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Conserved domains on  [gi|1972267204|ref|NP_001379183|]
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Serine/threonine-protein phosphatase 2B catalytic subunit [Caenorhabditis elegans]

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 ...
 66-370 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: 695.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  66 PRHEVLRDHFIKEGRIEEEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYV 145
Cdd:cd07416     1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 146 DRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHG 225
Cdd:cd07416    81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 226 GLSPEIHTLEDIRRIDRFKEPPAFGPMCDLLWSDPLEDFGNERNSEQFSHNSVRGCSYFYSYAACCDFLQHNNLLSIIRA 305
Cdd:cd07416   161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267204 306 HEAQDAGYRMYRKSQATGFPSLITIFSAPNYLDVYNNKAAILKYENNVMNIRQFNCSPHPYWLPN 370
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 ...
 66-370 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: 695.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  66 PRHEVLRDHFIKEGRIEEEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYV 145
Cdd:cd07416     1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 146 DRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHG 225
Cdd:cd07416    81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 226 GLSPEIHTLEDIRRIDRFKEPPAFGPMCDLLWSDPLEDFGNERNSEQFSHNSVRGCSYFYSYAACCDFLQHNNLLSIIRA 305
Cdd:cd07416   161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267204 306 HEAQDAGYRMYRKSQATGFPSLITIFSAPNYLDVYNNKAAILKYENNVMNIRQFNCSPHPYWLPN 370
Cdd:cd07416   241 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 83-354 4.69e-135

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: 392.35  E-value: 4.69e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204   83 EEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALK 162
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  163 ICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIDR 242
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  243 FKEPPAFGPMCDLLWSDPLEDFgnernsEQFSHNSvRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQat 322
Cdd:smart00156 163 PQEPPDDGLLIDLLWSDPDQPV------NGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK-- 233

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1972267204  323 gfpsLITIFSAPNYLDVYNNKAAILKYENNVM 354
Cdd:smart00156 234 ----LVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 76-363 8.90e-74

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 236.64  E-value: 8.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  76 IKEGRIEEEAAIRVIQE-CSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIEC 154
Cdd:PTZ00239   10 LLNGGCLPERDLKLICErAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVET 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 155 VLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHT 233
Cdd:PTZ00239   90 MEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 234 LEDIRRIDRFKEPPAFGPMCDLLWSDPLEdfgnernSEQFSHNSvRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGY 313
Cdd:PTZ00239  170 IDQIRTIDRKIEIPHEGPFCDLMWSDPEE-------VEYWAVNS-RGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1972267204 314 RMYRKSQatgfpSLITIFSAPNYLDVYNNKAAILKYENNV-MNIRQFNCSP 363
Cdd:PTZ00239  242 KYWFPDQ-----NLVTVWSAPNYCYRCGNIASILCLDENLqQTWKTFKEVP 287
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 109-216 1.00e-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: 79.18  E-value: 1.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 109 PVTVCGDIH--GQFYDLMKLFEVGGSPaTTKYLFL--GDYVDRGYFSiECVLYLWALKICYpTTLFLLRGNHECRHLtEY 184
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEE-GKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYG-EC 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1972267204 185 FTFKQEckIKYSERVYDVCMESFDALPLAALM 216
Cdd:pfam00149  78 LRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
112-177 1.02e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 40.28  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972267204 112 VCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKIcypttlFLLRGNHE 177
Cdd:COG0622     4 VISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLRELPI------VAVRGNHD 63
 
Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 66-370 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: 695.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  66 PRHEVLRDHFIKEGRIEEEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYV 145
Cdd:cd07416     1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 146 DRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHG 225
Cdd:cd07416    81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 226 GLSPEIHTLEDIRRIDRFKEPPAFGPMCDLLWSDPLEDFGNERNSEQFSHNSVRGCSYFYSYAACCDFLQHNNLLSIIRA 305
Cdd:cd07416   161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267204 306 HEAQDAGYRMYRKSQATGFPSLITIFSAPNYLDVYNNKAAILKYENNVMNIRQFNCSPHPYWLPN 370
Cdd:cd07416   241 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 83-354 4.69e-135

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: 392.35  E-value: 4.69e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204   83 EEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALK 162
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  163 ICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIDR 242
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  243 FKEPPAFGPMCDLLWSDPLEDFgnernsEQFSHNSvRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQat 322
Cdd:smart00156 163 PQEPPDDGLLIDLLWSDPDQPV------NGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK-- 233

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1972267204  323 gfpsLITIFSAPNYLDVYNNKAAILKYENNVM 354
Cdd:smart00156 234 ----LVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 99-363 1.13e-103

