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 1831510989  34 TIVGDIHGQFEDLVRLLNTRNSSENAKskpiYgfstkkwVFLGDYVDRGYKSLDCICLVFSLKICFPKQYILLRGNHETR 113
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDK----Y-------LFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFM 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989 114 AINFRYGFR---------------------------VCSVVVLKI----------------------------------- 131
Cdd:cd00144    70 LLNFLYGFYdertlrclrkggeelwrefnevfnylpLAALVDGKIlcvhgglspdltlldqirnirpienpddqlvedll 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989 132 ----PAKPSFIRNNKRGLSVCFNEAAVNETCRLLNISLIVRGHQMMPAGFKFFADRKLCTIFSAPRYMNEIDNSGAVMKV 207
Cdd:cd00144   150 wsdpDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229

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 1831510989  32 PVTIVGDIH--GQFEDLVRLLNtrnssENAKSKPIYGFstkkwVFLGDYVDRGYKSLDCICLVFSLKICFPkqYILLRGN 109
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLK-----KLLEEGKPDLV-----LHAGDLVDRGPPSEEVLELLERLIKYVP--VYLVRGN 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510989 110 HETRainfrygfrvcsvvVLKIPAKPSFIRNNKRGLSVCfneaavNETCRLLNISLIVRGHQMMP 174
Cdd:pfam00149  70 HDFD--------------YGECLRLYPYLGLLARPWKRF------LEVFNFLPLAGILSGHTHVP 114

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 1831510989  34 TIVGDIHGQFEDLVRLLNTRNSSENAKskpiYgfstkkwVFLGDYVDRGYKSLDCICLVFSLKICFPKQYILLRGNHETR 113
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDK----Y-------LFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFM 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989 114 AINFRYGFR---------------------------VCSVVVLKI----------------------------------- 131
Cdd:cd00144    70 LLNFLYGFYdertlrclrkggeelwrefnevfnylpLAALVDGKIlcvhgglspdltlldqirnirpienpddqlvedll 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989 132 ----PAKPSFIRNNKRGLSVCFNEAAVNETCRLLNISLIVRGHQMMPAGFKFFADRKLCTIFSAPRYMNEIDNSGAVMKV 207
Cdd:cd00144   150 wsdpDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229

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 1831510989   8 ELFCLLDMVIELFKKEKTLAEISPPVTIVGDIHGQFEDLVRLLNTRNSSENakskpiygfstKKWVFLGDYVDRGYKSLD 87
Cdd:cd07415    19 EVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPD-----------TNYLFLGDYVDRGYYSVE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  88 CICLVFSLKICFPKQYILLRGNHETRAINFRYGF--------------RVCSVV--VLKIPA-------------KPSF- 137
Cdd:cd07415    88 TFLLLLALKVRYPDRITLLRGNHESRQITQVYGFydeclrkygnanvwKYFTDLfdYLPLAAlidgqifcvhgglSPSIq 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989 138 ----IRN-----------------------------NKRGLSVCFNEAAVNETCRLLNISLIVRGHQMMPAGFKFFADRK 184
Cdd:cd07415   168 tldqIRAldrfqevphegpmcdllwsdpddregwgiSPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNK 247

                         250       260
                  ....*....|....*....|....*...
gi 1831510989 185 LCTIFSAPRYMNEIDNSGAVMKVASNGK 212
Cdd:cd07415   248 LVTVWSAPNYCYRCGNVASILELDEHLN 275

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 1831510989  18 ELFKKEKTLAEISPPVTIVGDIHGQFEDLVRLLNTRNSSEnakskpiygfsTKKWVFLGDYVDRGYKSLDCICLVFSLKI 97
Cdd:cd07416    30 EILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPA-----------NTRYLFLGDYVDRGYFSIECVLYLWALKI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  98 CFPKQYILLRGNHETRAI----NFR------YGFRVCSVVVLKIPAKP-------------------------------- 135
Cdd:cd07416    99 LYPKTLFLLRGNHECRHLteyfTFKqeckikYSERVYDACMEAFDCLPlaalmnqqflcvhgglspelktlddirkldrf 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989 136 ----------------------------SFIRNNKRGLSVCFNEAAVnetCRLL---NISLIVRGHQMMPAGFKFFadRK 184
Cdd:cd07416   179 reppsygpmcdllwsdpledfgnektqeHFVHNTVRGCSYFYSYRAV---CEFLqknNLLSIIRAHEAQDAGYRMY--RK 253

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1831510989 185 --------LCTIFSAPRYMNEIDNSGAVMKVASN 210
Cdd:cd07416   254 sqttgfpsLITIFSAPNYLDVYNNKAAVLKYENN 287

serine/threonine-protein phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  18 ELFKKEKTLAEISPPVTIVGDIHGQFEDLVRLLntrnssENAKSKPiygfsTKKWVFLGDYVDRGYKSLDCICLVFSLKI 97
Cdd:PTZ00480   46 DIFISQPILLELEAPLKICGDVHGQYFDLLRLF------EYGGYPP-----ESNYLFLGDYVDRGKQSLETICLLLAYKI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  98 CFPKQYILLRGNHETRAINFRYGFR-----------------------VCSVVVLKIPA-------------------KP 135
Cdd:PTZ00480  115 KYPENFFLLRGNHECASINRIYGFYdeckrrytiklwktftdcfnclpVAALIDEKILCmhgglspelsnleqirrimRP 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989 136 SFI---------------------RNNKRGLSVCFNEAAVNETCRLLNISLIVRGHQMMPAGFKFFADRKLCTIFSAPRY 194
Cdd:PTZ00480  195 TDVpdtgllcdllwsdpdkdvqgwADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNY 274

