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 72001139  68 STLMRVDedcLPVHIVGDLHGHFGDLRRIFGIHGAPGISHYVFLGDYVDRGRQGIETVMLLMAYHCLYPDHLFLCRGNHE 147
Cdd:cd07415  35 SNVQRVR---SPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHE 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 148 DYNTTMTYGFFDECRMKYGkkGTLAWLHIINAFNHLPLAALILDKVLCMHGGISPHIQKLEDIDKIQRPTFIPSYGLACD 227
Cdd:cd07415 112 SRQITQVYGFYDECLRKYG--NANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCD 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 228 LVWSDPEktSNVGWSLSARGISFSFDDITIEKFCQDNGLDLIVRAHQISSEmirgGHKWHANGRMVTIFSAANYL-SMGN 306
Cdd:cd07415 190 LLWSDPD--DREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVME----GYQWMFNNKLVTVWSAPNYCyRCGN 263

                       250       260
                ....*....|....*....|.
gi 72001139 307 DSCVIRIDEQKTMQFCLLRPV 327
Cdd:cd07415 264 VASILELDEHLNRSFKQFEAA 284

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 72001139    78 LPVHIVGDLH--GHFGDLRRIF-GIHGAPGISHYVFLGDYVDRGRQgIETVMLLMAYHCLYpDHLFLCRGNHEDYnttmt 154
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLkKLLEEGKPDLVLHAGDLVDRGPP-SEEVLELLERLIKY-VPVYLVRGNHDFD----- 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 72001139   155 ygfFDECRMKYGKKGTLA--WLHIINAFNHLPLAALI 189
Cdd:pfam00149  74 ---YGECLRLYPYLGLLArpWKRFLEVFNFLPLAGIL 107

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 72001139  68 STLMRVDedcLPVHIVGDLHGHFGDLRRIFGIHGAPGISHYVFLGDYVDRGRQGIETVMLLMAYHCLYPDHLFLCRGNHE 147
Cdd:cd07415  35 SNVQRVR---SPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHE 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 148 DYNTTMTYGFFDECRMKYGkkGTLAWLHIINAFNHLPLAALILDKVLCMHGGISPHIQKLEDIDKIQRPTFIPSYGLACD 227
Cdd:cd07415 112 SRQITQVYGFYDECLRKYG--NANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCD 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 228 LVWSDPEktSNVGWSLSARGISFSFDDITIEKFCQDNGLDLIVRAHQISSEmirgGHKWHANGRMVTIFSAANYL-SMGN 306
Cdd:cd07415 190 LLWSDPD--DREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVME----GYQWMFNNKLVTVWSAPNYCyRCGN 263

                       250       260
                ....*....|....*....|.
gi 72001139 307 DSCVIRIDEQKTMQFCLLRPV 327
Cdd:cd07415 264 VASILELDEHLNRSFKQFEAA 284

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139  81 HIVGDLHGHFGDLRRIFGIHGAPGISHYVFLGDYVDRGRQGIETVMLLMAYHCLYPDHLFLCRGNHEDYNTTMTYGFFDE 160
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 161 CRMKYGKK-GTLAWLHIINAFNHLPLAALILDKVLCMHGGISPHIQKLEDIDKIqRPTFIPSYGLACDLVWSDPEKTSNv 239
Cdd:cd00144  81 RTLRCLRKgGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVG- 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72001139 240 GWSLSARGISFSFDDITIEKFCQDNGLDLIVRAHQisseMIRGGHKWHANGRMVTIFSAANYL-SMGNDSCVIRI 313
Cdd:cd00144 159 DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHT----PVEGGYEFLHGGKLITIFSAPNYCgKGGNKLAALVV 229

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 72001139  53 IRIISNyAAASFGSFSTLMRVDEdclPVHIVGDLHGHFGDLRRIFGIHGAPGISHYVFLGDYVDRGRQGIETVMLLMAYH 132
Cdd:cd07416  22 LRIITE-GAEILRQEPNLLRIEA---PVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALK 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 133 CLYPDHLFLCRGNHEDYNTTMTYGFFDECRMKYGKKGTLAwlhIINAFNHLPLAALILDKVLCMHGGISPHIQKLEDIDK 212
Cdd:cd07416  98 ILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDA---CMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRK 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 213 IQRPTFIPSYGLACDLVWSDP------EKTSNVGWSLSARGISFSFDDITIEKFCQDNGLDLIVRAHQISSEmirgGHKW 286
Cdd:cd07416 175 LDRFREPPSYGPMCDLLWSDPledfgnEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDA----GYRM 250

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 72001139 287 HANGR------MVTIFSAANYLSM-GNDSCVIRIdEQKTM---QF 321
Cdd:cd07416 251 YRKSQttgfpsLITIFSAPNYLDVyNNKAAVLKY-ENNVMnirQF 294

