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 1196808651   7 YVVGDVQGCFEALKALLKEIRFDPDQDFLWFAGDLVARGENSVGALRFIKKLADRgaAATVLGNHDLTLIAGARGLKEIK 86
Cdd:cd07422     2 YAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDS--AVVVLGNHDLHLLAVAAGIKKLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651  87 EKDRTQDVIDAIDGDELIDWLRKQPLCLLPNEH-TILTHAGIPCIWDAQKTVTLAKEVEAVLANEDlsvLDAFLADMYGS 165
Cdd:cd07422    80 KKDTLDEILEAPDRDELLDWLRHQPLLHRDDELgIVMVHAGIPPQWDIEKALALAREVEAVLRGDN---YRDFLANMYGN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651 166 KPDLWEDNLTGSARLRCITNYLTRMRLTNAEGALEFSFKDSLDAPmPECYLPWFEFPSKAAQTHQIIFGHWAALEGRTID 245
Cdd:cd07422   157 EPDRWSDDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEA-PAGLRPWFDVPNRKTRDYTIVFGHWAALGGLTRP 235

                         250       260
                  ....*....|....*....|..
gi 1196808651 246 EQIQNIDGGCVWGRKLMAYRLE 267
Cdd:cd07422   236 NNIIALDTGCVWGGKLTALRLE 257

Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651  99 DGDELIDWLRKQPLCLLPNEH-TILTHAGIPCIWDAQKTVTLAKEVEAVLANEDLSVLDAFLADMYGSKPDLWEDNLTGS 177
Cdd:COG0639     3 DLLRLDLLLLLLRRLLLLLHDlHLLAHAGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLYGMYYNKPDRWSDDLQGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651 178 ARLRCITNYLTRMRLTNAEGALEFSFKDSLDAPMPEcYLPWFEFPSKAAQTHQIIFGHWAALEGRTIDEQIQNIDGGCVW 257
Cdd:COG0639    83 DRLRFIINAFTRMRFCTPDGRLDFKCKEPPETAPPG-LKPWFDVPGRRTADYTIVFGHWAALEGLGTPPNIYALDTGCVW 161

                         170
                  ....*....|....*..
gi 1196808651 258 GRKLMAYRLEDKEIFSV 274
Cdd:COG0639   162 GGKLTALRWEDKQRFQV 178

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 1196808651   7 YVVGDVQGCFEALKALLKEIRFDPDQDFLWFAGDLVARGENSVGALRFIKKLADRgaAATVLGNHDLTLIAGARGLKEIK 86
Cdd:cd07422     2 YAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDS--AVVVLGNHDLHLLAVAAGIKKLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651  87 EKDRTQDVIDAIDGDELIDWLRKQPLCLLPNEH-TILTHAGIPCIWDAQKTVTLAKEVEAVLANEDlsvLDAFLADMYGS 165
Cdd:cd07422    80 KKDTLDEILEAPDRDELLDWLRHQPLLHRDDELgIVMVHAGIPPQWDIEKALALAREVEAVLRGDN---YRDFLANMYGN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651 166 KPDLWEDNLTGSARLRCITNYLTRMRLTNAEGALEFSFKDSLDAPmPECYLPWFEFPSKAAQTHQIIFGHWAALEGRTID 245
Cdd:cd07422   157 EPDRWSDDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEA-PAGLRPWFDVPNRKTRDYTIVFGHWAALGGLTRP 235

                         250       260
                  ....*....|....*....|..
gi 1196808651 246 EQIQNIDGGCVWGRKLMAYRLE 267
Cdd:cd07422   236 NNIIALDTGCVWGGKLTALRLE 257

Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651  99 DGDELIDWLRKQPLCLLPNEH-TILTHAGIPCIWDAQKTVTLAKEVEAVLANEDLSVLDAFLADMYGSKPDLWEDNLTGS 177
Cdd:COG0639     3 DLLRLDLLLLLLRRLLLLLHDlHLLAHAGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLYGMYYNKPDRWSDDLQGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651 178 ARLRCITNYLTRMRLTNAEGALEFSFKDSLDAPMPEcYLPWFEFPSKAAQTHQIIFGHWAALEGRTIDEQIQNIDGGCVW 257
Cdd:COG0639    83 DRLRFIINAFTRMRFCTPDGRLDFKCKEPPETAPPG-LKPWFDVPGRRTADYTIVFGHWAALEGLGTPPNIYALDTGCVW 161

