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Conserved domains on  [gi|311293546|gb|EFQ72102|]
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endonuclease/exonuclease/phosphatase family protein [Enterococcus faecalis TX0470]

Protein Classification

endonuclease/exonuclease/phosphatase family protein( domain architecture ID 10173375)

endonuclease/exonuclease/phosphatase (EEP) family protein is among a diverse set of enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins

CATH:  3.60.10.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0016787|GO:0003677
PubMed:  10838565
SCOP:  4002213

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 2-249 8.62e-95

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: 278.33  E-value: 8.62e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   2 KIATYNVRVDTEYDQDWQWFFRKEAVCQLINFHDWSLCCIQEVRPNQVRDLKAY-TTFTCLSAEREGDGQ-GEGLAILYN 79
Cdd:cd09083    1 RVMTFNIRYDNPSDGENSWENRKDLVAELIKFYDPDIIGTQEALPHQLADLEELlPEYDWIGVGRDDGKEkGEFSAIFYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  80 EQKVKAIDTGYFWLSETPQ-QPSIHPEAGCPRIALWGLFKETTQNTPFLVINVHLDHISAHARLAGMTVILEELHDKIAQ 158
Cdd:cd09083   81 KDRFELLDSGTFWLSETPDvVGSKGWDAALPRICTWARFKDKKTGKEFYVFNTHLDHVGEEAREESAKLILERIKEIAGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 159 YPTLLMGDFNAESEEEVHQ-LVQKKFQDSKNLATH--YGPRGTFQNFtytKPWAELEEIDYIYV-KGWQVQQTASLTDSI 234
Cdd:cd09083  161 LPVILTGDFNAEPDSEPYKtLTSGGLKDARDTAATtdGGPEGTFHGF---KGPPGGSRIDYIFVsPGVKVLSYEILTDRY 237

                        250
                 ....*....|....*
gi 311293546 235 DGRFPSDHFPLEAEV 249
Cdd:cd09083  238 DGRYPSDHFPVVADL 252
 
Name Accession Description Interval E-value
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 2-249 8.62e-95

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: 278.33  E-value: 8.62e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   2 KIATYNVRVDTEYDQDWQWFFRKEAVCQLINFHDWSLCCIQEVRPNQVRDLKAY-TTFTCLSAEREGDGQ-GEGLAILYN 79
Cdd:cd09083    1 RVMTFNIRYDNPSDGENSWENRKDLVAELIKFYDPDIIGTQEALPHQLADLEELlPEYDWIGVGRDDGKEkGEFSAIFYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  80 EQKVKAIDTGYFWLSETPQ-QPSIHPEAGCPRIALWGLFKETTQNTPFLVINVHLDHISAHARLAGMTVILEELHDKIAQ 158
Cdd:cd09083   81 KDRFELLDSGTFWLSETPDvVGSKGWDAALPRICTWARFKDKKTGKEFYVFNTHLDHVGEEAREESAKLILERIKEIAGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 159 YPTLLMGDFNAESEEEVHQ-LVQKKFQDSKNLATH--YGPRGTFQNFtytKPWAELEEIDYIYV-KGWQVQQTASLTDSI 234
Cdd:cd09083  161 LPVILTGDFNAEPDSEPYKtLTSGGLKDARDTAATtdGGPEGTFHGF---KGPPGGSRIDYIFVsPGVKVLSYEILTDRY 237

                        250
                 ....*....|....*
gi 311293546 235 DGRFPSDHFPLEAEV 249
Cdd:cd09083  238 DGRYPSDHFPVVADL 252
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 1-249 6.55e-30

