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Conserved domains on  [gi|25149810|ref|NP_495415|]
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Sphingomyelin phosphodiesterase 1 [Caenorhabditis elegans]

Protein Classification

sphingomyelin phosphodiesterase( domain architecture ID 18382240)

sphingomyelin phosphodiesterase catalyzes the conversion of sphingomyelin to ceramide

CATH:  3.60.21.10
EC:  3.1.4.-
Gene Ontology:  GO:0004767|GO:0046872|GO:0006685|GO:0046513
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 ...
 160-456 3.14e-120

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: 356.61  E-value: 3.14e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 160 VLQLTDLHVDFEYKYPSE-ANCDDPVCCRVSV--SEPKKAAGYWGSVGkCDIPFWTVENMLSHINKTH-MIDMVIMTGDY 235
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEyANCRSPLCCRDESgpGDVKPPAGYWGTYG-CDSPWSLVESALEAIKKNHpKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 236 INHVDWEYSIEEHLSVLRKLHRLVQNTFPSTPIYWALGNHEGVPVNSFAPHSvderFWPTWLYKEFQTMSGPWLSEGAKD 315
Cdd:cd00842  80 VRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHS----NSPSWLYDALAELWKPWLPTEAKE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 316 SLLKRGSYSTQVMDGLKLITLNTGFCEVTNFFLYLNQSDPDSSMSWFVKELFESEKKGEQVYVLAHIPPGDSECLEGWAF 395
Cdd:cd00842 156 TFKKGGYYSVDVKDGLRVISLNTNLYYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDADWSE 235

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149810 396 NYYRVIQRFSSTIAAQFFGHDHLDYFTVFYEDMHNvsSKPISVGYASPSVTTFEYQNPAYR 456
Cdd:cd00842 236 RFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDT--GSPINVAYIAPSVTPYTGNNPSFR 294
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 39-113 2.87e-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: 53.65  E-value: 2.87e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25149810     39 PLCISCTGLISVASFFLKFDVSEPVILEFATIVCKLFAKQPWAVCDGISSQFRDEFFYVFRRlaNESPSQICGII 113
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQ--GLDPKDVCQKL 73
ASMase_C super family cl44707
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 434-548 2.15e-08

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: 53.14  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810   434 KPISVGYASPSVTTF------EYQNPAYRIYEIDPYNkFKIVDFTTYYADLEKATEDKKPVWEKLYSARQAHGMDDLSPL 507
Cdd:pfam19272   1 NPVNSLFVAPAVTPVksvlekESNNPGVRLYQYDPKD-YKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQ 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 25149810   508 SWNKVIQKLFTSEKKR-EKFYQYAFRNF--SPQCDSTCQMQLMC 548
Cdd:pfam19272  80 SLYGLAKQFAVPHSKQfEKYYNYFFVSYdsSIVCEGGCKALQIC 123
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 160-456 3.14e-120

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: 356.61  E-value: 3.14e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 160 VLQLTDLHVDFEYKYPSE-ANCDDPVCCRVSV--SEPKKAAGYWGSVGkCDIPFWTVENMLSHINKTH-MIDMVIMTGDY 235
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEyANCRSPLCCRDESgpGDVKPPAGYWGTYG-CDSPWSLVESALEAIKKNHpKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 236 INHVDWEYSIEEHLSVLRKLHRLVQNTFPSTPIYWALGNHEGVPVNSFAPHSvderFWPTWLYKEFQTMSGPWLSEGAKD 315
Cdd:cd00842  80 VRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHS----NSPSWLYDALAELWKPWLPTEAKE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 316 SLLKRGSYSTQVMDGLKLITLNTGFCEVTNFFLYLNQSDPDSSMSWFVKELFESEKKGEQVYVLAHIPPGDSECLEGWAF 395
Cdd:cd00842 156 TFKKGGYYSVDVKDGLRVISLNTNLYYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDADWSE 235

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149810 396 NYYRVIQRFSSTIAAQFFGHDHLDYFTVFYEDMHNvsSKPISVGYASPSVTTFEYQNPAYR 456
Cdd:cd00842 236 RFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDT--GSPINVAYIAPSVTPYTGNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
158-462 2.75e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.86  E-value: 2.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 158 LNVLQLTDLHVDFEYKYPSEAncddpvccrvsvsepkkaagywgsvgkcdipfwTVENMLSHINKTHmIDMVIMTGDYIN 237
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAE---------------------------------VLAAALADINAPR-PDFVVVTGDLTD 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 238 HvDWEYSIEEHLSVLRKLHrlvqntfpsTPIYWALGNHegvpvnsfaphsvDERFWPTWLYKEFQTMSGPwlsegakdsl 317
Cdd:COG1409  47 D-GEPEEYAAAREILARLG---------VPVYVVPGNH-------------DIRAAMAEAYREYFGDLPP---------- 93

