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Conserved domains on  [gi|2780227898|ref|NP_001419209|]
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bis(5'-adenosyl)-triphosphatase enpp4 isoform 4 [Mus musculus]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

alkaline phosphatase (ALP) family protein may catalyze the hydrolysis of substrates; the ALP superfamily includes alkaline phosphatases and sulfatases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 24-89 5.60e-20

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.


The actual alignment was detected with superfamily member cd16018:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 267  Bit Score: 83.40  E-value: 5.60e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2780227898  24 IILVAEEGWTitlnkssfKLGDHGYDNSLPSMHPFLAAHGPAFRKGYRQSTINTVDIYPMMCHILG 89
Cdd:cd16018   210 IIVVSDHGMT--------DVGTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 24-89 5.60e-20

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: 83.40  E-value: 5.60e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2780227898  24 IILVAEEGWTitlnkssfKLGDHGYDNSLPSMHPFLAAHGPAFRKGYRQSTINTVDIYPMMCHILG 89
Cdd:cd16018   210 IIVVSDHGMT--------DVGTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 3-91 2.15e-12

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 63.61  E-value: 2.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227898   3 VYLKEAIpNRFYYQHSsRIQPIILVAEEGWTItlnkSSFKLGDHGYDNSlPSMHPFLAAHGPAFRKGyrqstINTVDIYP 82
Cdd:COG1524   292 VLTREEL-AAGHFGPH-RIGDLVLVAKPGWAL----DAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAP 359


                  ....*....
gi 2780227898  83 MMCHILGLK 91
Cdd:COG1524   360 TIARLLGLP 368
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-49 9.93e-10

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: 55.89  E-value: 9.93e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2780227898   1 MNVYLKEAIPNRFYYqhSSRIQPIILVAEEGWTITLNKS----SFKLGDHGYD 49
Cdd:pfam01663 293 LAVYLKEEIPGRLHY--NPRIPDLVLVADPGWYITGKDGgdkeAAIHGTHGYD 343
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 24-89 5.60e-20

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: 83.40  E-value: 5.60e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2780227898  24 IILVAEEGWTitlnkssfKLGDHGYDNSLPSMHPFLAAHGPAFRKGYRQSTINTVDIYPMMCHILG 89
Cdd:cd16018   210 IIVVSDHGMT--------DVGTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 3-91 2.15e-12

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 63.61  E-value: 2.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227898   3 VYLKEAIpNRFYYQHSsRIQPIILVAEEGWTItlnkSSFKLGDHGYDNSlPSMHPFLAAHGPAFRKGyrqstINTVDIYP 82
Cdd:COG1524   292 VLTREEL-AAGHFGPH-RIGDLVLVAKPGWAL----DAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAP 359


                  ....*....
gi 2780227898  83 MMCHILGLK 91
Cdd:COG1524   360 TIARLLGLP 368
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-49 9.93e-10

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: 55.89  E-value: 9.93e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2780227898   1 MNVYLKEAIPNRFYYqhSSRIQPIILVAEEGWTITLNKS----SFKLGDHGYD 49
Cdd:pfam01663 293 LAVYLKEEIPGRLHY--NPRIPDLVLVADPGWYITGKDGgdkeAAIHGTHGYD 343
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 4-95 4.39e-03

SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 36.36  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227898   4 YLKEAIPNRFYYQHSSriqPIILVAEEGWTItlNKSSFKLGDHG----YDNSLPSMhpFLaahGPAFRKGYRQSTINTVD 79
Cdd:cd16016   364 GIRERLRNGYNPKRSG---DLIVVLKPGWIE--GDGSGKGTTHGspydYDTHVPLL--FY---GWGIKPGEIPRPVEITD 433

                          90
                  ....*....|....*.
gi 2780227898  80 IYPMMCHILGLKPhPN 95
Cdd:cd16016   434 IAPTLAALLGIQP-PN 448
 
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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