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Conserved domains on  [gi|116000572|emb|CAL50252|]
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unnamed product [Ostreococcus tauri]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10164683)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)| bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain; similar to Escherichia coli UshA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 59-352 4.08e-99

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: 295.40  E-value: 4.08e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572  59 FRLGLFADAQYANRDDETRddGSGRVKYFRAAEGRLRDAVAAFEREaSSLSGVVNLGDLYDGYNEDDktkrpvlrgvmsa 138
Cdd:cd07396    1 FSFGIIADIQYADIDDGKN--LGTRRRYYRNSLGVLERAVEEWNRE-SNLAFVVQLGDIIDGYNAKD------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 139 atleRNRHDLGKVASILNASNLRFHHCLGNHDLSVSRDEFL---RAVNAERGAYYSERL--PRRWLLIvldttdlnpryi 213
Cdd:cd07396   65 ----RSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLnhlKTLNGEDAYYYSFSPgpGFRFLVL------------ 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 214 aedtpeyqsaldfateayasgreDIAPWSGGIGPIQLAWFDNELKRAKERGERVIVASHNALQANAARPQMSAWNADQVS 293
Cdd:cd07396  129 -----------------------DFVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWNYEEVL 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 294 KIIEDSGCVKICLAGHDHPGMYNY-RHGVHYVTLEAMLEAKPAQKTSYAFLDVFEHEAVL 352
Cdd:cd07396  186 AILESYPCVKACFSGHNHEGGYEQdSHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR 245
 
Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 59-352 4.08e-99

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: 295.40  E-value: 4.08e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572  59 FRLGLFADAQYANRDDETRddGSGRVKYFRAAEGRLRDAVAAFEREaSSLSGVVNLGDLYDGYNEDDktkrpvlrgvmsa 138
Cdd:cd07396    1 FSFGIIADIQYADIDDGKN--LGTRRRYYRNSLGVLERAVEEWNRE-SNLAFVVQLGDIIDGYNAKD------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 139 atleRNRHDLGKVASILNASNLRFHHCLGNHDLSVSRDEFL---RAVNAERGAYYSERL--PRRWLLIvldttdlnpryi 213
Cdd:cd07396   65 ----RSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLnhlKTLNGEDAYYYSFSPgpGFRFLVL------------ 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 214 aedtpeyqsaldfateayasgreDIAPWSGGIGPIQLAWFDNELKRAKERGERVIVASHNALQANAARPQMSAWNADQVS 293
Cdd:cd07396  129 -----------------------DFVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWNYEEVL 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 294 KIIEDSGCVKICLAGHDHPGMYNY-RHGVHYVTLEAMLEAKPAQKTSYAFLDVFEHEAVL 352
Cdd:cd07396  186 AILESYPCVKACFSGHNHEGGYEQdSHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR 245
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
59-325 2.80e-17

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 80.51  E-value: 2.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572  59 FRLGLFADAQYANRDDETRDDgsgrvkyfraaegRLRDAVAAFEREASSLsgVVNLGDL-YDGYNEDdktkrpvlrgvms 137
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAE-------------VLAAALADINAPRPDF--VVVTGDLtDDGEPEE------------- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 138 aatlernrhdLGKVASILNASNLRFHHCLGNHDLSVSRDEFLRAV---NAERGAYYSERLPRrWLLIVLDTTDlnpryia 214
Cdd:COG1409   53 ----------YAAAREILARLGVPVYVVPGNHDIRAAMAEAYREYfgdLPPGGLYYSFDYGG-VRFIGLDSNV------- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 215 edtpeyqsaldfateayasgredIAPWSGGIGPIQLAWFDNELKRAKERgeRVIVASH-NALQANAARPQMSAWNADQVS 293
Cdd:COG1409  115 -----------------------PGRSSGELGPEQLAWLEEELAAAPAK--PVIVFLHhPPYSTGSGSDRIGLRNAEELL 169

                        250       260       270
                 ....*....|....*....|....*....|..
gi 116000572 294 KIIEDSGcVKICLAGHDHPGMYNYRHGVHYVT 325
Cdd:COG1409  170 ALLARYG-VDLVLSGHVHRYERTRRDGVPYIV 200
 
Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 59-352 4.08e-99

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: 295.40  E-value: 4.08e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572  59 FRLGLFADAQYANRDDETRddGSGRVKYFRAAEGRLRDAVAAFEREaSSLSGVVNLGDLYDGYNEDDktkrpvlrgvmsa 138
Cdd:cd07396    1 FSFGIIADIQYADIDDGKN--LGTRRRYYRNSLGVLERAVEEWNRE-SNLAFVVQLGDIIDGYNAKD------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 139 atleRNRHDLGKVASILNASNLRFHHCLGNHDLSVSRDEFL---RAVNAERGAYYSERL--PRRWLLIvldttdlnpryi 213
Cdd:cd07396   65 ----RSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLnhlKTLNGEDAYYYSFSPgpGFRFLVL------------ 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 214 aedtpeyqsaldfateayasgreDIAPWSGGIGPIQLAWFDNELKRAKERGERVIVASHNALQANAARPQMSAWNADQVS 293
Cdd:cd07396  129 -----------------------DFVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWNYEEVL 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 294 KIIEDSGCVKICLAGHDHPGMYNY-RHGVHYVTLEAMLEAKPAQKTSYAFLDVFEHEAVL 352
Cdd:cd07396  186 AILESYPCVKACFSGHNHEGGYEQdSHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR 245
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
59-325 2.80e-17

