sphingomyelin phosphodiesterase precursor [Mus musculus]
Protein Classification
sphingomyelin phosphodiesterase( domain architecture ID 18382240)
sphingomyelin phosphodiesterase catalyzes the conversion of sphingomyelin to ceramide
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| MPP_ASMase | cd00842 | acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ... |
199-494 | 2.43e-138 | |||||
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: 405.14 E-value: 2.43e-138
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| ASMase_C super family | cl44707 | Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ... |
472-593 | 1.39e-09 | |||||
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges. The actual alignment was detected with superfamily member pfam19272: Pssm-ID: 466022 Cd Length: 143 Bit Score: 56.61 E-value: 1.39e-09
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
85-158 | 8.35e-09 | |||||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. : Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 52.49 E-value: 8.35e-09
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| Name | Accession | Description | Interval | E-value | |||||
| MPP_ASMase | cd00842 | acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ... |
199-494 | 2.43e-138 | |||||
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: 405.14 E-value: 2.43e-138
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| CpdA | COG1409 | 3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; |
251-501 | 6.35e-11 | |||||
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; Pssm-ID: 441019 [Multi-domain] Cd Length: 234 Bit Score: 62.79 E-value: 6.35e-11
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| ASMase_C | pfam19272 | Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ... |
472-593 | 1.39e-09 | |||||
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges. Pssm-ID: 466022 Cd Length: 143 Bit Score: 56.61 E-value: 1.39e-09
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
85-158 | 8.35e-09 | |||||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 52.49 E-value: 8.35e-09
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| Metallophos | pfam00149 | Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ... |
252-349 | 7.05e-05 | |||||
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues. Pssm-ID: 459691 [Multi-domain] Cd Length: 114 Bit Score: 42.59 E-value: 7.05e-05
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| Name | Accession | Description | Interval | E-value | |||||
| MPP_ASMase | cd00842 | acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ... |
199-494 | 2.43e-138 | |||||
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: 405.14 E-value: 2.43e-138
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| CpdA | COG1409 | 3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; |
251-501 | 6.35e-11 | |||||
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; Pssm-ID: 441019 [Multi-domain] Cd Length: 234 Bit Score: 62.79 E-value: 6.35e-11
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| ASMase_C | pfam19272 | Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ... |
472-593 | 1.39e-09 | |||||
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges. Pssm-ID: 466022 Cd Length: 143 Bit Score: 56.61 E-value: 1.39e-09
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
85-158 | 8.35e-09 | |||||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 52.49 E-value: 8.35e-09
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| MPP_Nbla03831 | cd07396 | Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ... |
275-465 | 5.74e-08 | |||||
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 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: 277341 [Multi-domain] Cd Length: 245 Bit Score: 54.26 E-value: 5.74e-08
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| Metallophos | pfam00149 | Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ... |
252-349 | 7.05e-05 | |||||
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues. Pssm-ID: 459691 [Multi-domain] Cd Length: 114 Bit Score: 42.59 E-value: 7.05e-05
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