                         170
                  ....*....|....*..
gi 1196808651 258 GRKLMAYRLEDKEIFSV 274
Cdd:COG0639   162 GGKLTALRWEDKQRFQV 178

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 1196808651   8 VVGDVQGCFEALKALLKEIRFDPDQDFLW---------FAGDLVARGENSVGALRFIKKLADRGAAATVLGNHDLTLiag 78
Cdd:cd07423     2 IIGDVHGCYDELVELLEKLGYQKKEEGLYvhpegrklvFLGDLVDRGPDSIDVLRLVMNMVKAGKALYVPGNHCNKL--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651  79 ARGLK-----------------EIKEKDRTQDVidaidGDELIDWLRKQPLCL-LPNEHTILTHAGIPciwdaqktvtla 140
Cdd:cd07423    79 YRYLKgrnvqlahglettveelEALSKEERPEF-----RERFAEFLESLPSHLvLDGGRLVVAHAGIK------------ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651 141 keveavlanedlsvldaflADMYGSkpdlwednltGSARLR--CITNYLTRMrlTNAEGalefsfkdsldapMPECYlPW 218
Cdd:cd07423   142 -------------------EEMIGR----------GSKRVRdfCLYGDTTGE--TDEDG-------------LPVRR-DW 176

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196808651 219 F-EFPSKAAqthqIIFGHWAALE----GRTIdeqiqNIDGGCVWGRKLMAYRLEDKEIFSV 274
Cdd:cd07423   177 AkDYRGKAL----VVYGHTPVPEprwlNNTI-----NIDTGCVFGGKLTALRYPEMELVSV 228

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196808651   7 YVVGDVQGCFEALKALLKEIRFDPDQDFLWFAGDLVARGENSVGALRFIKKLADRgaaaTVLGNHDLTLIAGARGL 82
Cdd:cd07424     4 FVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPWFH----AVQGNHEQMAIDALRGG 75

protein-serine/threonine phosphatase;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196808651   4 RFNYVVGDVQGCFEALKALLKEIRFDPDQDFLWFAGDLVARGENSVGALRFIKKLADRGaaatVLGNHD 72
Cdd:PRK11439   17 RHIWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEEHWVRA----VRGNHE 81

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 1196808651   8 VVGDVQGCFEALKALLKEIRFD--------PDQDFLwFAGDLVARGENSVGALRFIKKLADRGAAATVLGNHDLTLIA-- 77
Cdd:cd07413     3 LIGDVHGCAHTLDRLLDLLGYRlqggvwrhPRRQAL-FVGDLIDRGPRIREVLHRVHAMVDAGEALCVMGNHEFNALAwh 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1196808651  78 -------GARGLKEIKEKDRTQ--DVIDAIDGDELID---WLRKQPLCLLPNE 118
Cdd:cd07413    82 tpappgsGRQYVREHSPKNARQhkATLDQFEGHDWRDflgWFQTLPLFLDLGR 134

protein-serine/threonine phosphatase;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196808651   4 RFNYVVGDVQGCFEALKALLKEIRFDPDQDFLWFAGDLVARGENSVGALRfikkLADRGAAATVLGNHD 72
Cdd:PRK09968   15 RHIWVVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLR----LLNQPWFISVKGNHE 79

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196808651  17 EALKALLKEIRfDPDQDFLWFAGDLVARGENS--VGALRFIKKLADRgaAATVLGNHDLTLIAGARGLKEIKEKDRTQD- 93
Cdd:COG1409    21 EVLAAALADIN-APRPDFVVVTGDLTDDGEPEeyAAAREILARLGVP--VYVVPGNHDIRAAMAEAYREYFGDLPPGGLy 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196808651  94 -----------VIDAID--------GDELIDWLRKQpLCLLPNEHTIL-THagIPCI----WDAQKTVTLAKEVEAVLA 148
Cdd:COG1409    98 ysfdyggvrfiGLDSNVpgrssgelGPEQLAWLEEE-LAAAPAKPVIVfLH--HPPYstgsGSDRIGLRNAEELLALLA 173

Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. 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 1196808651   8 VVGDVQGCFEAL-KALLKEIRfdPDqdFLWFAGDLvarGENSVGALRFIKKLadRGAAATVLGNHD--LTLIAGARGLKE 84
Cdd:cd07397     5 IVGDVHGQWDAEdERALRLLQ--PD--LVLFVGDF---GNENVQLVRRIASL--DLPKAVILGNHDawYTATRWGRCPYD 75

                          90       100
                  ....*....|....*....|....*.
gi 1196808651  85 IKEKDRTQDVIDAIdGDELIDWLRKQ 110
Cdd:cd07397    76 RSKGDRVQQQLEIL-GDEHVGYGRLD 100