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Conserved domains on  [gi|386766795|ref|NP_001247377|]
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calcineurin A1, isoform B [Drosophila melanogaster]

Protein Classification

serine/threonine-protein phosphatase 2B catalytic subunit( domain architecture ID 10164829)

serine/threonine-protein phosphatase 2B catalytic subunit is a calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals

CATH:  3.60.21.10
EC:  3.1.3.16
Gene Ontology:  GO:0097720|GO:0033192|GO:0005509|GO:0005516|GO:0004722|GO:0046872|GO:0006470
PubMed:  30401537|9646865|25837850|29925267|18488168

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 81-385 0e+00

PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, 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: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 687.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  81 PNFDALRQHFLLEGRIEEAVALRIITEGAALLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYV 160
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 161 DRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQFLCIHG 240
Cdd:cd07416   81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 241 GLSPEIFTLDDIKTLNRFREPPAYGPMCDLLWSDPLEDFGNEKTNEFFSHNSVRGCSYFFSYSACCEFLQKNNLLSIVRA 320
Cdd:cd07416  161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386766795 321 HEAQDAGYRMYRKNQVTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 385
Cdd:cd07416  241 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 305
 
Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 81-385 0e+00

PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, 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: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 687.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  81 PNFDALRQHFLLEGRIEEAVALRIITEGAALLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYV 160
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 161 DRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQFLCIHG 240
Cdd:cd07416   81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 241 GLSPEIFTLDDIKTLNRFREPPAYGPMCDLLWSDPLEDFGNEKTNEFFSHNSVRGCSYFFSYSACCEFLQKNNLLSIVRA 320
Cdd:cd07416  161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386766795 321 HEAQDAGYRMYRKNQVTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 385
Cdd:cd07416  241 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 98-369 2.13e-129

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 380.02  E-value: 2.13e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795    98 EAVALRIITEGAALLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLK 177
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795   178 ITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQFLCIHGGLSPEIFTLDDIKTLNR 257
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795   258 FREPPAYGPMCDLLWSDPledfgnEKTNEFFSHNSvRGCSYFFSYSACCEFLQKNNLLSIVRAHEAQDAGYRMYRKNQvt 337
Cdd:smart00156 163 PQEPPDDGLLIDLLWSDP------DQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK-- 233

                          250       260       270
                   ....*....|....*....|....*....|..
gi 386766795   338 gfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 369
Cdd:smart00156 234 ----LVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 91-378 3.50e-79

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 252.04  E-value: 3.50e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  91 LLEGRIEEAVALRIITEGAA-LLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIEC 169
Cdd:PTZ00239  10 LLNGGCLPERDLKLICERAKeIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVET 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 170 VLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESI-YDACMEAFDCLPLAALLNQQFLCIHGGLSPEIFT 248
Cdd:PTZ00239  90 MEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNpWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 249 LDDIKTLNRFREPPAYGPMCDLLWSDPlEDFGNEKTNEffshnsvRGCSYFFSYSACCEFLQKNNLLSIVRAHEAQDAGY 328
Cdd:PTZ00239 170 IDQIRTIDRKIEIPHEGPFCDLMWSDP-EEVEYWAVNS-------RGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386766795 329 RMYRKNQvtgfpSLITIFSAPNYLDVYNNKAAVLKYENNV-MNIRQFNCSP 378
Cdd:PTZ00239 242 KYWFPDQ-----NLVTVWSAPNYCYRCGNIASILCLDENLqQTWKTFKEVP 287
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 124-231 7.62e-17

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: 76.48  E-value: 7.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  124 PITVCGDIH--GQFFDLVKLFEVGGPPaTTRYLFL--GDYVDRGYFSiECVLYLWSLKITYPTTLsLLRGNHECRHLtEY 199
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEE-GKPDLVLhaGDLVDRGPPS-EEVLELLERLIKYVPVY-LVRGNHDFDYG-EC 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 386766795  200 FTFKQEciIKYSESIYDACMEAFDCLPLAALL 231
Cdd:pfam00149  78 LRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
125-192 1.79e-03

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 39.90  E-value: 1.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766795 125 ITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLKITYpttlslLRGNHE 192
Cdd:COG0622    2 IAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLRELPIVA------VRGNHD 63
 
Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 81-385 0e+00

PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, 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: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 687.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  81 PNFDALRQHFLLEGRIEEAVALRIITEGAALLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYV 160
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 161 DRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQFLCIHG 240
Cdd:cd07416   81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 241 GLSPEIFTLDDIKTLNRFREPPAYGPMCDLLWSDPLEDFGNEKTNEFFSHNSVRGCSYFFSYSACCEFLQKNNLLSIVRA 320
Cdd:cd07416  161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386766795 321 HEAQDAGYRMYRKNQVTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 385
Cdd:cd07416  241 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 98-369 2.13e-129

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 380.02  E-value: 2.13e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795    98 EAVALRIITEGAALLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLK 177
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795   178 ITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQFLCIHGGLSPEIFTLDDIKTLNR 257
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795   258 FREPPAYGPMCDLLWSDPledfgnEKTNEFFSHNSvRGCSYFFSYSACCEFLQKNNLLSIVRAHEAQDAGYRMYRKNQvt 337
Cdd:smart00156 163 PQEPPDDGLLIDLLWSDP------DQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK-- 233

                          250       260       270
                   ....*....|....*....|....*....|..
gi 386766795   338 gfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 369
Cdd:smart00156 234 ----LVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 111-378 2.00e-106

PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of phosphoprotein phosphatases (PPP's) including PP4 and PP6. PP2A (Protein phosphatase 2A) is a critical regulator of many cellular activities. PP2A comprises about 1% of total cellular proteins. PP2A, together with protein phosphatase 1 (PP1), accounts for more than 90% of all serine/threonine phosphatase activities in most cells and tissues. The PP2A subunit in addition to having a catalytic domain homologous to PP1, has a unique C-terminal tail, containing a motif that is conserved in the catalytic subunits of all PP2A-like phosphatases including PP4 and PP6, and has an important role in PP2A regulation. The PP2A-like family of phosphatases all share a similar heterotrimeric architecture, that includes: a 65kDa scaffolding subunit (A), a 36kDa catalytic subunit (C), and one of 18 regulatory subunits (B). The PPP (phosphoprotein phosphatase) family, to which PP2A belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, 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: 277360 [Multi-domain]  Cd Length: 285  Bit Score: 321.84  E-value: 2.00e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 111 LLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLKITYPTTLSLLRGN 190
Cdd:cd07415   30 ILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 191 HECRHLTEYFTFKQECIIKY-SESIYDACMEAFDCLPLAALLNQQFLCIHGGLSPEIFTLDDIKTLNRFREPPAYGPMCD 269
Cdd:cd07415  110 HESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCD 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 270 LLWSDPLEDfgnektnEFFsHNSVRGCSYFFSYSACCEFLQKNNLLSIVRAHEAQDAGYRMYRKNQvtgfpsLITIFSAP 349
Cdd:cd07415  190 LLWSDPDDR-------EGW-GISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNK------LVTVWSAP 255

                        250       260       270
                 ....*....|....*....|....*....|
gi 386766795 350 NYLDVYNNKAAVLKY-ENNVMNIRQFNCSP 378
Cdd:cd07415  256 NYCYRCGNVASILELdEHLNRSFKQFEAAP 285
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 126-364 1.12e-89

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: 276.56  E-value: 1.12e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 126 TVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQE 205
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 206 ----CIIKYSESIYDACMEAFDCLPLAALLNQQFLCIHGGLSPEIFTLDDIKTLnRFREPPAYGPMCDLLWSDPLEDFGn 281
Cdd:cd00144   81 rtlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVG- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 282 ektnefFSHNSVRGCSYFFSYSACCEFLQKNNLLSIVRAHEAQDAGYRMYRKNqvtgfpSLITIFSAPNYLDVYNNKAAV 361
Cdd:cd00144  159 ------DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGG------KLITIFSAPNYCGKGGNKLAA 226


                 ...
gi 386766795 362 LKY 364
Cdd:cd00144  227 LVV 229
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 83-380 7.15e-88

