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Conserved domains on  [gi|71043890|ref|NP_001020908|]
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acid sphingomyelinase-like phosphodiesterase 3b precursor [Rattus norvegicus]

Protein Classification

acid sphingomyelinase family protein( domain architecture ID 17655516)

acid sphingomyelinase family protein such as human acid sphingomyelinase-like phosphodiesterase 3b, a lipid-modulating phosphodiesterase active on the surface of macrophages and dendritic cells

CATH:  3.60.21.10
EC:  3.1.4.-
Gene Ontology:  GO:0004767|GO:0046872|GO:0006685
PubMed:  15052326|19536191|23579450|8003970|25837850

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 1.19e-108

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: 323.10  E-value: 1.19e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  23 FWHISDLHLDPNYTVSKDPLrVCPSAG--------SQPVLNAGPWGDYLCDSPWALINSSIYAMKEIEPKPDFIFWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  95 TPHVPNERLGEGAVLSMvDRLTNLIKEVFPGTKVYAALGNHDFHPKNQLPAQSNS---IYTHVAELWRPWLSNESFTLFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 172 EGAFYSeklpSPSKTG-RVVVLNTNLYYSSNEQT-AGMADPGQQFQWLGDVLSNASRNGEMVYIIGHVPPGFFEKTQDka 249
Cdd:cd00842 159 KGGYYS----VDVKDGlRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD-- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71043890 250 wfresFNEEYLKVVQQHHRVIAGQFFGHHHTDSFRMFYSSTGA--PISVMFLTPGVTPWKttlpgvvdgANNPAIR 323
Cdd:cd00842 233 -----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTgsPINVAYIAPSVTPYT---------GNNPSFR 294
ASMase_C super family cl44707
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-429 2.52e-28

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: 109.00  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890   293 PISVMFLTPGVTPWKTTLPGVvdgANNPAIRIFEYDRATLNLKDMVTYYLNLRQADTQETPQWEQEYRLTEAYEVQDAST 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71043890   373 SSMY---TALTRIASEQhiLQRYYVYNSVSY-SHQPCEDVCRREHVCAIQHVEFDTYATCL 429
Cdd:pfam19272  79 QSLYglaKQFAVPHSKQ--FEKYYNYFFVSYdSSIVCEGGCKALQICAIMYLDYSSYTDCI 137
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 1.19e-108

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: 323.10  E-value: 1.19e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  23 FWHISDLHLDPNYTVSKDPLrVCPSAG--------SQPVLNAGPWGDYLCDSPWALINSSIYAMKEIEPKPDFIFWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  95 TPHVPNERLGEGAVLSMvDRLTNLIKEVFPGTKVYAALGNHDFHPKNQLPAQSNS---IYTHVAELWRPWLSNESFTLFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 172 EGAFYSeklpSPSKTG-RVVVLNTNLYYSSNEQT-AGMADPGQQFQWLGDVLSNASRNGEMVYIIGHVPPGFFEKTQDka 249
Cdd:cd00842 159 KGGYYS----VDVKDGlRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD-- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71043890 250 wfresFNEEYLKVVQQHHRVIAGQFFGHHHTDSFRMFYSSTGA--PISVMFLTPGVTPWKttlpgvvdgANNPAIR 323
Cdd:cd00842 233 -----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTgsPINVAYIAPSVTPYT---------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-429 2.52e-28

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: 109.00  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890   293 PISVMFLTPGVTPWKTTLPGVvdgANNPAIRIFEYDRATLNLKDMVTYYLNLRQADTQETPQWEQEYRLTEAYEVQDAST 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71043890   373 SSMY---TALTRIASEQhiLQRYYVYNSVSY-SHQPCEDVCRREHVCAIQHVEFDTYATCL 429
Cdd:pfam19272  79 QSLYglaKQFAVPHSKQ--FEKYYNYFFVSYdSSIVCEGGCKALQICAIMYLDYSSYTDCI 137
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
22-332 2.83e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.09  E-value: 2.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  22 RFWHISDLHLDPNytvskdplrvcPSAGSQPVLNAgpwgdylcdspwalinssiyAMKEI-EPKPDFIFWTGDDTPHVPN 100
Cdd:COG1409   2 RFAHISDLHLGAP-----------DGSDTAEVLAA--------------------ALADInAPRPDFVVVTGDLTDDGEP 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 101 ERLgeGAVLSMVDRLtnlikevfpGTKVYAALGNHDfhpknqlpaqsnsIYTHVAELWRPWLSNESftlfKEGAFYSEKL 180
Cdd:COG1409  51 EEY--AAAREILARL---------GVPVYVVPGNHD-------------IRAAMAEAYREYFGDLP----PGGLYYSFDY 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 181 PSpsktGRVVVLNTNLYYSSNeqtaGMADPgQQFQWLGDVLSNASRNgeMVYIIGHVPPGFFEKTQDKAWFRESfnEEYL 260
Cdd:COG1409 103 GG----VRFIGLDSNVPGRSS----GELGP-EQLAWLEEELAAAPAK--PVIVFLHHPPYSTGSGSDRIGLRNA--EELL 169

