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Conserved domains on  [gi|62906890|sp|Q92485|]
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RecName: Full=Acid sphingomyelinase-like phosphodiesterase 3b; Short=ASM-like phosphodiesterase 3b; Flags: Precursor

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 1.26e-116

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: 343.51  E-value: 1.26e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  23 FWHIADLHLDPDYKVSKDpFQVCPSAG--------SQPVPDAGPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSE-YANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  95 TPHVPDEKLGEAAVLEIvERLTKLIREVFPDTKVYAALGNHDFHPKNQFPAGSNN---IYNQIAELWKPWLSNESIALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890 172 KGAFYCEKlpgPSGAGRIVVLNTNLYYTSNALT-ADMADPGQQFQWLEDVLTDASKAGDMVYIVGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62906890 251 fregFNEKYLKVVRKHHRVIAGQFFGHHHTDSFRMLYDD--AGVPISAMFITPGVTPWKttlpgvvngANNPAIR 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 1.60e-32

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: 120.55  E-value: 1.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890   293 PISAMFITPGVTPWKTTLPGVvngANNPAIRVFEYDRATLSLKDMVTYFMNLSQANAQGTPRWELEYQLTEAYGVPDASA 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 62906890   373 HSMHTVLDRIAGDQSTL-QRYYVYNSVSY-SAGVCDEACSMQHVCAMRQVDIDAYTTCL 429
Cdd:pfam19272  79 QSLYGLAKQFAVPHSKQfEKYYNYFFVSYdSSIVCEGGCKALQICAIMYLDYSSYTDCI 137
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 1.26e-116

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: 343.51  E-value: 1.26e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  23 FWHIADLHLDPDYKVSKDpFQVCPSAG--------SQPVPDAGPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSE-YANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  95 TPHVPDEKLGEAAVLEIvERLTKLIREVFPDTKVYAALGNHDFHPKNQFPAGSNN---IYNQIAELWKPWLSNESIALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890 172 KGAFYCEKlpgPSGAGRIVVLNTNLYYTSNALT-ADMADPGQQFQWLEDVLTDASKAGDMVYIVGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62906890 251 fregFNEKYLKVVRKHHRVIAGQFFGHHHTDSFRMLYDD--AGVPISAMFITPGVTPWKttlpgvvngANNPAIR 323
Cdd:cd00842 233 ----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDkdTGSPINVAYIAPSVTPYT---------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-429 1.60e-32

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: 120.55  E-value: 1.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890   293 PISAMFITPGVTPWKTTLPGVvngANNPAIRVFEYDRATLSLKDMVTYFMNLSQANAQGTPRWELEYQLTEAYGVPDASA 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 62906890   373 HSMHTVLDRIAGDQSTL-QRYYVYNSVSY-SAGVCDEACSMQHVCAMRQVDIDAYTTCL 429
Cdd:pfam19272  79 QSLYGLAKQFAVPHSKQfEKYYNYFFVSYdSSIVCEGGCKALQICAIMYLDYSSYTDCI 137
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
22-312 4.10e-11

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 62.79  E-value: 4.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  22 KFWHIADLHLDPDykvskdpfqvcpsAGSQPVPDAGPwgdylcdspwalinssiyAMKEI-EPEPDFILWTGDDTPHVPD 100
Cdd:COG1409   2 RFAHISDLHLGAP-------------DGSDTAEVLAA------------------ALADInAPRPDFVVVTGDLTDDGEP 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890 101 EKLgeAAVLEIVERLtklirevfpDTKVYAALGNHDfhpknqfpagsnnIYNQIAELWKPWLSNESIAlfkkGAFYCEKL 180
Cdd:COG1409  51 EEY--AAAREILARL---------GVPVYVVPGNHD-------------IRAAMAEAYREYFGDLPPG----GLYYSFDY 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890 181 PGpsgaGRIVVLNTNLYYTSN-ALTADmadpgqQFQWLEDVLTDASKagDMVYIVGHVPPGFFEKTQNKAWFREGfnEKY 259
Cdd:COG1409 103 GG----VRFIGLDSNVPGRSSgELGPE------QLAWLEEELAAAPA--KPVIVFLHHPPYSTGSGSDRIGLRNA--EEL 168

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62906890 260 LKVVRKHHrvIAGQFFGHHHTDSFRMlydDAGVPIsamFITPGVTPWKTTLPG 312
Cdd:COG1409 169 LALLARYG--VDLVLSGHVHRYERTR---RDGVPY---IVAGSTGGQVRLPPG 213
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 22-144 4.31e-04

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 39.89  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890    22 KFWHIADLHLDPDYKVSKDPFQVCPSagsqpvpdagpwgdylcdspwalinssiyamkeiEPEPDFILWTGDdtphVPDE 101
Cdd:pfam00149   2 RILVIGDLHLPGQLDDLLELLKKLLE----------------------------------EGKPDLVLHAGD----LVDR 43

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 62906890   102 KLGEAAVLEIVERLTKLIrevfpdtKVYAALGNHDFHPKNQFP 144
Cdd:pfam00149  44 GPPSEEVLELLERLIKYV-------PVYLVRGNHDFDYGECLR 79
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 1.26e-116

