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Conserved domains on  [gi|1685957836|gb|TNX00862|]
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exodeoxyribonuclease III [Enterococcus faecium]

Protein Classification

exodeoxyribonuclease III( domain architecture ID 10173395)

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

CATH:  3.60.10.10
EC:  3.1.11.2
Gene Ontology:  GO:0003677|GO:0046872|GO:0004519|GO:0004527|GO:0006281|GO:0008311
PubMed:  7885481|10838565
SCOP:  4002213

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 1-249 1.28e-155

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: 432.36  E-value: 1.28e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQIDLD----LPGYYQYWNYAERKGYSGTAIFAKKPALNA 76
Cdd:cd09087     1 LKIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  77 TYGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYLENLKKQKPVIVCGDLNVAHQKIDLKN 156
Cdd:cd09087    81 TYGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 157 WKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHTD 236
Cdd:cd09087   161 PKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSD 240

                         250
                  ....*....|...
gi 1685957836 237 IMGSDHCPVELDL 249
Cdd:cd09087   241 IMGSDHCPIGLEL 253
 
Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 1-249 1.28e-155

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: 432.36  E-value: 1.28e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQIDLD----LPGYYQYWNYAERKGYSGTAIFAKKPALNA 76
Cdd:cd09087     1 LKIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  77 TYGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYLENLKKQKPVIVCGDLNVAHQKIDLKN 156
Cdd:cd09087    81 TYGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 157 WKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHTD 236
Cdd:cd09087   161 PKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSD 240

                         250
                  ....*....|...
gi 1685957836 237 IMGSDHCPVELDL 249
Cdd:cd09087   241 IMGSDHCPIGLEL 253
XthA COG0708
Exonuclease III [Replication, recombination and repair];
1-250 4.84e-130

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 367.86  E-value: 4.84e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKnFLEVFHELDADFFCLQETKLQAGQIDLDL---PGYYQYWNYaeRKGYSGTAIFAKKPALNAT 77
Cdd:COG0708     1 MKIASWNVNGIRARLPK-LLDWLAEEDPDVLCLQETKAQDEQFPLEAfeaAGYHVYFHG--QKGYNGVAILSRLPPEDVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  78 YGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQS-ELKRLDYRLEWEEAFYNYLENL-KKQKPVIVCGDLNVAHQKIDLK 155
Cdd:COG0708    78 RGLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSvGSEKFDYKLRFLDALRAYLAELlAPGRPLILCGDFNIAPTEIDVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 156 NWKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHT 235
Cdd:COG0708   158 NPKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDR 237

                         250
                  ....*....|....*....
gi 1685957836 236 ----DIMGSDHCPVELDLK 250
Cdd:COG0708   238 eprgDERPSDHAPVVVELD 256
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 1-250 3.03e-115

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: 330.40  E-value: 3.03e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQI---DLDLPGYYQYWNYAERkGYSGTAIFAKKPALNAT 77
Cdd:TIGR00633   1 MKIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQFpaeLFEELGYHVFFHGAKK-GYSGVAILSKVEPLDVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  78 YGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSE-LKRLDYRLEWEEAFYNYLEN-LKKQKPVIVCGDLNVAHQKIDLK 155
Cdd:TIGR00633  80 YGFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGSRdLERLEYKLQFWDALFQYLEKeLDAGKPVVICGDMNVAHTEIDLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 156 NWKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHT 235
Cdd:TIGR00633 160 NPKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYIDS 239

                         250
                  ....*....|....*
gi 1685957836 236 DIMGSDHCPVELDLK 250
Cdd:TIGR00633 240 EIRGSDHCPIVLELD 254
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
 1-249 3.02e-104

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 302.38  E-value: 3.02e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQIDLDLPGYYQYWNYAERKGYSGTAIFAKKPALNATYGM 80
Cdd:PRK13911    1 MKLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQNTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSYGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  81 GIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYLENLKKQKPVIVCGDLNVAHQKIDLKNWKTN 160
Cdd:PRK13911   81 NIEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENPKTN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 161 QKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHTDIMGS 240
Cdd:PRK13911  161 RKNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDILGS 240


