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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 150 IKTLLACKGMTKIRTM-----DIFRLIHICKKIFTVQKSMVEIDGPVRICGDLHGQYPDLIRLFAQGGFPPDSNYLFLGD 224
Cdd:cd07414     6 IERLLEVRGSRPGKNVqlteaEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 225 YVDRGSFNLEVILLCLAYKARYPNNFMMLRGNHEVIHINEKYGFKDEVfnrKGEYHDELYPEFNEMMDMMPLVALVGGRI 304
Cdd:cd07414    86 YVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDEC---KRRYNIKLWKTFTDCFNCLPVAAIVDEKI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 305 LCMHGGLSQHIKSLDDLRNLRRPFHSEDECLENDIMWSDPAK-VSGWTANPRGASVQFGENEVKEMCKLLDIDLIVRGHQ 383
Cdd:cd07414   163 FCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKdVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQ 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1831510693 384 VVQDGYEFFAGKKLVTVFSAPHYMQSFTNSAAVCKVSAGLEVSFEVLKP 432
Cdd:cd07414   243 VVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291

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 1831510693 190 PVRICGDLH--GQYPDLIRLFaQGGFPPDSNYLFL--GDYVDRGSFNLEVILLcLAYKARYpNNFMMLRGNHEVIHinek 265
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELL-KKLLEEGKPDLVLhaGDLVDRGPPSEEVLEL-LERLIKY-VPVYLVRGNHDFDY---- 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1831510693 266 ygfkDEVFNRKGEYH--DELYPEFNEMMDMMPLVALVGG 302
Cdd:pfam00149  75 ----GECLRLYPYLGllARPWKRFLEVFNFLPLAGILSG 109

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 150 IKTLLACKGMTKIRTM-----DIFRLIHICKKIFTVQKSMVEIDGPVRICGDLHGQYPDLIRLFAQGGFPPDSNYLFLGD 224
Cdd:cd07414     6 IERLLEVRGSRPGKNVqlteaEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 225 YVDRGSFNLEVILLCLAYKARYPNNFMMLRGNHEVIHINEKYGFKDEVfnrKGEYHDELYPEFNEMMDMMPLVALVGGRI 304
Cdd:cd07414    86 YVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDEC---KRRYNIKLWKTFTDCFNCLPVAAIVDEKI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 305 LCMHGGLSQHIKSLDDLRNLRRPFHSEDECLENDIMWSDPAK-VSGWTANPRGASVQFGENEVKEMCKLLDIDLIVRGHQ 383
Cdd:cd07414   163 FCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKdVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQ 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1831510693 384 VVQDGYEFFAGKKLVTVFSAPHYMQSFTNSAAVCKVSAGLEVSFEVLKP 432
Cdd:cd07414   243 VVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291

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 1831510693 147 EHFIKTLLACKgmtKIRTMDIFRLIHICKKIFTVQKSMVEIDGPVRICGDLHGQYPDLIRLFAQGGFPPDSNYLFLGDYV 226
Cdd:cd07415     3 DQWIEQLKKCE---LLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 227 DRGSFNLEVILLCLAYKARYPNNFMMLRGNHEVIHINEKYGFKDEVFNRKGeyHDELYPEFNEMMDMMPLVALVGGRILC 306
Cdd:cd07415    80 DRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYG--NANVWKYFTDLFDYLPLAALIDGQIFC 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 307 MHGGLSQHIKSLDDLRNLRR----PfHSEDEClenDIMWSDPAKVSGWTANPRGASVQFGENEVKEMCKLLDIDLIVRGH 382
Cdd:cd07415   158 VHGGLSPSIQTLDQIRALDRfqevP-HEGPMC---DLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAH 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831510693 383 QVVQDGYEFFAGKKLVTVFSAPHYMQSFTNSAAVCKVSAGLEVSFEVLKP 432
Cdd:cd07415   234 QLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283

serine/threonine-protein phosphatase PP1; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 162 IRTMDIFRLIHICKKIFTVQKSMVEIDGPVRICGDLHGQYPDLIRLFAQGGFPPDSNYLFLGDYVDRGSFNLEVILLCLA 241
Cdd:PTZ00244   25 IREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFC 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 242 YKARYPNNFMMLRGNHEVIHINEKYGFKDEVfnrKGEYHDELYPEFNEMMDMMPLVALVGGRILCMHGGLSQHIKSLDDL 321
Cdd:PTZ00244  105 YKIVYPENFFLLRGNHECASINKMYGFFDDV---KRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 322 RNLRRPFHSEDECLENDIMWSDPA-KVSGWTANPRGASVQFGENEVKEMCKLLDIDLIVRGHQVVQDGYEFFAGKKLVTV 400
Cdd:PTZ00244  182 NEIERPCDVPDRGILCDLLWADPEdEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTV 261

                         250       260       270
                  ....*....|....*....|....*....|
gi 1831510693 401 FSAPHYMQSFTNSAAVCKVSAGLEVSFEVL 430
Cdd:PTZ00244  262 FSAPNYCGEFDNDAAVMNIDDKLQCSFLII 291

