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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290  25 LDVIIGQLktMAVGNRRAG---NLSEATITYICQASRELFLSQPMLLELSAPVKICGDLHGQFKDLLRIFQQCGVPPLSN 101
Cdd:cd07414   2 IDSIIERL--LEVRGSRPGknvQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 102 YLFLGDYVDRGHCSIETLSLLLTYKLRYPETFFLLRGNHESADLNRVYGFFDECKRRYSIKLWRSFVDCYDCMPVAAIIA 181
Cdd:cd07414  80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 182 DRIFCVHGGLSPDLNNLDDIRRLNRPTDVPSDGLLCDLLWSDPDETTGTWASNDRGVSFTFGANIVEGFLMQHKFNLIVR 261
Cdd:cd07414 160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17864290 262 AHQVVEDGYEFFADRQLVTIFSAPNYCDIFDNCGAVLVVDAKLVCHFVIIRP 313
Cdd:cd07414 240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 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 17864290  25 LDVIIGQLktMAVGNRRAG---NLSEATITYICQASRELFLSQPMLLELSAPVKICGDLHGQFKDLLRIFQQCGVPPLSN 101
Cdd:cd07414   2 IDSIIERL--LEVRGSRPGknvQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 102 YLFLGDYVDRGHCSIETLSLLLTYKLRYPETFFLLRGNHESADLNRVYGFFDECKRRYSIKLWRSFVDCYDCMPVAAIIA 181
Cdd:cd07414  80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 182 DRIFCVHGGLSPDLNNLDDIRRLNRPTDVPSDGLLCDLLWSDPDETTGTWASNDRGVSFTFGANIVEGFLMQHKFNLIVR 261
Cdd:cd07414 160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17864290 262 AHQVVEDGYEFFADRQLVTIFSAPNYCDIFDNCGAVLVVDAKLVCHFVIIRP 313
Cdd:cd07414 240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 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 17864290     45 LSEATITYICQASRELFLSQPMLLELSAPVKICGDLHGQFKDLLRIFQQCGVPPLSNYLFLGDYVDRGHCSIETLSLLLT 124
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290    125 YKLRYPETFFLLRGNHESADLNRVYGFFDECKRRYSIKLWRSFVDCYDCMPVAAIIADRIFCVHGGLSPDLNNLDDIRRL 204
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290    205 NRPTDVPSDGLLCDLLWSDPDETTGTWASNDRGVSFTFGANIVEGFLMQHKFNLIVRAHQVVEDGYEFFADRQLVTIFSA 284
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 17864290    285 PNYCDIFDNCGAVLVVDAKLVCHFVIIRPRP 315
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271

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 17864290  25 LDVIIGQLktMAVGNRRAG---NLSEATITYICQASRELFLSQPMLLELSAPVKICGDLHGQFKDLLRIFQQCGVPPLSN 101
Cdd:cd07414   2 IDSIIERL--LEVRGSRPGknvQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 102 YLFLGDYVDRGHCSIETLSLLLTYKLRYPETFFLLRGNHESADLNRVYGFFDECKRRYSIKLWRSFVDCYDCMPVAAIIA 181
Cdd:cd07414  80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 182 DRIFCVHGGLSPDLNNLDDIRRLNRPTDVPSDGLLCDLLWSDPDETTGTWASNDRGVSFTFGANIVEGFLMQHKFNLIVR 261
Cdd:cd07414 160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17864290 262 AHQVVEDGYEFFADRQLVTIFSAPNYCDIFDNCGAVLVVDAKLVCHFVIIRP 313
Cdd:cd07414 240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 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 17864290     45 LSEATITYICQASRELFLSQPMLLELSAPVKICGDLHGQFKDLLRIFQQCGVPPLSNYLFLGDYVDRGHCSIETLSLLLT 124
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290    125 YKLRYPETFFLLRGNHESADLNRVYGFFDECKRRYSIKLWRSFVDCYDCMPVAAIIADRIFCVHGGLSPDLNNLDDIRRL 204
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290    205 NRPTDVPSDGLLCDLLWSDPDETTGTWASNDRGVSFTFGANIVEGFLMQHKFNLIVRAHQVVEDGYEFFADRQLVTIFSA 284
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 17864290    285 PNYCDIFDNCGAVLVVDAKLVCHFVIIRPRP 315
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271

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 17864290  25 LDVIIGQLKtmavgnrRAGNLSEATITYICQASRELFLSQPMLLELSAPVKICGDLHGQFKDLLRIFQQCGVPPLSNYLF 104
Cdd:cd07415   2 LDQWIEQLK-------KCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 105 LGDYVDRGHCSIETLSLLLTYKLRYPETFFLLRGNHESADLNRVYGFFDECKRRY-SIKLWRSFVDCYDCMPVAAIIADR 183
Cdd:cd07415  75 LGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 184 IFCVHGGLSPDLNNLDDIRRLNRPTDVPSDGLLCDLLWSDPDETTGtWASNDRGVSFTFGANIVEGFLMQHKFNLIVRAH 263
Cdd:cd07415 155 IFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREG-WGISPRGAGYLFGQDVVEEFNHNNGLTLICRAH 233