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 110.00  E-value: 6.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   1 MKIATYNVRVDTEYDQDwqwfFRKEAVCQLINFHDWSLCCIQEVrpnqvrdlkayttftclsaeregdgqgeglAILYne 80
Cdd:COG3568    8 LRVMTYNIRYGLGTDGR----ADLERIARVIRALDPDVVALQEN------------------------------AILS-- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  81 qKVKAIDTGYFWLSETPQQPsihpeagcpRIALWGLFKetTQNTPFLVINVHLDHISAHARLAGMTVILEELHDKIAQYP 160
Cdd:COG3568   52 -RYPIVSSGTFDLPDPGGEP---------RGALWADVD--VPGKPLRVVNTHLDLRSAAARRRQARALAELLAELPAGAP 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 161 TLLMGDFNAeseeevhqlvqkkfqdsknlathygprgtfqnftytkpwaeleeIDYIYV-KGWQVQQTASLtDSIDGRFP 239
Cdd:COG3568  120 VILAGDFND--------------------------------------------IDYILVsPGLRVLSAEVL-DSPLGRAA 154

                        250
                 ....*....|
gi 311293546 240 SDHFPLEAEV 249
Cdd:COG3568  155 SDHLPVVADL 164
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 4-169 1.27e-09

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: 56.08  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546    4 ATYNVRVDTEYDQDWQwfFRKEAVCQLINFHDWSLCCIQEVRPNQVRDL----KAYTTFTCLSAEREGDGQGeGLAILYN 79
Cdd:pfam03372   1 LTWNVNGGNADAAGDD--RKLDALAALIRAYDPDVVALQETDDDDASRLllalLAYGGFLSYGGPGGGGGGG-GVAILSR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   80 eqkvkaidtgyFWLSETPQQPSIHPEAGCPRIALwGLFKETTQNTPFLVINVHLDHISAHARLAGMTVILEELHDKIAQY 159
Cdd:pfam03372  78 -----------YPLSSVILVDLGEFGDPALRGAI-APFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSE 145

                         170
                  ....*....|
gi 311293546  160 PTLLMGDFNA 169
Cdd:pfam03372 146 PVILAGDFNA 155
PRK05421 PRK05421
endonuclease/exonuclease/phosphatase family protein;
38-253 3.19e-08

endonuclease/exonuclease/phosphatase family protein;


Pssm-ID: 235454 [Multi-domain]  Cd Length: 263  Bit Score: 53.02  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  38 LCCIQEVRPNQvrDLKAYTTFTCLSAERegdgqgeglailyneqkVKAIdtgyfwlsETPQQPS-------IHPEAGCP- 109
Cdd:PRK05421  72 LVLLQEAQTTP--ELVQFATANYLAADQ-----------------APAF--------VLPQHPSgvmtlskAHPVYCCPl 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 110 --RIALWGLFKET------TQNTPFL-VINVHL-------DHISAHarlagmtviLEELHDKIAQY--PTLLMGDFNAES 171
Cdd:PRK05421 125 reREPWLRLPKSAliteypLPNGRTLlVVNIHAinfslgvDVYSKQ---------LEPIGDQIAHHsgPVILAGDFNTWS 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 172 EEEVHQLvqKKFQDSKNL-ATHYGPRGTFQNFTYTkpwaeleeIDYIYVKGWQVQQTASL-TDSidgrfpSDHFPLEAEV 249
Cdd:PRK05421 196 RKRMNAL--KRFARELGLkEVRFTDDQRRRAFGRP--------LDFVFYRGLNVSKASVLvTRA------SDHNPLLVEF 259


                 ....
gi 311293546 250 CIEE 253
Cdd:PRK05421 260 SLKK 263
 
Name Accession Description Interval E-value
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 2-249 8.62e-95

