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 392885016  45 VDITISEISQLTDKMKKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCL 124
Cdd:cd07414   21 VQLTEAEIRGLCLKSREIFLSQPILLELE-APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 125 LFCMKHRYPQHVFLLRGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLES 204
Cdd:cd07414  100 LLAYKIKYPENFFLLRGNHECASINRIYGFYDEC----KRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 205 LEDINSIERPLVVPPYGLACDLLWSDPaQPERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYPqgcvl 284
Cdd:cd07414  176 MEQIRRIMRPTDVPDQGLLCDLLWSDP-DKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYE----- 249

                        250       260
                 ....*....|....*....|...
gi 392885016 285 RFGGR-LISLFSALNYEGHKNNS 306
Cdd:cd07414  250 FFAKRqLVTLFSAPNYCGEFDNA 272

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 392885016   76 PITVVADMH--GQSIHLLRIFlTNEAPPNQKYLFL--GDYVDRGSQSVVVMcLLFCMKHRYpQHVFLLRGNHEDvnttln 151
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELL-KKLLEEGKPDLVLhaGDLVDRGPPSEEVL-ELLERLIKY-VPVYLVRGNHDF------ 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 392885016  152 ygFYDECLEQWKNDEG-EKVWRMFIDTFNCMPLAAVIGG 189
Cdd:pfam00149  73 --DYGECLRLYPYLGLlARPWKRFLEVFNFLPLAGILSG 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 392885016  45 VDITISEISQLTDKMKKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCL 124
Cdd:cd07414   21 VQLTEAEIRGLCLKSREIFLSQPILLELE-APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 125 LFCMKHRYPQHVFLLRGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLES 204
Cdd:cd07414  100 LLAYKIKYPENFFLLRGNHECASINRIYGFYDEC----KRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 205 LEDINSIERPLVVPPYGLACDLLWSDPaQPERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYPqgcvl 284
Cdd:cd07414  176 MEQIRRIMRPTDVPDQGLLCDLLWSDP-DKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYE----- 249

                        250       260
                 ....*....|....*....|...
gi 392885016 285 RFGGR-LISLFSALNYEGHKNNS 306
Cdd:cd07414  250 FFAKRqLVTLFSAPNYCGEFDNA 272

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 392885016  78 TVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLLRGNHEDVNTTLNYGFYDE 157
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 158 CLEQWKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIeRPLVVPPYGLACDLLWSDPAQPErN 237
Cdd:cd00144   81 RTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESV-G 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392885016 238 GWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYpqgcVLRFGGRLISLFSALNYEGHKNNS-SVLKL 311
Cdd:cd00144  159 DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGY----EFLHGGKLITIFSAPNYCGKGGNKlAALVV 229

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 392885016  47 ITISEISQLTDKMKKAFLEQPALLEIsNEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLF 126
Cdd:cd07416   16 LSEEDALRIITEGAEILRQEPNLLRI-EAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 127 CMKHRYPQHVFLLRGNHEDVNTTLNYGFYDECLEQWkndeGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLE 206
Cdd:cd07416   95 ALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY----SERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLD 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 207 DINSIERPLVVPPYGLACDLLWSDPAQPERNGWGLSH------RGISFTYGKSVVEEFCAKNDIALVIRGHQLFKE---M 277
Cdd:cd07416  171 DIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHfvhntvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAgyrM 250

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 392885016 278 YPQGCVLRFGGrLISLFSALNYEGHKNN-SSVLKLE 312
Cdd:cd07416  251 YRKSQTTGFPS-LITIFSAPNYLDVYNNkAAVLKYE 285