                  ....*....
gi 1685957836 241 DHCPVELDL 249
Cdd:PRK13911  241 DHCPVGLEL 249
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 4-147 4.91e-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: 81.89  E-value: 4.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   4 ISWNVNGLRA------IVNKNFLEVFHELDADFFCLQETKLQAGQID----LDLPGYYQYWNYAERKGYSGTAIFAKKPA 73
Cdd:pfam03372   1 LTWNVNGGNAdaagddRKLDALAALIRAYDPDVVALQETDDDDASRLllalLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1685957836  74 LNATYGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLE-WEEAFYNYLENLKKQKPVIVCGDLNV 147
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQrADLLLLLLALLAPRSEPVILAGDFNA 155
 
Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 1-249 1.28e-155

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: 432.36  E-value: 1.28e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQIDLD----LPGYYQYWNYAERKGYSGTAIFAKKPALNA 76
Cdd:cd09087     1 LKIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  77 TYGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYLENLKKQKPVIVCGDLNVAHQKIDLKN 156
Cdd:cd09087    81 TYGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 157 WKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHTD 236
Cdd:cd09087   161 PKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSD 240

                         250
                  ....*....|...
gi 1685957836 237 IMGSDHCPVELDL 249
Cdd:cd09087   241 IMGSDHCPIGLEL 253
XthA COG0708
Exonuclease III [Replication, recombination and repair];
1-250 4.84e-130

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 367.86  E-value: 4.84e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKnFLEVFHELDADFFCLQETKLQAGQIDLDL---PGYYQYWNYaeRKGYSGTAIFAKKPALNAT 77
Cdd:COG0708     1 MKIASWNVNGIRARLPK-LLDWLAEEDPDVLCLQETKAQDEQFPLEAfeaAGYHVYFHG--QKGYNGVAILSRLPPEDVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  78 YGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQS-ELKRLDYRLEWEEAFYNYLENL-KKQKPVIVCGDLNVAHQKIDLK 155
Cdd:COG0708    78 RGLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSvGSEKFDYKLRFLDALRAYLAELlAPGRPLILCGDFNIAPTEIDVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 156 NWKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHT 235
Cdd:COG0708   158 NPKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDR 237

                         250
                  ....*....|....*....
gi 1685957836 236 ----DIMGSDHCPVELDLK 250
Cdd:COG0708   238 eprgDERPSDHAPVVVELD 256
Mth212-like_AP-endo cd09085
Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic ...
 1-249 2.26e-119

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: 340.79  E-value: 2.26e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQIDLDL---PGYYQYWNYAERKGYSGTAIFAKKPALNAT 77
Cdd:cd09085     1 MKIISWNVNGLRAVHKKGFLDWFKEEKPDILCLQETKAQPEQLPEDLrniEGYHSYFNSAERKGYSGVALYSKIEPDSVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  78 YGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYLENLKKQ-KPVIVCGDLNVAHQKIDLKN 156
Cdd:cd09085    81 EGLGVEEFDNEGRILIADFDDFTLFNIYFPNGQMSEERLDYKLEFYDAFLEYLNELRDSgKNVIICGDFNTAHKEIDLAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 157 WKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPtQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHTD 236
Cdd:cd09085   161 PKENEKVSGFLPEERAWMDKFIENGYVDTFRMFNK-EPGQYTWWSYRTRARERNVGWRIDYFFVNEEFKPKVKDAGILPD 239

                         250
                  ....*....|...
gi 1685957836 237 IMGSDHCPVELDL 249
Cdd:cd09085   240 VMGSDHCPVSLEL 252
ExoIII_AP-endo cd09073
Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ...
 2-249 2.57e-118

