTfryfYPDQEGIYSWWSYRfsaraKNAGWRIDYFCVSESLKDRL 262
Cdd:cd08372  159 PSEVDSENPS----------SMLRLFVAL---NLVDS----FETLPHAYTFDTYM-----HNVKSRLDYIFVSKSLLPSV 216
                        250       260
                 ....*....|....*....|....*
gi 291561139 263 VDAKIHTEV----MGSDHCPVELDI 283
Cdd:cd08372  217 KSSKILSDAararIPSDHYPIEVTL 241
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
38-283 2.55e-26

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: 103.20  E-value: 2.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  38 ISWNVNGL-----RACLgkgfLEYLKESDADIFCIQESKL-QEGQVDLELPGYHQYWNYAEKKGYSGTA-MFTKE-EPIA 109
Cdd:cd09076    2 GTLNVRGLrspgkRAQL----LEELKRKKLDILGLQETHWtGEGELKKKREGGTILYSGSDSGKSRGVAiLLSKTaANKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 110 VTYglgieEHDHEGRVITAEF----PEYYVVTCYTPNSQDGlkrlDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQE 185
Cdd:cd09076   78 LEY-----TKVVSGRIIMVRFkikgKRLTIINVYAPTARDE----EEKEEFYDQLQDVLDKVPRHDTLIIGGDFNAVLGP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 186 IDLKNPKTNRKNagfSDEERAKFTELLEAGFVDTFRYFYPDQEGiYSWWSYRFSARAknagwRIDYFCVSESLKDRLVDA 265
Cdd:cd09076  149 KDDGRKGLDKRN---ENGERALSALIEEHDLVDVWRENNPKTRE-YTWRSPDHGSRS-----RIDRILVSKRLRVKVKKT 219
                        250
                 ....*....|....*...
gi 291561139 266 KIhTEVMGSDHCPVELDI 283
Cdd:cd09076  220 KI-TPGAGSDHRLVTLKL 236
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
38-181 3.40e-19

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: 83.04  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139   38 ISWNVNGLRA------CLGKGFLEYLKESDADIFCIQESKLQEGQVD----LELPGYHQYWNYAEKKGYSGTAMFTKEEP 107
Cdd:pfam03372   1 LTWNVNGGNAdaagddRKLDALAALIRAYDPDVVALQETDDDDASRLllalLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291561139  108 IAVTYGLGIEEHDHEGRVITAEFPEYYVV-TCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNV 181
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVpLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
37-283 2.26e-13

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: 68.09  E-value: 2.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  37 MISWNVNGLRAC----LGKGFLEYLKESDADIFCIQESKLQEGQ----VDLELPGY-HQYWNYAEKKGYSGTAMFTKeEP 107
Cdd:cd09084    1 VMSYNVRSFNRYkwkdDPDKILDFIKKQDPDILCLQEYYGSEGDkdddLRLLLKGYpYYYVVYKSDSGGTGLAIFSK-YP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 108 I----AVTYGLGIE-----EHDHEGRVIT-------------AEFPEYYVVTCYTPNSQDGLKRLDYRMQWE----DAFR 161
Cdd:cd09084   80 IlnsgSIDFPNTNNnaifaDIRVGGDTIRvynvhlesfritpSDKELYKEEKKAKELSRNLLRKLAEAFKRRaaqaDLLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 162 AYLKelETKKPVIFCGDLNvahqeidlknpktnrkNAGFSDEERakfteLLEAGFVDTFRyfypdqegiYSWWSYRFSAR 241
Cdd:cd09084  160 ADIA--ASPYPVIVCGDFN----------------DTPASYVYR-----TLKKGLTDAFV---------EAGSGFGYTFN 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 291561139 242 AKNAGWRIDYFCVSESLkdRLVDAKIHTEVMgSDHCPVELDI 283
Cdd:cd09084  208 GLFFPLRIDYILTSKGF--KVLRYRVDPGKY-SDHYPIVATL 246
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
36-279 1.14e-06

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 48.84  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  36 KMISWNVNGLRACLGKgFLEYLKESDADIFCIQE-SKLQEGQVDlELPGYHQYWNYAEKKGYSGTAMFTKEEPIAVTygl 114
Cdd:COG3021   96 RVLTANVLFGNADAEA-LAALVREEDPDVLVLQEtTPAWEEALA-ALEADYPYRVLCPLDNAYGMALLSRLPLTEAE--- 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 115 GIEEHDHEGRVITAEF------PEYYVVTCYTPnsqdglkrLDYRMQWEDAFRAYLKEL-ETKKPVIFCGDLN-VAHQei 186
Cdd:COG3021  171 VVYLVGDDIPSIRATVelpggpVRLVAVHPAPP--------VGGSAERDAELAALAKAVaALDGPVIVAGDFNaTPWS-- 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 187 dlknPKTNR--KNAGFSDEERAkftelleAGFVDTFRYFYPdqegiyswwsyrfsarakNAGWRIDYFCVSESLkdRLVD 264
Cdd:COG3021  241 ----PTLRRllRASGLRDARAG-------RGLGPTWPANLP------------------FLRLPIDHVLVSRGL--TVVD 289
                        250
                 ....*....|....*
gi 291561139 265 AKIHtEVMGSDHCPV 279
Cdd:COG3021  290 VRVL-PVIGSDHRPL 303
R1-I-EN cd09077
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ...
40-283 1.93e-05

Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat retrotransposons; This family contains the endonuclease (EN) domain of various non-long terminal repeat (non-LTR) retrotransposons, long interspersed nuclear elements (LINEs) which belong to the subtype 2, R1- and I-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. Most non-LTR retrotransposons are inserted throughout the host genome; however, many retrotransposons of the R1 clade exhibit target-specific retrotransposition. This family includes the endonucleases of SART1 and R1bm, from the silkworm Bombyx mori, which belong to the R1-clade. It also includes the endonuclease of snail (Biomphalaria glabrata) Nimbus/Bgl and mosquito Aedes aegypti (MosquI), both which belong to the I-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: 197311 [Multi-domain]  Cd Length: 205  Bit Score: 44.59  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139  40 WNVNGLRA--CLgkgFLEYLKESDADIFCIQEsklqegqvdlelpgyhQYWNYAEKKGY----SGTAMftkeepIAVTYG 113
Cdd:cd09077    6 INLNRCKAaqDL---LLQTAREEGADIALIQE----------------PYLVPVNNPNWvtdeSGRAA------IVVSDR 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 114 LG---IEEHDHEGRVITAEFPEYYVVTCYTPNSQDglkrldyrmqwEDAFRAYLKELETK-----KPVIFCGDLNVAHQE 185
Cdd:cd09077   61 LPrkpIQRLSLGLGIVAARVGGITVVSCYAPPSES-----------LEEFEEYLENLVRIvrglsRPVIIGGDFNAWSPA 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 186 IDlkNPKTNRKN---AGFSDEERAkftELLEAGFVDTFRyfypdQEGIYSWwsyrfsaraknagwrIDYFCVSESLKDRL 262
Cdd:cd09077  130 WG--SKRTDRRGrllEDWIANLGL---VLLNDGNSPTFV-----RPRGTSI---------------IDVTFCSPSLARRI 184
                        250       260
                 ....*....|....*....|.
gi 291561139 263 VDAKIHTEVMGSDHCPVELDI 283
Cdd:cd09077  185 SNWRVLEDETLSDHRYIRFTI 205
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
133-283 9.31e-05

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. 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: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 43.10  E-value: 9.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 133 YYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKK--PVIFCGDLNVahqeidlknpktnrkNAGFSDEERAKFTE 210
Cdd:cd09078  128 YHVFGTHLQASDGSCLDRAVRQKQLDELRAFIEEKNIPDnePVIIAGDFNV---------------DKRSSRDEYDDMLE 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 211 LLEAGFVDTFRYF----YPDQEGIYSWWSYRFSaraKNAGWRIDY-FCVSESL-----KDRLVDAKIHTEVMG------- 273
Cdd:cd09078  193 QLHDYNAPEPITAgetpLTWDPGTNLLAKYNYP---GGGGERLDYiLYSNDHLqpsswSNEVEVPKSPTWSVTngytfad 269
                        170
                 ....*....|.
gi 291561139 274 -SDHCPVELDI 283
Cdd:cd09078  270 lSDHYPVSATF 280
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
161-283 7.27e-04

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: 40.28  E-value: 7.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 161 RAYLKELETKKPVIFCGDLNvahqeidlknpktnrknagfSDEERAKFTELLEAGFVDTFR-YFYPDQEGIYSWWSYRFS 239
Cdd:cd09083  151 LERIKEIAGDLPVILTGDFN--------------------AEPDSEPYKTLTSGGLKDARDtAATTDGGPEGTFHGFKGP 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291561139 240 ARAKnagwRIDYFCVSESLKdrLVDAKIHTEVMG----SDHCPVELDI 283
Cdd:cd09083  211 PGGS----RIDYIFVSPGVK--VLSYEILTDRYDgrypSDHFPVVADL 252
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
161-284 9.41e-03

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 36.92  E-value: 9.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291561139 161 RAYLKELETKKP---VIFCGDLNvahqeidlknpktnrknagfSDEERAKFTELLEA-GFVDTFRYFYPDQEgiyswWSY 236
Cdd:COG2374  241 RAFVDSLLAADPdapVIVLGDFN--------------------DYPFEDPLRALLGAgGLTNLAEKLPAAER-----YSY 295
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291561139 237 RFSARAKnagwRIDYFCVSESLKDRLVDAKI-HTEVM-------------------GSDHCPVELDIQ 284
Cdd:COG2374  296 VYDGNSG----LLDHILVSPALAARVTGADIwHINADiynddfkpdfrtyaddpgrASDHDPVVVGLR 359
 
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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