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Conserved domains on  [gi|332660440|gb|AEE85840|]
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Calcineurin-like metallo-phosphoesterase superfamily protein [Arabidopsis thaliana]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CpdA super family cl26378
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
44-211 2.09e-06

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


The actual alignment was detected with superfamily member COG1409:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440  44 DLHFisvagGFRPLNHQTRLLRLMEKVAETYKAKFVVSS---SEQGEEDPFlQNATRLSSSLKLPWY-------TRMKGS 113
Cdd:COG1409    8 DLHL-----GAPDGSDTAEVLAAALADINAPRPDFVVVTgdlTDDGEPEEY-AAAREILARLGVPVYvvpgnhdIRAAMA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440 114 GYFREHIKMPFGGSLD---------VVFVDTGSLKQEvlGGAVNAymiSQLKGLTRILKAVDGDWRIVVGSDPLLAyTLT 184
Cdd:COG1409   82 EAYREYFGDLPPGGLYysfdyggvrFIGLDSNVPGRS--SGELGP---EQLAWLEEELAAAPAKPVIVFLHHPPYS-TGS 155

                        170       180
                 ....*....|....*....|....*..
gi 332660440 185 KEPEEPKRVARTFHQIMTKYGVNLYIS 211
Cdd:COG1409  156 GSDRIGLRNAEELLALLARYGVDLVLS 182
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
44-211 2.09e-06

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440  44 DLHFisvagGFRPLNHQTRLLRLMEKVAETYKAKFVVSS---SEQGEEDPFlQNATRLSSSLKLPWY-------TRMKGS 113
Cdd:COG1409    8 DLHL-----GAPDGSDTAEVLAAALADINAPRPDFVVVTgdlTDDGEPEEY-AAAREILARLGVPVYvvpgnhdIRAAMA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440 114 GYFREHIKMPFGGSLD---------VVFVDTGSLKQEvlGGAVNAymiSQLKGLTRILKAVDGDWRIVVGSDPLLAyTLT 184
Cdd:COG1409   82 EAYREYFGDLPPGGLYysfdyggvrFIGLDSNVPGRS--SGELGP---EQLAWLEEELAAAPAKPVIVFLHHPPYS-TGS 155

                        170       180
                 ....*....|....*....|....*..
gi 332660440 185 KEPEEPKRVARTFHQIMTKYGVNLYIS 211
Cdd:COG1409  156 GSDRIGLRNAEELLALLARYGVDLVLS 182
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 59-211 1.12e-04

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: 42.70  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440  59 HQTRLLRLMEKVAETYKAKFVVS-------SSEQGEEDPFLQNatRLSS-----SLKLPWYT----------------RM 110
Cdd:cd07378   20 AQSLVAKQMAKVASKLGIDFILSlgdnfydDGVKDVDDPRFQE--TFEDvysapSLQVPWYLvlgnhdhrgnvsaqiaYT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440 111 KGSGYFRE-------HIKMPFGG---SLDVVFVDTGSL--------KQEVLGGAVNAYMISQLKGLTRILKAVDGDWRIV 172
Cdd:cd07378   98 QRPNSKRWnfpnyyyDISFKFPSsdvTVAFIMIDTVLLcgntddeaSGQPRGPPNKKLAETQLAWLEKQLAASKADYKIV 177

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332660440 173 VGSDPLLAytlTKEPEEPKRVARTFHQIMTKYGVNLYIS 211
Cdd:cd07378  178 VGHYPIYS---SGEHGPTKCLVDILLPLLKKYKVDAYLS 213
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
44-211 2.09e-06

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440  44 DLHFisvagGFRPLNHQTRLLRLMEKVAETYKAKFVVSS---SEQGEEDPFlQNATRLSSSLKLPWY-------TRMKGS 113
Cdd:COG1409    8 DLHL-----GAPDGSDTAEVLAAALADINAPRPDFVVVTgdlTDDGEPEEY-AAAREILARLGVPVYvvpgnhdIRAAMA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440 114 GYFREHIKMPFGGSLD---------VVFVDTGSLKQEvlGGAVNAymiSQLKGLTRILKAVDGDWRIVVGSDPLLAyTLT 184
Cdd:COG1409   82 EAYREYFGDLPPGGLYysfdyggvrFIGLDSNVPGRS--SGELGP---EQLAWLEEELAAAPAKPVIVFLHHPPYS-TGS 155

                        170       180
                 ....*....|....*....|....*..
gi 332660440 185 KEPEEPKRVARTFHQIMTKYGVNLYIS 211
Cdd:COG1409  156 GSDRIGLRNAEELLALLARYGVDLVLS 182
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 59-211 1.12e-04

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: 42.70  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440  59 HQTRLLRLMEKVAETYKAKFVVS-------SSEQGEEDPFLQNatRLSS-----SLKLPWYT----------------RM 110
Cdd:cd07378   20 AQSLVAKQMAKVASKLGIDFILSlgdnfydDGVKDVDDPRFQE--TFEDvysapSLQVPWYLvlgnhdhrgnvsaqiaYT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660440 111 KGSGYFRE-------HIKMPFGG---SLDVVFVDTGSL--------KQEVLGGAVNAYMISQLKGLTRILKAVDGDWRIV 172
Cdd:cd07378   98 QRPNSKRWnfpnyyyDISFKFPSsdvTVAFIMIDTVLLcgntddeaSGQPRGPPNKKLAETQLAWLEKQLAASKADYKIV 177

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332660440 173 VGSDPLLAytlTKEPEEPKRVARTFHQIMTKYGVNLYIS 211
Cdd:cd07378  178 VGHYPIYS---SGEHGPTKCLVDILLPLLKKYKVDAYLS 213
 
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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