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Conserved domains on  [gi|220955982|gb|ACL90534|]
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CG3376-PA [synthetic construct]

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 ...
 272-571 1.11e-145

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: 427.49  E-value: 1.11e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 272 VLHISDTHYDPHYAEGSN-ADCNEPLCCRLSSGrPATPNAAAGKWGDYRkCDTPKRTVDHMLSHIAETHKDIDYILWTGD 350
Cdd:cd00842    1 FLHISDIHYDPLYKVGSEyANCRSPLCCRDESG-PGDVKPPAGYWGTYG-CDSPWSLVESALEAIKKNHPKPDFILWTGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 351 LPPHDVWNQTKEENLAIIKDTVKQMVEMFPGVPIFPALGNHESAPVNSFPPPyvnqvDISISWLYDELDIQWRRWLPQSV 430
Cdd:cd00842   79 LVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPH-----SNSPSWLYDALAELWKPWLPTEA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 431 THTVRRGAFYSVLVRPGFRIISLNMNYCNNKNWWLLLNSTDPATELQWFIYELQSAEFSNEKVHVIGHIPPGHSDCLKVW 510
Cdd:cd00842  154 KETFKKGGYYSVDVKDGLRVISLNTNLYYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDADW 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 220955982 511 SRNFYKIISRYESTVTAQFYGHTHYDEFEMFYDPHDLNHPNGIAYIGPSVSPYYDLNPGYR 571
Cdd:cd00842  234 SERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPINVAYIAPSVTPYTGNNPSFR 294
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 157-229 8.98e-10

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: 55.58  E-value: 8.98e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 220955982   157 TCTACRAGAGMLQHQIQSGKTDAELIRMITDYCTNLNIQSARVCQGVAQLFGSELIYVLKRVnLSPDELCSFV 229
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQG-LDPKDVCQKL 73
ASMase_C super family cl44707
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 555-668 1.05e-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: 51.60  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982  555 YIGPSVSPYYDL------NPGYRIYYVDgDHDATtrlVIDHESWIMNLKEANLYGYPIWYKLYTARAAYNMKALRP-SDW 627
Cdd:pfam19272   7 FVAPAVTPVKSVlekesnNPGVRLYQYD-PKDYK---LLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPqSLY 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 220955982  628 NNLLNELTNNQELFELYYKYYWKNSPARPTCDAECKKRLIC 668
Cdd:pfam19272  83 GLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQIC 123
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 272-571 1.11e-145

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: 427.49  E-value: 1.11e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 272 VLHISDTHYDPHYAEGSN-ADCNEPLCCRLSSGrPATPNAAAGKWGDYRkCDTPKRTVDHMLSHIAETHKDIDYILWTGD 350
Cdd:cd00842    1 FLHISDIHYDPLYKVGSEyANCRSPLCCRDESG-PGDVKPPAGYWGTYG-CDSPWSLVESALEAIKKNHPKPDFILWTGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 351 LPPHDVWNQTKEENLAIIKDTVKQMVEMFPGVPIFPALGNHESAPVNSFPPPyvnqvDISISWLYDELDIQWRRWLPQSV 430
Cdd:cd00842   79 LVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPH-----SNSPSWLYDALAELWKPWLPTEA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 431 THTVRRGAFYSVLVRPGFRIISLNMNYCNNKNWWLLLNSTDPATELQWFIYELQSAEFSNEKVHVIGHIPPGHSDCLKVW 510
Cdd:cd00842  154 KETFKKGGYYSVDVKDGLRVISLNTNLYYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDADW 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 220955982 511 SRNFYKIISRYESTVTAQFYGHTHYDEFEMFYDPHDLNHPNGIAYIGPSVSPYYDLNPGYR 571
Cdd:cd00842  234 SERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPINVAYIAPSVTPYTGNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
270-578 6.59e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 74.73  E-value: 6.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 270 FKVLHISDTHYDPHyaEGSNADcneplccrlssgrpatpnaaagkwgdyrkcdtpkRTVDHMLSHIAEthKDIDYILWTG 349
Cdd:COG1409    1 FRFAHISDLHLGAP--DGSDTA----------------------------------EVLAAALADINA--PRPDFVVVTG 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 350 DLpphdVWNQTKEEnLAIIKDTVKQMvemfpGVPIFPALGNHEsapvnsfpppyvnqvdisiswLYDELDIQWRRWLPQs 429
Cdd:COG1409   43 DL----TDDGEPEE-YAAAREILARL-----GVPVYVVPGNHD---------------------IRAAMAEAYREYFGD- 90

