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Conserved domains on  [gi|294658978|ref|XP_461311|]
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DEHA2F22264p [Debaryomyces hansenii CBS767]

Protein Classification

PPN1 endopolyphosphatase family protein( domain architecture ID 10096153)

PPN1 endopolyphosphatase family protein such as human sphingomyelinase-like phosphodiesterase 3a, which does not have sphingomyelinase activity, but has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates such as ATP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 97-379 1.28e-80

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


:

Pssm-ID: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 258.38  E-value: 1.28e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978  97 FLHITDMHPDKYYKTGADVgSLCHSGKGS------------AGKYGDAvlGCDSPMVLMEDTLKWVKENLkDKIDFVVWT 164
Cdd:cd00842    1 FLHISDIHYDPLYKVGSEY-ANCRSPLCCrdesgpgdvkppAGYWGTY--GCDSPWSLVESALEAIKKNH-PKPDFILWT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978 165 GDNVRHDNDRRYPRTESNIfdmNQRVSELMYETFKeenprggrprqlKIPLVPSLGNNDVFPHNLFSP---GPTLQTREL 241
Cdd:cd00842   77 GDLVRHDVDEQTPEETVES---ESNLTNLLKKYFP------------NVPVYPALGNHDSYPVNQFPPhsnSPSWLYDAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978 242 FKIWHDFVPAAQLHIFNRGAYFFKEIIPNeLAVLSINTLYLFQSNPLVDncDRKKDPGHkLFEWLGYTLKEMRARNMKVW 321
Cdd:cd00842  142 AELWKPWLPTEAKETFKKGGYYSVDVKDG-LRVISLNTNLYYKKNFWLY--SNNTDPCG-QLQWLEDELEDAEQKGEKVW 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294658978 322 LSGHVPPNEKNYDISCLRKYIVWMHEYRDVIIGGLYGHMNIDHFIPLDSKEAYKSIKN 379
Cdd:cd00842  218 IIGHIPPGLNSYDADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPIN 275
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 97-379 1.28e-80

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 258.38  E-value: 1.28e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978  97 FLHITDMHPDKYYKTGADVgSLCHSGKGS------------AGKYGDAvlGCDSPMVLMEDTLKWVKENLkDKIDFVVWT 164
Cdd:cd00842    1 FLHISDIHYDPLYKVGSEY-ANCRSPLCCrdesgpgdvkppAGYWGTY--GCDSPWSLVESALEAIKKNH-PKPDFILWT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978 165 GDNVRHDNDRRYPRTESNIfdmNQRVSELMYETFKeenprggrprqlKIPLVPSLGNNDVFPHNLFSP---GPTLQTREL 241
Cdd:cd00842   77 GDLVRHDVDEQTPEETVES---ESNLTNLLKKYFP------------NVPVYPALGNHDSYPVNQFPPhsnSPSWLYDAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978 242 FKIWHDFVPAAQLHIFNRGAYFFKEIIPNeLAVLSINTLYLFQSNPLVDncDRKKDPGHkLFEWLGYTLKEMRARNMKVW 321
Cdd:cd00842  142 AELWKPWLPTEAKETFKKGGYYSVDVKDG-LRVISLNTNLYYKKNFWLY--SNNTDPCG-QLQWLEDELEDAEQKGEKVW 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294658978 322 LSGHVPPNEKNYDISCLRKYIVWMHEYRDVIIGGLYGHMNIDHFIPLDSKEAYKSIKN 379
Cdd:cd00842  218 IIGHIPPGLNSYDADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPIN 275
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
96-264 3.58e-04

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 42.76  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978  96 RFLHITDMHPDKYyktgadvgslchsgkgsagkygdavLGCDSPMVLmEDTLKWVKENlkdKIDFVVWTGDNVRHDNDRR 175
Cdd:COG1409    2 RFAHISDLHLGAP-------------------------DGSDTAEVL-AAALADINAP---RPDFVVVTGDLTDDGEPEE 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978 176 YprtesnifdmnQRVSELMyetfkeenprggrpRQLKIPLVPSLGNNDVFPHNlfspgptlqTRELFKIWHDFVPAAQLH 255
Cdd:COG1409   53 Y-----------AAAREIL--------------ARLGVPVYVVPGNHDIRAAM---------AEAYREYFGDLPPGGLYY 98


                 ....*....
gi 294658978 256 IFNRGAYFF 264
Cdd:COG1409   99 SFDYGGVRF 107
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 97-379 1.28e-80

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 258.38  E-value: 1.28e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978  97 FLHITDMHPDKYYKTGADVgSLCHSGKGS------------AGKYGDAvlGCDSPMVLMEDTLKWVKENLkDKIDFVVWT 164
Cdd:cd00842    1 FLHISDIHYDPLYKVGSEY-ANCRSPLCCrdesgpgdvkppAGYWGTY--GCDSPWSLVESALEAIKKNH-PKPDFILWT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978 165 GDNVRHDNDRRYPRTESNIfdmNQRVSELMYETFKeenprggrprqlKIPLVPSLGNNDVFPHNLFSP---GPTLQTREL 241
Cdd:cd00842   77 GDLVRHDVDEQTPEETVES---ESNLTNLLKKYFP------------NVPVYPALGNHDSYPVNQFPPhsnSPSWLYDAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978 242 FKIWHDFVPAAQLHIFNRGAYFFKEIIPNeLAVLSINTLYLFQSNPLVDncDRKKDPGHkLFEWLGYTLKEMRARNMKVW 321
Cdd:cd00842  142 AELWKPWLPTEAKETFKKGGYYSVDVKDG-LRVISLNTNLYYKKNFWLY--SNNTDPCG-QLQWLEDELEDAEQKGEKVW 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294658978 322 LSGHVPPNEKNYDISCLRKYIVWMHEYRDVIIGGLYGHMNIDHFIPLDSKEAYKSIKN 379
Cdd:cd00842  218 IIGHIPPGLNSYDADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPIN 275
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
96-264 3.58e-04

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 42.76  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978  96 RFLHITDMHPDKYyktgadvgslchsgkgsagkygdavLGCDSPMVLmEDTLKWVKENlkdKIDFVVWTGDNVRHDNDRR 175
Cdd:COG1409    2 RFAHISDLHLGAP-------------------------DGSDTAEVL-AAALADINAP---RPDFVVVTGDLTDDGEPEE 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294658978 176 YprtesnifdmnQRVSELMyetfkeenprggrpRQLKIPLVPSLGNNDVFPHNlfspgptlqTRELFKIWHDFVPAAQLH 255
Cdd:COG1409   53 Y-----------AAAREIL--------------ARLGVPVYVVPGNHDIRAAM---------AEAYREYFGDLPPGGLYY 98


                 ....*....
gi 294658978 256 IFNRGAYFF 264
Cdd:COG1409   99 SFDYGGVRF 107
 
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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