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Conserved domains on  [gi|17539256|ref|NP_502650|]
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Serine/threonine-protein phosphatase [Caenorhabditis elegans]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-298 1.14e-138

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.


The actual alignment was detected with superfamily member cd07414:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 291  Bit Score: 394.01  E-value: 1.14e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256   5 VVDSIIIDVLSASTHEKPLCKVITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANY 84
Cdd:cd07414   1 DIDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  85 LFLGDYVDRGRFSIETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIA 164
Cdd:cd07414  81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NIKLWKTFTDCFNCLPVAAIVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 165 TKILCMHGGLSPLMTkefTLDTLRKIERPTE-GKEGLVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDL 243
Cdd:cd07414 160 EKIFCCHGGLSPDLQ---SMEQIRRIMRPTDvPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDL 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17539256 244 VCRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQFDNCAAFMSCDEKLQCSFEILRP 298
Cdd:cd07414 237 ICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 5-298 1.14e-138

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.


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 394.01  E-value: 1.14e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256   5 VVDSIIIDVLSASTHEKPLCKVITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANY 84
Cdd:cd07414   1 DIDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  85 LFLGDYVDRGRFSIETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIA 164
Cdd:cd07414  81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NIKLWKTFTDCFNCLPVAAIVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 165 TKILCMHGGLSPLMTkefTLDTLRKIERPTE-GKEGLVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDL 243
Cdd:cd07414 160 EKIFCCHGGLSPDLQ---SMEQIRRIMRPTDvPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDL 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17539256 244 VCRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQFDNCAAFMSCDEKLQCSFEILRP 298
Cdd:cd07414 237 ICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 27-299 3.54e-134

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 381.56  E-value: 3.54e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256     27 ITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANYLFLGDYVDRGRFSIETIVLLLA 106
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    107 YKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIATKILCMHGGLSPlmtKEFTLDT 186
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY-GERIYEKFNEAFSWLPLAALINGKILCMHGGLSP---DLTTLDD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    187 LRKIERPTE-GKEGLVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQVVQDGYEFFAGRKLVT 265
Cdd:smart00156 157 IRKLKRPQEpPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVT 236

                          250       260       270
                   ....*....|....*....|....*....|....
gi 17539256    266 IFSAPHYCGQFDNCAAFMSCDEKLQCSFEILRPT 299
Cdd:smart00156 237 IFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPG 270
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 6-298 2.87e-113

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 330.47  E-value: 2.87e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    6 VDSIIIDVLSASTHEKPLCKVITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANYL 85
Cdd:PTZ00480  11 VDNIIERLLSVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256   86 FLGDYVDRGRFSIETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIAT 165
Cdd:PTZ00480  91 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-TIKLWKTFTDCFNCLPVAALIDE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  166 KILCMHGGLSPLMTkefTLDTLRKIERPTEGKE-GLVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLV 244
Cdd:PTZ00480 170 KILCMHGGLSPELS---NLEQIRRIMRPTDVPDtGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLI 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17539256  245 CRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQFDNCAAFMSCDEKLQCSFEILRP 298
Cdd:PTZ00480 247 CRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKP 300
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 55-164 7.15e-20

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.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 83.42  E-value: 7.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    55 PIKVCGDIH--GQFPDLLRLFHRGGwPPTANYLFL--GDYVDRGRFSiETIVLLLAYKVKFpCNFFLLRGNHECefvnkt 130
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDF------ 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 17539256   131 ygFYEECQKRYQ----SVRMYAAFQDVFNWLPLTGLIA 164
Cdd:pfam00149  73 --DYGECLRLYPylglLARPWKRFLEVFNFLPLAGILS 108
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 5-298 1.14e-138

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.


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 394.01  E-value: 1.14e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256   5 VVDSIIIDVLSASTHEKPLCKVITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANY 84
Cdd:cd07414   1 DIDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  85 LFLGDYVDRGRFSIETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIA 164
Cdd:cd07414  81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NIKLWKTFTDCFNCLPVAAIVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 165 TKILCMHGGLSPLMTkefTLDTLRKIERPTE-GKEGLVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDL 243
Cdd:cd07414 160 EKIFCCHGGLSPDLQ---SMEQIRRIMRPTDvPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDL 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17539256 244 VCRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQFDNCAAFMSCDEKLQCSFEILRP 298
Cdd:cd07414 237 ICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 27-299 3.54e-134

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 381.56  E-value: 3.54e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256     27 ITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANYLFLGDYVDRGRFSIETIVLLLA 106
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    107 YKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIATKILCMHGGLSPlmtKEFTLDT 186
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY-GERIYEKFNEAFSWLPLAALINGKILCMHGGLSP---DLTTLDD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    187 LRKIERPTE-GKEGLVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQVVQDGYEFFAGRKLVT 265
Cdd:smart00156 157 IRKLKRPQEpPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVT 236