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: 275.29  E-value: 7.15e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  83 FDALRQHFLLEGRIEEAVALRIITEGAALLREEKNMIDVEAP----ITVCGDIHGQFFDLVKLFEVGGPPA-TTRYLFLG 157
Cdd:cd07417   16 VKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSeTNPYLFNG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 158 DYVDRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQFLC 237
Cdd:cd07417   96 DFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 238 IHGGL-SPEIFTLDDIKTLNRFREPPAYGPMCDLLWSDPLEDFGNektneffsHNSVRGCSYFFSYSACCEFLQKNNLLS 316
Cdd:cd07417  176 VHGGLfSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGR--------GPSKRGVGCQFGPDVTKRFLEENNLDY 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386766795 317 IVRAHEAQDAGYrmyrknQVTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIR--QFNCSPHP 380
Cdd:cd07417  248 IIRSHEVKDEGY------EVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKftQFEAVPHP 307
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 91-378 3.50e-79

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 252.04  E-value: 3.50e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  91 LLEGRIEEAVALRIITEGAA-LLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIEC 169
Cdd:PTZ00239  10 LLNGGCLPERDLKLICERAKeIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVET 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 170 VLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESI-YDACMEAFDCLPLAALLNQQFLCIHGGLSPEIFT 248
Cdd:PTZ00239  90 MEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNpWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 249 LDDIKTLNRFREPPAYGPMCDLLWSDPlEDFGNEKTNEffshnsvRGCSYFFSYSACCEFLQKNNLLSIVRAHEAQDAGY 328
Cdd:PTZ00239 170 IDQIRTIDRKIEIPHEGPFCDLMWSDP-EEVEYWAVNS-------RGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386766795 329 RMYRKNQvtgfpSLITIFSAPNYLDVYNNKAAVLKYENNV-MNIRQFNCSP 378
Cdd:PTZ00239 242 KYWFPDQ-----NLVTVWSAPNYCYRCGNIASILCLDENLqQTWKTFKEVP 287
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 75-369 1.85e-78

PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 (protein phosphatase type 1) is a serine/threonine phosphatase that regulates many cellular processes including: cell-cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling, through its interaction with at least 180 known targeting proteins. PP1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Also included here are the PPKL (PP1 and kelch-like) enzymes including the PPQ, PPZ1, and PPZ2 fungal phosphatases. These PPKLs have a large N-terminal kelch repeat in addition to a C-terminal phosphoesterase domain. The PPP (phosphoprotein phosphatase) family, to which PP1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: 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: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 249.95  E-value: 1.85e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  75 DPKTGKPNfdalRQHFLLEGRIEeavalRIITEGAALLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYL 154
Cdd:cd07414   11 EVRGSRPG----KNVQLTEAEIR-----GLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 155 FLGDYVDRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQ 234
Cdd:cd07414   82 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 235 FLCIHGGLSPEIFTLDDIKTLNRFREPPAYGPMCDLLWSDPLEDFGNEKTNEffshnsvRGCSYFFSYSACCEFLQKNNL 314
Cdd:cd07414  162 IFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGEND-------RGVSFTFGADVVAKFLHKHDL 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386766795 315 LSIVRAHEAQDAGYRMYRKNQvtgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 369
Cdd:cd07414  235 DLICRAHQVVEDGYEFFAKRQ------LVTLFSAPNYCGEFDNAGAMMSVDETLM 283
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 118-369 6.42e-70

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 228.78  E-value: 6.42e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 118 MIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLT 197
Cdd:PTZ00480  54 LLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASIN 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 198 EYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQFLCIHGGLSPEIFTLDDIKTLNRFREPPAYGPMCDLLWSDPLE 277
Cdd:PTZ00480 134 RIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDK 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 278 DFGNEKTNEffshnsvRGCSYFFSYSACCEFLQKNNLLSIVRAHEAQDAGYRMYRKNQvtgfpsLITIFSAPNYLDVYNN 357
Cdd:PTZ00480 214 DVQGWADNE-------RGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQ------LVTLFSAPNYCGEFDN 280

                        250
                 ....*....|..
gi 386766795 358 KAAVLKYENNVM 369
Cdd:PTZ00480 281 AGSMMTIDESLM 292
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 104-368 1.46e-58

