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Conserved domains on  [gi|2444586889|ref|WP_273604469|]
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MULTISPECIES: endonuclease/exonuclease/phosphatase family protein [unclassified Pseudoalteromonas]

Protein Classification

endonuclease/exonuclease/phosphatase family protein( domain architecture ID 10789901)

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
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
2-321 3.02e-110

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


:

Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 324.26  E-value: 3.02e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889   2 LIALAIIIGFFLLVTLLPMSY-SQHYLVRSCDFVRLQVFYIASAVAIISFYLLWQSGnsgylytALTALLTMALQGKWIF 80
Cdd:COG3021     6 LLALLWAALLLLLATLLPLGLgADHWLIRLLDFFRPQLAVLALLLLLLALLRRRWAL-------AAAALLLLLVQAALIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889  81 PYTWLAKKEVKTAsvseDHSVRIMSANVLMSNHNSEQLISLVDKHQPDLLITLESDSWWENKLAVLKKNYPFYIECPKDN 160
Cdd:COG3021    79 PYTLPAPKSAPAG----GPDLRVLTANVLFGNADAEALAALVREEDPDVLVLQETTPAWEEALAALEADYPYRVLCPLDN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 161 RYGMHLYSKFKILDGQICELIEDDIPSIHILFE-NNEGLEMqgHFIHPAPPSPTeedsSRPRDSELIMVAKALKKPTRPT 239
Cdd:COG3021   155 AYGMALLSRLPLTEAEVVYLVGDDIPSIRATVElPGGPVRL--VAVHPAPPVGG----SAERDAELAALAKAVAALDGPV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 240 IVAGDLNDVAWSRSTRLFMQISGFLDPRKGRGFYNTFHANYFFMRWPLDHLFHSPGFKVKRIKRLAKYGSDHFALLTELV 319
Cdd:COG3021   229 IVAGDFNATPWSPTLRRLLRASGLRDARAGRGLGPTWPANLPFLRLPIDHVLVSRGLTVVDVRVLPVIGSDHRPLLAELA 308

                  ..
gi 2444586889 320 YE 321
Cdd:COG3021   309 LP 310
 
Name Accession Description Interval E-value
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
2-321 3.02e-110

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 324.26  E-value: 3.02e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889   2 LIALAIIIGFFLLVTLLPMSY-SQHYLVRSCDFVRLQVFYIASAVAIISFYLLWQSGnsgylytALTALLTMALQGKWIF 80
Cdd:COG3021     6 LLALLWAALLLLLATLLPLGLgADHWLIRLLDFFRPQLAVLALLLLLLALLRRRWAL-------AAAALLLLLVQAALIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889  81 PYTWLAKKEVKTAsvseDHSVRIMSANVLMSNHNSEQLISLVDKHQPDLLITLESDSWWENKLAVLKKNYPFYIECPKDN 160
Cdd:COG3021    79 PYTLPAPKSAPAG----GPDLRVLTANVLFGNADAEALAALVREEDPDVLVLQETTPAWEEALAALEADYPYRVLCPLDN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 161 RYGMHLYSKFKILDGQICELIEDDIPSIHILFE-NNEGLEMqgHFIHPAPPSPTeedsSRPRDSELIMVAKALKKPTRPT 239
Cdd:COG3021   155 AYGMALLSRLPLTEAEVVYLVGDDIPSIRATVElPGGPVRL--VAVHPAPPVGG----SAERDAELAALAKAVAALDGPV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 240 IVAGDLNDVAWSRSTRLFMQISGFLDPRKGRGFYNTFHANYFFMRWPLDHLFHSPGFKVKRIKRLAKYGSDHFALLTELV 319
Cdd:COG3021   229 IVAGDFNATPWSPTLRRLLRASGLRDARAGRGLGPTWPANLPFLRLPIDHVLVSRGLTVVDVRVLPVIGSDHRPLLAELA 308