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: 312.98  E-value: 1.13e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  99 NEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTTLFLLRGNHEC 178
Cdd:cd07415    33 KESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHES 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 179 RHLTEYFTFKQECKIKY-SERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIDRFKEPPAFGPMCDLLW 257
Cdd:cd07415   113 RQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLW 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 258 SDPLEDfgnernsEQFsHNSVRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQatgfpsLITIFSAPNYL 337
Cdd:cd07415   193 SDPDDR-------EGW-GISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNK------LVTVWSAPNYC 258

                         250       260
                  ....*....|....*....|....*..
gi 1972267204 338 DVYNNKAAILKY-ENNVMNIRQFNCSP 363
Cdd:cd07415   259 YRCGNVASILELdEHLNRSFKQFEAAP 285
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 111-349 1.88e-91

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: 279.26  E-value: 1.88e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 111 TVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQE 190
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 191 ----CKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIdRFKEPPAFGPMCDLLWSDPLEDFGn 266
Cdd:cd00144    81 rtlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVG- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 267 ernseqFSHNSVRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRksqatgFPSLITIFSAPNYLDVYNNKAAI 346
Cdd:cd00144   159 ------DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLH------GGKLITIFSAPNYCGKGGNKLAA 226


                  ...
gi 1972267204 347 LKY 349
Cdd:cd00144   227 LVV 229
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 71-365 8.85e-91

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: 280.68  E-value: 8.85e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  71 LRDHFIKEGRIEEEAAIRVIQECSSLFRNEKTMLEIEAP----VTVCGDIHGQFYDLMKLFEVGGSPA-TTKYLFLGDYV 145
Cdd:cd07417    19 MMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSeTNPYLFNGDFV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 146 DRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHG 225
Cdd:cd07417    99 DRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 226 GL-SPEIHTLEDIRRIDRFKEPPAFGPMCDLLWSDPLEDFGNernseqfsHNSVRGCSYFYSYAACCDFLQHNNLLSIIR 304
Cdd:cd07417   179 GLfSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGR--------GPSKRGVGCQFGPDVTKRFLEENNLDYIIR 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972267204 305 AHEAQDAGYRMyrksQATGfpSLITIFSAPNYLDVYNNKAAILKYENNVMNIR--QFNCSPHP 365
Cdd:cd07417   251 SHEVKDEGYEV----EHDG--KCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKftQFEAVPHP 307
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 84-354 4.13e-88

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: 273.06  E-value: 4.13e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  84 EAAIR-VIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALK 162
Cdd:cd07414    25 EAEIRgLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 163 ICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIDR 242
Cdd:cd07414   105 IKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMR 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 243 FKEPPAFGPMCDLLWSDPledfgnERNSEQFSHNSvRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQat 322
Cdd:cd07414   185 PTDVPDQGLLCDLLWSDP------DKDVQGWGEND-RGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQ-- 255

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1972267204 323 gfpsLITIFSAPNYLDVYNNKAAILKYENNVM 354
Cdd:cd07414   256 ----LVTLFSAPNYCGEFDNAGAMMSVDETLM 283
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 76-363 8.90e-74

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 236.64  E-value: 8.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  76 IKEGRIEEEAAIRVIQE-CSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIEC 154
Cdd:PTZ00239   10 LLNGGCLPERDLKLICErAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVET 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 155 VLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHT 233
Cdd:PTZ00239   90 MEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 234 LEDIRRIDRFKEPPAFGPMCDLLWSDPLEdfgnernSEQFSHNSvRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGY 313
Cdd:PTZ00239  170 IDQIRTIDRKIEIPHEGPFCDLMWSDPEE-------VEYWAVNS-RGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1972267204 314 RMYRKSQatgfpSLITIFSAPNYLDVYNNKAAILKYENNV-MNIRQFNCSP 363
Cdd:PTZ00239  242 KYWFPDQ-----NLVTVWSAPNYCYRCGNIASILCLDENLqQTWKTFKEVP 287
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 96-354 6.39e-73

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 234.94  E-value: 6.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  96 LFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTTLFLLRGN 175
Cdd:PTZ00480   47 IFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGN 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 176 HECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIDRFKEPPAFGPMCDL 255
Cdd:PTZ00480  127 HECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDL 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 256 LWSDPLEDFGNERNSEqfshnsvRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQatgfpsLITIFSAPN 335
Cdd:PTZ00480  207 LWSDPDKDVQGWADNE-------RGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQ------LVTLFSAPN 273

                         250
                  ....*....|....*....
gi 1972267204 336 YLDVYNNKAAILKYENNVM 354
Cdd:PTZ00480  274 YCGEFDNAGSMMTIDESLM 292
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 81-362 1.56e-66