                          250       260       270
                   ....*....|....*....|....*....|....
gi 17539256    266 IFSAPHYCGQFDNCAAFMSCDEKLQCSFEILRPT 299
Cdd:smart00156 237 IFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPG 270
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 6-298 2.87e-113

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 330.47  E-value: 2.87e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    6 VDSIIIDVLSASTHEKPLCKVITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANYL 85
Cdd:PTZ00480  11 VDNIIERLLSVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256   86 FLGDYVDRGRFSIETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIAT 165
Cdd:PTZ00480  91 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-TIKLWKTFTDCFNCLPVAALIDE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  166 KILCMHGGLSPLMTkefTLDTLRKIERPTEGKE-GLVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLV 244
Cdd:PTZ00480 170 KILCMHGGLSPELS---NLEQIRRIMRPTDVPDtGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLI 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17539256  245 CRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQFDNCAAFMSCDEKLQCSFEILRP 298
Cdd:PTZ00480 247 CRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKP 300
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 24-298 3.96e-113

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.


Pssm-ID: 277360 [Multi-domain]  Cd Length: 285  Bit Score: 328.78  E-value: 3.96e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  24 CKVITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANYLFLGDYVDRGRFSIETIVL 103
Cdd:cd07415  12 CELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLL 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 104 LLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYQSVRMYAAFQDVFNWLPLTGLIATKILCMHGGLSPLMTkefT 183
Cdd:cd07415  92 LLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQ---T 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 184 LDTLRKIERPTE-GKEGLVADLLWADPISGlSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQVVQDGYEFFAGRK 262
Cdd:cd07415 169 LDQIRALDRFQEvPHEGPMCDLLWSDPDDR-EGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNK 247

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17539256 263 LVTIFSAPHYCGQFDNCAAFMSCDEKLQCSFEILRP 298
Cdd:cd07415 248 LVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 5-296 9.37e-111

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 323.40  E-value: 9.37e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    5 VVDSIIIDVLSASTHEKPLCKVITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANY 84
Cdd:PTZ00244   3 LVQTLIEKMLTVKGNRTQRQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256   85 LFLGDYVDRGRFSIETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIA 164
Cdd:PTZ00244  83 LFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRY-NIKLFKAFTDVFNTMPVCCVIS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  165 TKILCMHGGLSPLMTkefTLDTLRKIERPTEGKE-GLVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDL 243
Cdd:PTZ00244 162 EKIICMHGGLSPDLT---SLASVNEIERPCDVPDrGILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17539256  244 VCRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQFDNCAAFMSCDEKLQCSFEIL 296
Cdd:PTZ00244 239 IVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFLII 291
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 58-283 1.29e-95

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.


Pssm-ID: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 282.34  E-value: 1.29e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  58 VCGDIHGQFPDLLRLFHRGGWPPTANYLFLGDYVDRGRFSIETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEEC 137
Cdd:cd00144   2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDER 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 138 ---QKRYQSVRMYAAFQDVFNWLPLTGLIATKILCMHGGLSPLMTkefTLDTLRKIERPTEGKEGLVADLLWADPISGLS 214
Cdd:cd00144  82 tlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLT---LLDQIRNIRPIENPDDQLVEDLLWSDPDESVG 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539256 215 GFMNNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQFDNCAAFM 283
Cdd:cd00144 159 DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAAL 227
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 42-282 4.09e-86

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.


Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 261.04  E-value: 4.09e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  42 VFKAQKPMVEVNAP----IKVCGDIHGQFPDLLRLFHRGGWP-PTANYLFLGDYVDRGRFSIETIVLLLAYKVKFPCNFF 116
Cdd:cd07417  44 ILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPsETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFH 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 117 LLRGNHECEFVNKTYGFYEECQKRYQSvRMYAAFQDVFNWLPLTGLIATKILCMHGGLspLMTKEFTLDTLRKIERPTE- 195
Cdd:cd07417 124 LNRGNHETDNMNKIYGFEGEVKAKYNE-QMFNLFSEVFNWLPLAHLINGKVLVVHGGL--FSDDGVTLDDIRKIDRFRQp 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 196 GKEGLVADLLWADPiSGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQ 275
Cdd:cd07417 201 PDSGLMCELLWSDP-QPQPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQ 279


                ....*..
gi 17539256 276 FDNCAAF 282
Cdd:cd07417 280 MGNKGAF 286
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 30-297 3.43e-81