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 167 IFRLIHICKKIFTVQKSMVEIDGPVRICGDLHGQYPDLIRLFAQGGFPPDS--------NYLFLGDYVDRGSFNLEVILL 238
Cdd:cd07419    26 IAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEeagdieyiDYLFLGDYVDRGSHSLETICL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 239 CLAYKARYPNNFMMLRGNHEVIHINEKYGFKDEVFNRKGEYH---DELYPEFNEMMDMMPLVALVGGRILCMHGGLSQHI 315
Cdd:cd07419   106 LLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDIrdgDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSI 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 316 KSLDDLRNLRRPFHSE-DECLENDIMWSDPAK---VSGWTANPR-----GASVQFGENEVKEMCKLLDIDLIVRGHQVVQ 386
Cdd:cd07419   186 NHIHQIENLKRPITMEaGSPVVMDLLWSDPTEndsVLGLRPNAIdprgtGLIVKFGPDRVMEFLEENDLQMIIRAHECVM 265

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1831510693 387 DGYEFFAGKKLVTVFSAPHYMQSFTNSAAVCKVSAGLEVSFEVLKP 432
Cdd:cd07419   266 DGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311

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 1831510693 140 ESNKMFAEhFIKTLLA-CKGMTKIRTMDIFRLIHICKKIFTVQKSMVEIDGP----VRICGDLHGQYPDLIRLFAQGGFP 214
Cdd:cd07417     7 EDGKVTLE-FVKEMMEwFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 215 PDSN-YLFLGDYVDRGSFNLEVILLCLAYKARYPNNFMMLRGNHEVIHINEKYGFKDEVfnrKGEYHDELYPEFNEMMDM 293
Cdd:cd07417    86 SETNpYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEV---KAKYNEQMFNLFSEVFNW 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 294 MPLVALVGGRILCMHGGL-SQHIKSLDDLRNLRRPFHSEDECLENDIMWSDPAKVSGWTANPRGASVQFGENEVKEMCKL 372
Cdd:cd07417   163 LPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFLEE 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831510693 373 LDIDLIVRGHQVVQDGYEFFAGKKLVTVFSAPHYMQSFTNSAAVCKVSAG 422
Cdd:cd07417   243 NNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGS 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 1831510693 169 RLIHICKKIFTVQKSMVEID----GPVRICGDLHGQYPDLIRLFAQGGFP-PDSNYLFLGDYVDRGSFNLEVILLCLAYK 243
Cdd:cd07418    42 SLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPdQNRFYVFNGDYVDRGAWGLETFLLLLSWK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 244 ARYPNNFMMLRGNHEVIHINEKYGFKDEVFNRKGEYHDELYPEFNEMMDMMPLVALVGGRILCMHGGL------------ 311
Cdd:cd07418   122 VLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkq 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 312 ---------------SQHIKSLDDLRNLRR----PFHSEDECLENDIMWSDPAKVSGWTAN-PRGASVQFGENEVKEMCK 371
Cdd:cd07418   202 kgknrrvlllepeseSLKLGTLDDLMKARRsvldPPGEGSNLIPGDVLWSDPSLTPGLSPNkQRGIGLLWGPDCTEEFLE 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831510693 372 LLDIDLIVRGHQ------------VVQDGY----EFFAGkKLVTVFSAPHYMQ 408
Cdd:cd07418   282 KNNLKLIIRSHEgpdarekrpglaGMNKGYtvdhDVESG-KLITLFSAPDYPQ 333

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510693 193 ICGDLHGQYPDLIRLF--AQGGFPPDSNYLFLGDYVDRGSFNLEVILLCLAYKARyPNNFMMLRGNHEVI--HI 262
Cdd:cd00838     2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLA-GIPVYVVPGNHDILvtHG 74

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 193 ICGDLHGQYPDL---IRLFAQGGFppdSNYLFLGDYVDRGSFNLEVILLCLAykarypNNFMMLRGNHEvihinekygfk 269
Cdd:COG0622     4 VISDTHGNLPALeavLEDLEREGV---DLIVHLGDLVGYGPDPPEVLDLLRE------LPIVAVRGNHD----------- 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510693 270 DEVFNRKGEyhdelYPEFNEmmdmmplVALVGGRILCMHGGLSQHIKSLDDLRNLRRPFHSED 332
Cdd:COG0622    64 GAVLRGLRS-----LPETLR-------LELEGVRILLVHGSPNEYLLPDTPAERLRALAAEGD 114

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.

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gi 1831510693 191 VRIC-GDLHGQYPDLIRLFA--QGGFPPD----SNYLFLGDYVDRGSFNLEVILLCLAYKARYPNN-FMMLRGNHE 258
Cdd:cd07421     3 VVICvGDIHGYISKLNNLWLnlQSALGPSdfasALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQrHVFLCGNHD 78

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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510693 193 ICGDLHGQYPDLIRLFAQGGFPPDSNYL----------FLGDYVDRGSFNLEVILLCL-AYKArypNNFMMLRGNHE--- 258
Cdd:cd07423     2 IIGDVHGCYDELVELLEKLGYQKKEEGLyvhpegrklvFLGDLVDRGPDSIDVLRLVMnMVKA---GKALYVPGNHCnkl 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510693 259 ----------VIHINEKYGfkDEVFNRKGEYHDELYPEFNEMMDMMPLVA-LVGGRILCMHGGLSQH 314
Cdd:cd07423    79 yrylkgrnvqLAHGLETTV--EELEALSKEERPEFRERFAEFLESLPSHLvLDGGRLVVAHAGIKEE 143

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 1831510693 195 GDLHGQYPDLIRLFAQGGFPPDSNYL-FLGDYVDRGSFNLEVILLCLAYKaryPNNFMMLrGNHEvIH 261
Cdd:cd07422     5 GDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLETLRFVKSLG---DSAVVVL-GNHD-LH 67