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Conserved domains on  [gi|32566354|ref|NP_501020|]
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Endonuclease/exonuclease/phosphatase family protein [Caenorhabditis elegans]

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 662)

exonuclease/endonuclease/phosphatase (EEP) family protein may cleave phosphodiester bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 20-399 6.55e-22

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.


The actual alignment was detected with superfamily member cd09092:

Pssm-ID: 469791  Cd Length: 383  Bit Score: 96.38  E-value: 6.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354  20 DDDLIRAWCSEVAKEIYEQKCEFAVVHVQ---GLHSAENPDYAARVIcGCITDNPEIYRaFDSSMAFFDT------KLTG 90
Cdd:cd09092  17 PENLEKNWLREFLQTVHAHKPSFVALHLQevgGKNYEASMEHVEKFI-RELLSSDAMKD-FDRVRVYVDEdfksaeHFTA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354  91 LGNLY-LFKNHSDIQYYDrFSSTGYINVRSGHQHSigsnecDGFIQNTFGQNYTFRRDFYNDdgtrdLANQRTGFLLARF 169
Cdd:cd09092  95 LGSLYfIHKSLKNIYQFD-FHAKKYKKVTGKEIYS------GTLESVPTVEKEKFPQDFFPE-----CKWSRKGFMRTRW 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354 170 RIHGKELTFVNLNLhsvpFEDVNEIATKNSSITKAASKREQQIEMLLKELDEEGLRNDAILVAGSFNSQLHETDLLNYLA 249
Cdd:cd09092 163 KINNCVFDLVNIHL----FHDASNLAACESSPSVYSQNRHRALGYVLERLTDERFEKVPFFVFGDFNFRLDTKSVVETLC 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354 250 KTQLVQTVAKKDEDGNVESI-EHVDRHGRRTTTVERTRFDLHsiHDWFFRLGRGQMVKRYNGELANiaFKGNLKEETCFF 328
Cdd:cd09092 239 AKATMQTVRKADSNIVVKLEfREKDNDNKVVLQIEKKKFDYF--NQDVFRDNNGKALLKFDKELEV--FKDVLYELDISF 314

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566354 329 QPSRHYELNDSGKEEFQRTLCPAWSDRILYNDRMNELFKHDSfcASGLYYGLVAEEKFVGPHKPVALHASI 399
Cdd:cd09092 315 PPSYPYSEDPEQGTQYMNTRCPAWCDRILMSHSARELKSENE--EKSVTYDMIGPNVCMGDHKPVFLTFRI 383
 
Name Accession Description Interval E-value
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 20-399 6.55e-22

Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I (INPP5A) hydrolyzes the 5-phosphate from inositol 1,3,4,5-tetrakisphosphate [I(1,3,4,5)P4] and inositol 1,4,5-trisphosphate [I(1,4,5)P3]. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. As the substrates of INPP5A mobilize intracellular calcium ions, INPP5A is a calcium signal-terminating enzyme. In platelets, phosphorylated pleckstrin binds and activates INPP5A in a 1:1 complex, and accelerates the degradation of the calcium ion-mobilizing I(1,4,5)P3.


Pssm-ID: 197326  Cd Length: 383  Bit Score: 96.38  E-value: 6.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354  20 DDDLIRAWCSEVAKEIYEQKCEFAVVHVQ---GLHSAENPDYAARVIcGCITDNPEIYRaFDSSMAFFDT------KLTG 90
Cdd:cd09092  17 PENLEKNWLREFLQTVHAHKPSFVALHLQevgGKNYEASMEHVEKFI-RELLSSDAMKD-FDRVRVYVDEdfksaeHFTA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354  91 LGNLY-LFKNHSDIQYYDrFSSTGYINVRSGHQHSigsnecDGFIQNTFGQNYTFRRDFYNDdgtrdLANQRTGFLLARF 169
Cdd:cd09092  95 LGSLYfIHKSLKNIYQFD-FHAKKYKKVTGKEIYS------GTLESVPTVEKEKFPQDFFPE-----CKWSRKGFMRTRW 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354 170 RIHGKELTFVNLNLhsvpFEDVNEIATKNSSITKAASKREQQIEMLLKELDEEGLRNDAILVAGSFNSQLHETDLLNYLA 249
Cdd:cd09092 163 KINNCVFDLVNIHL----FHDASNLAACESSPSVYSQNRHRALGYVLERLTDERFEKVPFFVFGDFNFRLDTKSVVETLC 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354 250 KTQLVQTVAKKDEDGNVESI-EHVDRHGRRTTTVERTRFDLHsiHDWFFRLGRGQMVKRYNGELANiaFKGNLKEETCFF 328
Cdd:cd09092 239 AKATMQTVRKADSNIVVKLEfREKDNDNKVVLQIEKKKFDYF--NQDVFRDNNGKALLKFDKELEV--FKDVLYELDISF 314

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566354 329 QPSRHYELNDSGKEEFQRTLCPAWSDRILYNDRMNELFKHDSfcASGLYYGLVAEEKFVGPHKPVALHASI 399
Cdd:cd09092 315 PPSYPYSEDPEQGTQYMNTRCPAWCDRILMSHSARELKSENE--EKSVTYDMIGPNVCMGDHKPVFLTFRI 383
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 163-237 3.65e-04

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 41.05  E-value: 3.65e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32566354 163 GFLLARFRIHGKELTFVNLNLHSVpfedvneiatknssitkAASKREQQIEMLLKELDEEGlRNDAILVAGSFNS 237
Cdd:COG3568  72 GALWADVDVPGKPLRVVNTHLDLR-----------------SAAARRRQARALAELLAELP-AGAPVILAGDFND 128
 
Name Accession Description Interval E-value
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 20-399 6.55e-22

Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I (INPP5A) hydrolyzes the 5-phosphate from inositol 1,3,4,5-tetrakisphosphate [I(1,3,4,5)P4] and inositol 1,4,5-trisphosphate [I(1,4,5)P3]. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. As the substrates of INPP5A mobilize intracellular calcium ions, INPP5A is a calcium signal-terminating enzyme. In platelets, phosphorylated pleckstrin binds and activates INPP5A in a 1:1 complex, and accelerates the degradation of the calcium ion-mobilizing I(1,4,5)P3.