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: 338.11  E-value: 2.57e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   2 KFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQIDLDL---PGYYQYWNYAERKGYSGTAIFAKKPALNATY 78
Cdd:cd09073     1 KIISWNVNGLRARLKKGVLKWLKEEKPDILCLQETKADEDKLPEELqhvEGYHSYWSPARKKGYSGVATLSKEEPLDVSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  79 GMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYLENL-KKQKPVIVCGDLNVAHQKIDLKNW 157
Cdd:cd09073    81 GIGGEEFDSEGRVITAEFDDFYLINVYFPNGGRGLERLDYKLRFYEAFLEFLEKLrKRGKPVVICGDFNVAHEEIDLARP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 158 KTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPtQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHTDI 237
Cdd:cd09073   161 KKNEKNAGFTPEERAWFDKLLSLGYVDTFRHFHP-EPGAYTWWSYRGNARERNVGWRIDYFLVSEELAEKVKDSGILSKV 239

                         250
                  ....*....|..
gi 1685957836 238 MGSDHCPVELDL 249
Cdd:cd09073   240 KGSDHAPVTLEL 251
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 1-250 3.03e-115

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: 330.40  E-value: 3.03e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQI---DLDLPGYYQYWNYAERkGYSGTAIFAKKPALNAT 77
Cdd:TIGR00633   1 MKIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQFpaeLFEELGYHVFFHGAKK-GYSGVAILSKVEPLDVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  78 YGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSE-LKRLDYRLEWEEAFYNYLEN-LKKQKPVIVCGDLNVAHQKIDLK 155
Cdd:TIGR00633  80 YGFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGSRdLERLEYKLQFWDALFQYLEKeLDAGKPVVICGDMNVAHTEIDLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 156 NWKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHT 235
Cdd:TIGR00633 160 NPKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYIDS 239

                         250
                  ....*....|....*
gi 1685957836 236 DIMGSDHCPVELDLK 250
Cdd:TIGR00633 240 EIRGSDHCPIVLELD 254
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
 1-249 5.03e-105

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: 304.31  E-value: 5.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKnFLEVFHELDADFFCLQETKLQAGQIDLDLP---GYYQYWNYAerKGYSGTAIFAKKPALNAT 77
Cdd:TIGR00195   1 MKIISWNVNGLRARPHK-GLAWLKENQPDVLCLQETKVQDEQFPLEPFhkeGYHVFFSGQ--KGYSGVAIFSKEEPISVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  78 YGMGIDIHDTEGRLITLEYSDFFLVTCYTPN-SQSELKRLDYRLEWEEAFYNYLENL-KKQKPVIVCGDLNVAHQKIDLK 155
Cdd:TIGR00195  78 RGFGVEEEDAEGRIIMAEFDSFLVINGYFPNgSRDDSEKLPYKLQWLEALQNYLEKLvDKDKPVLICGDMNIAPTEIDLH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 156 NWKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPtQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHT 235
Cdd:TIGR00195 158 IPDENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNP-DEGAYSWWDYRTKARDRNRGWRIDYFLVSEPLKERCVDCGIDY 236

                         250
                  ....*....|....*...
gi 1685957836 236 DIMG----SDHCPVELDL 249
Cdd:TIGR00195 237 DIRGsekpSDHCPVVLEF 254
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
 1-249 3.02e-104

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 302.38  E-value: 3.02e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQIDLDLPGYYQYWNYAERKGYSGTAIFAKKPALNATYGM 80
Cdd:PRK13911    1 MKLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQNTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSYGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  81 GIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYLENLKKQKPVIVCGDLNVAHQKIDLKNWKTN 160
Cdd:PRK13911   81 NIEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENPKTN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 161 QKNAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHTDIMGS 240
Cdd:PRK13911  161 RKNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDILGS 240


                  ....*....
gi 1685957836 241 DHCPVELDL 249
Cdd:PRK13911  241 DHCPVGLEL 249
Nape_like_AP-endo cd10281
Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) ...
 1-248 6.37e-91