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71043890 261 KVVQQHHrvIAGQFFGHHHTDSFRMFYsstgapiSVMFLTPGVTPWKTTLPgvvdgannPAIRIFEYDRATL 332
Cdd:COG1409 170 ALLARYG--VDLVLSGHVHRYERTRRD-------GVPYIVAGSTGGQVRLP--------PGYRVIEVDGDGL 224
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 22-159 2.99e-03

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: 37.58  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890    22 RFWHISDLHLDPNYTVSKDPLRVCPSagsqpvlnagpwgdylcdspwalinssiyamkeiEPKPDFIFWTGDDTPHVPNE 101
Cdd:pfam00149   2 RILVIGDLHLPGQLDDLLELLKKLLE----------------------------------EGKPDLVLHAGDLVDRGPPS 47

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 71043890   102 rlgegavlsmvDRLTNLIKEVFPGTKVYAALGNHDFHPKNQLPAQSNsiYTHVAELWR 159
Cdd:pfam00149  48 -----------EEVLELLERLIKYVPVYLVRGNHDFDYGECLRLYPY--LGLLARPWK 92
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 1.19e-108

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: 323.10  E-value: 1.19e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  23 FWHISDLHLDPNYTVSKDPLrVCPSAG--------SQPVLNAGPWGDYLCDSPWALINSSIYAMKEIEPKPDFIFWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  95 TPHVPNERLGEGAVLSMvDRLTNLIKEVFPGTKVYAALGNHDFHPKNQLPAQSNS---IYTHVAELWRPWLSNESFTLFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 172 EGAFYSeklpSPSKTG-RVVVLNTNLYYSSNEQT-AGMADPGQQFQWLGDVLSNASRNGEMVYIIGHVPPGFFEKTQDka 249
Cdd:cd00842 159 KGGYYS----VDVKDGlRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD-- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71043890 250 wfresFNEEYLKVVQQHHRVIAGQFFGHHHTDSFRMFYSSTGA--PISVMFLTPGVTPWKttlpgvvdgANNPAIR 323
Cdd:cd00842 233 -----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTgsPINVAYIAPSVTPYT---------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-429 2.52e-28

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: 109.00  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890   293 PISVMFLTPGVTPWKTTLPGVvdgANNPAIRIFEYDRATLNLKDMVTYYLNLRQADTQETPQWEQEYRLTEAYEVQDAST 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71043890   373 SSMY---TALTRIASEQhiLQRYYVYNSVSY-SHQPCEDVCRREHVCAIQHVEFDTYATCL 429
Cdd:pfam19272  79 QSLYglaKQFAVPHSKQ--FEKYYNYFFVSYdSSIVCEGGCKALQICAIMYLDYSSYTDCI 137
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
22-332 2.83e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.09  E-value: 2.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  22 RFWHISDLHLDPNytvskdplrvcPSAGSQPVLNAgpwgdylcdspwalinssiyAMKEI-EPKPDFIFWTGDDTPHVPN 100
Cdd:COG1409   2 RFAHISDLHLGAP-----------DGSDTAEVLAA--------------------ALADInAPRPDFVVVTGDLTDDGEP 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 101 ERLgeGAVLSMVDRLtnlikevfpGTKVYAALGNHDfhpknqlpaqsnsIYTHVAELWRPWLSNESftlfKEGAFYSEKL 180
Cdd:COG1409  51 EEY--AAAREILARL---------GVPVYVVPGNHD-------------IRAAMAEAYREYFGDLP----PGGLYYSFDY 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 181 PSpsktGRVVVLNTNLYYSSNeqtaGMADPgQQFQWLGDVLSNASRNgeMVYIIGHVPPGFFEKTQDKAWFRESfnEEYL 260
Cdd:COG1409 103 GG----VRFIGLDSNVPGRSS----GELGP-EQLAWLEEELAAAPAK--PVIVFLHHPPYSTGSGSDRIGLRNA--EELL 169