                  ..
gi 2444586889 320 YE 321
Cdd:COG3021   309 LP 310
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
104-311 1.33e-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: 85.35  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 104 MSANVLMSNHNSE-------QLISLVDKHQPDLLITLESDSWWENKLAVLKKNYPFYIEC----PKDNRYGMHLYSKFKI 172
Cdd:pfam03372   1 LTWNVNGGNADAAgddrkldALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYggpgGGGGGGGVAILSRYPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 173 LDGQICELIEDDIPSIHILFENNEGLEMQGHFIHPAPPSPTEEDSSRPRDSELIMVAKALKKPTRPTIVAGDLNDvawsr 252
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA----- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2444586889 253 strlfmqisgfldprkgrgfyntfhanyffmrwplDHLFHSPGFKVKRIKRL----AKYGSDH 311
Cdd:pfam03372 156 -----------------------------------DYILVSGGLTVLSVGVLpdlgPRTGSDH 183
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
103-318 2.45e-19

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: 85.81  E-value: 2.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 103 IMSANVLMSNHNS-----EQLISLVDKHQPDLLITLE---SDSWWENKLAVLKKNYPFYI--ECPKDNRYGMHLYSKFKI 172
Cdd:cd09084     1 VMSYNVRSFNRYKwkddpDKILDFIKKQDPDILCLQEyygSEGDKDDDLRLLLKGYPYYYvvYKSDSGGTGLAIFSKYPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 173 LDGQicelieddipSIHILFENNEGL----EMQG--------HF----IHPAPPSPTEEDSSRPRDSELI---------- 226
Cdd:cd09084    81 LNSG----------SIDFPNTNNNAIfadiRVGGdtirvynvHLesfrITPSDKELYKEEKKAKELSRNLlrklaeafkr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 227 ------MVAKALKKPTRPTIVAGDLNDVAWSRSTRlfmQISGFLDP---RKGRGFYNTFHANYFFMRwpLDHLFHSPGFK 297
Cdd:cd09084   151 raaqadLLAADIAASPYPVIVCGDFNDTPASYVYR---TLKKGLTDafvEAGSGFGYTFNGLFFPLR--IDYILTSKGFK 225
                         250       260
                  ....*....|....*....|.
gi 2444586889 298 VKRIKRLAKYGSDHFALLTEL 318
Cdd:cd09084   226 VLRYRVDPGKYSDHYPIVATL 246
 
Name Accession Description Interval E-value
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
2-321 3.02e-110

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 324.26  E-value: 3.02e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889   2 LIALAIIIGFFLLVTLLPMSY-SQHYLVRSCDFVRLQVFYIASAVAIISFYLLWQSGnsgylytALTALLTMALQGKWIF 80
Cdd:COG3021     6 LLALLWAALLLLLATLLPLGLgADHWLIRLLDFFRPQLAVLALLLLLLALLRRRWAL-------AAAALLLLLVQAALIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889  81 PYTWLAKKEVKTAsvseDHSVRIMSANVLMSNHNSEQLISLVDKHQPDLLITLESDSWWENKLAVLKKNYPFYIECPKDN 160
Cdd:COG3021    79 PYTLPAPKSAPAG----GPDLRVLTANVLFGNADAEALAALVREEDPDVLVLQETTPAWEEALAALEADYPYRVLCPLDN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 161 RYGMHLYSKFKILDGQICELIEDDIPSIHILFE-NNEGLEMqgHFIHPAPPSPTeedsSRPRDSELIMVAKALKKPTRPT 239
Cdd:COG3021   155 AYGMALLSRLPLTEAEVVYLVGDDIPSIRATVElPGGPVRL--VAVHPAPPVGG----SAERDAELAALAKAVAALDGPV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 240 IVAGDLNDVAWSRSTRLFMQISGFLDPRKGRGFYNTFHANYFFMRWPLDHLFHSPGFKVKRIKRLAKYGSDHFALLTELV 319
Cdd:COG3021   229 IVAGDFNATPWSPTLRRLLRASGLRDARAGRGLGPTWPANLPFLRLPIDHVLVSRGLTVVDVRVLPVIGSDHRPLLAELA 308