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 197.82  E-value: 1.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 104 IITEGAALLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLKITYPTT 183
Cdd:PTZ00244  33 VLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPEN 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 184 LSLLRGNHECRHLTEYFTFKQECIIKYSESIYDACMEAFDCLPLAALLNQQFLCIHGGLSPEIFTLDDIKTLNRFREPPA 263
Cdd:PTZ00244 113 FFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPD 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 264 YGPMCDLLWSDPLEDfgnekTNEFFShnSVRGCSYFFSYSACCEFLQKNNLLSIVRAHEAQDAGYRMYRKNQvtgfpsLI 343
Cdd:PTZ00244 193 RGILCDLLWADPEDE-----VRGFLE--SDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQ------LV 259

                        250       260
                 ....*....|....*....|....*
gi 386766795 344 TIFSAPNYLDVYNNKAAVLKYENNV 368
Cdd:PTZ00244 260 TVFSAPNYCGEFDNDAAVMNIDDKL 284
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 76-367 3.08e-57

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. 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: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 194.97  E-value: 3.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  76 PKTGKPNFDalRQHFLLEGRIEEavalrIITEGAALLREEKNMIDVEAPITVCGDIHGQFFDLVKLFEVGGPPATTR--- 152
Cdd:cd07419    8 PRGWKPPVE--RRFFFDCQEIAE-----LCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 153 -----YLFLGDYVDRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSE------SIYDACMEA 221
Cdd:cd07419   81 ieyidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdirdgdSVWQRINRL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 222 FDCLPLAALLNQQFLCIHGGLSPEIFTLDDIKTLNRFREPPAYGP-MCDLLWSDPLEDFGNEKTNEffSHNSVRGCSYFF 300
Cdd:cd07419  161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPvVMDLLWSDPTENDSVLGLRP--NAIDPRGTGLIV 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766795 301 SYSA--CCEFLQKNNLLSIVRAHEAQDAGYRMYRKNQvtgfpsLITIFSAPNYLDVYNNKAAVLKYENN 367
Cdd:cd07419  239 KFGPdrVMEFLEENDLQMIIRAHECVMDGFERFAQGH------LITLFSATNYCGTAGNAGAILVLGRD 301
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 100-380 2.64e-54

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, 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: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 188.86  E-value: 2.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 100 VALRIITEGAALLREEKNMIDVE----APITVCGDIHGQFFDLVKLFEVGGPPATTR-YLFLGDYVDRGYFSIECVLYLW 174
Cdd:cd07418   39 VFDSLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRfYVFNGDYVDRGAWGLETFLLLL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 175 SLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKYSES---IYDACMEAFDCLPLAALLNQQFLCIHGGL--------- 242
Cdd:cd07418  119 SWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKgkhVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkr 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 243 ------------------SPEIFTLDDI-KTLNRFREPPAYGPMC---DLLWSDPLEDFGnektnefFSHNSVRGCSYFF 300
Cdd:cd07418  199 kkqkgknrrvlllepeseSLKLGTLDDLmKARRSVLDPPGEGSNLipgDVLWSDPSLTPG-------LSPNKQRGIGLLW 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 301 SYSACCEFLQKNNLLSIVRAHEAQDAGYRM---------YRKNQVTGFPSLITIFSAPNYL------DVYNNKAAVLkye 365
Cdd:cd07418  272 GPDCTEEFLEKNNLKLIIRSHEGPDAREKRpglagmnkgYTVDHDVESGKLITLFSAPDYPqfqateERYNNKGAYI--- 348

                        330
                 ....*....|....*
gi 386766795 366 nnVMNIRQFNCSPHP 380
Cdd:cd07418  349 --ILQPPDFSDPQFH 361
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 80-369 4.76e-47

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, 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: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 167.20  E-value: 4.76e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  80 KPNFDALRQHFLLEGRIEEAVALRIITEGAALLREEKNMIDVEA----PITVCGDIHGQFFDLVKLFEVGGPPATTR-YL 154
Cdd:cd07420    4 KTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLPSPENpYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 155 FLGDYVDRGYFSIECVLYLWSLKITYPTTLSLLRGNHECRHLTEYFTFKQECIIKY---SESIYDACMEAFDCLPLAALL 231
Cdd:cd07420   84 FNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYkdhGKKILRLLEDVFSWLPLATII 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 232 NQQFLCIHGGLSpEIFTLDDIKTLNRFR---EPPAYGPMCDLLWSDPledfgneKTNEFFSHNSVRGCSYFFSYSACCEF 308
Cdd:cd07420  164 DNKVLVVHGGIS-DSTDLDLLDKIDRHKyvsTKTEWQQVVDILWSDP-------KATKGCKPNTFRGGGCYFGPDVTSQF 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766795 309 LQKNNLLSIVRAHEAQDAGYRMYRKNQVtgfpslITIFSAPNYLDVYNNKAAVLKYENNVM 369
Cdd:cd07420  236 LQKHGLSLLIRSHECKPEGYEFCHNNKV------ITIFSASNYYEEGSNRGAYVKLGPQLT 290
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 124-231 7.62e-17