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 248.19  E-value: 3.43e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256   30 ERVLKLL-DLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANYLFLGDYVDRGRFSIETIVLLLAYK 108
Cdd:PTZ00239  18 ERDLKLIcERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVETMEYLLCLK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  109 VKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYQSVRMYAAFQDVFNWLPLTGLIATKILCMHGGLSPLMTkefTLDTLR 188
Cdd:PTZ00239  98 VKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMR---TIDQIR 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  189 KIERPTE-GKEGLVADLLWADPiSGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQVVQDGYEF-FAGRKLVTI 266
Cdd:PTZ00239 175 TIDRKIEiPHEGPFCDLMWSDP-EEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTV 253

                        250       260       270
                 ....*....|....*....|....*....|.
gi 17539256  267 FSAPHYCGQFDNCAAFMSCDEKLQCSFEILR 297
Cdd:PTZ00239 254 WSAPNYCYRCGNIASILCLDENLQQTWKTFK 284
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 27-281 2.40e-78

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.


Pssm-ID: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 241.06  E-value: 2.40e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  27 ITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTANYLFLGDYVDRGRFSIETIVLLLA 106
Cdd:cd07416  16 LSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 107 YKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYqSVRMYAAFQDVFNWLPLTGLIATKILCMHGGLSPLMTkefTLDT 186
Cdd:cd07416  96 LKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELK---TLDD 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 187 LRKIERPTE-GKEGLVADLLWADPISGLSG------FM-NNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQVVQDGYEFF 258
Cdd:cd07416 172 IRKLDRFREpPSYGPMCDLLWSDPLEDFGNektqehFVhNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMY 251

                       250       260       270
                ....*....|....*....|....*....|.
gi 17539256 259 agRK--------LVTIFSAPHYCGQFDNCAA 281
Cdd:cd07416 252 --RKsqttgfpsLITIFSAPNYLDVYNNKAA 280
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 27-281 9.31e-74

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.


Pssm-ID: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 229.63  E-value: 9.31e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  27 ITEERVLKLLDLALGVFKAQKPMVEVNAPIKVCGDIHGQFPDLLRLFHRGGWPPTA--------NYLFLGDYVDRGRFSI 98
Cdd:cd07419  21 FDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEeagdieyiDYLFLGDYVDRGSHSL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  99 ETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYQS-----VRMYAAFQDVFNWLPLTGLIATKILCMHGG 173
Cdd:cd07419 101 ETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdirdgDSVWQRINRLFNWLPLAALIEDKIICVHGG 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 174 LSPLMTKeftLDTLRKIERP--TEGKEGLVADLLWADPISG--LSGFMNN---QRGAG--CGFGRDSVLNLCSEFQLDLV 244
Cdd:cd07419 181 IGRSINH---IHQIENLKRPitMEAGSPVVMDLLWSDPTENdsVLGLRPNaidPRGTGliVKFGPDRVMEFLEENDLQMI 257

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17539256 245 CRAHQVVQDGYEFFAGRKLVTIFSAPHYCGQFDNCAA 281
Cdd:cd07419 258 IRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGA 294
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 32-283 2.24e-62

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC 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, 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.


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 199.94  E-value: 2.24e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  32 VLKLLDLALGVFKaQKPMVE-----VNAPIKVCGDIHGQFPDLLRLFHRGGWPPTAN-YLFLGDYVDRGRFSIETIVLLL 105
Cdd:cd07420  25 VLLILREARKSLK-QLPNISrvstsYSKEVTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILF 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 106 AYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRYQ--SVRMYAAFQDVFNWLPLTGLIATKILCMHGGLSplmtkEFT 183
Cdd:cd07420 104 AFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKdhGKKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-----DST 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 184 -LDTLRKIER------PTEGKEglVADLLWADPISGLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQVVQDGYE 256
Cdd:cd07420 179 dLDLLDKIDRhkyvstKTEWQQ--VVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYE 256

                       250       260
                ....*....|....*....|....*..
gi 17539256 257 FFAGRKLVTIFSAPHYCGQFDNCAAFM 283
Cdd:cd07420 257 FCHNNKVITIFSASNYYEEGSNRGAYV 283
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 4-300 9.76e-47

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.


Pssm-ID: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 161.51  E-value: 9.76e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256   4 NVVDSIiidVLSASthekplcKVITEERVLKLLDlalgvfkaqkpmVEVNAPIKVCGDIHGQFPDLLRLFHRGGWP-PTA 82
Cdd:cd07418  38 NVFDSL---VLTAH-------KILHREPNCVRID------------VEDVCEVVVVGDVHGQLHDVLFLLEDAGFPdQNR 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  83 NYLFLGDYVDRGRFSIETIVLLLAYKVKFPCNFFLLRGNHECEFVNKTYGFYEECQKRY--QSVRMYAAFQDVFNWLPLT 160
Cdd:cd07418  96 FYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYgdKGKHVYRKCLGCFEGLPLA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 161 GLIATKILCMHGGL-----SPLMTKEF-------------------TLDTLRKIER-----PTEGKEGLVADLLWADPIS 211
Cdd:cd07418 176 SIIAGRVYTAHGGLfrspsLPKRKKQKgknrrvlllepeseslklgTLDDLMKARRsvldpPGEGSNLIPGDVLWSDPSL 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256 212 GLSGFMNNQRGAGCGFGRDSVLNLCSEFQLDLVCRAHQ------------VVQDGY----EFFAGrKLVTIFSAPHYcgq 275
Cdd:cd07418 256 TPGLSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYtvdhDVESG-KLITLFSAPDY--- 331

