purple acid phosphatase (PAP) is a binuclear metallohydrolase that catalyzes the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters, and anhydrides; belongs to the metallophosphoesterase (MPP) superfamily; may be inactive
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
286-595
9.04e-98
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain] Cd Length: 296 Bit Score: 300.75 E-value: 9.04e-98
Fn3-like domain from Purple Acid Phosphatase; This entry represents an N-terminal Fn3-like ...
52-168
3.02e-45
Fn3-like domain from Purple Acid Phosphatase; This entry represents an N-terminal Fn3-like domain found at the N-terminus of purple acid phosphatase enzymes.
The actual alignment was detected with superfamily member pfam17808:
Pssm-ID: 375345 Cd Length: 118 Bit Score: 156.18 E-value: 3.02e-45
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
286-595
9.04e-98
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain] Cd Length: 296 Bit Score: 300.75 E-value: 9.04e-98
Fn3-like domain from Purple Acid Phosphatase; This entry represents an N-terminal Fn3-like ...
52-168
3.02e-45
Fn3-like domain from Purple Acid Phosphatase; This entry represents an N-terminal Fn3-like domain found at the N-terminus of purple acid phosphatase enzymes.
Pssm-ID: 375345 Cd Length: 118 Bit Score: 156.18 E-value: 3.02e-45
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
286-595
9.04e-98
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain] Cd Length: 296 Bit Score: 300.75 E-value: 9.04e-98
Fn3-like domain from Purple Acid Phosphatase; This entry represents an N-terminal Fn3-like ...
52-168
3.02e-45
Fn3-like domain from Purple Acid Phosphatase; This entry represents an N-terminal Fn3-like domain found at the N-terminus of purple acid phosphatase enzymes.
Pssm-ID: 375345 Cd Length: 118 Bit Score: 156.18 E-value: 3.02e-45
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
291-384
2.14e-05
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: 44.13 E-value: 2.14e-05
Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an ...
309-382
3.85e-03
Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an uncharacterized Bacillus subtilis protein with a metallophosphatase domain. This family includes bacterial and eukaryotic proteins similar to YvnB. YvnB 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: 277344 [Multi-domain] Cd Length: 207 Bit Score: 39.01 E-value: 3.85e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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