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Conserved domains on  [gi|18394613|ref|NP_564053|]
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Calcineurin-like metallo-phosphoesterase superfamily protein [Arabidopsis thaliana]

Protein Classification

shewanella-like protein phosphatase( domain architecture ID 10164864)

shewanella-like protein phosphatase similar to Shewanella sp. cold-active protein-tyrosine phosphatase (CAPTPase) that shows high catalytic activity below 20 degrees C; belongs to the metallophosphoesterase (MPP) superfamily

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0042578|GO:0046872|GO:0016311
PubMed:  21960277|8003970|25837850

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 57-343 1.07e-93

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, 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: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 279.57  E-value: 1.07e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613  57 VAIGDLHGDLEKSREAFKIAGLIDSSDRWTGGSTMVVQVGDVLDRGGEELKILYFLEKLKREAERAGGKILTMNGNHEIM 136
Cdd:cd07425   1 VAIGDLHGDLDRLRTILKLAGVIDSNDRWIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKAGGKVILLLGNHELM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613 137 NIEGDFRYVTKKGLEEFQIWAdwyclgnkmktlcsgldkpkdpyegipmsfprmradcfegirARIAALRPDGPIAKRFL 216
Cdd:cd07425  81 NLCGDFRYVHPRGLNEFGGVA------------------------------------------KRRYALLSDGGYIGRYL 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613 217 TKNQTVAVVGDSVFVHGGLlaehieyglerineevrgwingfkggryapaycrggnSVVWLRKFSEEMAHKCDCAALEHA 296
Cdd:cd07425 119 RTHPVVLVVNDILFVHGGL-------------------------------------GPLWSRGYSLETKNGACERSALDK 161

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 18394613 297 LSTIPGVKRMIMGHTIQDAGINGV-CNDKAIRIDVGMSKGCADGLPEV 343
Cdd:cd07425 162 ALAKLGVKRMVVGHTPQEGGVVNTlCGGKLIRIDVGMSRGKYGGLPEV 209
 
Name Accession Description Interval E-value
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 57-343 1.07e-93

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, 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: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 279.57  E-value: 1.07e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613  57 VAIGDLHGDLEKSREAFKIAGLIDSSDRWTGGSTMVVQVGDVLDRGGEELKILYFLEKLKREAERAGGKILTMNGNHEIM 136
Cdd:cd07425   1 VAIGDLHGDLDRLRTILKLAGVIDSNDRWIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKAGGKVILLLGNHELM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613 137 NIEGDFRYVTKKGLEEFQIWAdwyclgnkmktlcsgldkpkdpyegipmsfprmradcfegirARIAALRPDGPIAKRFL 216
Cdd:cd07425  81 NLCGDFRYVHPRGLNEFGGVA------------------------------------------KRRYALLSDGGYIGRYL 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613 217 TKNQTVAVVGDSVFVHGGLlaehieyglerineevrgwingfkggryapaycrggnSVVWLRKFSEEMAHKCDCAALEHA 296
Cdd:cd07425 119 RTHPVVLVVNDILFVHGGL-------------------------------------GPLWSRGYSLETKNGACERSALDK 161

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 18394613 297 LSTIPGVKRMIMGHTIQDAGINGV-CNDKAIRIDVGMSKGCADGLPEV 343
Cdd:cd07425 162 ALAKLGVKRMVVGHTPQEGGVVNTlCGGKLIRIDVGMSRGKYGGLPEV 209
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 55-160 4.80e-06

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: 45.28  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613    55 RLVAIGDLH--GDLEKSREAFKIAGLIDSSDrwtggstMVVQVGDVLDRGGEELKILYFLEKLKREAEraggKILTMnGN 132
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPD-------LVLHAGDLVDRGPPSEEVLELLERLIKYVP----VYLVR-GN 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 18394613   133 HEIMNIEGDFRY----VTKKGLEEFQIWADWY 160
Cdd:pfam00149  70 HDFDYGECLRLYpylgLLARPWKRFLEVFNFL 101
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
55-143 4.40e-04