                       330       340
                ....*....|....*....|....*..
gi 17539256 276 fdncAAFMSCDEKL--QCSFEILRPTT 300
Cdd:cd07418 332 ----PQFQATEERYnnKGAYIILQPPD 354
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 55-164 7.15e-20

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.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 83.42  E-value: 7.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256    55 PIKVCGDIH--GQFPDLLRLFHRGGwPPTANYLFL--GDYVDRGRFSiETIVLLLAYKVKFpCNFFLLRGNHECefvnkt 130
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDF------ 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 17539256   131 ygFYEECQKRYQ----SVRMYAAFQDVFNWLPLTGLIA 164
Cdd:pfam00149  73 --DYGECLRLYPylglLARPWKRFLEVFNFLPLAGILS 108
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 58-123 1.82e-07

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.


Pssm-ID: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 50.78  E-value: 1.82e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539256  58 VCGDIHGQFPDLLRLFHRGGWPPTANYLF-LGDYVDRGRFSIETIVLLlaykvKFPCnFFLLRGNHE 123
Cdd:cd07424   5 VVGDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLEVLELL-----KQPW-FHAVQGNHE 65
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 60-189 4.37e-06

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


Pssm-ID: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 46.91  E-value: 4.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539256  60 GDIHGQFPDLLRLFHRGG-------WppTANYLF---LGDYVDRGRFSIETIVLLLAYK---VKFPCNFFLLRGNHEC-- 124
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGvidsndrW--IGGDTVvvqTGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELmn 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539256 125 -----EFVNKTY--GFYEECQKRYqsvRMYAAFQDVFNWLPLTGLIA--TKILCMHGGLSPLMTKEFTLDTLRK 189
Cdd:cd07425  82 lcgdfRYVHPRGlnEFGGVAKRRY---ALLSDGGYIGRYLRTHPVVLvvNDILFVHGGLGPLWSRGYSLETKNG 152
PHA02239 PHA02239
putative protein phosphatase
 56-128 2.92e-05

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 44.60  E-value: 2.92e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539256   56 IKVCGDIHGQFPDLLRLFHR--GGWPPTANYLFLGDYVDRGRFSIETIVLLLAYKVKFPcNFFLLRGNHECEFVN 128
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKinNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDD-NVVTLLGNHDDEFYN 76
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 58-123 4.92e-05

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.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 42.25  E-value: 4.92e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539256  58 VCGDIHGQFPDLLRLFHRGGW--PPTANYLFLGDYVDRGRFSIETiVLLLAYKVKFPCNFFLLRGNHE 123
Cdd:cd00838   2 VISDIHGNLEALEAVLEAALAkaEKPDLVICLGDLVDYGPDPEEV-ELKALRLLLAGIPVYVVPGNHD 68
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 60-101 1.05e-03

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.


Pssm-ID: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 39.81  E-value: 1.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17539256  60 GDIHGQFPDLLRLFHRGGWPPTANYL----------FLGDYVDRGRFSIETI 101
Cdd:cd07423   4 GDVHGCYDELVELLEKLGYQKKEEGLyvhpegrklvFLGDLVDRGPDSIDVL 55
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 58-126 3.41e-03

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.


Pssm-ID: 163664  Cd Length: 304  Bit Score: 38.64  E-value: 3.41e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539256  58 VC-GDIHGQFPDLLRLFH--RGGWPP----TANYLFLGDYVDRGRFSIETIVLLLAYKVKFPCN-FFLLRGNHECEF 126
Cdd:cd07421   5 ICvGDIHGYISKLNNLWLnlQSALGPsdfaSALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQrHVFLCGNHDFAF 81
PRK09968 PRK09968
protein-serine/threonine phosphatase;
56-123 4.72e-03

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 37.57  E-value: 4.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539256   56 IKVCGDIHGQFPDLLRLFHRGGWPPTANYLF-LGDYVDRGRFSIETIVLLlaykvkfpcN---FFLLRGNHE 123
Cdd:PRK09968  17 IWVVGDIHGEYQLLQSRLHQLSFCPETDLLIsVGDNIDRGPESLNVLRLL---------NqpwFISVKGNHE 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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