unnamed protein product [Homo sapiens]
PPP5 domain-containing protein( domain architecture ID 10550879)
PPP5 domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||
PPP5 | pfam08321 | PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ... |
44-119 | 8.47e-37 | ||
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine phosphatases and contains TPR repeats. : Pssm-ID: 462427 Cd Length: 92 Bit Score: 122.20 E-value: 8.47e-37
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Name | Accession | Description | Interval | E-value | ||
PPP5 | pfam08321 | PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ... |
44-119 | 8.47e-37 | ||
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine phosphatases and contains TPR repeats. Pssm-ID: 462427 Cd Length: 92 Bit Score: 122.20 E-value: 8.47e-37
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MPP_PP5_C | cd07417 | PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ... |
84-119 | 3.11e-14 | ||
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs 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: 277362 [Multi-domain] Cd Length: 316 Bit Score: 68.82 E-value: 3.11e-14
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Name | Accession | Description | Interval | E-value | ||
PPP5 | pfam08321 | PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ... |
44-119 | 8.47e-37 | ||
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine phosphatases and contains TPR repeats. Pssm-ID: 462427 Cd Length: 92 Bit Score: 122.20 E-value: 8.47e-37
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MPP_PP5_C | cd07417 | PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ... |
84-119 | 3.11e-14 | ||
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs 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: 277362 [Multi-domain] Cd Length: 316 Bit Score: 68.82 E-value: 3.11e-14
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Blast search parameters | ||||
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