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Conserved domains on  [gi|17864626|ref|NP_524947|]
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protein phosphatase D6 [Drosophila melanogaster]

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 ...
 51-317 1.71e-171

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: 477.99  E-value: 1.71e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  51 PLLESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNSVETITLLL 130
Cdd:cd07414  22 QLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 131 ALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQLKELSNIES 210
Cdd:cd07414 102 AYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRR 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 211 IARPTEVPETGLLCDLLWSDPDRYGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVFS 290
Cdd:cd07414 182 IMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFS 261

                       250       260
                ....*....|....*....|....*..
gi 17864626 291 APNYCGLYDNAGASMGVDKDLVISFDI 317
Cdd:cd07414 262 APNYCGEFDNAGAMMSVDETLMCSFQI 288
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 51-317 1.71e-171

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: 477.99  E-value: 1.71e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  51 PLLESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNSVETITLLL 130
Cdd:cd07414  22 QLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 131 ALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQLKELSNIES 210
Cdd:cd07414 102 AYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRR 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 211 IARPTEVPETGLLCDLLWSDPDRYGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVFS 290
Cdd:cd07414 182 IMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFS 261

                       250       260
                ....*....|....*....|....*..
gi 17864626 291 APNYCGLYDNAGASMGVDKDLVISFDI 317
Cdd:cd07414 262 APNYCGEFDNAGAMMSVDETLMCSFQI 288
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 40-317 5.26e-138

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 394.03  E-value: 5.26e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626   40 MSFRRSKM-QRLPLLESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDR 118
Cdd:PTZ00480  19 LSVRGSKPgKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  119 GKNSVETITLLLALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGL 198
Cdd:PTZ00480  99 GKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  199 SPQLKELSNIESIARPTEVPETGLLCDLLWSDPDRYGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYE 278
Cdd:PTZ00480 179 SPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYE 258

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 17864626  279 FFAKRQLVTVFSAPNYCGLYDNAGASMGVDKDLVISFDI 317
Cdd:PTZ00480 259 FFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQI 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 54-315 2.37e-135

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: 385.41  E-value: 2.37e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626     54 ESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNSVETITLLLALR 133
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626    134 VKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQLKELSNIESIAR 213
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626    214 PTEVPETGLLCDLLWSDPDRYGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVFSAPN 293
Cdd:smart00156 163 PQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPN 242

                          250       260
                   ....*....|....*....|..
gi 17864626    294 YCGLYDNAGASMGVDKDLVISF 315
Cdd:smart00156 243 YCDRFGNKAAVLKVDKDLKLTF 264
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 80-188 1.83e-18

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: 79.56  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626    80 PIRVVGDIH--GQFYDLLKILDQCGyPPQTRYLFL--GDYVDRGKNSvETITLLLALRVKFpKHIYLLRGNHESqsvnrv 155
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDF------ 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 17864626   156 ygFFDECKRRY-----TVKLWKTFVDCYNCMPVAAIIS 188
Cdd:pfam00149  73 --DYGECLRLYpylglLARPWKRFLEVFNFLPLAGILS 108
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
81-156 2.11e-04

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 41.92  E-value: 2.11e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864626  81 IRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKnsVETITLLLALRVKFPKHIYLLRGNHESQSVNRVY 156
Cdd:COG2129   2 ILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGT--AEEAREVLEELAALGVPVLAVPGNHDDPEVLDAL 75
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 51-317 1.71e-171

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: 477.99  E-value: 1.71e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  51 PLLESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNSVETITLLL 130
Cdd:cd07414  22 QLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 131 ALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQLKELSNIES 210
Cdd:cd07414 102 AYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRR 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 211 IARPTEVPETGLLCDLLWSDPDRYGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVFS 290
Cdd:cd07414 182 IMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFS 261

                       250       260
                ....*....|....*....|....*..
gi 17864626 291 APNYCGLYDNAGASMGVDKDLVISFDI 317
Cdd:cd07414 262 APNYCGEFDNAGAMMSVDETLMCSFQI 288
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 40-317 5.26e-138

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 394.03  E-value: 5.26e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626   40 MSFRRSKM-QRLPLLESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDR 118
Cdd:PTZ00480  19 LSVRGSKPgKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  119 GKNSVETITLLLALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGL 198
Cdd:PTZ00480  99 GKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  199 SPQLKELSNIESIARPTEVPETGLLCDLLWSDPDRYGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYE 278
Cdd:PTZ00480 179 SPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYE 258