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 41.15  E-value: 4.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613  55 RLVAIGDLHGDLEKSREAFKIAGL--IDssdrwtggstMVVQVGDVLDRGGEELKILYFleklkREAERAGGKILTMNGN 132
Cdd:COG2129   1 KILAVSDLHGNFDLLEKLLELARAedAD----------LVILAGDLTDFGTAEEAREVL-----EELAALGVPVLAVPGN 65

                        90
                ....*....|.
gi 18394613 133 HEIMNIEGDFR 143
Cdd:COG2129  66 HDDPEVLDALE 76
pphA PRK11439
protein-serine/threonine phosphatase;
59-160 4.05e-03

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 38.21  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613   59 IGDLHGDLEKSREAFKIAGLIDSSDrwtggstMVVQVGDVLDRGGEELKILYFLEKLKREAERaggkiltmnGNHEIMNI 138
Cdd:PRK11439  22 VGDIHGCFEQLMRKLRHCRFDPWRD-------LLISVGDLIDRGPQSLRCLQLLEEHWVRAVR---------GNHEQMAL 85

                         90       100
                 ....*....|....*....|....*.
gi 18394613  139 E----GDFRYVTKKGleefqiwADWY 160
Cdd:PRK11439  86 DalasQQMSLWLMNG-------GDWF 104
 
Name Accession Description Interval E-value
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 57-343 1.07e-93

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, 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: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 279.57  E-value: 1.07e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613  57 VAIGDLHGDLEKSREAFKIAGLIDSSDRWTGGSTMVVQVGDVLDRGGEELKILYFLEKLKREAERAGGKILTMNGNHEIM 136
Cdd:cd07425   1 VAIGDLHGDLDRLRTILKLAGVIDSNDRWIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKAGGKVILLLGNHELM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613 137 NIEGDFRYVTKKGLEEFQIWAdwyclgnkmktlcsgldkpkdpyegipmsfprmradcfegirARIAALRPDGPIAKRFL 216
Cdd:cd07425  81 NLCGDFRYVHPRGLNEFGGVA------------------------------------------KRRYALLSDGGYIGRYL 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613 217 TKNQTVAVVGDSVFVHGGLlaehieyglerineevrgwingfkggryapaycrggnSVVWLRKFSEEMAHKCDCAALEHA 296
Cdd:cd07425 119 RTHPVVLVVNDILFVHGGL-------------------------------------GPLWSRGYSLETKNGACERSALDK 161

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 18394613 297 LSTIPGVKRMIMGHTIQDAGINGV-CNDKAIRIDVGMSKGCADGLPEV 343
Cdd:cd07425 162 ALAKLGVKRMVVGHTPQEGGVVNTlCGGKLIRIDVGMSRGKYGGLPEV 209
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 55-160 4.80e-06

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: 45.28  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613    55 RLVAIGDLH--GDLEKSREAFKIAGLIDSSDrwtggstMVVQVGDVLDRGGEELKILYFLEKLKREAEraggKILTMnGN 132
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPD-------LVLHAGDLVDRGPPSEEVLELLERLIKYVP----VYLVR-GN 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 18394613   133 HEIMNIEGDFRY----VTKKGLEEFQIWADWY 160
Cdd:pfam00149  70 HDFDYGECLRLYpylgLLARPWKRFLEVFNFL 101
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 57-329 1.21e-04