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71043890 261 KVVQQHHrvIAGQFFGHHHTDSFRMFYsstgapiSVMFLTPGVTPWKTTLPgvvdgannPAIRIFEYDRATL 332
Cdd:COG1409 170 ALLARYG--VDLVLSGHVHRYERTRRD-------GVPYIVAGSTGGQVRLP--------PGYRVIEVDGDGL 224
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 82-302 3.50e-07

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: 51.18  E-value: 3.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  82 EPKPDFIFWTGDDTPHVPNERLGE---GAVLSMVDRltnlikevFPGtKVYAALGNHDFhpknqlpaqsnsiythvAELW 158
Cdd:cd07396  44 ESNLAFVVQLGDIIDGYNAKDRSKealDAVLSILDR--------LKG-PVHHVLGNHEF-----------------YNFP 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 159 RPWLSNESFTLFKEGAFYSEklpSPSKTGRVVVLNTNLYyssneqTAGMADpgQQFQWLGDVLSNASRNGEMVYIIGHVP 238
Cdd:cd07396  98 REYLNHLKTLNGEDAYYYSF---SPGPGFRFLVLDFVKF------NGGIGE--EQLAWLRNELTSADANGEKVIVLSHLP 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71043890 239 --PGFFEKtQDKAWFResfnEEYLKVVQQHHRVIAgQFFGHHH-----TDSFRMFYSSTGAPISVMFLTPG 302
Cdd:cd07396 167 iyPEAADP-QCLLWNY----EEVLAILESYPCVKA-CFSGHNHeggyeQDSHGVHHVTLEGVLETPPDSQA 231
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 69-295 6.87e-04

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 41.15  E-value: 6.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890  69 ALINSSIYAMKEIEPKPDFIFWTGDDTPHVPNERLGEgavlSMVDRLTNLIKEVFPGTKVYAALGNHDFhpKNQLPAQSN 148
Cdd:cd07395  35 ELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFRE----QQVSDLKDVLSKLDPDIPLVCVCGNHDV--GNTPTPETI 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 149 SIYTHVaelwrpwLSNESFTLFKEGAFYseklpspsktgrvVVLNTNLYYSSNEqTAGMADpgQQFQWLGDVLSNA-SRN 227
Cdd:cd07395 109 QRYRDD-------FGDDYFSFWVGGVFF-------------IVLNSQLFKDPSK-VPELAS--AQDQWLEEQLQIArESD 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890 228 GEMVYIIGHVPpgffektqdkaWFRESFNEE--YLKVVQQ---------HHRVIAGQFFGHHH------TDSFRMFYSS- 289
Cdd:cd07395 166 AKHVVVFQHIP-----------LFLEDPDEEddYFNIPKSvrrelldkfKKAGVKAVFSGHYHrnaggrYRDLEMVVTSa 234


                ....*.
gi 71043890 290 TGAPIS 295
Cdd:cd07395 235 VGCQLG 240
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 22-159 2.99e-03

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: 37.58  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043890    22 RFWHISDLHLDPNYTVSKDPLRVCPSagsqpvlnagpwgdylcdspwalinssiyamkeiEPKPDFIFWTGDDTPHVPNE 101
Cdd:pfam00149   2 RILVIGDLHLPGQLDDLLELLKKLLE----------------------------------EGKPDLVLHAGDLVDRGPPS 47

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 71043890   102 rlgegavlsmvDRLTNLIKEVFPGTKVYAALGNHDFHPKNQLPAQSNsiYTHVAELWR 159
Cdd:pfam00149  48 -----------EEVLELLERLIKYVPVYLVRGNHDFDYGECLRLYPY--LGLLARPWK 92
 
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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