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 757799480  17 RHVWVVGDIHGCFSLLMAKLRHCHFDPWQDLLVSVGDVIDRGPDSLRCLKLLRKSWIVAVRGNHEQMGLDALAMGEQSLW 96
Cdd:cd07424    1 GRDFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPWFHAVQGNHEQMAIDALRGGDDVMW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757799480  97 FMNGGSWFAQAEQPAAKFALEECQQLPWILELRCSNGIHVIAHADYPDDDYQWQ---KDIDLQRVLWDRSRLMNK-GNGI 172
Cdd:cd07424   81 RANGGGWFFDLPDEEAKVLLEKLHHLPIAIEVESRNGKVGIVHADYPFDEYSFGfveKPEDEEEALWSRDRLQKSqTQPV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 757799480 173 RGADHFWFGHTPLRQRLDYENLHYIDTGAVFGGELTLVQLQ 213
Cdd:cd07424  161 AGADAFIFGHTPVPEPLDLGNVYYIDTGGVFDGNLTLVKLQ 201

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757799480   20 WVVGDIHGCFSLLMAKLRHCHFDPWQDLLVSVGDVIDRGPDSLRCLKLLrKSWIVAVR---GNHE 81
Cdd:TIGR00668   4 YLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYV-KSLGDAVRlvlGNHD 67

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757799480    19 VWVVGDIHGCFSLLMAKLRHCHFDPwQDLLVSVGDVIDRGPDSLRC------LKLLRKSWIVAVRGNHE 81
Cdd:smart00156  30 VTVCGDIHGQFDDLLRLFDKNGQPP-ETNYVFLGDYVDRGPFSIEVilllfaLKILYPNRIVLLRGNHE 97

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 757799480  17 RHVWVVGDIHGCFSLLMAKLRHCHFDPWQDLLVSVGDVIDRGPDSLRCLKLLRKSWIVAVRGNHEQMGLDALAMGEQSLW 96
Cdd:cd07424    1 GRDFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPWFHAVQGNHEQMAIDALRGGDDVMW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757799480  97 FMNGGSWFAQAEQPAAKFALEECQQLPWILELRCSNGIHVIAHADYPDDDYQWQ---KDIDLQRVLWDRSRLMNK-GNGI 172
Cdd:cd07424   81 RANGGGWFFDLPDEEAKVLLEKLHHLPIAIEVESRNGKVGIVHADYPFDEYSFGfveKPEDEEEALWSRDRLQKSqTQPV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 757799480 173 RGADHFWFGHTPLRQRLDYENLHYIDTGAVFGGELTLVQLQ 213
Cdd:cd07424  161 AGADAFIFGHTPVPEPLDLGNVYYIDTGGVFDGNLTLVKLQ 201

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757799480  20 WVVGDIHGCFSLLMAKLrHCHFDPWQDLLVSVGDVIDRGPDS------LRCLKLLRKSWIVAVRGNHEQM 83
Cdd:cd00144    1 IVVGDIHGCFDDLLRLL-EKLGFPPEDKYLFLGDYVDRGPDSvevidlLLALKILYPDNVFLLRGNHEFM 69

Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and PrpA/PrpB. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757799480  19 VWVVGDIHGCFSLLMAKLRHCHFDPWQDLLVSVGDVIDRGPDSLRCLKLLR--KSWIVAVRGNHE 81
Cdd:cd07422    1 TYAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKslGDSAVVVLGNHD 65

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757799480   18 HVWVVGDIH--GCFSLLMAKLRHCHFDPWQDLLVSVGDVIDRGPDSLRCLKLLRKSW----IVAVRGNHEQMGLDALAM 90
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIkyvpVYLVRGNHDFDYGECLRL 80

Predicted phosphodiesterase, calcineurin family [General function prediction only];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757799480  21 VVGDIHGCFSLLMAKLRHchFDPWQ-DLLVSVGDVIDRGPDSLRCLKLLRKSWIVAVRGNHEQMGLDALA 89
Cdd:COG0622    4 VISDTHGNLPALEAVLED--LEREGvDLIVHLGDLVGYGPDPPEVLDLLRELPIVAVRGNHDGAVLRGLR 71

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 757799480  21 VVGDIHGCFSLLMAKLRHCHF----DPW---QDLLVSVGDVIDRGPDSLRCLKLLRK---------SWIVAVRGNHEQMG 84
Cdd:cd07425    2 AIGDLHGDLDRLRTILKLAGVidsnDRWiggDTVVVQTGDILDRGDDEIEILKLLEKlkrqarkagGKVILLLGNHELMN 81

                 .
gi 757799480  85 L 85
Cdd:cd07425   82 L 82

serine/threonine-protein phosphatase PP1; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757799480  19 VWVVGDIHGCFSLLMAKLRHCHFDPWQDLLVsVGDVIDRGPDSLR------CLKLLRKSWIVAVRGNHE 81
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFPPYSNYLF-LGDYVDRGKHSVEtitlqfCYKIVYPENFFLLRGNHE 121

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 757799480  21 VVGDIHGCFSLLMAKLRHCHF---DPwqDLLVSVGDVIDRGPDSLRCLK-----LLRKSWIVAVRGNHE 81
Cdd:cd00838    2 VISDIHGNLEALEAVLEAALAkaeKP--DLVICLGDLVDYGPDPEEVELkalrlLLAGIPVYVVPGNHD 68

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757799480  19 VWVVGDIHGCFSLLMAKLR---HChfdPWQDLLVsVGDVIDRGPDS------LRCLKLLRKSWIVAVRGNHE 81
Cdd:cd07415   44 VTVCGDIHGQFYDLLELFRiggDV---PDTNYLF-LGDYVDRGYYSvetfllLLALKVRYPDRITLLRGNHE 111

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757799480  21 VVGDIHGCFSLLMAKLRHCHFDPWQDLLVsVGDVIDRGPDSLR--CL----KLLRKSWIVAVRGNHE 81
Cdd:cd07414   54 ICGDIHGQYYDLLRLFEYGGFPPESNYLF-LGDYVDRGKQSLEtiCLllayKIKYPENFFLLRGNHE 119