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Conserved domains on  [gi|320091592|gb|ADW09000|]
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sphingomyelin phosphodiesterase 1 precursor isoform 5 [Homo sapiens]

Protein Classification

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 ...
 201-473 9.37e-121

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: 359.31  E-value: 9.37e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 201 ILFLTDLHWDHDYLEG-TDPDCADPLCCRRGSGLPPASrPGAGYWGEYsKCDLPLRTLESLLSGLGP-AGPFDMVYWTGD 278
Cdd:cd00842    1 FLHISDIHYDPLYKVGsEYANCRSPLCCRDESGPGDVK-PPAGYWGTY-GCDSPWSLVESALEAIKKnHPKPDFILWTGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 279 IPAHDVWHQTRQDQLRALTTVTALVRKFLGPVPVYPAVGNHESTPVNSFPPPfiegNHSSRWLYEAMAKAWEPWLPAEA- 357
Cdd:cd00842   79 LVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPH----SNSPSWLYDALAELWKPWLPTEAk 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 358 ----------------LRTLS------SRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGH--CLKSWS 413
Cdd:cd00842  155 etfkkggyysvdvkdgLRVISlntnlyYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLnsYDADWS 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 414 WNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAFLAPSATTYIGLNPGYR 473
Cdd:cd00842  235 ERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPINVAYIAPSVTPYTGNNPSFR 294
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 87-160 1.01e-07

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: 49.41  E-value: 1.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320091592    87 LTCPICKGLFTAINLGLKKEPNVARVGSVAIKLCNLLKIAPPAVCQSIVHLFEDDMVEVWRRsVLSPSEACGLL 160
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQ-GLDPKDVCQKL 73
ASMase_C super family cl44707
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 451-572 3.05e-07

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: 50.06  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592  451 RPLAVAFLAPSATTYIGL------NPGYRVYQID-GNYSrsshvVLDHETYILNLTQANIPGAiPHWQLLYRARETYGLP 523
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVlekesnNPGVRLYQYDpKDYK-----LLDMLQYYLNLTEANLKGE-SNWKLEYILTKAYGIE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 320091592  524 NTLPTAWHNLVYR-MRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCA 572
Cdd:pfam19272  75 DLQPQSLYGLAKQfAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICA 124
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 201-473 9.37e-121

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: 359.31  E-value: 9.37e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 201 ILFLTDLHWDHDYLEG-TDPDCADPLCCRRGSGLPPASrPGAGYWGEYsKCDLPLRTLESLLSGLGP-AGPFDMVYWTGD 278
Cdd:cd00842    1 FLHISDIHYDPLYKVGsEYANCRSPLCCRDESGPGDVK-PPAGYWGTY-GCDSPWSLVESALEAIKKnHPKPDFILWTGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 279 IPAHDVWHQTRQDQLRALTTVTALVRKFLGPVPVYPAVGNHESTPVNSFPPPfiegNHSSRWLYEAMAKAWEPWLPAEA- 357
Cdd:cd00842   79 LVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPH----SNSPSWLYDALAELWKPWLPTEAk 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 358 ----------------LRTLS------SRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGH--CLKSWS 413
Cdd:cd00842  155 etfkkggyysvdvkdgLRVISlntnlyYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLnsYDADWS 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 414 WNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAFLAPSATTYIGLNPGYR 473
Cdd:cd00842  235 ERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPINVAYIAPSVTPYTGNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
253-480 4.70e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.09  E-value: 4.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 253 PLRTLESLLSGLgPAGPFDMVYWTGDIpAHDvwhqTRQDQLRALTtvtALVRKFlgPVPVYPAVGNHEstpvnsfpppfi 332
Cdd:COG1409   19 TAEVLAAALADI-NAPRPDFVVVTGDL-TDD----GEPEEYAAAR---EILARL--GVPVYVVPGNHD------------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 333 egnhssrwLYEAMAKAWEPWLPAEALRTL--SSRENFWLLI--NSTDP--------AGQLQWLVGELQAAEDRgdKVHII 400
Cdd:COG1409   76 --------IRAAMAEAYREYFGDLPPGGLyySFDYGGVRFIglDSNVPgrssgelgPEQLAWLEEELAAAPAK--PVIVF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 401 GHIPPGHCLkSWSWNYY--------RIVARYENTLAaqFFGHTHVDEFEVFYdeetlSRPLAVaflAPSATTYIGLNPGY 472
Cdd:COG1409  146 LHHPPYSTG-SGSDRIGlrnaeellALLARYGVDLV--LSGHVHRYERTRRD-----GVPYIV---AGSTGGQVRLPPGY 214


                 ....*...
gi 320091592 473 RVYQIDGN 480
Cdd:COG1409  215 RVIEVDGD 222
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 87-160 1.01e-07

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: 49.41  E-value: 1.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320091592    87 LTCPICKGLFTAINLGLKKEPNVARVGSVAIKLCNLLKIAPPAVCQSIVHLFEDDMVEVWRRsVLSPSEACGLL 160
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQ-GLDPKDVCQKL 73
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 451-572 3.05e-07

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: 50.06  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592  451 RPLAVAFLAPSATTYIGL------NPGYRVYQID-GNYSrsshvVLDHETYILNLTQANIPGAiPHWQLLYRARETYGLP 523
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVlekesnNPGVRLYQYDpKDYK-----LLDMLQYYLNLTEANLKGE-SNWKLEYILTKAYGIE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 320091592  524 NTLPTAWHNLVYR-MRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCA 572
Cdd:pfam19272  75 DLQPQSLYGLAKQfAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICA 124
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 254-351 6.31e-06

