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 30697179  14 LDDIIRRLLDYRNPKPGtKQAMLNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTANY 93
Cdd:cd07414   2 IDSIIERLLEVRGSRPG-KNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179  94 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFSVRLWKVFTDSFNCLPVAAVIDD 173
Cdd:cd07414  81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179 174 KILCMHGGLSPDLTNVEQIKNIKRPTDVPDSGLLCDLLWSDPSKDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICRA 253
Cdd:cd07414 161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 30697179 254 HQVVEDGYEFFADRQLVTIFSAPNYCGEFDNAGAMMSVDESLMCSFQILKP 304
Cdd:cd07414 241 HQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 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 30697179  14 LDDIIRRLLDYRNPKPGtKQAMLNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTANY 93
Cdd:cd07414   2 IDSIIERLLEVRGSRPG-KNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179  94 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFSVRLWKVFTDSFNCLPVAAVIDD 173
Cdd:cd07414  81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179 174 KILCMHGGLSPDLTNVEQIKNIKRPTDVPDSGLLCDLLWSDPSKDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICRA 253
Cdd:cd07414 161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 30697179 254 HQVVEDGYEFFADRQLVTIFSAPNYCGEFDNAGAMMSVDESLMCSFQILKP 304
Cdd:cd07414 241 HQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 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 30697179     36 LNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTANYLFLGDYVDRGKQSLETICLLLA 115
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179    116 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRFSVRLWKVFTDSFNCLPVAAVIDDKILCMHGGLSPDLTNVEQIKNI 195
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179    196 KRPTDVPDSGLLCDLLWSDPSKDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICRAHQVVEDGYEFFADRQLVTIFSA 275
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260       270
                   ....*....|....*....|....*....|
gi 30697179    276 PNYCGEFDNAGAMMSVDESLMCSFQILKPA 305
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKPG 270

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 30697179  14 LDDIIRRLLDYRNPKPGtKQAMLNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTANY 93
Cdd:cd07414   2 IDSIIERLLEVRGSRPG-KNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179  94 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFSVRLWKVFTDSFNCLPVAAVIDD 173
Cdd:cd07414  81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179 174 KILCMHGGLSPDLTNVEQIKNIKRPTDVPDSGLLCDLLWSDPSKDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICRA 253
Cdd:cd07414 161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 30697179 254 HQVVEDGYEFFADRQLVTIFSAPNYCGEFDNAGAMMSVDESLMCSFQILKP 304
Cdd:cd07414 241 HQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 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 30697179     36 LNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTANYLFLGDYVDRGKQSLETICLLLA 115
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179    116 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRFSVRLWKVFTDSFNCLPVAAVIDDKILCMHGGLSPDLTNVEQIKNI 195
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179    196 KRPTDVPDSGLLCDLLWSDPSKDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICRAHQVVEDGYEFFADRQLVTIFSA 275
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260       270
                   ....*....|....*....|....*....|
gi 30697179    276 PNYCGEFDNAGAMMSVDESLMCSFQILKPA 305
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKPG 270

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 30697179  14 LDDIIRRLLDYRnpkpgtkqaMLNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTANY 93
Cdd:cd07415   2 LDQWIEQLKKCE---------LLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179  94 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRF-SVRLWKVFTDSFNCLPVAAVID 172
Cdd:cd07415  73 LFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALID 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179 173 DKILCMHGGLSPDLTNVEQIKNIKRPTDVPDSGLLCDLLWSDPSkDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICR 252
Cdd:cd07415 153 GQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPD-DREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICR 231

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 30697179 253 AHQVVEDGYEFFADRQLVTIFSAPNYCGEFDNAGAMMSVDESLMCSFQILKPA 305
Cdd:cd07415 232 AHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAA 284

serine/threonine protein phosphatase 2A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179   36 LNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTANYLFLGDYVDRGKQSLETICLLLA 115
Cdd:PTZ00239  16 LPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVETMEYLLC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179  116 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRF-SVRLWKVFTDSFNCLPVAAVIDDKILCMHGGLSPDLTNVEQIKN 194
Cdd:PTZ00239  96 LKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRT 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179  195 IKRPTDVPDSGLLCDLLWSDPsKDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICRAHQVVEDGYEF-FADRQLVTIF 273
Cdd:PTZ00239 176 IDRKIEIPHEGPFCDLMWSDP-EEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTVW 254