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: 76.48  E-value: 7.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795  124 PITVCGDIH--GQFFDLVKLFEVGGPPaTTRYLFL--GDYVDRGYFSiECVLYLWSLKITYPTTLsLLRGNHECRHLtEY 199
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEE-GKPDLVLhaGDLVDRGPPS-EEVLELLERLIKYVPVY-LVRGNHDFDYG-EC 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 386766795  200 FTFKQEciIKYSESIYDACMEAFDCLPLAALL 231
Cdd:pfam00149  78 LRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
PHA02239 PHA02239
putative protein phosphatase
 125-223 8.16e-05

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 44.60  E-value: 8.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 125 ITVCGDIHGQFFDLV----KLFEVGGPPATTryLFLGDYVDRGYFSIECVLYLWSLKITYPTTLSLLrGNHEcrhlTEYF 200
Cdd:PHA02239   3 IYVVPDIHGEYQKLLtimdKINNERKPEETI--VFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHD----DEFY 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 386766795 201 TfkqecIIKYSE--SIYDA------CMEAFD 223
Cdd:PHA02239  76 N-----IMENVDrlSIYDIewlsryCIETLN 101
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 125-192 1.44e-04

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: 43.07  E-value: 1.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766795 125 ITVCGDIHGQFFDLV-KLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLwslkiTYPTTLSlLRGNHE 192
Cdd:cd07424    3 DFVVGDIHGHFQRLQrALDAVGFDPARDRLISVGDLVDRGPESLEVLELL-----KQPWFHA-VQGNHE 65
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 124-192 4.46e-04

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, is one of two known protein phosphatase families specific for serine and threonine. 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: 163664  Cd Length: 304  Bit Score: 42.49  E-value: 4.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766795 124 PITVC--GDIHGQFFDLVKLF---EVGGPP---ATTRYLFLGDYVDRGYFSIECVLYLWSLKITYPT-TLSLLRGNHE 192
Cdd:cd07421    1 PRVVIcvGDIHGYISKLNNLWlnlQSALGPsdfASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKqRHVFLCGNHD 78
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 127-192 6.27e-04

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: 40.33  E-value: 6.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766795 127 VCGDIHGQFFDLVKLF--EVGGPPATTRYLFLGDYVDRGYFSiECVLYLWSLKITYPTTLSLLRGNHE 192
Cdd:cd00838    2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDP-EEVELKALRLLLAGIPVYVVPGNHD 68
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 129-245 1.55e-03

Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and PrpA/PrpB. 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: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 40.60  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766795 129 GDIHGQFFDLVKLFE-VGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLKITYPTTLsllrGNHECRHLTEYFTFKQeci 207
Cdd:cd07422    5 GDIQGCYDELQRLLEkINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVL----GNHDLHLLAVAAGIKK--- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386766795 208 IKYSESIyDACMEAFDCLPLAALLNQQ----------FLCIHGGLSPE 245
Cdd:cd07422   78 LKKKDTL-DEILEAPDRDELLDWLRHQpllhrddelgIVMVHAGIPPQ 124
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
125-192 1.79e-03

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 39.90  E-value: 1.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766795 125 ITVCGDIHGQFFDLVKLFEVGGPPATTRYLFLGDYVDRGYFSIECVLYLWSLKITYpttlslLRGNHE 192
Cdd:COG0622    2 IAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLRELPIVA------VRGNHD 63
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 129-176 3.54e-03

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, 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: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 39.42  E-value: 3.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 386766795 129 GDIHGQFFDLVKLFEVGG----------PPATTRYLFLGDYVDRGYFSIECVLYLWSL 176
Cdd:cd07423    4 GDVHGCYDELVELLEKLGyqkkeeglyvHPEGRKLVFLGDLVDRGPDSIDVLRLVMNM 61
 
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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