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Conserved domains on  [gi|57242800|ref|NP_001009568|]
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acid sphingomyelinase-like phosphodiesterase 3b isoform 2 precursor [Homo sapiens]

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 ...
 23-323 3.83e-118

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: 344.28  E-value: 3.83e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  23 FWHIADLHLDPDYKVSKDpFQVCPSAG--------SQPVPDAGPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSE-YANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  95 TPHVPDEKLGEAAVLEIvERLTKLIREVFPDTKVYAALGNHDFHPKNQFPAGSNN---IYNQIAELWKPWLSNESIALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 172 KGAFYCEKlpgPSGAGRIVVLNTNLYYTSNALT-ADMADPGQQFQWLEDVLTDASKAGDMVYIVGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57242800 251 fregFNEKYLKVVRKHHRVIAGQFFGHHHTDSFRMLYDD--AGVPISAMFITPGVTPWKttlpgvvngANNPAIR 323
Cdd:cd00842 233 ----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDkdTGSPINVAYIAPSVTPYT---------GNNPSFR 294
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 3.83e-118

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: 344.28  E-value: 3.83e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  23 FWHIADLHLDPDYKVSKDpFQVCPSAG--------SQPVPDAGPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSE-YANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  95 TPHVPDEKLGEAAVLEIvERLTKLIREVFPDTKVYAALGNHDFHPKNQFPAGSNN---IYNQIAELWKPWLSNESIALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 172 KGAFYCEKlpgPSGAGRIVVLNTNLYYTSNALT-ADMADPGQQFQWLEDVLTDASKAGDMVYIVGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57242800 251 fregFNEKYLKVVRKHHRVIAGQFFGHHHTDSFRMLYDD--AGVPISAMFITPGVTPWKttlpgvvngANNPAIR 323
Cdd:cd00842 233 ----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDkdTGSPINVAYIAPSVTPYT---------GNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
22-338 8.55e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 64.33  E-value: 8.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  22 KFWHIADLHLDPDykvskdpfqvcpsAGSQPVPDAGPwgdylcdspwalinssiyAMKEI-EPEPDFILWTGDDTPHVPD 100
Cdd:COG1409   2 RFAHISDLHLGAP-------------DGSDTAEVLAA------------------ALADInAPRPDFVVVTGDLTDDGEP 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 101 EKLgeAAVLEIVERLtklirevfpDTKVYAALGNHDfhpknqfpagsnnIYNQIAELWKPWLSNESIAlfkkGAFYCEKL 180
Cdd:COG1409  51 EEY--AAAREILARL---------GVPVYVVPGNHD-------------IRAAMAEAYREYFGDLPPG----GLYYSFDY 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 181 PGpsgaGRIVVLNTNLYYTSN-ALTADmadpgqQFQWLEDVLTDASKagDMVYIVGHVPPGFFEKTQNKAWFREGfnEKY 259
Cdd:COG1409 103 GG----VRFIGLDSNVPGRSSgELGPE------QLAWLEEELAAAPA--KPVIVFLHHPPYSTGSGSDRIGLRNA--EEL 168

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57242800 260 LKVVRKHHrvIAGQFFGHHHTDSFRMlydDAGVPIsamFITPGVTPWKTTLPGVvngannpaiRVFEYDRATLSLKVRS 338
Cdd:COG1409 169 LALLARYG--VDLVLSGHVHRYERTR---RDGVPY---IVAGSTGGQVRLPPGY---------RVIEVDGDGLTVEVRR 230
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 22-144 7.65e-04

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: 38.73  E-value: 7.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800    22 KFWHIADLHLDPDYKVSKDPFQVCPSagsqpvpdagpwgdylcdspwalinssiyamkeiEPEPDFILWTGDdtphVPDE 101
Cdd:pfam00149   2 RILVIGDLHLPGQLDDLLELLKKLLE----------------------------------EGKPDLVLHAGD----LVDR 43

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 57242800   102 KLGEAAVLEIVERLTKLIrevfpdtKVYAALGNHDFHPKNQFP 144
Cdd:pfam00149  44 GPPSEEVLELLERLIKYV-------PVYLVRGNHDFDYGECLR 79
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 3.83e-118

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: 344.28  E-value: 3.83e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  23 FWHIADLHLDPDYKVSKDpFQVCPSAG--------SQPVPDAGPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSE-YANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  95 TPHVPDEKLGEAAVLEIvERLTKLIREVFPDTKVYAALGNHDFHPKNQFPAGSNN---IYNQIAELWKPWLSNESIALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 172 KGAFYCEKlpgPSGAGRIVVLNTNLYYTSNALT-ADMADPGQQFQWLEDVLTDASKAGDMVYIVGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57242800 251 fregFNEKYLKVVRKHHRVIAGQFFGHHHTDSFRMLYDD--AGVPISAMFITPGVTPWKttlpgvvngANNPAIR 323
Cdd:cd00842 233 ----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDkdTGSPINVAYIAPSVTPYT---------GNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
22-338 8.55e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 64.33  E-value: 8.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  22 KFWHIADLHLDPDykvskdpfqvcpsAGSQPVPDAGPwgdylcdspwalinssiyAMKEI-EPEPDFILWTGDDTPHVPD 100
Cdd:COG1409   2 RFAHISDLHLGAP-------------DGSDTAEVLAA------------------ALADInAPRPDFVVVTGDLTDDGEP 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 101 EKLgeAAVLEIVERLtklirevfpDTKVYAALGNHDfhpknqfpagsnnIYNQIAELWKPWLSNESIAlfkkGAFYCEKL 180
Cdd:COG1409  51 EEY--AAAREILARL---------GVPVYVVPGNHD-------------IRAAMAEAYREYFGDLPPG----GLYYSFDY 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 181 PGpsgaGRIVVLNTNLYYTSN-ALTADmadpgqQFQWLEDVLTDASKagDMVYIVGHVPPGFFEKTQNKAWFREGfnEKY 259
Cdd:COG1409 103 GG----VRFIGLDSNVPGRSSgELGPE------QLAWLEEELAAAPA--KPVIVFLHHPPYSTGSGSDRIGLRNA--EEL 168