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: 268.71  E-value: 6.37e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKNFLEVFHELDADFFCLQETKLQAGQIDLDL---PGYYQYWNYAERKGYSGTAIFAKKPALNAT 77
Cdd:cd10281     1 MRVISVNVNGIRAAAKKGFLEWLAAQDADVVCLQEVRAQEEQLDDDFfepEGYNAYFFDAEKKGYAGVAIYSRTQPKAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  78 YGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYLENLKKQKP-VIVCGDLNVAHQKIDLKN 156
Cdd:cd10281    81 YGLGFEEFDDEGRYIEADFDNVSVASLYVPSGSSGDERQEAKMAFLDAFLEHLKELRRKRReFIVCGDFNIAHTEIDIKN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 157 WKTNQKNAGFTPEERAALSRLLDN-GFIDTFRYFYPtQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHT 235
Cdd:cd10281   161 WKANQKNSGFLPEERAWLDQVFGElGYVDAFRELNP-DEGQYTWWSNRGQARANNVGWRIDYQIATPGLASKVVSAWIYR 239

                         250
                  ....*....|...
gi 1685957836 236 DIMGSDHCPVELD 248
Cdd:cd10281   240 EERFSDHAPLIVD 252
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
 1-249 1.51e-70

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: 216.61  E-value: 1.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRA---IVnKNFLEvfhELDADFFCLQETKLQAGQIDLDL---PGYYQYWNyaERKGYSGTAIFAKKPAL 74
Cdd:cd09086     1 MKIATWNVNSIRArleQV-LDWLK---EEDPDVLCLQETKVEDDQFPADAfeaLGYHVAVH--GQKAYNGVAILSRLPLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  75 NATYGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSE-LKRLDYRLEWEEAFYNYL-ENLKKQKPVIVCGDLNVAHQKI 152
Cdd:cd09086    75 DVRTGFPGDPDDDQARLIAARVGGVRVINLYVPNGGDIgSPKFAYKLDWLDRLIRYLqKLLKPDDPLVLVGDFNIAPEDI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 153 DLKNWKTNQKNAGFTPEERAALSRLLDNGFIDTFRYFYPtQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAK 232
Cdd:cd09086   155 DVWDPKQLLGKVLFTPEEREALRALLDLGFVDAFRALHP-DEKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVG 233

                         250       260
                  ....*....|....*....|.
gi 1685957836 233 IHTDIMG----SDHCPVELDL 249
Cdd:cd09086   234 IDREPRGwekpSDHAPVVAEL 254
Ape2-like_AP-endo cd09088
Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This ...
 2-249 4.71e-61

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: 194.46  E-value: 4.71e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   2 KFISWNVNGLRA-------IVNKNFLEVFHELDADFFCLQETKLQAGQIDLD---LPGYYQYWNY-AERKGYSGTAIFAK 70
Cdd:cd09088     1 RIVTWNVNGIRTrlqyqpwNKENSLKSFLDSLDADIICLQETKLTRDELDEPsaiVEGYDSFFSFsRGRKGYSGVATYCR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  71 KPA---LNATYGM---------------GIDIH-----------------DTEGRLITLEYSDFFLVTCYTPNSQSE-LK 114
Cdd:cd09088    81 DSAatpVAAEEGLtgvlsspnqknelseNDDIGcygemleftdskellelDSEGRCVLTDHGTFVLINVYCPRADPEkEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 115 RLDYRLeweeAFYNYLEN-----LKKQKPVIVCGDLNVAHQKIDLKNWKTNQKNAGFTPEE---RAALSRLLDNG----- 181
Cdd:cd09088   161 RLEFKL----DFYRLLEErvealLKAGRRVILVGDVNVSHRPIDHCDPDDSEDFGGESFEDnpsRQWLDQLLGDSgeggg 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1685957836 182 -----FIDTFRYFYPTQEGVYSWWNYRFNSRKNNAGWRIDYFLTSKDLEPGLADAKIHTDIMGSDHCPVELDL 249
Cdd:cd09088   237 spgglLIDSFRYFHPTRKGAYTCWNTLTGARPTNYGTRIDYILADRGLLPWVKAADILPEVEGSDHCPVYADL 309
PRK11756 PRK11756
exonuclease III; Provisional
 1-250 9.77e-44