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 217.47  E-value: 1.56e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  81 IEEEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWA 160
Cdd:PTZ00244   25 IREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFC 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 161 LKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRI 240
Cdd:PTZ00244  105 YKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 241 DRFKEPPAFGPMCDLLWSDPLEDFGNERNSEqfshnsvRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQ 320
Cdd:PTZ00244  185 ERPCDVPDRGILCDLLWADPEDEVRGFLESD-------RGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQ 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1972267204 321 atgfpsLITIFSAPNYLDVYNNKAAilkyennVMNI-RQFNCS 362
Cdd:PTZ00244  258 ------LVTVFSAPNYCGEFDNDAA-------VMNIdDKLQCS 287
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 80-352 3.79e-63

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: 208.83  E-value: 3.79e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  80 RIEEEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTK--------YLFLGDYVDRGYFS 151
Cdd:cd07419    20 FFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagdieyidYLFLGDYVDRGSHS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 152 IECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSER------VYDVCMESFDALPLAALMNQQFLCVHG 225
Cdd:cd07419   100 LETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirdgdsVWQRINRLFNWLPLAALIEDKIICVHG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 226 GLSPEIHTLEDIRRIDRFKEPPAFGP-MCDLLWSDPLEDfgnerNSEQFSHNSVR-----GCSYFYSYAACCDFLQHNNL 299
Cdd:cd07419   180 GIGRSINHIHQIENLKRPITMEAGSPvVMDLLWSDPTEN-----DSVLGLRPNAIdprgtGLIVKFGPDRVMEFLEENDL 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972267204 300 LSIIRAHEAQDAGYRMYrksqATGfpSLITIFSAPNYLDVYNNKAAILKYENN 352
Cdd:cd07419   255 QMIIRAHECVMDGFERF----AQG--HLITLFSATNYCGTAGNAGAILVLGRD 301
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 94-365 1.66e-52

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: 183.08  E-value: 1.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204  94 SSLFRNEKTMLEIE----APVTVCGDIHGQFYDLMKLFEVGGSPATTK-YLFLGDYVDRGYFSIECVLYLWALKICYPTT 168
Cdd:cd07418    48 HKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRfYVFNGDYVDRGAWGLETFLLLLSWKVLLPDR 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 169 LFLLRGNHECRHLTEYFTFKQECKIKYSER---VYDVCMESFDALPLAALMNQQFLCVHGGL------------------ 227
Cdd:cd07418   128 VYLLRGNHESKFCTSMYGFEQEVLTKYGDKgkhVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknrr 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 228 ---------SPEIHTLEDIRRIDR-FKEPPAFGPMC---DLLWSDPLEDFGnernseqFSHNSVRGCSYFYSYAACCDFL 294
Cdd:cd07418   208 vlllepeseSLKLGTLDDLMKARRsVLDPPGEGSNLipgDVLWSDPSLTPG-------LSPNKQRGIGLLWGPDCTEEFL 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 295 QHNNLLSIIRAHEAQDA------------GYRMYRKSQATGfpsLITIFSAPNYL------DVYNNKAAILkyennVMNI 356
Cdd:cd07418   281 EKNNLKLIIRSHEGPDArekrpglagmnkGYTVDHDVESGK---LITLFSAPDYPqfqateERYNNKGAYI-----ILQP 352


                  ....*....
gi 1972267204 357 RQFNCSPHP 365
Cdd:cd07418   353 PDFSDPQFH 361
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 110-354 1.54e-43

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: 156.41  E-value: 1.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 110 VTVCGDIHGQFYDLMKLFEVGGSPATTK-YLFLGDYVDRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFK 188
Cdd:cd07420    53 VTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFT 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 189 QECKIKY---SERVYDVCMESFDALPLAALMNQQFLCVHGGLSpEIHTLEDIRRIDRFK---EPPAFGPMCDLLWSDPle 262
Cdd:cd07420   133 KEVMQKYkdhGKKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-DSTDLDLLDKIDRHKyvsTKTEWQQVVDILWSDP-- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 263 dfgneRNSEQFSHNSVRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQatgfpsLITIFSAPNYLDVYNN 342
Cdd:cd07420   210 -----KATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNK------VITIFSASNYYEEGSN 278

                         250
                  ....*....|..
gi 1972267204 343 KAAILKYENNVM 354
Cdd:cd07420   279 RGAYVKLGPQLT 290
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 109-216 1.00e-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: 79.18  E-value: 1.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 109 PVTVCGDIH--GQFYDLMKLFEVGGSPaTTKYLFL--GDYVDRGYFSiECVLYLWALKICYpTTLFLLRGNHECRHLtEY 184
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEE-GKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYG-EC 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1972267204 185 FTFKQEckIKYSERVYDVCMESFDALPLAALM 216
Cdd:pfam00149  78 LRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 112-177 6.57e-06

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: 45.72  E-value: 6.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972267204 112 VCGDIHGQFYDLMKLF--EVGGSPATTKYLFLGDYVDRGYFSiECVLYLWALKICYPTTLFLLRGNHE 177
Cdd:cd00838     2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDP-EEVELKALRLLLAGIPVYVVPGNHD 68
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 112-177 1.17e-05