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57242800 260 LKVVRKHHrvIAGQFFGHHHTDSFRMlydDAGVPIsamFITPGVTPWKTTLPGVvngannpaiRVFEYDRATLSLKVRS 338
Cdd:COG1409 169 LALLARYG--VDLVLSGHVHRYERTR---RDGVPY---IVAGSTGGQVRLPPGY---------RVIEVDGDGLTVEVRR 230
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 82-279 9.57e-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: 52.33  E-value: 9.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  82 EPEPDFILWTGDDTPHVPDEKLGEAAVLEIVERLTKLirevfpDTKVYAALGNHDFhpknqfpagsnniYNqiaeLWKPW 161
Cdd:cd07396  44 ESNLAFVVQLGDIIDGYNAKDRSKEALDAVLSILDRL------KGPVHHVLGNHEF-------------YN----FPREY 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 162 LSNESIALFKKGAFYCEKlpgPSGAGRIVVLNTNLYytsNALTADmadpgQQFQWLEDVLTDASKAGDMVYIVGHVP--P 239
Cdd:cd07396 101 LNHLKTLNGEDAYYYSFS---PGPGFRFLVLDFVKF---NGGIGE-----EQLAWLRNELTSADANGEKVIVLSHLPiyP 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 57242800 240 GFFEKTQNkAWFREGFnekyLKVVRKHHRVIAgQFFGHHH 279
Cdd:cd07396 170 EAADPQCL-LWNYEEV----LAILESYPCVKA-CFSGHNH 203
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 25-305 1.68e-05

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 45.73  E-value: 1.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  25 HIADLHLDPDykvskdpfqvcpsagsqpvpdagPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDDTPHVPDEKLG 104
Cdd:cd07402   3 QISDTHLFAP-----------------------GEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYE 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 105 EAAvlEIVERLTKlirevfpdtKVYAALGNHDFHPKnqfpagsnniYNQIAELwKPWLSNESIALFKkgafyceklpgPS 184
Cdd:cd07402  60 RLR--ELLAPLPA---------PVYWIPGNHDDRAA----------MREALPE-PPYDDNGPVQYVV-----------DF 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800 185 GAGRIVVLNtnlyyTSNALTADMADPGQQFQWLEDVLtdaSKAGDM-VYIVGHVPP---GFfektqnkAWFRE---GFNE 257
Cdd:cd07402 107 GGWRLILLD-----TSVPGVHHGELSDEQLDWLEAAL---AEAPDRpTLIFLHHPPfplGI-------PWMDAirlRNSQ 171

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 57242800 258 KYLKVVRKHHRVIAgQFFGHHHTDSFRMLyddAGVPISamfITPGVTP 305
Cdd:cd07402 172 ALFAVLARHPQVKA-ILCGHIHRPISGSF---RGIPFS---TAPSTCH 212
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 22-144 7.65e-04

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: 38.73  E-value: 7.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800    22 KFWHIADLHLDPDYKVSKDPFQVCPSagsqpvpdagpwgdylcdspwalinssiyamkeiEPEPDFILWTGDdtphVPDE 101
Cdd:pfam00149   2 RILVIGDLHLPGQLDDLLELLKKLLE----------------------------------EGKPDLVLHAGD----LVDR 43

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 57242800   102 KLGEAAVLEIVERLTKLIrevfpdtKVYAALGNHDFHPKNQFP 144
Cdd:pfam00149  44 GPPSEEVLELLERLIKYV-------PVYLVRGNHDFDYGECLR 79
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-328 1.53e-03

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: 38.51  E-value: 1.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 57242800   293 PISAMFITPGVTPWKTTLPGVvngANNPAIRVFEYD 328
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYD 34
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
84-174 2.89e-03

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 39.01  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  84 EPDFILWTGD--DTPHVPDEklgeaAVLEIVERLTKlirevfPDtKVYAALGNHDFHpknqfpAGSNNIYNQIAEL-WKp 160
Cdd:COG1408  73 KPDLVVLTGDlvDGSVAELE-----ALLELLKKLKA------PL-GVYAVLGNHDYY------AGLEELRAALEEAgVR- 133

                        90
                ....*....|....
gi 57242800 161 WLSNESIALFKKGA 174
Cdd:COG1408 134 VLRNEAVTLERGGD 147
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
22-145 5.77e-03

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 37.97  E-value: 5.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242800  22 KFWHIADLHLD-PDYKVS--KDPFQVCpsagsqpvpdagpwgDYLCDspwalinssiYAmkeIEPEPDFILWTGD--DTP 96
Cdd:COG0420   2 RFLHTADWHLGkPLHGASrrEDQLAAL---------------DRLVD----------LA---IEEKVDAVLIAGDlfDSA 53

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 57242800  97 HVPDEklgeaAVLEIVERLTKLIREvfpDTKVYAALGNHDFHPKNQFPA 145
Cdd:COG0420  54 NPSPE-----AVRLLAEALRRLSEA---GIPVVLIAGNHDSPSRLSAGS 94
 
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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