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: 278.33  E-value: 8.62e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   2 KIATYNVRVDTEYDQDWQWFFRKEAVCQLINFHDWSLCCIQEVRPNQVRDLKAY-TTFTCLSAEREGDGQ-GEGLAILYN 79
Cdd:cd09083    1 RVMTFNIRYDNPSDGENSWENRKDLVAELIKFYDPDIIGTQEALPHQLADLEELlPEYDWIGVGRDDGKEkGEFSAIFYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  80 EQKVKAIDTGYFWLSETPQ-QPSIHPEAGCPRIALWGLFKETTQNTPFLVINVHLDHISAHARLAGMTVILEELHDKIAQ 158
Cdd:cd09083   81 KDRFELLDSGTFWLSETPDvVGSKGWDAALPRICTWARFKDKKTGKEFYVFNTHLDHVGEEAREESAKLILERIKEIAGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 159 YPTLLMGDFNAESEEEVHQ-LVQKKFQDSKNLATH--YGPRGTFQNFtytKPWAELEEIDYIYV-KGWQVQQTASLTDSI 234
Cdd:cd09083  161 LPVILTGDFNAEPDSEPYKtLTSGGLKDARDTAATtdGGPEGTFHGF---KGPPGGSRIDYIFVsPGVKVLSYEILTDRY 237

                        250
                 ....*....|....*
gi 311293546 235 DGRFPSDHFPLEAEV 249
Cdd:cd09083  238 DGRYPSDHFPVVADL 252
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 1-249 6.55e-30

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 110.00  E-value: 6.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   1 MKIATYNVRVDTEYDQDwqwfFRKEAVCQLINFHDWSLCCIQEVrpnqvrdlkayttftclsaeregdgqgeglAILYne 80
Cdd:COG3568    8 LRVMTYNIRYGLGTDGR----ADLERIARVIRALDPDVVALQEN------------------------------AILS-- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  81 qKVKAIDTGYFWLSETPQQPsihpeagcpRIALWGLFKetTQNTPFLVINVHLDHISAHARLAGMTVILEELHDKIAQYP 160
Cdd:COG3568   52 -RYPIVSSGTFDLPDPGGEP---------RGALWADVD--VPGKPLRVVNTHLDLRSAAARRRQARALAELLAELPAGAP 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 161 TLLMGDFNAeseeevhqlvqkkfqdsknlathygprgtfqnftytkpwaeleeIDYIYV-KGWQVQQTASLtDSIDGRFP 239
Cdd:COG3568  120 VILAGDFND--------------------------------------------IDYILVsPGLRVLSAEVL-DSPLGRAA 154

                        250
                 ....*....|
gi 311293546 240 SDHFPLEAEV 249
Cdd:COG3568  155 SDHLPVVADL 164
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 3-249 2.86e-21

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: 89.08  E-value: 2.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   3 IATYNVRVDTEYDqdwqwffRKEAVCQLINFHDWSLCCIQEVRPNQVRDL----KAYTTFTCLSAEREGDGQGEGLAILY 78
Cdd:cd08372    1 VASYNVNGLNAAT-------RASGIARWVRELDPDIVCLQEVKDSQYSAValnqLLPEGYHQYQSGPSRKEGYEGVAILS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  79 NEQKVKAIDTGYFWLSETPQQPsihpeagcpRIALWGLFKETTQNtpFLVINVHLDHISAHA--RLAGMTVILEELHDKI 156
Cdd:cd08372   74 KTPKFKIVEKHQYKFGEGDSGE---------RRAVVVKFDVHDKE--LCVVNAHLQAGGTRAdvRDAQLKEVLEFLKRLR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 157 AQ--YPTLLMGDFNAESEEEVHQLVQK--------KFQDS-KNLATHYgprgTFQNFTYTKPWAeleeIDYIYVKG---W 222
Cdd:cd08372  143 QPnsAPVVICGDFNVRPSEVDSENPSSmlrlfvalNLVDSfETLPHAY----TFDTYMHNVKSR----LDYIFVSKsllP 214

                        250       260
                 ....*....|....*....|....*..
gi 311293546 223 QVQQTASLTDSIDGRFPSDHFPLEAEV 249
Cdd:cd08372  215 SVKSSKILSDAARARIPSDHYPIEVTL 241
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 1-248 3.35e-14