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 430 vthtVRRGAFYSVLVRPGFRIISLNMNYCNNKNWWLllnstdPATELQWFIYELQSAefSNEKVHVIGHIPP----GHSD 505
Cdd:COG1409   91 ----LPPGGLYYSFDYGGVRFIGLDSNVPGRSSGEL------GPEQLAWLEEELAAA--PAKPVIVFLHHPPystgSGSD 158

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 220955982 506 CLKVWSR-NFYKIISRYesTVTAQFYGHTHYDEFemfydphdlNHPNGIAYIG-PSVSPYYDLNPGYRIYYVDGD 578
Cdd:COG1409  159 RIGLRNAeELLALLARY--GVDLVLSGHVHRYER---------TRRDGVPYIVaGSTGGQVRLPPGYRVIEVDGD 222
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 157-229 8.98e-10

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: 55.58  E-value: 8.98e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 220955982   157 TCTACRAGAGMLQHQIQSGKTDAELIRMITDYCTNLNIQSARVCQGVAQLFGSELIYVLKRVnLSPDELCSFV 229
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQG-LDPKDVCQKL 73
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 555-668 1.05e-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: 51.60  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982  555 YIGPSVSPYYDL------NPGYRIYYVDgDHDATtrlVIDHESWIMNLKEANLYGYPIWYKLYTARAAYNMKALRP-SDW 627
Cdd:pfam19272   7 FVAPAVTPVKSVlekesnNPGVRLYQYD-PKDYK---LLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPqSLY 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 220955982  628 NNLLNELTNNQELFELYYKYYWKNSPARPTCDAECKKRLIC 668
Cdd:pfam19272  83 GLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQIC 123
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 270-427 2.36e-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: 38.35  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982  270 FKVLHISDTHYDPHYAEgsnadcneplccrlssgrpatpnaaagkwgdyrkcdtpkrtVDHMLSHIAEtHKDIDYILWTG 349
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD-----------------------------------------LLELLKKLLE-EGKPDLVLHAG 38

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 220955982  350 DLPPHDVWNQTKEENLAiikdtvkqmvEMFPGVPIFPALGNHESaPVNSFPPPYVNQVDISISWLYdelDIQWRRWLP 427
Cdd:pfam00149  39 DLVDRGPPSEEVLELLE----------RLIKYVPVYLVRGNHDF-DYGECLRLYPYLGLLARPWKR---FLEVFNFLP 102
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 272-571 1.11e-145

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: 427.49  E-value: 1.11e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 272 VLHISDTHYDPHYAEGSN-ADCNEPLCCRLSSGrPATPNAAAGKWGDYRkCDTPKRTVDHMLSHIAETHKDIDYILWTGD 350
Cdd:cd00842    1 FLHISDIHYDPLYKVGSEyANCRSPLCCRDESG-PGDVKPPAGYWGTYG-CDSPWSLVESALEAIKKNHPKPDFILWTGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 351 LPPHDVWNQTKEENLAIIKDTVKQMVEMFPGVPIFPALGNHESAPVNSFPPPyvnqvDISISWLYDELDIQWRRWLPQSV 430
Cdd:cd00842   79 LVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPH-----SNSPSWLYDALAELWKPWLPTEA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 431 THTVRRGAFYSVLVRPGFRIISLNMNYCNNKNWWLLLNSTDPATELQWFIYELQSAEFSNEKVHVIGHIPPGHSDCLKVW 510
Cdd:cd00842  154 KETFKKGGYYSVDVKDGLRVISLNTNLYYKKNFWLYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDADW 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 220955982 511 SRNFYKIISRYESTVTAQFYGHTHYDEFEMFYDPHDLNHPNGIAYIGPSVSPYYDLNPGYR 571
Cdd:cd00842  234 SERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTGSPINVAYIAPSVTPYTGNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
270-578 6.59e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 74.73  E-value: 6.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 270 FKVLHISDTHYDPHyaEGSNADcneplccrlssgrpatpnaaagkwgdyrkcdtpkRTVDHMLSHIAEthKDIDYILWTG 349
Cdd:COG1409    1 FRFAHISDLHLGAP--DGSDTA----------------------------------EVLAAALADINA--PRPDFVVVTG 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 350 DLpphdVWNQTKEEnLAIIKDTVKQMvemfpGVPIFPALGNHEsapvnsfpppyvnqvdisiswLYDELDIQWRRWLPQs 429
Cdd:COG1409   43 DL----TDDGEPEE-YAAAREILARL-----GVPVYVVPGNHD---------------------IRAAMAEAYREYFGD- 90