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 392885016  42 QLRVDITISEISQLTDKMKKAFLEQPALLEIsNEPITVVADMHGQSIHLLRIFLTNEAPPNQK--------YLFLGDYVD 113
Cdd:cd07419   16 ERRFFFDCQEIAELCDEAERIFRQEPSVLRL-RAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagdieyidYLFLGDYVD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 114 RGSQSVVVMCLLFCMKHRYPQHVFLLRGNHEDVNTTLNYGFYDECLEQWKND--EGEKVWRMFIDTFNCMPLAAVIGGKV 191
Cdd:cd07419   95 RGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirDGDSVWQRINRLFNWLPLAALIEDKI 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 192 FCAHGGISPWLESLEDINSIERPLVVPPYG-LACDLLWSDPAQP------ERNGWGLSHRGISFTYGKSVVEEFCAKNDI 264
Cdd:cd07419  175 ICVHGGIGRSINHIHQIENLKRPITMEAGSpVVMDLLWSDPTENdsvlglRPNAIDPRGTGLIVKFGPDRVMEFLEENDL 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392885016 265 ALVIRGHQlfkemypqgCVL----RF-GGRLISLFSALNYEG-HKNNSSVLKL 311
Cdd:cd07419  255 QMIIRAHE---------CVMdgfeRFaQGHLITLFSATNYCGtAGNAGAILVL 298

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 392885016  54 QLTDKMKKAFLEQPALLEISNEP---ITVVADMHGQSIHLLRIFLTNEAP-PNQKYLFLGDYVDRGSQSVVVMCLLFCMK 129
Cdd:cd07417   36 QILLQVKEILKKLPSLVEITIPEgekITVCGDTHGQFYDLLNIFELNGLPsETNPYLFNGDFVDRGSFSVEVILTLFAFK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 130 HRYPQHVFLLRGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGispwLES----- 204
Cdd:cd07417  116 LLYPNHFHLNRGNHETDNMNKIYGFEGEV----KAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGG----LFSddgvt 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 205 LEDINSIERPLVVPPYGLACDLLWSDPaQPeRNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHqlfkEMYPQGCVL 284
Cdd:cd07417  188 LDDIRKIDRFRQPPDSGLMCELLWSDP-QP-QPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSH----EVKDEGYEV 261

                        250
                 ....*....|....*
gi 392885016 285 RFGGRLISLFSALNY 299
Cdd:cd07417  262 EHDGKCITVFSAPNY 276

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 392885016  49 ISEISQLTDKMKKAFLEQPALLEI---SNEPITVVADMHGQSIHLLRIFLTNEAP-PNQKYLFLGDYVDRGSQSVVVMCL 124
Cdd:cd07418   37 VNVFDSLVLTAHKILHREPNCVRIdveDVCEVVVVGDVHGQLHDVLFLLEDAGFPdQNRFYVFNGDYVDRGAWGLETFLL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 125 LFCMKHRYPQHVFLLRGNHEDVNTTLNYGFYDECLEQWkNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGI------ 198
Cdd:cd07418  117 LLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKY-GDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspsl 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 199 ---------------------SPWLESLEDINSIERPLVVPPYG----LACDLLWSDPAQPErngwGLSH---RGISFTY 250
Cdd:cd07418  196 pkrkkqkgknrrvlllepeseSLKLGTLDDLMKARRSVLDPPGEgsnlIPGDVLWSDPSLTP----GLSPnkqRGIGLLW 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885016 251 GKSVVEEFCAKNDIALVIRGHQL--FKEMYPQGCVLRFG---------GRLISLFSALNY-------EGHKNNSSVLKLE 312
Cdd:cd07418  272 GPDCTEEFLEKNNLKLIIRSHEGpdAREKRPGLAGMNKGytvdhdvesGKLITLFSAPDYpqfqateERYNNKGAYIILQ 351

putative protein phosphatase

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392885016  77 ITVVADMHGQSIHLLRIF--LTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRyPQHVFLLRGNHED 145
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMdkINNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSN-DDNVVTLLGNHDD 72

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 392885016  80 VADMHGQSIHL------LRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQ--HVFLLrGNHE 144
Cdd:cd07421    7 VGDIHGYISKLnnlwlnLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKqrHVFLC-GNHD 78

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.

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gi 392885016  79 VVADMHGQSIHLLRIFLTN--EAPPNQKYLFLGDYVDRGSQSVVVMCLLFCM-KHRYPqhVFLLRGNHE 144
Cdd:cd00838    2 VISDIHGNLEALEAVLEAAlaKAEKPDLVICLGDLVDYGPDPEEVELKALRLlLAGIP--VYVVPGNHD 68