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 70.07  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   1 MKIATYNVRVDTEYDQDwqwfFRKEAVCQLINFHDWSLCCIQEVRPNQVRDLKA----YTTFTCLSAEREGDGQGEGLAI 76
Cdd:cd09080    1 LKVLTWNVDFLDDVNLA----ERMRAILKLLEELDPDVIFLQEVTPPFLAYLLSqpwvRKNYYFSEGPPSPAVDPYGVLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  77 LYneqKVKAIDTGYFWlsetpqqPSIHPEAGCPRIALwglfkETTQNTPFLVINVHLDHISAHA--RLAGMTVILEELHD 154
Cdd:cd09080   77 LS---KKSLVVRRVPF-------TSTRMGRNLLAAEI-----NLGSGEPLRLATTHLESLKSHSseRTAQLEEIAKKLKK 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 155 KIAQYPTLLMGDFNAESEEEVHQLVQKKFQDS-KNLATHYGPRGTFQnfTYTKPWAELEE------IDYIYVKG--WQVQ 225
Cdd:cd09080  142 PPGAANVILGGDFNLRDKEDDTGGLPNGFVDAwEELGPPGEPGYTWD--TQKNPMLRKGEagprkrFDRVLLRGsdLKPK 219

                        250       260
                 ....*....|....*....|....*...
gi 311293546 226 Q-----TASLTDSIDGRFPSDHFPLEAE 248
Cdd:cd09080  220 SieligTEPIPGDEEGLFPSDHFGLLAE 247
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 2-249 3.79e-11

Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197338 [Multi-domain]  Cd Length: 266  Bit Score: 61.65  E-value: 3.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   2 KIATYNVRVDTEYDQDWQWFFRKEAVCQLinfhDWSLCCIQEVRPNQ-----VRDL-----KAYTTFTCL--SAEREGDG 69
Cdd:cd10283    2 RIASWNILNFGNSKGKEKNPAIAEIISAF----DLDLIALQEVMDNGggldaLAKLvnelnKPGGTWKYIvsDKTGGSSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  70 QGEGLAILYNEQKVKAIDTGYFWLSETPQQPSIHPEAGCprialwglFKETTQNTPFLVINVHLD------HISAHARLA 143
Cdd:cd10283   78 DKERYAFLYKSSKVRKVGKAVLEKDSNTDGFARPPYAAK--------FKSGGTGFDFTLVNVHLKsggsskSGQGAKRVA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 144 ---GMTVILEELHDKIAQYPTLLMGDFNAESEEEVHQ-LVQKKFQ----DSKNLATHYGPR-GTFQNFTYTKPWAELEEI 214
Cdd:cd10283  150 eaqALAEYLKELADEDPDDDVILLGDFNIPADEDAFKaLTKAGFKsllpDSTNLSTSFKGYaNSYDNIFVSGNLKEKFSN 229

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 311293546 215 DYIYVKGWQV---QQTASLTDSIDGRFpSDHFPLEAEV 249
Cdd:cd10283  230 SGVFDFNILVdeaGEEDLDYSKWRKQI-SDHDPVWVEF 266
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 4-169 1.27e-09

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: 56.08  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546    4 ATYNVRVDTEYDQDWQwfFRKEAVCQLINFHDWSLCCIQEVRPNQVRDL----KAYTTFTCLSAEREGDGQGeGLAILYN 79
Cdd:pfam03372   1 LTWNVNGGNADAAGDD--RKLDALAALIRAYDPDVVALQETDDDDASRLllalLAYGGFLSYGGPGGGGGGG-GVAILSR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   80 eqkvkaidtgyFWLSETPQQPSIHPEAGCPRIALwGLFKETTQNTPFLVINVHLDHISAHARLAGMTVILEELHDKIAQY 159
Cdd:pfam03372  78 -----------YPLSSVILVDLGEFGDPALRGAI-APFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSE 145