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 430 vthtVRRGAFYSVLVRPGFRIISLNMNYCNNKNWWLllnstdPATELQWFIYELQSAefSNEKVHVIGHIPP----GHSD 505
Cdd:COG1409   91 ----LPPGGLYYSFDYGGVRFIGLDSNVPGRSSGEL------GPEQLAWLEEELAAA--PAKPVIVFLHHPPystgSGSD 158

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 220955982 506 CLKVWSR-NFYKIISRYesTVTAQFYGHTHYDEFemfydphdlNHPNGIAYIG-PSVSPYYDLNPGYRIYYVDGD 578
Cdd:COG1409  159 RIGLRNAeELLALLARY--GVDLVLSGHVHRYER---------TRRDGVPYIVaGSTGGQVRLPPGYRVIEVDGD 222
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 157-229 8.98e-10

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: 55.58  E-value: 8.98e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 220955982   157 TCTACRAGAGMLQHQIQSGKTDAELIRMITDYCTNLNIQSARVCQGVAQLFGSELIYVLKRVnLSPDELCSFV 229
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQG-LDPKDVCQKL 73
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 325-549 1.50e-09

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: 59.27  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 325 KRTVDHMlshiaETHKDIDYILWTGDLPPHDVWNQTKEENLaiikDTVKQMVEMFPGvPIFPALGNHESApvnSFPPPYV 404
Cdd:cd07396   35 ERAVEEW-----NRESNLAFVVQLGDIIDGYNAKDRSKEAL----DAVLSILDRLKG-PVHHVLGNHEFY---NFPREYL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 405 NQVDISISwlydeldiqwrrwlpqsvthtvRRGAFYSVLVRPGFRIISLNmnycnnknwWLLLNSTDPATELQWFIYELQ 484
Cdd:cd07396  102 NHLKTLNG----------------------EDAYYYSFSPGPGFRFLVLD---------FVKFNGGIGEEQLAWLRNELT 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982 485 SAEFSNEKVHVIGHIP--PGHSD--CLkVWSRN-FYKIISRYEStVTAQFYGHTHydEFEMFYDPHDLNH 549
Cdd:cd07396  151 SADANGEKVIVLSHLPiyPEAADpqCL-LWNYEeVLAILESYPC-VKACFSGHNH--EGGYEQDSHGVHH 216
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 555-668 1.05e-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: 51.60  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982  555 YIGPSVSPYYDL------NPGYRIYYVDgDHDATtrlVIDHESWIMNLKEANLYGYPIWYKLYTARAAYNMKALRP-SDW 627
Cdd:pfam19272   7 FVAPAVTPVKSVlekesnNPGVRLYQYD-PKDYK---LLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPqSLY 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 220955982  628 NNLLNELTNNQELFELYYKYYWKNSPARPTCDAECKKRLIC 668
Cdd:pfam19272  83 GLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQIC 123
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 270-427 2.36e-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: 38.35  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220955982  270 FKVLHISDTHYDPHYAEgsnadcneplccrlssgrpatpnaaagkwgdyrkcdtpkrtVDHMLSHIAEtHKDIDYILWTG 349
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD-----------------------------------------LLELLKKLLE-EGKPDLVLHAG 38

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 220955982  350 DLPPHDVWNQTKEENLAiikdtvkqmvEMFPGVPIFPALGNHESaPVNSFPPPYVNQVDISISWLYdelDIQWRRWLP 427
Cdd:pfam00149  39 DLVDRGPPSEEVLELLE----------RLIKYVPVYLVRGNHDF-DYGECLRLYPYLGLLARPWKR---FLEVFNFLP 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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