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, 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: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 43.13  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613  57 VAIGDLHGDLEKSREAFKIAGLIDssdrwtggSTMVVQVGDVLDRGGEELKILYFLEKLKreaERAGGKILTMNGNHEIM 136
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPP--------EDKYLFLGDYVDRGPDSVEVIDLLLALK---ILYPDNVFLLRGNHEFM 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613 137 NIEGDFRYvtkkgleEFQIWADWYCLGNKmktlcsgldkpkdpyegipmSFPRMRADCFEGIrariaalrpdgPIAkrfl 216
Cdd:cd00144  70 LLNFLYGF-------YDERTLRCLRKGGE--------------------ELWREFNEVFNYL-----------PLA---- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613 217 tknqtvAVVGDSVF-VHGGL-----LAEHIEYGLERINEEvRGWINGFKGGRYAPAYCRGGNSVVWLRKFSEEMAHKcdc 290
Cdd:cd00144 108 ------ALVDGKILcVHGGLspdltLLDQIRNIRPIENPD-DQLVEDLLWSDPDESVGDFESSSRGGGYLFGEDAVD--- 177

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 18394613 291 AALEHAlstipGVKRMIMGHTIQDAGINGVCNDKAIRID 329
Cdd:cd00144 178 EFLKKN-----GLKLIVRGHTPVEGGYEFLHGGKLITIF 211
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
55-143 4.40e-04

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 41.15  E-value: 4.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613  55 RLVAIGDLHGDLEKSREAFKIAGL--IDssdrwtggstMVVQVGDVLDRGGEELKILYFleklkREAERAGGKILTMNGN 132
Cdd:COG2129   1 KILAVSDLHGNFDLLEKLLELARAedAD----------LVILAGDLTDFGTAEEAREVL-----EELAALGVPVLAVPGN 65

                        90
                ....*....|.
gi 18394613 133 HEIMNIEGDFR 143
Cdd:COG2129  66 HDDPEVLDALE 76
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 55-140 1.23e-03

PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, 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: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 39.61  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613  55 RLVAIGDLHGDLEKSREAFKIAGLIDSSDRwtggstmVVQVGDVLDRGGEELKILYFLEKLKREAERaggkiltmnGNHE 134
Cdd:cd07424   2 RDFVVGDIHGHFQRLQRALDAVGFDPARDR-------LISVGDLVDRGPESLEVLELLKQPWFHAVQ---------GNHE 65


                ....*.
gi 18394613 135 IMNIEG 140
Cdd:cd07424  66 QMAIDA 71
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 57-137 3.08e-03

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: 37.63  E-value: 3.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613  57 VAIGDLHGDLEKSrEAFKIAGLIDSsdrwtGGSTMVVQVGDVLDRGGEElkilYFLEKLKREAERAGGKILTMNGNHEIM 136
Cdd:cd00838   1 LVISDIHGNLEAL-EAVLEAALAKA-----EKPDLVICLGDLVDYGPDP----EEVELKALRLLLAGIPVYVVPGNHDIL 70


                .
gi 18394613 137 N 137
Cdd:cd00838  71 V 71
pphA PRK11439
protein-serine/threonine phosphatase;
59-160 4.05e-03

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 38.21  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394613   59 IGDLHGDLEKSREAFKIAGLIDSSDrwtggstMVVQVGDVLDRGGEELKILYFLEKLKREAERaggkiltmnGNHEIMNI 138
Cdd:PRK11439  22 VGDIHGCFEQLMRKLRHCRFDPWRD-------LLISVGDLIDRGPQSLRCLQLLEEHWVRAVR---------GNHEQMAL 85

                         90       100
                 ....*....|....*....|....*.
gi 18394613  139 E----GDFRYVTKKGleefqiwADWY 160
Cdd:PRK11439  86 DalasQQMSLWLMNG-------GDWF 104
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 59-134 9.07e-03

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, 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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 37.14  E-value: 9.07e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394613  59 IGDLHGDLEKSREAFKIAGLIDSSDRWTGGSTMVVQVGDVLDRGGEELKILYFLeklkREAERAGGKILTMnGNHE 134
Cdd:cd07413   4 IGDVHGCAHTLDRLLDLLGYRLQGGVWRHPRRQALFVGDLIDRGPRIREVLHRV----HAMVDAGEALCVM-GNHE 74
 
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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