                         170
                  ....*....|
gi 311293546  160 PTLLMGDFNA 169
Cdd:pfam03372 146 PVILAGDFNA 155
PRK05421 PRK05421
endonuclease/exonuclease/phosphatase family protein;
38-253 3.19e-08

endonuclease/exonuclease/phosphatase family protein;


Pssm-ID: 235454 [Multi-domain]  Cd Length: 263  Bit Score: 53.02  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  38 LCCIQEVRPNQvrDLKAYTTFTCLSAERegdgqgeglailyneqkVKAIdtgyfwlsETPQQPS-------IHPEAGCP- 109
Cdd:PRK05421  72 LVLLQEAQTTP--ELVQFATANYLAADQ-----------------APAF--------VLPQHPSgvmtlskAHPVYCCPl 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 110 --RIALWGLFKET------TQNTPFL-VINVHL-------DHISAHarlagmtviLEELHDKIAQY--PTLLMGDFNAES 171
Cdd:PRK05421 125 reREPWLRLPKSAliteypLPNGRTLlVVNIHAinfslgvDVYSKQ---------LEPIGDQIAHHsgPVILAGDFNTWS 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 172 EEEVHQLvqKKFQDSKNL-ATHYGPRGTFQNFTYTkpwaeleeIDYIYVKGWQVQQTASL-TDSidgrfpSDHFPLEAEV 249
Cdd:PRK05421 196 RKRMNAL--KRFARELGLkEVRFTDDQRRRAFGRP--------LDFVFYRGLNVSKASVLvTRA------SDHNPLLVEF 259


                 ....
gi 311293546 250 CIEE 253
Cdd:PRK05421 260 SLKK 263
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
1-247 6.53e-08

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 52.72  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546   1 MKIATYNVR--VDTEYDQDWQW--------FFRK-EAVCQLINFHDWSLCCIQEV--RPNQVRDL-----KAYTTFTCLS 62
Cdd:COG2374   69 LRVATFNVEnlFDTDDDDDDFGrgadtpeeYERKlAKIAAAIAALDADIVGLQEVenNGSALQDLvaalnLAGGTYAFVH 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  63 AEREGDGQGEGLAILYNEQKVKAIDTG-YFWLSETPQQPSIHPeagcpRIALWGLFkETTQNTPFLVINVHL-------- 133
Cdd:COG2374  149 PPDGPDGDGIRVALLYRPDRVTLVGSAtIADLPDSPGNPDRFS-----RPPLAVTF-ELANGEPFTVIVNHFkskgsddp 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 134 ---DHISAHARLA---GMTVILEELHDKIAQYPTLLMGDFNAESEEEVHQLVQKKfQDSKNLATHYGP--RGT--FQNft 203
Cdd:COG2374  223 gdgQGASEAKRTAqaeALRAFVDSLLAADPDAPVIVLGDFNDYPFEDPLRALLGA-GGLTNLAEKLPAaeRYSyvYDG-- 299

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311293546 204 ytkpwaELEEIDYI--------YVKGWQV------------QQTASLTDSIDGRFpSDHFPLEA 247
Cdd:COG2374  300 ------NSGLLDHIlvspalaaRVTGADIwhinadiynddfKPDFRTYADDPGRA-SDHDPVVV 356
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
 120-252 1.75e-06

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 48.07  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 120 TTQNTPFLVINVHLD--HISAHARLAGmtviLEELHDKIAQ--YPTLLMGDFNAESEEEVHQLVQK--KFQDSknlATHY 193
Cdd:COG3021  187 ELPGGPVRLVAVHPAppVGGSAERDAE----LAALAKAVAAldGPVIVAGDFNATPWSPTLRRLLRasGLRDA---RAGR 259