                  ..
gi 2444586889 320 YE 321
Cdd:COG3021   309 LP 310
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
104-311 1.33e-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: 85.35  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 104 MSANVLMSNHNSE-------QLISLVDKHQPDLLITLESDSWWENKLAVLKKNYPFYIEC----PKDNRYGMHLYSKFKI 172
Cdd:pfam03372   1 LTWNVNGGNADAAgddrkldALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYggpgGGGGGGGVAILSRYPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 173 LDGQICELIEDDIPSIHILFENNEGLEMQGHFIHPAPPSPTEEDSSRPRDSELIMVAKALKKPTRPTIVAGDLNDvawsr 252
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA----- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2444586889 253 strlfmqisgfldprkgrgfyntfhanyffmrwplDHLFHSPGFKVKRIKRL----AKYGSDH 311
Cdd:pfam03372 156 -----------------------------------DYILVSGGLTVLSVGVLpdlgPRTGSDH 183
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
103-318 2.45e-19

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: 85.81  E-value: 2.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 103 IMSANVLMSNHNS-----EQLISLVDKHQPDLLITLE---SDSWWENKLAVLKKNYPFYI--ECPKDNRYGMHLYSKFKI 172
Cdd:cd09084     1 VMSYNVRSFNRYKwkddpDKILDFIKKQDPDILCLQEyygSEGDKDDDLRLLLKGYPYYYvvYKSDSGGTGLAIFSKYPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 173 LDGQicelieddipSIHILFENNEGL----EMQG--------HF----IHPAPPSPTEEDSSRPRDSELI---------- 226
Cdd:cd09084    81 LNSG----------SIDFPNTNNNAIfadiRVGGdtirvynvHLesfrITPSDKELYKEEKKAKELSRNLlrklaeafkr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 227 ------MVAKALKKPTRPTIVAGDLNDVAWSRSTRlfmQISGFLDP---RKGRGFYNTFHANYFFMRwpLDHLFHSPGFK 297
Cdd:cd09084   151 raaqadLLAADIAASPYPVIVCGDFNDTPASYVYR---TLKKGLTDafvEAGSGFGYTFNGLFFPLR--IDYILTSKGFK 225
                         250       260
                  ....*....|....*....|.
gi 2444586889 298 VKRIKRLAKYGSDHFALLTEL 318
Cdd:cd09084   226 VLRYRVDPGKYSDHYPIVATL 246
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
94-318 2.77e-07

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 49.91  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889  94 SVSEDHSVRIMSANVLMSNH-----NSEQLISLVDKHQPDLlITLEsdswwENklAVLkknypfyiecpkdnrygmhlyS 168
Cdd:COG3568     1 AAAAAATLRVMTYNIRYGLGtdgraDLERIARVIRALDPDV-VALQ-----EN--AIL---------------------S 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 169 KFKILDGQICELIEDDIPS---IHILFENNEG-LemqgHFI--HPAPPSPTEedssrpRDSELIMVAKALKK--PTRPTI 240
Cdd:COG3568    52 RYPIVSSGTFDLPDPGGEPrgaLWADVDVPGKpL----RVVntHLDLRSAAA------RRRQARALAELLAElpAGAPVI 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 241 VAGDLNDvawsrstrlfmqisgfldprkgrgfyntfhanyffmrwpLDHLFHSPGFKVKRIK----RLAKYGSDHFALLT 316
Cdd:COG3568   122 LAGDFND---------------------------------------IDYILVSPGLRVLSAEvldsPLGRAASDHLPVVA 162

                  ..
gi 2444586889 317 EL 318
Cdd:COG3568   163 DL 164
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
227-318 4.22e-06