                        250       260       270
                 ....*....|....*....|....*....|
gi 30697179  274 SAPNYCGEFDNAGAMMSVDESLMCSFQILK 303
Cdd:PTZ00239 255 SAPNYCYRCGNIASILCLDENLQQTWKTFK 284

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179  17 IIRRLLDYRNPKPGTK-QAMLNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTA---- 91
Cdd:cd07419   1 IIAHLLKPRGWKPPVErRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEeagd 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179  92 ----NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFS------VRLWKVFTDS 161
Cdd:cd07419  81 ieyiDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGedirdgDSVWQRINRL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179 162 FNCLPVAAVIDDKILCMHGGLSPDLTNVEQIKNIKRPTDVPDSG-LLCDLLWSDPSKD--VKGWGMNDR-----GVSYTF 233
Cdd:cd07419 161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSpVVMDLLWSDPTENdsVLGLRPNAIdprgtGLIVKF 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30697179 234 GPDKVAEFLIKNDMDLICRAHQVVEDGYEFFADRQLVTIFSAPNYCGEFDNAGAMM 289
Cdd:cd07419 241 GPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAIL 296

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 30697179  48 SREIFLQQPNLLELEA----PIKICGDIHGQYSDLLRLFEYGGFPPTAN-YLFLGDYVDRGKQSLETICLLLAYKIKYPE 122
Cdd:cd07420  32 ARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPN 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179 123 NFFLLRGNHECASINRIYGFYDECKRRFSV---RLWKVFTDSFNCLPVAAVIDDKILCMHGGLSpDLTNVEQIKNIKR-- 197
Cdd:cd07420 112 AVHLNRGNHEDHIMNLRYGFTKEVMQKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-DSTDLDLLDKIDRhk 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179 198 -PTDVPDSGLLCDLLWSDPSKDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICRAHQVVEDGYEFFADRQLVTIFSAP 276
Cdd:cd07420 191 yVSTKTEWQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSAS 270

                       250       260
                ....*....|....*....|...
gi 30697179 277 NYCGEFDNAGAMMSVDESLMCSF 299
Cdd:cd07420 271 NYYEEGSNRGAYVKLGPQLTPHF 293

Serine-threonine protein phosphatase N-terminal domain; This family is often found at the N-terminus of Metallophos family, in serine-threonine protein phosphatases.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 30697179    14 LDDIIRRLLDYRNpKPGTKQAMLNESEIRQLCIVSREIFLQQPNLLELE 62
Cdd:pfam16891   1 LDDIIERLLEVRG-KPGGKQVQLSEAEIRALCRKAREIFLSQPMLLELE 48

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30697179  69 GDIHGQYSDLLRLFEYGGFPPTANYLF-LGDYVDRGKQSLEtiCLLLaykIKYPEnFFLLRGNHECASINR 138
Cdd:cd07424   7 GDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLE--VLEL---LKQPW-FHAVQGNHEQMAIDA 71

putative protein phosphatase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697179   65 IKICGDIHGQYSDLLRLFE--YGGFPPTANYLFLGDYVDRGKQSLETICLLLAYkIKYPENFFLLRGNHE------CASI 136
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDkiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHDdefyniMENV 81

                 ....*...
gi 30697179  137 NRIyGFYD 144
Cdd:PHA02239  82 DRL-SIYD 88

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 30697179  69 GDIHGQYSDLLRLFEYGGFPPTANYL-FLGDYVDRGKQSLETicllLAYKIKYPENFFLLRGNHE 132
Cdd:cd07422   5 GDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLET----LRFVKSLGDSAVVVLGNHD 65

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30697179  67 ICGDIHGQYSDLLRLF--EYGGFPPTANYLFLGDYVDRGKQSLETICLLLAyKIKYPENFFLLRGNHE 132
Cdd:cd00838   2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDPEEVELKALR-LLLAGIPVYVVPGNHD 68

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 30697179  67 ICGDIHGQYSDLLRLFEYGGFPPTANYL----------FLGDYVDRGKQSLEtiCLLLAYKIKYPENFFLLRGNHEcasi 136
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGYQKKEEGLyvhpegrklvFLGDLVDRGPDSID--VLRLVMNMVKAGKALYVPGNHC---- 75

                ....*.
gi 30697179 137 NRIYGF 142
Cdd:cd07423  76 NKLYRY 81