Pssm-ID: 197326  Cd Length: 383  Bit Score: 96.38  E-value: 6.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354  20 DDDLIRAWCSEVAKEIYEQKCEFAVVHVQ---GLHSAENPDYAARVIcGCITDNPEIYRaFDSSMAFFDT------KLTG 90
Cdd:cd09092  17 PENLEKNWLREFLQTVHAHKPSFVALHLQevgGKNYEASMEHVEKFI-RELLSSDAMKD-FDRVRVYVDEdfksaeHFTA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354  91 LGNLY-LFKNHSDIQYYDrFSSTGYINVRSGHQHSigsnecDGFIQNTFGQNYTFRRDFYNDdgtrdLANQRTGFLLARF 169
Cdd:cd09092  95 LGSLYfIHKSLKNIYQFD-FHAKKYKKVTGKEIYS------GTLESVPTVEKEKFPQDFFPE-----CKWSRKGFMRTRW 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354 170 RIHGKELTFVNLNLhsvpFEDVNEIATKNSSITKAASKREQQIEMLLKELDEEGLRNDAILVAGSFNSQLHETDLLNYLA 249
Cdd:cd09092 163 KINNCVFDLVNIHL----FHDASNLAACESSPSVYSQNRHRALGYVLERLTDERFEKVPFFVFGDFNFRLDTKSVVETLC 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354 250 KTQLVQTVAKKDEDGNVESI-EHVDRHGRRTTTVERTRFDLHsiHDWFFRLGRGQMVKRYNGELANiaFKGNLKEETCFF 328
Cdd:cd09092 239 AKATMQTVRKADSNIVVKLEfREKDNDNKVVLQIEKKKFDYF--NQDVFRDNNGKALLKFDKELEV--FKDVLYELDISF 314

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566354 329 QPSRHYELNDSGKEEFQRTLCPAWSDRILYNDRMNELFKHDSfcASGLYYGLVAEEKFVGPHKPVALHASI 399
Cdd:cd09092 315 PPSYPYSEDPEQGTQYMNTRCPAWCDRILMSHSARELKSENE--EKSVTYDMIGPNVCMGDHKPVFLTFRI 383
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 163-237 3.65e-04

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 41.05  E-value: 3.65e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32566354 163 GFLLARFRIHGKELTFVNLNLHSVpfedvneiatknssitkAASKREQQIEMLLKELDEEGlRNDAILVAGSFNS 237
Cdd:COG3568  72 GALWADVDVPGKPLRVVNTHLDLR-----------------SAAARRRQARALAELLAELP-AGAPVILAGDFND 128
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 142-261 1.85e-03

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: 39.77  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566354 142 YTFRRDFYNDDGTRDLANQR----TGFLLARFRIHGKELTFVNLNLHsvpfedvneiatknsSITKAASKREQQIEMLLK 217
Cdd:cd08372  72 LSKTPKFKIVEKHQYKFGEGdsgeRRAVVVKFDVHDKELCVVNAHLQ---------------AGGTRADVRDAQLKEVLE 136

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32566354 218 ELDEEGLRNDA-ILVAGSFNSQLHETDLLNYLAKTQLVQTVAKKD 261
Cdd:cd08372 137 FLKRLRQPNSApVVICGDFNVRPSEVDSENPSSMLRLFVALNLVD 181
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 317-395 1.89e-03

Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate 5-phosphatases (5-phosphatases) are signal-modifying enzymes, which hydrolyze the 5-phosphate from the inositol ring of specific 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), such as PI(4,5)P2, PI(3,4,5)P3, PI(3,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4. These enzymes are Mg2+-dependent, 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. In addition to this INPP5c domain, 5-phosphatases often contain additional domains and motifs, such as the SH2 domain, the Sac-1 domain, the proline-rich domain (PRD), CAAX, RhoGAP (RhoGTPase-activating protein), and SKICH [SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) carboxyl homology] domains, that are important for protein-protein interactions and/or for the subcellular localization of these enzymes. 5-phosphatases incorporate into large signaling complexes, and regulate diverse cellular processes including postsynaptic vesicular trafficking, insulin signaling, cell growth and survival, and endocytosis. Loss or gain of function of 5-phosphatases is implicated in certain human diseases. This family also contains a functionally unrelated nitric oxide transport protein, Cimex lectularius (bedbug) nitrophorin, which catalyzes a heme-assisted S-nitrosation of a proximal thiolate; the heme however binds at a site distinct from the active site of the 5-phosphatases.


Pssm-ID: 197308 [Multi-domain]  Cd Length: 299  Bit Score: 40.01  E-value: 1.89e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32566354 317 FKGNLKEETCFFQPSRHYELNDSGKEEFQRTLCPAWSDRILYNDRmNELFkhdsfcASGLYYGLVAEEKFvGPHKPVAL 395
Cdd:cd09074 225 VFDGFQELPITFPPTYKFDPGTDEYDTSDKKRIPAWCDRILYKSK-AGSE------IQPLSYTSVPLYKT-SDHKPVRA 295
 
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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