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 194 GPRGTFQNFTYTKPWAeleeIDYIYV-KGWQVQQTASLTDSidGrfpSDHFPLEAEVCIE 252
Cdd:COG3021  260 GLGPTWPANLPFLRLP----IDHVLVsRGLTVVDVRVLPVI--G---SDHRPLLAELALP 310
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
 72-250 2.05e-05

C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the C-terminal catalytic domain of the deadenylase, nocturnin, and related domains. Nocturnin is a poly(A)-specific 3' exonuclease that specifically degrades the 3' poly(A) tail of RNA in a process known as deadenylation. This nuclease activity is manganese dependent. Nocturnin is expressed in the cytoplasm of Xenopus laevis retinal photoreceptor cells in a rhythmic fashion, and it has been proposed that it participates in posttranscriptional regulation of the circadian clock or its outputs, and that the mRNA target(s) of this deadenylase are circadian clock-related. In mouse, the nocturnin gene, mNoc, is expressed in a circadian pattern in a range of tissues including retina, spleen, heart, kidney, and liver. It is highly expressed in bone-marrow stromal cells, adipocytes and hepatocytes. In mammals, nocturnin plays a role in regulating mesenchymal stem-cell lineage allocation, perhaps through regulating PPAR-gamma (peroxisome proliferator-activated receptor-gamma) nuclear translocation. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197330 [Multi-domain]  Cd Length: 280  Bit Score: 44.72  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546  72 EGLAILYNEQKVKAIDTGYFWLSETPQQPSihpeagcpRIALWGLFKETTQNTPFLVINVHLDHISAHARL--AGMTVIL 149
Cdd:cd09096   91 DGCALFFRKDRFELVNTEKIRLSAMTLKTN--------QVAIACTLRCKETGREICLAVTHLKARTGWERLrsEQGKDLL 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 150 EELhDKIAQY---PTLLMGDFNAESEEEVHQLVQkkfQDSKNLATHY---GPRGTfQNFTYTKpWAELEE------IDYI 217
Cdd:cd09096  163 QNL-QSFIEGakiPLIICGDFNAEPTEPVYKTFS---NSSLNLNSAYkllSADGQ-SEPPYTT-WKIRTSgecrhtLDYI 236

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 311293546 218 -YVK-GWQVQQTASL--TDSI-DGR-----FPSDHFPLEAEVC 250
Cdd:cd09096  237 fYSKdALSVEQLLDLptEEQIgPNRlpsfnYPSDHLSLVCDFS 279
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 125-248 8.19e-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: 8.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 125 PFLVINVHL-----DHISAHARLAGMTVILEELHDKI--AQYPTLLMGDFNAE---SEEEVHQLVQKKFQDSKNLATHYG 194
Cdd:cd09078  127 VYHVFGTHLqasdgSCLDRAVRQKQLDELRAFIEEKNipDNEPVIIAGDFNVDkrsSRDEYDDMLEQLHDYNAPEPITAG 206

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311293546 195 ------PRGTFQNFTYTKPWAELEEIDYIYV-------KGW--QVQQTASLTDSIDGRFP----SDHFPLEAE 248
Cdd:cd09078  207 etpltwDPGTNLLAKYNYPGGGGERLDYILYsndhlqpSSWsnEVEVPKSPTWSVTNGYTfadlSDHYPVSAT 279
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 128-249 2.87e-04

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: 41.13  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 128 VINVHL-----------DHISAHARLAGMTVILEELH----------DKIAQ------YPTLLMGDFNAESEEEVHQLVQ 180
Cdd:cd09084  109 VYNVHLesfritpsdkeLYKEEKKAKELSRNLLRKLAeafkrraaqaDLLAAdiaaspYPVIVCGDFNDTPASYVYRTLK 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 181 KKFQDSkNLATHYGPRGTFQnfTYTKPWaeleEIDYIYV-KGWQVqqtasLTDSIDGRFPSDHFPLEAEV 249
Cdd:cd09084  189 KGLTDA-FVEAGSGFGYTFN--GLFFPL----RIDYILTsKGFKV-----LRYRVDPGKYSDHYPIVATL 246
RgfB-like cd09079
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, ...
 157-249 9.98e-04

Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, and related proteins; This family includes Streptococcus agalactiae RgfB (for regulator of fibrinogen binding) and related proteins. The function of RgfB is unknown. It is part of a putative two component signal transduction system designated rgfBDAC (the rgf locus was identified in a screen for mutants of Streptococcus agalactiae with altered binding to fibrinogen). RgfA,-C,and -D do not belong to this superfamily: rgfA encodes a putative response regulator, and rgfC, a putative histidine kinase. All four genes are co-transcribed, and may be involved in regulating expression of bacterial cell surface components. 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: 197313 [Multi-domain]  Cd Length: 259  Bit Score: 39.55  E-value: 9.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 157 AQYPTLLMGDFNAESEEEVHQLV---QKKFQDSKNLATHygprgTFQNFTYTKP---WAELEE---IDYIYV-KGWQVQQ 226
Cdd:cd09079  162 AGRPVLLMGDFNNPAGSRGEGYDlisSLGLQDTYDLAEE-----KDGGVTVEKAidgWRGNKEakrIDYIFVnRKVKVKS 236

                         90       100
                 ....*....|....*....|...
gi 311293546 227 TASLTDSIDGRFPSDHFPLEAEV 249
Cdd:cd09079  237 SRVIFNGKNPPIVSDHFGVEVEL 259
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 124-248 7.22e-03

C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the C-terminal catalytic domain of the deadenylases, Saccharomyces cerevisiae Ccr4p and two vertebrate homologs (CCR4a and CCR4b), and related domains. CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1 (called Pop2 in yeast), is a DEDD-type protein and does not belong in this superfamily. Saccharomyces cerevisiae CCR4 (or Ccr4p) is a 3'-5' poly(A) RNA and ssDNA exonuclease. It is the catalytic subunit of the yeast mRNA deadenylase (Ccr4p/Pop2p/Not complex). This complex participates in various ways in mRNA metabolism, including transcription initiation and elongation, and mRNA degradation. Ccr4p degrades both poly(A) and single-stranded DNA. There are two vertebrate homologs of Ccr4p, CCR4a (also called CCR4-NOT transcription complex subunit 6 or CNOT6) and CCR4b (also called CNOT6-like or CNOT6L), which independently associate with other components to form distinct CCR4-NOT multisubunit complexes. The nuclease domain of CNOT6 and CNOT6L exhibits Mg2+-dependent deadenylase activity, with specificity for poly (A) RNA as substrate. CCR4a is a component of P-bodies and is necessary for foci formation. CCR4b regulates p27/Kip1 mRNA levels, thereby influencing cell cycle progression. They both contribute to the prevention of cell death by regulating insulin-like growth factor-binding protein 5.


Pssm-ID: 197331 [Multi-domain]  Cd Length: 329  Bit Score: 37.28  E-value: 7.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 124 TPFLVINVHL--DH-------ISAHARLAGMTVILEEL----HDKIAQYPTLLMGDFNAESEEEVHQLVQK--------- 181
Cdd:cd09097  157 QLLIVANTHIhwDPefsdvklVQTMMLLEELEKIAEKFsrypYEDSADIPLVVCGDFNSLPDSGVYELLSNgsvspnhpd 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311293546 182 -------KFQDSKNLATHYGPRGTFQN-----FT-YTKPWAELeeIDYIYVKGWQVQQTASL--------TDSIDG---- 236
Cdd:cd09097  237 fkedpygEYLTASGLTHSFKLKSAYANlgelpFTnYTPDFKGV--IDYIFYSADTLSVLGLLgppdedwyLNKVVGlpnp 314

                        170
                 ....*....|..
gi 311293546 237 RFPSDHFPLEAE 248
Cdd:cd09097  315 HFPSDHIALLAE 326
 
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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