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 80.51  E-value: 2.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572  59 FRLGLFADAQYANRDDETRDDgsgrvkyfraaegRLRDAVAAFEREASSLsgVVNLGDL-YDGYNEDdktkrpvlrgvms 137
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAE-------------VLAAALADINAPRPDF--VVVTGDLtDDGEPEE------------- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 138 aatlernrhdLGKVASILNASNLRFHHCLGNHDLSVSRDEFLRAV---NAERGAYYSERLPRrWLLIVLDTTDlnpryia 214
Cdd:COG1409   53 ----------YAAAREILARLGVPVYVVPGNHDIRAAMAEAYREYfgdLPPGGLYYSFDYGG-VRFIGLDSNV------- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 215 edtpeyqsaldfateayasgredIAPWSGGIGPIQLAWFDNELKRAKERgeRVIVASH-NALQANAARPQMSAWNADQVS 293
Cdd:COG1409  115 -----------------------PGRSSGELGPEQLAWLEEELAAAPAK--PVIVFLHhPPYSTGSGSDRIGLRNAEELL 169

                        250       260       270
                 ....*....|....*....|....*....|..
gi 116000572 294 KIIEDSGcVKICLAGHDHPGMYNYRHGVHYVT 325
Cdd:COG1409  170 ALLARYG-VDLVLSGHVHRYERTRRDGVPYIV 200
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 91-357 1.81e-05

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 45.73  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572  91 EGRLRDAVAAFEREASSLSGVVNLGDLYDGYneddktkrpvlrgvmSAATLERNRHDLGKVasilnasNLRFHHCLGNHD 170
Cdd:cd07402   23 AARLAAAVAQVNALHPRPDLVVVTGDLSDDG---------------SPESYERLRELLAPL-------PAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 171 lsvSRDEFLRAVNaerGAYYSERLPRR-------WLLIVLDTTDlnpryiaEDTPEyqsaldfateayasgrediapwsG 243
Cdd:cd07402   81 ---DRAAMREALP---EPPYDDNGPVQyvvdfggWRLILLDTSV-------PGVHH-----------------------G 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 244 GIGPIQLAWFDNELKRAKERGerVIVASHNALqANAARPQMSAW---NADQVSKIIEDSGCVKICLAGHDHPGMYNYRHG 320
Cdd:cd07402  125 ELSDEQLDWLEAALAEAPDRP--TLIFLHHPP-FPLGIPWMDAIrlrNSQALFAVLARHPQVKAILCGHIHRPISGSFRG 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 116000572 321 VHYVTleamleakpAQKTSYAF---LDVFEHEAVLTGVGA 357
Cdd:cd07402  202 IPFST---------APSTCHQFaldLDDFALDAEAPGPRN 232
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 156-325 2.22e-03

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 39.62  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 156 NASNLRFHHCLGNHDLSVSRD---EFLRAVNAER----GAYYSER--LPRRWL---LIVLDTTDL--NPRYIAEDTPEyq 221
Cdd:cd07378   71 PSLQVPWYLVLGNHDHRGNVSaqiAYTQRPNSKRwnfpNYYYDISfkFPSSDVtvaFIMIDTVLLcgNTDDEASGQPR-- 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 222 sALDFATEAYAsgrediapwsggigpiQLAWFDNELKRAKERgeRVIVASHNALQANAA-RPqmSAWNADQVSKIIEDSg 300
Cdd:cd07378  149 -GPPNKKLAET----------------QLAWLEKQLAASKAD--YKIVVGHYPIYSSGEhGP--TKCLVDILLPLLKKY- 206

                        170       180       190
                 ....*....|....*....|....*....|
gi 116000572 301 CVKICLAGHDHpgmyNYRH-----GVHYVT 325
Cdd:cd07378  207 KVDAYLSGHDH----NLQHivdesGTYYVI 232
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 185-272 4.99e-03

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: 38.43  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116000572 185 ERGAYYSERLPRRWLLIVLDTTDLNPryiaEDTPEYQSALDFATeayasgrediapwsggigpiQLAWFDNELKRAKERG 264
Cdd:cd00842  158 KKGGYYSVDVKDGLRVISLNTNLYYK----KNFWLYSNNTDPCG--------------------QLQWLEDELEDAEQKG 213


                 ....*...
gi 116000572 265 ERVIVASH 272
Cdd:cd00842  214 EKVWIIGH 221
 
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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