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: 45.67  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592  254 LRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDqlralttvtaLVRKFLGPVPVYPAVGNHESTPVNSFPPPFIE 333
Cdd:pfam00149  15 LDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLE----------LLERLIKYVPVYLVRGNHDFDYGECLRLYPYL 84

                          90
                  ....*....|....*...
gi 320091592  334 GNHSSRWLYEAMAKAWEP 351
Cdd:pfam00149  85 GLLARPWKRFLEVFNFLP 102
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 201-473 9.37e-121

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: 359.31  E-value: 9.37e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 201 ILFLTDLHWDHDYLEG-TDPDCADPLCCRRGSGLPPASrPGAGYWGEYsKCDLPLRTLESLLSGLGP-AGPFDMVYWTGD 278
Cdd:cd00842    1 FLHISDIHYDPLYKVGsEYANCRSPLCCRDESGPGDVK-PPAGYWGTY-GCDSPWSLVESALEAIKKnHPKPDFILWTGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 279 IPAHDVWHQTRQDQLRALTTVTALVRKFLGPVPVYPAVGNHESTPVNSFPPPfiegNHSSRWLYEAMAKAWEPWLPAEA- 357
Cdd:cd00842   79 LVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPH----SNSPSWLYDALAELWKPWLPTEAk 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 358 ----------------LRTLS------SRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGH--CLKSWS 413
Cdd:cd00842  155 etfkkggyysvdvkdgLRVISlntnlyYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLnsYDADWS 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 414 WNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAFLAPSATTYIGLNPGYR 473
Cdd:cd00842  235 ERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPINVAYIAPSVTPYTGNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
253-480 4.70e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.09  E-value: 4.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 253 PLRTLESLLSGLgPAGPFDMVYWTGDIpAHDvwhqTRQDQLRALTtvtALVRKFlgPVPVYPAVGNHEstpvnsfpppfi 332
Cdd:COG1409   19 TAEVLAAALADI-NAPRPDFVVVTGDL-TDD----GEPEEYAAAR---EILARL--GVPVYVVPGNHD------------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 333 egnhssrwLYEAMAKAWEPWLPAEALRTL--SSRENFWLLI--NSTDP--------AGQLQWLVGELQAAEDRgdKVHII 400
Cdd:COG1409   76 --------IRAAMAEAYREYFGDLPPGGLyySFDYGGVRFIglDSNVPgrssgelgPEQLAWLEEELAAAPAK--PVIVF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 401 GHIPPGHCLkSWSWNYY--------RIVARYENTLAaqFFGHTHVDEFEVFYdeetlSRPLAVaflAPSATTYIGLNPGY 472
Cdd:COG1409  146 LHHPPYSTG-SGSDRIGlrnaeellALLARYGVDLV--LSGHVHRYERTRRD-----GVPYIV---AGSTGGQVRLPPGY 214


                 ....*...
gi 320091592 473 RVYQIDGN 480
Cdd:COG1409  215 RVIEVDGD 222
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 87-160 1.01e-07

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: 49.41  E-value: 1.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320091592    87 LTCPICKGLFTAINLGLKKEPNVARVGSVAIKLCNLLKIAPPAVCQSIVHLFEDDMVEVWRRsVLSPSEACGLL 160
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQ-GLDPKDVCQKL 73
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 277-444 2.70e-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: 51.95  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 277 GDIpahdVWHQTRQDQ-LRALTTVTALVRKFlgPVPVYPAVGNHEstpVNSFPPPFIEGNHSSrwlyEAMAKAWEPWLPA 355
Cdd:cd07396   54 GDI----IDGYNAKDRsKEALDAVLSILDRL--KGPVHHVLGNHE---FYNFPREYLNHLKTL----NGEDAYYYSFSPG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592 356 EALRtlssrenfWLLINSTDPAG-----QLQWLVGELQAAEDRGDKVHIIGHIP------PGHCLkswSWNYYRIVA--- 421
Cdd:cd07396  121 PGFR--------FLVLDFVKFNGgigeeQLAWLRNELTSADANGEKVIVLSHLPiypeaaDPQCL---LWNYEEVLAile 189

                        170       180
                 ....*....|....*....|....*...
gi 320091592 422 RYENtLAAQFFGHTH-----VDEFEVFY 444
Cdd:cd07396  190 SYPC-VKACFSGHNHeggyeQDSHGVHH 216
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 451-572 3.05e-07

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: 50.06  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592  451 RPLAVAFLAPSATTYIGL------NPGYRVYQID-GNYSrsshvVLDHETYILNLTQANIPGAiPHWQLLYRARETYGLP 523
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVlekesnNPGVRLYQYDpKDYK-----LLDMLQYYLNLTEANLKGE-SNWKLEYILTKAYGIE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 320091592  524 NTLPTAWHNLVYR-MRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCA 572
Cdd:pfam19272  75 DLQPQSLYGLAKQfAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICA 124
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 254-351 6.31e-06

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: 45.67  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320091592  254 LRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDqlralttvtaLVRKFLGPVPVYPAVGNHESTPVNSFPPPFIE 333
Cdd:pfam00149  15 LDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLE----------LLERLIKYVPVYLVRGNHDFDYGECLRLYPYL 84

                          90
                  ....*....|....*...
gi 320091592  334 GNHSSRWLYEAMAKAWEP 351
Cdd:pfam00149  85 GLLARPWKRFLEVFNFLP 102
 
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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