exonuclease III; Provisional


Pssm-ID: 236970 [Multi-domain]  Cd Length: 268  Bit Score: 148.50  E-value: 9.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAivnknfleVFHELDA-------DFFCLQETKLqagqIDLDLP-------GYYQYwnYAERKGYSGTA 66
Cdd:PRK11756    1 MKFVSFNINGLRA--------RPHQLEAiiekhqpDVIGLQETKV----HDEMFPleevealGYHVF--YHGQKGHYGVA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  67 IFAKKPALNATYGMGIDIHDTEGRLITLEY-SDFFLVT---CYTPNSQS---ELKrldyrLEWEEAFY----NYLE-NLK 134
Cdd:PRK11756   67 LLSKQTPIAVRKGFPTDDEEAQRRIIMATIpTPNGNLTvinGYFPQGESrdhPTK-----FPAKRQFYqdlqNYLEtELS 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 135 KQKPVIVCGDLNVAHQKIDL-------KNWKTNQKnAGFTPEERAALSRLLDNGFIDTFRYFYPTQEGVYSWWNYRFNSR 207
Cdd:PRK11756  142 PDNPLLIMGDMNISPTDLDIgigeenrKRWLRTGK-CSFLPEEREWLDRLMDWGLVDTFRQLNPDVNDRFSWFDYRSKGF 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1685957836 208 KNNAGWRIDYFLTSKDLEPGLADAKIHTDIMG----SDHCPVELDLK 250
Cdd:PRK11756  221 DDNRGLRIDLILATQPLAERCVETGIDYDIRGmekpSDHAPIWATFK 267
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 4-249 3.16e-33

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


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 120.66  E-value: 3.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   4 ISWNVNGLRAIVN-KNFLEVFHELDADFFCLQETKL----QAGQIDLDLPGYYQYWNYAER-KGYSGTAIFAKKPALNAT 77
Cdd:cd08372     2 ASYNVNGLNAATRaSGIARWVRELDPDIVCLQEVKDsqysAVALNQLLPEGYHQYQSGPSRkEGYEGVAILSKTPKFKIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  78 ---YGMGIDIHDTEGRL----ITLEYSDFFLVTCYTPNSQSelkRLDYRLEWEEAFYNYLENL--KKQKPVIVCGDLNVA 148
Cdd:cd08372    82 ekhQYKFGEGDSGERRAvvvkFDVHDKELCVVNAHLQAGGT---RADVRDAQLKEVLEFLKRLrqPNSAPVVICGDFNVR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 149 HQKIDLKNWKtnqknagftpeerAALSRLLDNGFIDTfryfYPTQEGVYSWWNYRfnsrkNNAGWRIDYFLTSKDLEPGL 228
Cdd:cd08372   159 PSEVDSENPS-------------SMLRLFVALNLVDS----FETLPHAYTFDTYM-----HNVKSRLDYIFVSKSLLPSV 216

                         250       260
                  ....*....|....*....|....*
gi 1685957836 229 ADAKIHTD----IMGSDHCPVELDL 249
Cdd:cd08372   217 KSSKILSDaaraRIPSDHYPIEVTL 241
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
 3-249 8.93e-28

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: 106.28  E-value: 8.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   3 FISWNVNGLRAIVN-KNFLEVFHELDADFFCLQETKL-QAGQIDLDLPGYYQYWNYAERKGYSGTAIFAKKPALNATygm 80
Cdd:cd09076     1 IGTLNVRGLRSPGKrAQLLEELKRKKLDILGLQETHWtGEGELKKKREGGTILYSGSDSGKSRGVAILLSKTAANKL--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  81 gID-IHDTEGRLITL----EYSDFFLVTCYTPNSQSELKRldyrleweEAFYN----YLENLKKQKPVIVCGDLN-VAHQ 150
Cdd:cd09076    78 -LEyTKVVSGRIIMVrfkiKGKRLTIINVYAPTARDEEEK--------EEFYDqlqdVLDKVPRHDTLIIGGDFNaVLGP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 151 KIDLKNWKTNQKNAGftpeERAALSRLLDNGFIDTFRYFYPTQEGvyswwnYRFNSRKNNAGWRIDYFLTSKDLEPGLAD 230
Cdd:cd09076   149 KDDGRKGLDKRNENG----ERALSALIEEHDLVDVWRENNPKTRE------YTWRSPDHGSRSRIDRILVSKRLRVKVKK 218