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 72001139  28 ISRLMTAPMKEKSPAEVDVTVSKEEIRIISNYAAASFGSFSTLMRVDedcLPVHIVGDLHGHFGDLRRIFGIHGAP---- 103
Cdd:cd07419   1 IIAHLLKPRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLR---APIKIFGDIHGQFGDLMRLFDEYGSPvtee 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 104 --GISH--YVFLGDYVDRGRQGIETVMLLMAYHCLYPDHLFLCRGNHEDYNTTMTYGFFDECRMKYGKK---GTLAWLHI 176
Cdd:cd07419  78 agDIEYidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirdGDSVWQRI 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 177 INAFNHLPLAALILDKVLCMHGGISPHIQKLEDIDKIQRP-TFIPSYGLACDLVWSDP-EKTSNVGWSLSAR-----GIS 249
Cdd:cd07419 158 NRLFNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPiTMEAGSPVVMDLLWSDPtENDSVLGLRPNAIdprgtGLI 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72001139 250 FSFDDITIEKFCQDNGLDLIVRAHqissEMIRGGHKWHANGRMVTIFSAANYL-SMGNDSCVIRI 313
Cdd:cd07419 238 VKFGPDRVMEFLEENDLQMIIRAH----ECVMDGFERFAQGHLITLFSATNYCgTAGNAGAILVL 298

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 72001139  64 FGSFSTLMRVD-EDCLPVHIVGDLHGHFGDLRRIFGIHGAPGISH-YVFLGDYVDRGRQGIETVMLLMAYHCLYPDHLFL 141
Cdd:cd07417  45 LKKLPSLVEITiPEGEKITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHL 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 142 CRGNHEDYNTTMTYGFFDECRMKYGKKGTLAWLHIinaFNHLPLAALILDKVLCMHGGI-SPHIQKLEDIDKIQRPTFIP 220
Cdd:cd07417 125 NRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEV---FNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFRQPP 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 221 SYGLACDLVWSDPEKtsNVGWSLSARGISFSF-DDITiEKFCQDNGLDLIVRAHqissEMIRGGHKWHANGRMVTIFSAA 299
Cdd:cd07417 202 DSGLMCELLWSDPQP--QPGRGPSKRGVGCQFgPDVT-KRFLEENNLDYIIRSH----EVKDEGYEVEHDGKCITVFSAP 274

                       250
                ....*....|....*.
gi 72001139 300 NYL-SMGNDSCVIRID 314
Cdd:cd07417 275 NYCdQMGNKGAFIRFK 290

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139  69 TLMRVD-EDCLPVHIVGDLHGHFGDLRRIFGIHGAP-GISHYVFLGDYVDRGRQGIETVMLLMAYHCLYPDHLFLCRGNH 146
Cdd:cd07418  56 NCVRIDvEDVCEVVVVGDVHGQLHDVLFLLEDAGFPdQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNH 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 147 EDYNTTMTYGFFDECRMKYGKKGTLAWLHIINAFNHLPLAALILDKVLCMHGGI-------------------------- 200
Cdd:cd07418 136 ESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknrrvlllepes 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001139 201 -SPHIQKLEDIDKIQRPTFIPSYG----LACDLVWSDPEKTSnvGWSLSA-RGISFSFDDITIEKFCQDNGLDLIVRAHQ 274
Cdd:cd07418 216 eSLKLGTLDDLMKARRSVLDPPGEgsnlIPGDVLWSDPSLTP--GLSPNKqRGIGLLWGPDCTEEFLEKNNLKLIIRSHE 293

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 72001139 275 ISSE---------MIRGGHKWH--ANGRMVTIFSAANY 301
Cdd:cd07418 294 GPDArekrpglagMNKGYTVDHdvESGKLITLFSAPDY 331

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 72001139  83 VGDLHGHFGDLRRIF---GI-----HGAPGISHYVFLGDYVDRGRQGIETVMLLMAyhcLYPD------HLFLCRGNHED 148
Cdd:cd07425   3 IGDLHGDLDRLRTILklaGVidsndRWIGGDTVVVQTGDILDRGDDEIEILKLLEK---LKRQarkaggKVILLLGNHEL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72001139 149 YNTT-----------MTYGFFDECRMKYGKKGTLAWLHIINafnhLPLAALILDkVLCMHGGISP 202
Cdd:cd07425  80 MNLCgdfryvhprglNEFGGVAKRRYALLSDGGYIGRYLRT----HPVVLVVND-ILFVHGGLGP 139

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

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 72001139  80 VHIVGDLHGHFGDLRRIFGIHGAPGISHYVFLGDYVDRGRqgIETVMLLMAYHCLYPDHLFLCRGNHEDYNTT 152
Cdd:COG2129   2 ILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGT--AEEAREVLEELAALGVPVLAVPGNHDDPEVL 72

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72001139  82 IVGDLHGHFGDLRRIFGIHG-APGISHYVFLGDYVDRGRQGIETVMLLMAyhclypdHLFLC-RGNHED 148
Cdd:cd07424   5 VVGDIHGHFQRLQRALDAVGfDPARDRLISVGDLVDRGPESLEVLELLKQ-------PWFHAvQGNHEQ 66

MBG domain; This domain is found in a variety of bacterial extracellular proteins. Although initially described as having a divergent Ig fold this domain has a novel topology that is like a mirror image of the beta grasp fold. Hence the name of Mirror Beta Grasp (MBG) domain.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72001139   211 DKIQRPTFIPSYGLACDLVWSDPEKTSNVG---WSLSARGI----------SFSFDDI-----TIEK 259
Cdd:pfam17883  32 DGGTAPTLLTDYTLQGDFDWSDVTGNTNVGtytVKLTAAGLaklkaananyTWTDDTVgtgtyTITK 98