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


Pssm-ID: 197317 [Multi-domain]  Cd Length: 252  Bit Score: 47.60  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 227 MVAKALKK--PTRPTIVAGDLNDVAWSRSTRLFMQiSGFLDPR-----KGRGFYNTFHAnyfFMRWP----LDHLFHSPG 295
Cdd:cd09083   149 LILERIKEiaGDLPVILTGDFNAEPDSEPYKTLTS-GGLKDARdtaatTDGGPEGTFHG---FKGPPggsrIDYIFVSPG 224
                          90       100
                  ....*....|....*....|....*...
gi 2444586889 296 FKVKRIKRLA-----KYGSDHFALLTEL 318
Cdd:cd09083   225 VKVLSYEILTdrydgRYPSDHFPVVADL 252
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
102-318 5.83e-05

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: 43.87  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 102 RIMSANVLMSN-HNSEQ----LISLVDKHQPDL----------LITLESDSWWenklavlKKNYPFyIECPKDNR---YG 163
Cdd:cd09080     2 KVLTWNVDFLDdVNLAErmraILKLLEELDPDViflqevtppfLAYLLSQPWV-------RKNYYF-SEGPPSPAvdpYG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 164 MHLYSKFkildgqicELIEDDIPSIHILFENNeGLEMQGHFIHPAP--------PSPTEEDSSRPRdsELIMVAKALKKP 235
Cdd:cd09080    74 VLILSKK--------SLVVRRVPFTSTRMGRN-LLAAEINLGSGEPlrlatthlESLKSHSSERTA--QLEEIAKKLKKP 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 236 T--RPTIVAGDLNdvAWSRSTRLFMQISGFLD------PRKGRGF--------YNTFHANYFFMRwpLDH-LFHSPGFKV 298
Cdd:cd09080   143 PgaANVILGGDFN--LRDKEDDTGGLPNGFVDaweelgPPGEPGYtwdtqknpMLRKGEAGPRKR--FDRvLLRGSDLKP 218
                         250       260       270
                  ....*....|....*....|....*....|
gi 2444586889 299 KRIKRLAK----------YGSDHFALLTEL 318
Cdd:cd09080   219 KSIELIGTepipgdeeglFPSDHFGLLAEL 248
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
233-296 7.43e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 41.16  E-value: 7.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 233 KKPTRPTIVAGDLNDVAWSRSTRLFMQISGFLD-----PRKGRGFYntfhanYFFMRW-PLDHLFHSPGF 296
Cdd:COG2374   250 ADPDAPVIVLGDFNDYPFEDPLRALLGAGGLTNlaeklPAAERYSY------VYDGNSgLLDHILVSPAL 313
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
103-318 9.12e-04

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: 40.16  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 103 IMSANV--LMSNHNSEQLISLVDKHQPDLLITLE--SDSWWENKLAVLKKNYPFYIECPKDNRY---GMHLYSK---FKI 172
Cdd:cd08372     1 VASYNVngLNAATRASGIARWVRELDPDIVCLQEvkDSQYSAVALNQLLPEGYHQYQSGPSRKEgyeGVAILSKtpkFKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 173 LDGQICELIEDDIPS-----IHILFENNEGLEMQGHFihpaPPSPTEEDssrPRDSELIMVAKALK----KPTRPTIVAG 243
Cdd:cd08372    81 VEKHQYKFGEGDSGErravvVKFDVHDKELCVVNAHL----QAGGTRAD---VRDAQLKEVLEFLKrlrqPNSAPVVICG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444586889 244 DLN--DVAWSRSTRlfmqiSGFLDPRKGRGF---YNTFHANY---FFMR---WPLDHLFHSPGF--KVKRIK-----RLA 305
Cdd:cd08372   154 DFNvrPSEVDSENP-----SSMLRLFVALNLvdsFETLPHAYtfdTYMHnvkSRLDYIFVSKSLlpSVKSSKilsdaARA 228
                         250
                  ....*....|...
gi 2444586889 306 KYGSDHFALLTEL 318
Cdd:cd08372   229 RIPSDHYPIEVTL 241
 
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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