                         250
                  ....*....|....*....
gi 1685957836 231 AKIhTDIMGSDHCPVELDL 249
Cdd:cd09076   219 TKI-TPGAGSDHRLVTLKL 236
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 4-147 4.91e-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: 81.89  E-value: 4.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   4 ISWNVNGLRA------IVNKNFLEVFHELDADFFCLQETKLQAGQID----LDLPGYYQYWNYAERKGYSGTAIFAKKPA 73
Cdd:pfam03372   1 LTWNVNGGNAdaagddRKLDALAALIRAYDPDVVALQETDDDDASRLllalLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1685957836  74 LNATYGMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSELKRLDYRLE-WEEAFYNYLENLKKQKPVIVCGDLNV 147
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQrADLLLLLLALLAPRSEPVILAGDFNA 155
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 4-249 9.16e-15

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: 71.56  E-value: 9.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   4 ISWNVNGLR----AIVNKNFLEVFHELDADFFCLQETKLQAGQ----IDLDLPGY-YQYWNYAERKGYSGTAIFAKKPAL 74
Cdd:cd09084     2 MSYNVRSFNrykwKDDPDKILDFIKKQDPDILCLQEYYGSEGDkdddLRLLLKGYpYYYVVYKSDSGGTGLAIFSKYPIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  75 NA-------TYGMGI--DIhDTEGRLITLeYSDFFLVTCYTPNSQSELKRLDYRLEWEEAFYNYL-ENLKKQ-------- 136
Cdd:cd09084    82 NSgsidfpnTNNNAIfaDI-RVGGDTIRV-YNVHLESFRITPSDKELYKEEKKAKELSRNLLRKLaEAFKRRaaqadlla 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 137 -------KPVIVCGDLN------VAHQkidlknwktnqknagftpeeraaLSRLLDNGFID-------TFRYFYPTqegv 196
Cdd:cd09084   160 adiaaspYPVIVCGDFNdtpasyVYRT-----------------------LKKGLTDAFVEagsgfgyTFNGLFFP---- 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1685957836 197 yswwnyrfnsrknnagWRIDYFLTSKDLEPglADAKIHTDIMgSDHCPVELDL 249
Cdd:cd09084   213 ----------------LRIDYILTSKGFKV--LRYRVDPGKY-SDHYPIVATL 246
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
 1-249 2.90e-11

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 62.32  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAIVNKnFLEVFHELDADFFCLQETKlQAGQIDLD-LPGYYQYWNYAERKGYSGTAIFAKKPALNATyg 79
Cdd:COG3021    95 LRVLTANVLFGNADAEA-LAALVREEDPDVLVLQETT-PAWEEALAaLEADYPYRVLCPLDNAYGMALLSRLPLTEAE-- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  80 mGIDIHDTEGRLI----TLEYSDFFLVTC--YTPNSQSElkrldyrlEWEEafynYLENLKKQ-----KPVIVCGDLN-V 147
Cdd:COG3021   171 -VVYLVGDDIPSIratvELPGGPVRLVAVhpAPPVGGSA--------ERDA----ELAALAKAvaaldGPVIVAGDFNaT 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 148 AHQkidlknwktnqknagftpeerAALSRLLD-NGFID--TFRYFYPTqegvyswwnyrFNSRKNNAGWRIDYFLTSKDL 224
Cdd:COG3021   238 PWS---------------------PTLRRLLRaSGLRDarAGRGLGPT-----------WPANLPFLRLPIDHVLVSRGL 285

                         250       260
                  ....*....|....*....|....*
gi 1685957836 225 EpgLADAKIHTDImGSDHCPVELDL 249
Cdd:COG3021   286 T--VVDVRVLPVI-GSDHRPLLAEL 307
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 1-250 7.86e-07