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 318 lkRGSYSTQVMDGLKLITLNTGFCEVTNFFLylnqsdPDSSMSWFVKELfeSEKKGEQVYVLAHIPP------GDSECLE 391
Cdd:COG1409  94 --GGLYYSFDYGGVRFIGLDSNVPGRSSGEL------GPEQLAWLEEEL--AAAPAKPVIVFLHHPPystgsgSDRIGLR 163

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149810 392 GwAFNYYRVIQRFSstIAAQFFGHDHLDYFTVFYEDMHnvsskpisvgYASPSVTTFEYQNPAYRIYEIDP 462
Cdd:COG1409 164 N-AEELLALLARYG--VDLVLSGHVHRYERTRRDGVPY----------IVAGSTGGQVRLPPGYRVIEVDG 221
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 39-113 2.87e-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: 53.65  E-value: 2.87e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25149810     39 PLCISCTGLISVASFFLKFDVSEPVILEFATIVCKLFAKQPWAVCDGISSQFRDEFFYVFRRlaNESPSQICGII 113
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQ--GLDPKDVCQKL 73
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 434-548 2.15e-08

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: 53.14  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810   434 KPISVGYASPSVTTF------EYQNPAYRIYEIDPYNkFKIVDFTTYYADLEKATEDKKPVWEKLYSARQAHGMDDLSPL 507
Cdd:pfam19272   1 NPVNSLFVAPAVTPVksvlekESNNPGVRLYQYDPKD-YKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQ 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 25149810   508 SWNKVIQKLFTSEKKR-EKFYQYAFRNF--SPQCDSTCQMQLMC 548
Cdd:pfam19272  80 SLYGLAKQFAVPHSKQfEKYYNYFFVSYdsSIVCEGGCKALQIC 123
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 210-298 3.01e-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: 46.44  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810   210 FWTVENMLSHINKTHMIDMVIMTGDYINHVDWEYSIEEhlsvlrklhrLVQNTFPSTPIYWALGNHEGVPVNSFAPHSVD 289
Cdd:pfam00149  15 LDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLE----------LLERLIKYVPVYLVRGNHDFDYGECLRLYPYL 84


                  ....*....
gi 25149810   290 ERFWPTWLY 298
Cdd:pfam00149  85 GLLARPWKR 93
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 160-456 3.14e-120

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: 356.61  E-value: 3.14e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 160 VLQLTDLHVDFEYKYPSE-ANCDDPVCCRVSV--SEPKKAAGYWGSVGkCDIPFWTVENMLSHINKTH-MIDMVIMTGDY 235
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEyANCRSPLCCRDESgpGDVKPPAGYWGTYG-CDSPWSLVESALEAIKKNHpKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 236 INHVDWEYSIEEHLSVLRKLHRLVQNTFPSTPIYWALGNHEGVPVNSFAPHSvderFWPTWLYKEFQTMSGPWLSEGAKD 315
Cdd:cd00842  80 VRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHS----NSPSWLYDALAELWKPWLPTEAKE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 316 SLLKRGSYSTQVMDGLKLITLNTGFCEVTNFFLYLNQSDPDSSMSWFVKELFESEKKGEQVYVLAHIPPGDSECLEGWAF 395
Cdd:cd00842 156 TFKKGGYYSVDVKDGLRVISLNTNLYYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDADWSE 235

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149810 396 NYYRVIQRFSSTIAAQFFGHDHLDYFTVFYEDMHNvsSKPISVGYASPSVTTFEYQNPAYR 456
Cdd:cd00842 236 RFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDT--GSPINVAYIAPSVTPYTGNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
158-462 2.75e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.86  E-value: 2.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 158 LNVLQLTDLHVDFEYKYPSEAncddpvccrvsvsepkkaagywgsvgkcdipfwTVENMLSHINKTHmIDMVIMTGDYIN 237
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAE---------------------------------VLAAALADINAPR-PDFVVVTGDLTD 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 238 HvDWEYSIEEHLSVLRKLHrlvqntfpsTPIYWALGNHegvpvnsfaphsvDERFWPTWLYKEFQTMSGPwlsegakdsl 317
Cdd:COG1409  47 D-GEPEEYAAAREILARLG---------VPVYVVPGNH-------------DIRAAMAEAYREYFGDLPP---------- 93