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: 343.51  E-value: 1.26e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  23 FWHIADLHLDPDYKVSKDpFQVCPSAG--------SQPVPDAGPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSE-YANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  95 TPHVPDEKLGEAAVLEIvERLTKLIREVFPDTKVYAALGNHDFHPKNQFPAGSNN---IYNQIAELWKPWLSNESIALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSNSpswLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890 172 KGAFYCEKlpgPSGAGRIVVLNTNLYYTSNALT-ADMADPGQQFQWLEDVLTDASKAGDMVYIVGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62906890 251 fregFNEKYLKVVRKHHRVIAGQFFGHHHTDSFRMLYDD--AGVPISAMFITPGVTPWKttlpgvvngANNPAIR 323
Cdd:cd00842 233 ----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDkdTGSPINVAYIAPSVTPYT---------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-429 1.60e-32

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: 120.55  E-value: 1.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890   293 PISAMFITPGVTPWKTTLPGVvngANNPAIRVFEYDRATLSLKDMVTYFMNLSQANAQGTPRWELEYQLTEAYGVPDASA 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 62906890   373 HSMHTVLDRIAGDQSTL-QRYYVYNSVSY-SAGVCDEACSMQHVCAMRQVDIDAYTTCL 429
Cdd:pfam19272  79 QSLYGLAKQFAVPHSKQfEKYYNYFFVSYdSSIVCEGGCKALQICAIMYLDYSSYTDCI 137
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
22-312 4.10e-11

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 62.79  E-value: 4.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  22 KFWHIADLHLDPDykvskdpfqvcpsAGSQPVPDAGPwgdylcdspwalinssiyAMKEI-EPEPDFILWTGDDTPHVPD 100
Cdd:COG1409   2 RFAHISDLHLGAP-------------DGSDTAEVLAA------------------ALADInAPRPDFVVVTGDLTDDGEP 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890 101 EKLgeAAVLEIVERLtklirevfpDTKVYAALGNHDfhpknqfpagsnnIYNQIAELWKPWLSNESIAlfkkGAFYCEKL 180
Cdd:COG1409  51 EEY--AAAREILARL---------GVPVYVVPGNHD-------------IRAAMAEAYREYFGDLPPG----GLYYSFDY 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890 181 PGpsgaGRIVVLNTNLYYTSN-ALTADmadpgqQFQWLEDVLTDASKagDMVYIVGHVPPGFFEKTQNKAWFREGfnEKY 259
Cdd:COG1409 103 GG----VRFIGLDSNVPGRSSgELGPE------QLAWLEEELAAAPA--KPVIVFLHHPPYSTGSGSDRIGLRNA--EEL 168

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62906890 260 LKVVRKHHrvIAGQFFGHHHTDSFRMlydDAGVPIsamFITPGVTPWKTTLPG 312
Cdd:COG1409 169 LALLARYG--VDLVLSGHVHRYERTR---RDGVPY---IVAGSTGGQVRLPPG 213
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 82-279 9.79e-08

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 52.72  E-value: 9.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  82 EPEPDFILWTGDDTPHVPDEKLGEAAVLEIVERLTKLirevfpDTKVYAALGNHDFhpknqfpagsnniYNqiaeLWKPW 161
Cdd:cd07396  44 ESNLAFVVQLGDIIDGYNAKDRSKEALDAVLSILDRL------KGPVHHVLGNHEF-------------YN----FPREY 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890 162 LSNESIALFKKGAFYCEKlpgPSGAGRIVVLNTNLYytsNALTADmadpgQQFQWLEDVLTDASKAGDMVYIVGHVP--P 239
Cdd:cd07396 101 LNHLKTLNGEDAYYYSFS---PGPGFRFLVLDFVKF---NGGIGE-----EQLAWLRNELTSADANGEKVIVLSHLPiyP 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 62906890 240 GFFEKTQNkAWFREGFnekyLKVVRKHHRVIAgQFFGHHH 279
Cdd:cd07396 170 EAADPQCL-LWNYEEV----LAILESYPCVKA-CFSGHNH 203
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 22-144 4.31e-04

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 39.89  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890    22 KFWHIADLHLDPDYKVSKDPFQVCPSagsqpvpdagpwgdylcdspwalinssiyamkeiEPEPDFILWTGDdtphVPDE 101
Cdd:pfam00149   2 RILVIGDLHLPGQLDDLLELLKKLLE----------------------------------EGKPDLVLHAGD----LVDR 43

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 62906890   102 KLGEAAVLEIVERLTKLIrevfpdtKVYAALGNHDFHPKNQFP 144
Cdd:pfam00149  44 GPPSEEVLELLERLIKYV-------PVYLVRGNHDFDYGECLR 79
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
84-174 1.65e-03

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 40.16  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  84 EPDFILWTGD--DTPHVPDEklgeaAVLEIVERLTKlirevfPDtKVYAALGNHDFHpknqfpAGSNNIYNQIAEL-WKp 160
Cdd:COG1408  73 KPDLVVLTGDlvDGSVAELE-----ALLELLKKLKA------PL-GVYAVLGNHDYY------AGLEELRAALEEAgVR- 133

                        90
                ....*....|....
gi 62906890 161 WLSNESIALFKKGA 174
Cdd:COG1408 134 VLRNEAVTLERGGD 147
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
22-145 3.84e-03

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 38.74  E-value: 3.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62906890  22 KFWHIADLHLD-PDYKVS--KDPFQVCpsagsqpvpdagpwgDYLCDspwalinssiYAmkeIEPEPDFILWTGD--DTP 96
Cdd:COG0420   2 RFLHTADWHLGkPLHGASrrEDQLAAL---------------DRLVD----------LA---IEEKVDAVLIAGDlfDSA 53

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 62906890  97 HVPDEklgeaAVLEIVERLTKLIREvfpDTKVYAALGNHDFHPKNQFPA 145
Cdd:COG0420  54 NPSPE-----AVRLLAEALRRLSEA---GIPVVLIAGNHDSPSRLSAGS 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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