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Conserved domains on  [gi|6114760|emb|CAB59427|]
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phosphodiesterase I/nucleotide pyrophosphatase, partial [Rattus norvegicus]

Protein Classification

nucleotide pyrophosphatase/phosphodiesterase family protein( domain architecture ID 12025720)

nucleotide pyrophosphatase/phosphodiesterase family protein catalyzes the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and/or nucleotide sugars; belongs to the alkaline phosphatase superfamily

CATH:  3.40.720.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  12757929|11027689|11202013

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-151 4.87e-37

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


:

Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 129.46  E-value: 4.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760      1 SVPYESRIATLL--QWLDLPKA----ERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCV 74
Cdd:pfam01663 135 SVPFEDRVDTAVlqTWLDLPFAdvaaERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDT 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760     75 NIIVLADHGMDQTSCDRVEYMTDYFPEINFY--MYQGPAPRIRTR-----NIPQDFFTFNSEKIVRDLSCR--KSDQHFK 145
Cdd:pfam01663 215 NVIVVSDHGMTPVSDDKVIFLNDYLREKGLLhlVDGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLA 294


                  ....*.
gi 6114760    146 PYLTPD 151
Cdd:pfam01663 295 VYLKEE 300
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-151 4.87e-37

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 129.46  E-value: 4.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760      1 SVPYESRIATLL--QWLDLPKA----ERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCV 74
Cdd:pfam01663 135 SVPFEDRVDTAVlqTWLDLPFAdvaaERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDT 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760     75 NIIVLADHGMDQTSCDRVEYMTDYFPEINFY--MYQGPAPRIRTR-----NIPQDFFTFNSEKIVRDLSCR--KSDQHFK 145
Cdd:pfam01663 215 NVIVVSDHGMTPVSDDKVIFLNDYLREKGLLhlVDGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLA 294


                  ....*.
gi 6114760    146 PYLTPD 151
Cdd:pfam01663 295 VYLKEE 300
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 1-87 5.85e-32

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 114.22  E-value: 5.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760    1 SVPYESRIATLLQWLDLpkaERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLA 80
Cdd:cd16018 138 SFPFEERVDTILEWLDL---ERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVS 214


                ....*..
gi 6114760   81 DHGMDQT 87
Cdd:cd16018 215 DHGMTDV 221
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 4-88 1.90e-22

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 90.96  E-value: 1.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760    4 YESRIATLLQWLDLPKAERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHG 83
Cdd:COG1524 164 PAADRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243


                ....*
gi 6114760   84 MDQTS 88
Cdd:COG1524 244 MVDVP 248
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-151 4.87e-37

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 129.46  E-value: 4.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760      1 SVPYESRIATLL--QWLDLPKA----ERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCV 74
Cdd:pfam01663 135 SVPFEDRVDTAVlqTWLDLPFAdvaaERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDT 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760     75 NIIVLADHGMDQTSCDRVEYMTDYFPEINFY--MYQGPAPRIRTR-----NIPQDFFTFNSEKIVRDLSCR--KSDQHFK 145
Cdd:pfam01663 215 NVIVVSDHGMTPVSDDKVIFLNDYLREKGLLhlVDGGPVVAIYPKarelgHVPPGEVEEVYAELKEKLLGLriQDGEHLA 294


                  ....*.
gi 6114760    146 PYLTPD 151
Cdd:pfam01663 295 VYLKEE 300
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 1-87 5.85e-32

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 114.22  E-value: 5.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760    1 SVPYESRIATLLQWLDLpkaERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLA 80
Cdd:cd16018 138 SFPFEERVDTILEWLDL---ERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVS 214


                ....*..
gi 6114760   81 DHGMDQT 87
Cdd:cd16018 215 DHGMTDV 221
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 4-88 1.90e-22

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 90.96  E-value: 1.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760    4 YESRIATLLQWLDLPKAERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHG 83
Cdd:COG1524 164 PAADRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243


                ....*
gi 6114760   84 MDQTS 88
Cdd:COG1524 244 MVDVP 248
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 4-85 8.46e-13

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 63.21  E-value: 8.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6114760    4 YESRIATLLQWLDLPKAERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHG 83
Cdd:cd00016 101 YRTGVIGLLKAIDETSKEKPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180


                ..
gi 6114760   84 MD 85
Cdd:cd00016 181 GI 182
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
 4-82 5.82e-04

uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).


Pssm-ID: 293735  Cd Length: 368  Bit Score: 38.61  E-value: 5.82e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6114760    4 YESRIATLLQWLDlpkaeRPSFYTIYVEEPDSAGHKSGPvsAGVIKALQLVDDAFGMLMEGLKQRnlhNCVNIIVLADH 82
Cdd:cd16011 243 YEGKAEAALEALK-----DYDFVFVHVKAPDEAGHDGDP--EAKVKAIERIDKAIVGPLLELLDG---EDFVIVVTPDH 311
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 54-98 6.02e-03

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 35.67  E-value: 6.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6114760   54 VDDAFGMLMEGLKQRNLHNCVNIIVLADHGmdqtscdrvEYMTDY 98
Cdd:cd16150 209 LDHQFGRLLEALKETGLYDDTAVFFFSDHG---------DYTGDY 244
 
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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