                         250       260
                  ....*....|....*....|....*
gi 1831510989 195 MNEIDNSGAVMKVASNGKISISIMK 219
Cdd:PTZ00480  275 CGEFDNAGSMMTIDESLMCSFQILK 299

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 1831510989  16 VIELFKKEKTLAEISPP----VTIVGDIHGQFEDLVRL--LNTRNSSENakskpiygfstkKWVFLGDYVDRGYKSLDCI 89
Cdd:cd07417    41 VKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIfeLNGLPSETN------------PYLFNGDFVDRGSFSVEVI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  90 CLVFSLKICFPKQYILLRGNHETRAINFRYGFR-----------------------VCSVVVLKI-------PAKPSF-- 137
Cdd:cd07417   109 LTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEgevkakyneqmfnlfsevfnwlpLAHLINGKVlvvhgglFSDDGVtl 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989 138 --IRN-----------------------------NKRGLSVCFNEAAVNETCRLLNISLIVRGHQMMPAGFKFFADRKLC 186
Cdd:cd07417   189 ddIRKidrfrqppdsglmcellwsdpqpqpgrgpSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCI 268

                         250       260
                  ....*....|....*....|....
gi 1831510989 187 TIFSAPRYMNEIDNSGAVMKVASN 210
Cdd:cd07417   269 TVFSAPNYCDQMGNKGAFIRFKGS 292

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 1831510989  19 LFKKEKTLAEI----SPPVTIVGDIHGQFEDLVRLLNtrnssenakskpIYGF--STKKWVFLGDYVDRGYKSLDCICLV 92
Cdd:cd07418    50 ILHREPNCVRIdvedVCEVVVVGDVHGQLHDVLFLLE------------DAGFpdQNRFYVFNGDYVDRGAWGLETFLLL 117

                          90       100
                  ....*....|....*....|....*....
gi 1831510989  93 FSLKICFPKQYILLRGNHETRAINFRYGF 121
Cdd:cd07418   118 LSWKVLLPDRVYLLRGNHESKFCTSMYGF 146

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 1831510989  35 IVGDIHGQFEDLVRLLN----TRNSSENAKSKPiyGfstKKWVFLGDYVDRGYKSLDCICLVFSL-----KICFPkqyil 105
Cdd:cd07423     2 IIGDVHGCYDELVELLEklgyQKKEEGLYVHPE--G---RKLVFLGDLVDRGPDSIDVLRLVMNMvkagkALYVP----- 71

                  ....*.
gi 1831510989 106 lrGNHE 111
Cdd:cd07423    72 --GNHC 75

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  31 PPVTI-VGDIHGQFEDLVRLLNTRNSSENAKSkpiygFSTKKWVFLGDYVDRGYKSLDCICLVFSLKICFPKQ-YILLRG 108
Cdd:cd07421     1 PRVVIcVGDIHGYISKLNNLWLNLQSALGPSD-----FASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQrHVFLCG 75

                  ...
gi 1831510989 109 NHE 111
Cdd:cd07421    76 NHD 78

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  35 IVGDIHGQFEDLVRLLNTrnssenakskpiYGFSTKK--WVFLGDYVDRGYKSLDCICLvfslkICFPkQYILLRGNHET 112
Cdd:cd07424     5 VVGDIHGHFQRLQRALDA------------VGFDPARdrLISVGDLVDRGPESLEVLEL-----LKQP-WFHAVQGNHEQ 66

                  ....
gi 1831510989 113 RAIN 116
Cdd:cd07424    67 MAID 70

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. 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 1831510989  35 IVGDIHGQFEDLVRLLNTRnssENAKSKPIYGFSTKKWVFLGDYVDRGYKSLDCICLVFSLkiCFPKQYILLRGNHETRA 114
Cdd:cd07413     3 LIGDVHGCAHTLDRLLDLL---GYRLQGGVWRHPRRQALFVGDLIDRGPRIREVLHRVHAM--VDAGEALCVMGNHEFNA 77

                  ...
gi 1831510989 115 INF 117
Cdd:cd07413    78 LAW 80

symmetrical bis(5'-nucleosyl)-tetraphosphatase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  35 IVGDIHGQFEDLVRLLntrnssenAKSKpiygFSTKK---WvFLGDYVDRGYKSLDCICLVFSLKicfpKQYILLRGNHE 111
Cdd:PRK00166    5 AIGDIQGCYDELQRLL--------EKID----FDPAKdtlW-LVGDLVNRGPDSLEVLRFVKSLG----DSAVTVLGNHD 67

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510989  35 IVGDIHGQFEDLVRLLNTRNssenakskpiygFSTKK---WvFLGDYVDRGYKSLDCICLVFSLKicfPKQYILLrGNHE 111
Cdd:cd07422     3 AIGDIQGCYDELQRLLEKIN------------FDPAKdrlW-LVGDLVNRGPDSLETLRFVKSLG---DSAVVVL-GNHD 65