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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  17 LEGLIQRLLEGRNNR-GKRIQLTEPEIHQLCVTAKQVFLAQPVLLALEAPINICGDIHGQYPDLLRLFEYGGFPPDSNYL 95
Cdd:cd07414     2 IDSIIERLLEVRGSRpGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  96 FLGDYVDRGKQSIETICLLLAYKIKFPDNFFLLRGNHECASINRIYGFYDECKRRFSVRLWKTFTDCFNCLPVAAVVDDK 175
Cdd:cd07414    82 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 176 ILCMHGGLSPEMDSLDQIRAIERPADVPDQGLLCDLLWSDPDRDTKGWGDNDRGVSYTFGADRVTEFLKKHDLDLVCRAH 255
Cdd:cd07414   162 IFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAH 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2277055344 256 QVVEDGYEFFADRQLVTIFSAPNYCGEFNNAGALMCVDASLLCSFQILKP 305
Cdd:cd07414   242 QVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  17 LEGLIQRLLEGRNNR-GKRIQLTEPEIHQLCVTAKQVFLAQPVLLALEAPINICGDIHGQYPDLLRLFEYGGFPPDSNYL 95
Cdd:cd07414     2 IDSIIERLLEVRGSRpGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  96 FLGDYVDRGKQSIETICLLLAYKIKFPDNFFLLRGNHECASINRIYGFYDECKRRFSVRLWKTFTDCFNCLPVAAVVDDK 175
Cdd:cd07414    82 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 176 ILCMHGGLSPEMDSLDQIRAIERPADVPDQGLLCDLLWSDPDRDTKGWGDNDRGVSYTFGADRVTEFLKKHDLDLVCRAH 255
Cdd:cd07414   162 IFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAH 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2277055344 256 QVVEDGYEFFADRQLVTIFSAPNYCGEFNNAGALMCVDASLLCSFQILKP 305
Cdd:cd07414   242 QVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344   37 LTEPEIHQLCVTAKQVFLAQPVLLALEAPINICGDIHGQYPDLLRLFEYGGFPPDSNYLFLGDYVDRGKQSIETICLLLA 116
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  117 YKIKFPDNFFLLRGNHECASINRIYGFYDECKRRFSVRLWKTFTDCFNCLPVAAVVDDKILCMHGGLSPEMDSLDQIRAI 196
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  197 ERPADVPDQGLLCDLLWSDPDRDTKGWGDNDRGVSYTFGADRVTEFLKKHDLDLVCRAHQVVEDGYEFFADRQLVTIFSA 276
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260
                   ....*....|....*....|....*....
gi 2277055344  277 PNYCGEFNNAGALMCVDASLLCSFQILKP 305
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKP 269

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  17 LEGLIQRLLEGRNNR-GKRIQLTEPEIHQLCVTAKQVFLAQPVLLALEAPINICGDIHGQYPDLLRLFEYGGFPPDSNYL 95
Cdd:cd07414     2 IDSIIERLLEVRGSRpGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  96 FLGDYVDRGKQSIETICLLLAYKIKFPDNFFLLRGNHECASINRIYGFYDECKRRFSVRLWKTFTDCFNCLPVAAVVDDK 175
Cdd:cd07414    82 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 176 ILCMHGGLSPEMDSLDQIRAIERPADVPDQGLLCDLLWSDPDRDTKGWGDNDRGVSYTFGADRVTEFLKKHDLDLVCRAH 255
Cdd:cd07414   162 IFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAH 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2277055344 256 QVVEDGYEFFADRQLVTIFSAPNYCGEFNNAGALMCVDASLLCSFQILKP 305
Cdd:cd07414   242 QVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344   37 LTEPEIHQLCVTAKQVFLAQPVLLALEAPINICGDIHGQYPDLLRLFEYGGFPPDSNYLFLGDYVDRGKQSIETICLLLA 116
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  117 YKIKFPDNFFLLRGNHECASINRIYGFYDECKRRFSVRLWKTFTDCFNCLPVAAVVDDKILCMHGGLSPEMDSLDQIRAI 196
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  197 ERPADVPDQGLLCDLLWSDPDRDTKGWGDNDRGVSYTFGADRVTEFLKKHDLDLVCRAHQVVEDGYEFFADRQLVTIFSA 276
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260
                   ....*....|....*....|....*....
gi 2277055344  277 PNYCGEFNNAGALMCVDASLLCSFQILKP 305
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKP 269

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  17 LEGLIQRLLEGRnnrgkriQLTEPEIHQLCVTAKQVFLAQPVLLALEAPINICGDIHGQYPDLLRLFEYGGFPPDSNYLF 96
Cdd:cd07415     2 LDQWIEQLKKCE-------LLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  97 LGDYVDRGKQSIETICLLLAYKIKFPDNFFLLRGNHECASINRIYGFYDECKRRF-SVRLWKTFTDCFNCLPVAAVVDDK 175
Cdd:cd07415    75 LGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 176 ILCMHGGLSPEMDSLDQIRAIERPADVPDQGLLCDLLWSDPDrDTKGWGDNDRGVSYTFGADRVTEFLKKHDLDLVCRAH 255
Cdd:cd07415   155 IFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPD-DREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAH 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2277055344 256 QVVEDGYEFFADRQLVTIFSAPNYCGEFNNAGALMCVDASLLCSFQILKP 305
Cdd:cd07415   234 QLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283

serine/threonine protein phosphatase 2A; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  21 IQRLLEGRNnrgkriqLTEPEIHQLCVTAKQVFLAQPVLLALEAPINICGDIHGQYPDLLRLFEYGGFPPDSNYLFLGDY 100
Cdd:PTZ00239    7 IATLLNGGC-------LPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 101 VDRGKQSIETICLLLAYKIKFPDNFFLLRGNHECASINRIYGFYDECKRRF-SVRLWKTFTDCFNCLPVAAVVDDKILCM 179
Cdd:PTZ00239   80 VDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 180 HGGLSPEMDSLDQIRAIERPADVPDQGLLCDLLWSDPDrDTKGWGDNDRGVSYTFGADRVTEFLKKHDLDLVCRAHQVVE 259
Cdd:PTZ00239  160 HGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPE-EVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVM 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2277055344 260 DGYEF-FADRQLVTIFSAPNYCGEFNNAGALMCVDASLLCSFQILK 304
Cdd:PTZ00239  239 EGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFK 284