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17864290 264 QVVEDGYEFFADRQLVTIFSAPNYCDIFDNCGAVLVVDAKLVCHFVIIRPRP 315
Cdd:cd07415 234 QLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290  40 RRAGNLSEATITYICQASRELFLSQPMLLELSAPVKICGDLHGQFKDLLRIFQQCGVPPLSNYLFLGDYVDRGHCSIETL 119
Cdd:cd07416  11 MREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECV 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 120 SLLLTYKLRYPETFFLLRGNHESADLNRVYGFFDECKRRYSIKLWRSFVDCYDCMPVAAIIADRIFCVHGGLSPDLNNLD 199
Cdd:cd07416  91 LYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLD 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 200 DIRRLNRPTDVPSDGLLCDLLWSDP------DETTGTWASND-RGVSFTFGANIVEGFLMQHKFNLIVRAHQVVEDGYEF 272
Cdd:cd07416 171 DIRKLDRFREPPSYGPMCDLLWSDPledfgnEKTQEHFVHNTvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRM 250

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17864290 273 FADRQ------LVTIFSAPNYCDIFDNCGAVLVVDAKLVChfviIR-----PRPFSRP 319
Cdd:cd07416 251 YRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVMN----IRqfncsPHPYWLP 304

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 17864290  52 YICQ---ASRELFLSQPMLLELSAP----VKICGDLHGQFKDLLRIFQQCGVPPLSN-YLFLGDYVDRGHCSIETLSLLL 123
Cdd:cd07417  33 YAYQillQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLF 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 124 TYKLRYPETFFLLRGNHESADLNRVYGFFDECKRRYSIKLWRSFVDCYDCMPVAAIIADRIFCVHGGL-SPDLNNLDDIR 202
Cdd:cd07417 113 AFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIR 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 203 RLNRPTDVPSDGLLCDLLWSDPDETTGTWASNdRGVSFTFGANIVEGFLMQHKFNLIVRAHQVVEDGYEFFADRQLVTIF 282
Cdd:cd07417 193 KIDRFRQPPDSGLMCELLWSDPQPQPGRGPSK-RGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVF 271

                       250       260
                ....*....|....*....|
gi 17864290 283 SAPNYCDIFDNCGAVLVVDA 302
Cdd:cd07417 272 SAPNYCDQMGNKGAFIRFKG 291

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 17864290  71 SAPVKICGDLHGQFKDLLRIFQQCGVPPLSN-YLFLGDYVDRGHCSIETLSLLLTYKLRYPETFFLLRGNHESADLNRVY 149
Cdd:cd07420  50 SKEVTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRY 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 150 GFFDECKRRYSI---KLWRSFVDCYDCMPVAAIIADRIFCVHGGLS--PDLNNLDDIRRLNRPTDVPSDGLLCDLLWSDP 224
Cdd:cd07420 130 GFTKEVMQKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGISdsTDLDLLDKIDRHKYVSTKTEWQQVVDILWSDP 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290 225 DETTGTWASNDRGVSFTFGANIVEGFLMQHKFNLIVRAHQVVEDGYEFFADRQLVTIFSAPNYCDIFDNCGAVLVVDAKL 304
Cdd:cd07420 210 KATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQL 289

                ....*
gi 17864290 305 VCHFV 309
Cdd:cd07420 290 TPHFV 294

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 17864290    73 PVKICGDLH--GQFKDLLRIFQQCgVPPLSNYLFL--GDYVDRGHCSiETLSLLLTYKLRYpETFFLLRGNHESAdlnrv 148
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKL-LEEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD----- 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 17864290   149 ygfFDECKRRY-----SIKLWRSFVDCYDCMPVAAIIA 181
Cdd:pfam00149  74 ---YGECLRLYpylglLARPWKRFLEVFNFLPLAGILS 108

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 17864290  78 GDLHGQFKDLLRIFQQCGVPPLSNY--------LFLGDYVDRGHCSIETLSLLltYKLRyPE------TFFLLRGNHE-- 141
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGVIDSNDRwiggdtvvVQTGDILDRGDDEIEILKLL--EKLK-RQarkaggKVILLLGNHElm 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17864290 142 --SADLNRVY-----GFFDECKRRYSIKLWRSFVDCY-DCMPVAAIIADRIFcVHGGLSPDLNNL 198
Cdd:cd07425  81 nlCGDFRYVHprglnEFGGVAKRRYALLSDGGYIGRYlRTHPVVLVVNDILF-VHGGLGPLWSRG 144

protein-serine/threonine phosphatase;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864290   76 ICGDLHGQFKDLLRIFQQCGVPPLSNYLF-LGDYVDRGHCSIETLSLLltyKLRYpetFFLLRGNHE 141
Cdd:PRK11439  21 LVGDIHGCFEQLMRKLRHCRFDPWRDLLIsVGDLIDRGPQSLRCLQLL---EEHW---VRAVRGNHE 81

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 17864290  76 ICGDLHGQFKDLLRIF--QQCGVPPLSNYLFLGDYVDRGHCSIETLSLLLTYKLRyPETFFLLRGNHE 141
Cdd:cd00838   2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLA-GIPVYVVPGNHD 68

protein-serine/threonine phosphatase;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864290   78 GDLHGQFKDLLRIFQQCGVPPLSNYLF-LGDYVDRGHCSIETLSLLLTyklrypETFFLLRGNHESADLN 146
Cdd:PRK09968  21 GDIHGEYQLLQSRLHQLSFCPETDLLIsVGDNIDRGPESLNVLRLLNQ------PWFISVKGNHEAMALD 84