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 318 lkRGSYSTQVMDGLKLITLNTGFCEVTNFFLylnqsdPDSSMSWFVKELfeSEKKGEQVYVLAHIPP------GDSECLE 391
Cdd:COG1409  94 --GGLYYSFDYGGVRFIGLDSNVPGRSSGEL------GPEQLAWLEEEL--AAAPAKPVIVFLHHPPystgsgSDRIGLR 163

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149810 392 GwAFNYYRVIQRFSstIAAQFFGHDHLDYFTVFYEDMHnvsskpisvgYASPSVTTFEYQNPAYRIYEIDP 462
Cdd:COG1409 164 N-AEELLALLARYG--VDLVLSGHVHRYERTRRDGVPY----------IVAGSTGGQVRLPPGYRVIEVDG 221
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 39-113 2.87e-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: 53.65  E-value: 2.87e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25149810     39 PLCISCTGLISVASFFLKFDVSEPVILEFATIVCKLFAKQPWAVCDGISSQFRDEFFYVFRRlaNESPSQICGII 113
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQ--GLDPKDVCQKL 73
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 434-548 2.15e-08

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: 53.14  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810   434 KPISVGYASPSVTTF------EYQNPAYRIYEIDPYNkFKIVDFTTYYADLEKATEDKKPVWEKLYSARQAHGMDDLSPL 507
Cdd:pfam19272   1 NPVNSLFVAPAVTPVksvlekESNNPGVRLYQYDPKD-YKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQ 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 25149810   508 SWNKVIQKLFTSEKKR-EKFYQYAFRNF--SPQCDSTCQMQLMC 548
Cdd:pfam19272  80 SLYGLAKQFAVPHSKQfEKYYNYFFVSYdsSIVCEGGCKALQIC 123
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 219-417 2.71e-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: 2.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 219 HINKTHMIDMVIMTGDYINHVDWEYSIEEHL-SVLRKLHRLvqntfpSTPIYWALGNHEgvpvnsfaphsvderfwptwL 297
Cdd:cd07396  40 EWNRESNLAFVVQLGDIIDGYNAKDRSKEALdAVLSILDRL------KGPVHHVLGNHE--------------------F 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 298 Y---KEFQTMSGPWLSEGAKdsllkrgSYSTQVMDGLKLITLNtgfcevtnfFLYLNQSDPDSSMSWFVKELFESEKKGE 374
Cdd:cd07396  94 YnfpREYLNHLKTLNGEDAY-------YYSFSPGPGFRFLVLD---------FVKFNGGIGEEQLAWLRNELTSADANGE 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 25149810 375 QVYVLAHIP--PGDSE--CLegwAFNYYRV---IQRFSStIAAQFFGHDH 417
Cdd:cd07396 158 KVIVLSHLPiyPEAADpqCL---LWNYEEVlaiLESYPC-VKACFSGHNH 203
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 210-298 3.01e-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: 46.44  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810   210 FWTVENMLSHINKTHMIDMVIMTGDYINHVDWEYSIEEhlsvlrklhrLVQNTFPSTPIYWALGNHEGVPVNSFAPHSVD 289
Cdd:pfam00149  15 LDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLE----------LLERLIKYVPVYLVRGNHDFDYGECLRLYPYL 84


                  ....*....
gi 25149810   290 ERFWPTWLY 298
Cdd:pfam00149  85 GLLARPWKR 93
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
156-276 6.46e-04

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 41.70  E-value: 6.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149810 156 QNLNVLQLTDLHVdfeykypseancddpvccrvsvsepkkaaGYWGSVGKcdipfwtVENMLSHINKTHmIDMVIMTGDY 235
Cdd:COG1408  41 DGLRIVQLSDLHL-----------------------------GPFIGGER-------LERLVEKINALK-PDLVVLTGDL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 25149810 236 INHVDWEysIEEHLSVLRKLHrlvqntfPSTPIYWALGNHE 276
Cdd:COG1408  84 VDGSVAE--LEALLELLKKLK-------APLGVYAVLGNHD 115
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 227-276 5.15e-03

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE 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: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 38.80  E-value: 5.15e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 25149810 227 DMVIMTGDYINHVDWEysIEEHLSVLRKLHrlvqntfPSTPIYWALGNHE 276
Cdd:cd07385  34 DLIVITGDLVDGDVSV--LRLLASPLSKLK-------APLGVYFVLGNHD 74
 
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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