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  44 QLCVTAKQVFLAQPVLLALEAP----INICGDIHGQYPDLLRLFEYGGFPPDSN-YLFLGDYVDRGKQSIETICLLLAYK 118
Cdd:cd07417    36 QILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 119 IKFPDNFFLLRGNHECASINRIYGFYDECKRRFSVRLWKTFTDCFNCLPVAAVVDDKILCMHGGL-SPEMDSLDQIRAIE 197
Cdd:cd07417   116 LLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKID 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 198 RPADVPDQGLLCDLLWSDPdRDTKGWGDNDRGVSYTFGADrVTE-FLKKHDLDLVCRAHQVVEDGYEFFADRQLVTIFSA 276
Cdd:cd07417   196 RFRQPPDSGLMCELLWSDP-QPQPGRGPSKRGVGCQFGPD-VTKrFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSA 273

                         250
                  ....*....|....*....
gi 2277055344 277 PNYCGEFNNAGALMCVDAS 295
Cdd:cd07417   274 PNYCDQMGNKGAFIRFKGS 292

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  49 AKQVFLAQP----VLLALEAPINICGDIHGQYPDLLRLFEYGGFPPDSN-YLFLGDYVDRGKQSIETICLLLAYKIKFPD 123
Cdd:cd07420    32 ARKSLKQLPnisrVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 124 NFFLLRGNHECASINRIYGFYDECKRRFSV---RLWKTFTDCFNCLPVAAVVDDKILCMHGGLSPEMDsLDQIRAIERPA 200
Cdd:cd07420   112 AVHLNRGNHEDHIMNLRYGFTKEVMQKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGISDSTD-LDLLDKIDRHK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344 201 DVPDQG---LLCDLLWSDPdRDTKG-WGDNDRGVSYTFGADRVTEFLKKHDLDLVCRAHQVVEDGYEFFADRQLVTIFSA 276
Cdd:cd07420   191 YVSTKTewqQVVDILWSDP-KATKGcKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSA 269

                         250
                  ....*....|....
gi 2277055344 277 PNYCGEFNNAGALM 290
Cdd:cd07420   270 SNYYEEGSNRGAYV 283

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  65 PINICGDIH--GQYPDLLRLFEYGGfPPDSNYLFL--GDYVDRGKQSiETICLLLAYKIKFpDNFFLLRGNHECAsinri 140
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD----- 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2277055344 141 ygfYDECKRRF-----SVRLWKTFTDCFNCLPVAAVV 172
Cdd:pfam00149  74 ---YGECLRLYpylglLARPWKRFLEVFNFLPLAGIL 107

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  70 GDIHGQYPDLLRLFEYGGFPPDSNY--------LFLGDYVDRGKQSIETICLLLAYK---IKFPDNFFLLRGNHECASI- 137
Cdd:cd07425     4 GDLHGDLDRLRTILKLAGVIDSNDRwiggdtvvVQTGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELMNLc 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2277055344 138 --------NRIYGFYDECKRRFSvrLWKTFTDCFNCL---PVAAVVDDkILCMHGGLSP 185
Cdd:cd07425    84 gdfryvhpRGLNEFGGVAKRRYA--LLSDGGYIGRYLrthPVVLVVND-ILFVHGGLGP 139

putative protein phosphatase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  66 INICGDIHGQYPDLLRLFE--YGGFPPDSNYLFLGDYVDRGKQSIETICLLLAYKIKfPDNFFLLRGNHE------CASI 137
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMDkiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSN-DDNVVTLLGNHDdefyniMENV 81

                  ....*...
gi 2277055344 138 NRIyGFYD 145
Cdd:PHA02239   82 DRL-SIYD 88

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277055344  68 ICGDIHGQYPDLLRLFE---------YGGFPPDSNYL-FLGDYVDRGKQSIEtiCLLLAYKIKFPDNFFLLRGNHEcasi 137
Cdd:cd07423     2 IIGDVHGCYDELVELLEklgyqkkeeGLYVHPEGRKLvFLGDLVDRGPDSID--VLRLVMNMVKAGKALYVPGNHC---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2277055344 138 NRIYGF------------------YDECKRRFSVRLWKTFTDCFNCLPVAAVVDD-KILCMHGGLSPEM 187
Cdd:cd07423    76 NKLYRYlkgrnvqlahglettveeLEALSKEERPEFRERFAEFLESLPSHLVLDGgRLVVAHAGIKEEM 144

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277055344  70 GDIHGQYPDLLRLFEYGGFPPDSNYL-FLGDYVDRGKQSIETicllLAYKIKFPDNFFLLRGNHE 133
Cdd:cd07422     5 GDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLET----LRFVKSLGDSAVVVLGNHD 65

protein-serine/threonine phosphatase;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2277055344  66 INICGDIHGQYPDLLRLFEYGGFPPDSNYLF-LGDYVDRGKQSIETICLLlaykikfpdN---FFLLRGNHECASIN 138
Cdd:PRK09968   17 IWVVGDIHGEYQLLQSRLHQLSFCPETDLLIsVGDNIDRGPESLNVLRLL---------NqpwFISVKGNHEAMALD 84