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: 46.16  E-value: 1.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 112 VCGDIHGQFYDLM-KLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYL---WalkicypttLFLLRGNHE 177
Cdd:cd07424     5 VVGDIHGHFQRLQrALDAVGFDPARDRLISVGDLVDRGPESLEVLELLkqpW---------FHAVQGNHE 65
PHA02239 PHA02239
putative protein phosphatase
 110-209 3.79e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 42.29  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 110 VTVCGDIHGQFYDLMKLFEV---GGSPATTkYLFLGDYVDRGYFSIECVLYLWALKICYPTTLFLLrGNHEcrhlTEYFT 186
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMDKinnERKPEET-IVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHD----DEFYN 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1972267204 187 FkqeckIKYSER--VYDV------CMESFDA 209
Cdd:PHA02239   77 I-----MENVDRlsIYDIewlsryCIETLNS 102
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 114-232 5.23e-04

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: 41.73  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 114 GDIHGQFYDLMKLFEVGG----------SPATTKYLFLGDYVDRGYFSIECVLYLWAL-----KICYPttlfllrGNHE- 177
Cdd:cd07423     4 GDVHGCYDELVELLEKLGyqkkeeglyvHPEGRKLVFLGDLVDRGPDSIDVLRLVMNMvkagkALYVP-------GNHCn 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972267204 178 --CRHL---------------TEYFTFKQECKIKYSERVydvcMESFDALPL-AALMNQQFLCVHGGLSPEIH 232
Cdd:cd07423    77 klYRYLkgrnvqlahglettvEELEALSKEERPEFRERF----AEFLESLPShLVLDGGRLVVAHAGIKEEMI 145
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 114-230 8.01e-04

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: 41.38  E-value: 8.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 114 GDIHGQFYDLMKLFE-VGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTTLfllrGNHECRHLTEYFTFKqecK 192
Cdd:cd07422     5 GDIQGCYDELQRLLEkINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVL----GNHDLHLLAVAAGIK---K 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1972267204 193 IKYSERVYDVcMESFDA---------LPLAALMNQ-QFLCVHGGLSPE 230
Cdd:cd07422    78 LKKKDTLDEI-LEAPDRdelldwlrhQPLLHRDDElGIVMVHAGIPPQ 124
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
112-177 1.02e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 40.28  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972267204 112 VCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKIcypttlFLLRGNHE 177
Cdd:COG0622     4 VISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLRELPI------VAVRGNHD 63
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 110-177 1.16e-03

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: 40.95  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972267204 110 VTVC-GDIHGQFYDLMKLF-----EVGGSP-ATTKYLFLGDYVDRGYFSIECVLYLWALKICYP--TTLFLLrGNHE 177
Cdd:cd07421     3 VVICvGDIHGYISKLNNLWlnlqsALGPSDfASALVIFLGDYCDRGPETRKVIDFLISLPEKHPkqRHVFLC-GNHD 78
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
114-229 4.20e-03

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 39.38  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 114 GDIHGQFYDLMKLFE-VGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTTLfllrGNHECRHLTEYFTFKqecK 192
Cdd:PRK00166    7 GDIQGCYDELQRLLEkIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVL----GNHDLHLLAVAAGIK---R 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1972267204 193 IKYSERVYDVcMES--FDAL-------PLAA-LMNQQFLCVHGGLSP 229
Cdd:PRK00166   80 NKKKDTLDPI-LEApdRDELldwlrhqPLLHvDEELGLVMVHAGIPP 125
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
114-185 5.47e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 38.46  E-value: 5.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267204 114 GDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTtlFLLRGNHECRHLTEYF 185
Cdd:COG2129     6 SDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPV--LAVPGNHDDPEVLDAL 75
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 112-185 6.85e-03

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 38.53  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267204 112 VCGDIHGQFYDLMKLFEVGG---------SPATTKYLFLGDYVDRGYFSIECVLYLWAL----KICYpttlflLRGNHeC 178
Cdd:PRK13625    5 IIGDIHGCYQEFQALTEKLGynwssglpvHPDQRKLAFVGDLTDRGPHSLRMIEIVWELvekkAAYY------VPGNH-C 77


                  ....*..
gi 1972267204 179 RHLTEYF 185
Cdd:PRK13625   78 NKLYRFF 84
pphA PRK11439
protein-serine/threonine phosphatase;
110-177 7.07e-03

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 38.21  E-value: 7.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267204 110 VTVCGDIHGQFYDLM-KLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYL---WALKIcypttlfllRGNHE 177
Cdd:PRK11439   19 IWLVGDIHGCFEQLMrKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLeehWVRAV---------RGNHE 81
 
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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