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Conserved domains on  [gi|2232488367|gb|UPQ63520|]
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acid phosphatase type V, partial [Scarturus elater caucasicus]

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
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 1-59 2.44e-29

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing 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. This 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.


The actual alignment was detected with superfamily member cd07378:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 286  Bit Score: 103.94  E-value: 2.44e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2232488367   1 IARTVQIMGADFIMSLGDNFYFTGVHDADDKRFQETFEDVFSDRALrNVPWYVLAGNHD 59
Cdd:cd07378    28 MAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWYLVLGNHD 85
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 1-59 2.44e-29

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: 103.94  E-value: 2.44e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2232488367   1 IARTVQIMGADFIMSLGDNFYFTGVHDADDKRFQETFEDVFSDRALrNVPWYVLAGNHD 59
Cdd:cd07378    28 MAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWYLVLGNHD 85
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 12-59 5.61e-04

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 35.57  E-value: 5.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2232488367  12 FIMSLGDNFyFTGVHDADDKRFQETFEDVFSDRA-LRNVPWYVLAGNHD 59
Cdd:PTZ00422   60 FLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPFFTVLGQAD 107
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-59 8.14e-04

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 35.05  E-value: 8.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2232488367   1 IARTVQIMGADFIMSLGDNfyftgVHDADDKRFQEtFEDVFSDRalrNVPWYVLAGNHD 59
Cdd:COG1409    26 ALADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILARL---GVPVYVVPGNHD 75
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 1-59 2.44e-29

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: 103.94  E-value: 2.44e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2232488367   1 IARTVQIMGADFIMSLGDNFYFTGVHDADDKRFQETFEDVFSDRALrNVPWYVLAGNHD 59
Cdd:cd07378    28 MAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWYLVLGNHD 85
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 9-59 9.96e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing 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. This 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: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 36.86  E-value: 9.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2232488367   9 GADFIMSLGDNFYFTGVHDADDKRFQEtfedvfsdRALRNVPWYVLAGNHD 59
Cdd:cd00838    26 KPDLVICLGDLVDYGPDPEEVELKALR--------LLLAGIPVYVVPGNHD 68
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 12-59 5.61e-04

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 35.57  E-value: 5.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2232488367  12 FIMSLGDNFyFTGVHDADDKRFQETFEDVFSDRA-LRNVPWYVLAGNHD 59
Cdd:PTZ00422   60 FLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPFFTVLGQAD 107
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-59 8.14e-04

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 35.05  E-value: 8.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2232488367   1 IARTVQIMGADFIMSLGDNfyftgVHDADDKRFQEtFEDVFSDRalrNVPWYVLAGNHD 59
Cdd:COG1409    26 ALADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILARL---GVPVYVVPGNHD 75
 
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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