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 1267225629   4 DIIGDIHGCFQEFQDLTTKLGYNWNSD-LPFHPDQRKLAFVGDITDRGPHSLRMIEIVWELVINKKvAYYAPGNHCNKLY 82
Cdd:cd07423     1 DIIGDVHGCYDELVELLEKLGYQKKEEgLYVHPEGRKLVFLGDLVDRGPDSIDVLRLVMNMVKAGK-ALYVPGNHCNKLY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267225629  83 RFFLGRNVTIAHGLETTVAEYEALPSHKQNIIKEKFITLYEQSPLYHVLDEKRLIVCHAGIRQDYIGRQDKKVQTFVLYG 162
Cdd:cd07423    80 RYLKGRNVQLAHGLETTVEELEALSKEERPEFRERFAEFLESLPSHLVLDGGRLVVAHAGIKEEMIGRGSKRVRDFCLYG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267225629 163 DITGEKHADGSPVRRDWANEYIGKAWIVYGHTPVKEPRFVNHTVNIDTGAVFGGKLTGLRYPEMETVSIPSSLSF 237
Cdd:cd07423   160 DTTGETDEDGLPVRRDWAKDYRGKALVVYGHTPVPEPRWLNNTINIDTGCVFGGKLTALRYPEMELVSVPAKQPY 234

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 1267225629   1 MKFDIIGDIH--GCFQEFQDLTTKLGYNWNSDLpfhpdqrkLAFVGDITDRGPHSLRMIEIVWELVINKKVaYYAPGNH 77
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEEGKPDL--------VLHAGDLVDRGPPSEEVLELLERLIKYVPV-YLVRGNH 70

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 1267225629   4 DIIGDIHGCFQEFQDLTTKLGYNWNSD-LPFHPDQRKLAFVGDITDRGPHSLRMIEIVWELVINKKvAYYAPGNHCNKLY 82
Cdd:cd07423     1 DIIGDVHGCYDELVELLEKLGYQKKEEgLYVHPEGRKLVFLGDLVDRGPDSIDVLRLVMNMVKAGK-ALYVPGNHCNKLY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267225629  83 RFFLGRNVTIAHGLETTVAEYEALPSHKQNIIKEKFITLYEQSPLYHVLDEKRLIVCHAGIRQDYIGRQDKKVQTFVLYG 162
Cdd:cd07423    80 RYLKGRNVQLAHGLETTVEELEALSKEERPEFRERFAEFLESLPSHLVLDGGRLVVAHAGIKEEMIGRGSKRVRDFCLYG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267225629 163 DITGEKHADGSPVRRDWANEYIGKAWIVYGHTPVKEPRFVNHTVNIDTGAVFGGKLTGLRYPEMETVSIPSSLSF 237
Cdd:cd07423   160 DTTGETDEDGLPVRRDWAKDYRGKALVVYGHTPVPEPRWLNNTINIDTGCVFGGKLTALRYPEMELVSVPAKQPY 234

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 1267225629   5 IIGDIHGCFQEFQDLTTKLGYnwnsdlpfhPDQRKLAFVGDITDRGPHSLRMIEIVWELVINKKV-AYYAPGNH----CN 79
Cdd:cd00144     2 VVGDIHGCFDDLLRLLEKLGF---------PPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDnVFLLRGNHefmlLN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267225629  80 KLYRFFlgrnvtiahglettvAEYEALPSHKQN-IIKEKFITLYEQSPLYHVLDEKRLIVcHAGIRQDYIGRQDKKVQTF 158
Cdd:cd00144    73 FLYGFY---------------DERTLRCLRKGGeELWREFNEVFNYLPLAALVDGKILCV-HGGLSPDLTLLDQIRNIRP 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267225629 159 VLYGDITGEK---HADGSPVRRDWANEYIGKAW------------------IVYGHTPV---KEPRFVNHTVNIDTGAVF 214
Cdd:cd00144   137 IENPDDQLVEdllWSDPDESVGDFESSSRGGGYlfgedavdeflkknglklIVRGHTPVeggYEFLHGGKLITIFSAPNY 216

                  ....*.
gi 1267225629 215 GGKLTG 220
Cdd:cd00144   217 CGKGGN 222

symmetrical bis(5'-nucleosyl)-tetraphosphatase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267225629   5 IIGDIHGCFQEFQDLTTKLGynwnsdlpFHPDQRKLAFVGDITDRGPHSLRMIEIVWEL------VInkkvayyapGNHc 78
Cdd:PRK00166    5 AIGDIQGCYDELQRLLEKID--------FDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLgdsavtVL---------GNH- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267225629  79 nKLYrfFLGrnvtIAHGLETtvaeyeALPSHK-QNIIK----EKFITLYEQSPLYHVLDEKRLIVCHAGIR--------- 144
Cdd:PRK00166   67 -DLH--LLA----VAAGIKR------NKKKDTlDPILEapdrDELLDWLRHQPLLHVDEELGLVMVHAGIPpqwdlatal 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267225629 145 ------QDYIgrQDKKVQTFV--LYG--------DITGEK---------------HADGspvRRDWA-NEYIGKA----- 187
Cdd:PRK00166  134 alarevEAVL--RSDDYRDFLanMYGnepdrwspDLTGLErlryiinaftrmrfcTPDG---RLDFKcKGPPDEApaglk 208

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267225629 188 -W------------IVYGH--------TPvkeprfvNHTVNIDTGAVFGGKLTGLRYPEMETVSIPS 233
Cdd:PRK00166  209 pWfevpgrktrdytIVFGHwaalegltTP-------PNIIALDTGCVWGGKLTALRLEDKQIFQVPC 268

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 1267225629   5 IIGDIHGCFQEFQDLTTKLGYNWNSDlpfhpdqrKLAFVGDITDRGPHSLRMIEIVWELVINKKVAYyapGNHcnKLYrf 84
Cdd:cd07422     3 AIGDIQGCYDELQRLLEKINFDPAKD--------RLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVL---GNH--DLH-- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267225629  85 FLGrnvtIAHGLETtvaeyealPSHK---QNIIK----EKFITLYEQSPLYHVLDEKRLIVCHAGI 143
Cdd:cd07422    68 LLA----VAAGIKK--------LKKKdtlDEILEapdrDELLDWLRHQPLLHRDDELGIVMVHAGI 121

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 1267225629   1 MKFDIIGDIH--GCFQEFQDLTTKLGYNWNSDLpfhpdqrkLAFVGDITDRGPHSLRMIEIVWELVINKKVaYYAPGNH 77
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEEGKPDL--------VLHAGDLVDRGPPSEEVLELLERLIKYVPV-YLVRGNH 70

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 1267225629   5 IIGDIHGcfqEFQDLTTKLgynwnsDLPFHPDQRKLAFVGDITDRGPHSLRMIEIVWELVIN-KKVAYYAPGNH-CNKLY 82
Cdd:cd07416    47 VCGDIHG---QFYDLLKLF------EVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILyPKTLFLLRGNHeCRHLT 117

                  ...
gi 1267225629  83 RFF 85
Cdd:cd07416   118 EYF 120

protein-serine/threonine phosphatase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267225629   5 IIGDIHGCFQEFQdltTKLgynwnSDLPFHPDQRKLAFVGDITDRGPHSLRMIEIV 60
Cdd:PRK09968   19 VVGDIHGEYQLLQ---SRL-----HQLSFCPETDLLISVGDNIDRGPESLNVLRLL 66