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 47.60  E-value: 7.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNV---NGLRAIVNK-NFLEVFHELDADFFCLQE----TK---LQAGQIDLDLPGYyqywnyaERKGysgtAIFA 69
Cdd:COG3568     8 LRVMTYNIrygLGTDGRADLeRIARVIRALDPDVVALQEnailSRypiVSSGTFDLPDPGG-------EPRG----ALWA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  70 kkpalnatygmgiDIHDTEGRLitleysdFFLVTCYTPNSQSElkrldyRLEWEEAFYNYLENLKKQKPVIVCGDLNVah 149
Cdd:COG3568    77 -------------DVDVPGKPL-------RVVNTHLDLRSAAA------RRRQARALAELLAELPAGAPVILAGDFND-- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 150 qkidlknwktnqknagftpeeraalsrlldngfidtfryfyptqegvyswwnyrfnsrknnagwrIDYFLTSKDLEPglA 229
Cdd:COG3568   129 -----------------------------------------------------------------IDYILVSPGLRV--L 141

                         250       260
                  ....*....|....*....|....
gi 1685957836 230 DAKIHTDIMG---SDHCPVELDLK 250
Cdd:COG3568   142 SAEVLDSPLGraaSDHLPVVADLE 165
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 21-249 7.30e-05

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: 42.97  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  21 EVFHELDADFFCLQETKL-QAGQIDLDLPGYYQYwNYAERKGYSG---TAIFAKKpalnatygmgidihdteGRLITLEY 96
Cdd:cd09083    28 ELIKFYDPDIIGTQEALPhQLADLEELLPEYDWI-GVGRDDGKEKgefSAIFYRK-----------------DRFELLDS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  97 SDFFLV-TCYTPNSQS--------------ELKR-----------LDY-----RLEWEEAFYNYLENLKKQKPVIVCGDL 145
Cdd:cd09083    90 GTFWLSeTPDVVGSKGwdaalprictwarfKDKKtgkefyvfnthLDHvgeeaREESAKLILERIKEIAGDLPVILTGDF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 146 NVahqkidlknwktnqknagfTPEErAALSRLLDNGFIDTfryfYPTQEGVYSWWNYRFNS-RKNNAGWRIDYFLTSKDL 224
Cdd:cd09083   170 NA-------------------EPDS-EPYKTLTSGGLKDA----RDTAATTDGGPEGTFHGfKGPPGGSRIDYIFVSPGV 225

                         250       260
                  ....*....|....*....|....*....
gi 1685957836 225 EPglADAKIHTDIMG----SDHCPVELDL 249
Cdd:cd09083   226 KV--LSYEILTDRYDgrypSDHFPVVADL 252
R1-I-EN cd09077
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ...
 1-150 8.20e-04

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: 39.58  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836   1 MKFISWNVNGLRAivNKNFLEVF-HELDADFFCLQETklqagqidldlpgyyqYWNYAERKGYS-----GTAIFAKKPAL 74
Cdd:cd09077     1 LRILQINLNRCKA--AQDLLLQTaREEGADIALIQEP----------------YLVPVNNPNWVtdesgRAAIVVSDRLP 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836  75 NatygMGIDIHDTEGRLITLEYSDFFLVTCYTPNSQSElkrldyrleweEAFYNYLENL-----KKQKPVIVCGDLNVAH 149
Cdd:cd09077    63 R----KPIQRLSLGLGIVAARVGGITVVSCYAPPSESL-----------EEFEEYLENLvrivrGLSRPVIIGGDFNAWS 127


                  .
gi 1685957836 150 Q 150
Cdd:cd09077   128 P 128
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 132-249 4.42e-03

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: 37.71  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685957836 132 NLKKQKPVIVCGDLNVAHQKidlknwktnqknagFTPEERAALSRLLDNG--FIDTFRYFYPT-QEGVYSWWNYRFnsrK 208
Cdd:cd09078   163 NIPDNEPVIIAGDFNVDKRS--------------SRDEYDDMLEQLHDYNapEPITAGETPLTwDPGTNLLAKYNY---P 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1685957836 209 NNAGWRIDYFLTSKDlepGLADAKIHTDIMG-----------------SDHCPVELDL 249
Cdd:cd09078   226 GGGGERLDYILYSND---HLQPSSWSNEVEVpksptwsvtngytfadlSDHYPVSATF 280
 
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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