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 17864626  279 FFAKRQLVTVFSAPNYCGLYDNAGASMGVDKDLVISFDI 317
Cdd:PTZ00480 259 FFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQI 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 54-315 2.37e-135

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: 385.41  E-value: 2.37e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626     54 ESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNSVETITLLLALR 133
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626    134 VKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQLKELSNIESIAR 213
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626    214 PTEVPETGLLCDLLWSDPDRYGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVFSAPN 293
Cdd:smart00156 163 PQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPN 242

                          250       260
                   ....*....|....*....|..
gi 17864626    294 YCGLYDNAGASMGVDKDLVISF 315
Cdd:smart00156 243 YCDRFGNKAAVLKVDKDLKLTF 264
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 40-317 3.55e-124

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 358.06  E-value: 3.55e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626   40 MSFRRSKMQRLPLL-ESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDR 118
Cdd:PTZ00244  12 LTVKGNRTQRQILIrEEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  119 GKNSVETITLLLALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGL 198
Cdd:PTZ00244  92 GKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  199 SPQLKELSNIESIARPTEVPETGLLCDLLWSDPDRYGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYE 278
Cdd:PTZ00244 172 SPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYG 251

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 17864626  279 FFAKRQLVTVFSAPNYCGLYDNAGASMGVDKDLVISFDI 317
Cdd:PTZ00244 252 FFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFLI 290
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 51-317 6.31e-124

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: 356.90  E-value: 6.31e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  51 PLLESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNSVETITLLL 130
Cdd:cd07415  14 LLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 131 ALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRY-TVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQLKELSNIE 209
Cdd:cd07415  94 ALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIR 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 210 SIARPTEVPETGLLCDLLWSDPDRYGfGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVF 289
Cdd:cd07415 174 ALDRFQEVPHEGPMCDLLWSDPDDRE-GWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVW 252

                       250       260
                ....*....|....*....|....*...
gi 17864626 290 SAPNYCGLYDNAGASMGVDKDLVISFDI 317
Cdd:cd07415 253 SAPNYCYRCGNVASILELDEHLNRSFKQ 280
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 83-305 4.58e-102

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: 299.29  E-value: 4.58e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  83 VVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNSVETITLLLALRVKFPKHIYLLRGNHESQSVNRVYGFFDE- 161
Cdd:cd00144   2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDEr 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 162 ---CKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQLKELSNIESIaRPTEVPETGLLCDLLWSDPDRYGFGW 238
Cdd:cd00144  82 tlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGDF 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864626 239 TSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVFSAPNYCGLYDNAGASM 305
Cdd:cd00144 161 ESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAAL 227
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 44-303 1.75e-95

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: 285.35  E-value: 1.75e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  44 RSKMQRLPLLESEVNL-LCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNS 122
Cdd:cd07416   7 KAHFMREGRLSEEDALrIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFS 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 123 VETITLLLALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQL 202
Cdd:cd07416  87 IECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPEL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 203 KELSNIESIARPTEVPETGLLCDLLWSDP-DRYGFGWTSSD------RGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVED 275
Cdd:cd07416 167 KTLDDIRKLDRFREPPSYGPMCDLLWSDPlEDFGNEKTQEHfvhntvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDA 246

                       250       260       270
                ....*....|....*....|....*....|....
gi 17864626 276 GYEFFAKRQ------LVTVFSAPNYCGLYDNAGA 303
Cdd:cd07416 247 GYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAA 280
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 52-311 5.14e-95

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 284.40  E-value: 5.14e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626   52 LLESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKNSVETITLLLA 131
Cdd:PTZ00239  16 LPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVETMEYLLC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  132 LRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRY-TVKLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQLKELSNIES 210
Cdd:PTZ00239  96 LKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRT 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  211 IARPTEVPETGLLCDLLWSDPDRYGFgWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEF-FAKRQLVTVF 289
Cdd:PTZ00239 176 IDRKIEIPHEGPFCDLMWSDPEEVEY-WAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTVW 254

                        250       260
                 ....*....|....*....|..
gi 17864626  290 SAPNYCGLYDNAGASMGVDKDL 311
Cdd:PTZ00239 255 SAPNYCYRCGNIASILCLDENL 276
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 49-313 2.62e-87

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: 265.07  E-value: 2.62e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  49 RLPLLESEVNLLCTLARELFLDEPMLLNVPAPIRVVGDIHGQFYDLLKILDQCGYPPQTR--------YLFLGDYVDRGK 120
Cdd:cd07419  18 RFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagdieyidYLFLGDYVDRGS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 121 NSVETITLLLALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRYT------VKLWKTFVDCYNCMPVAAIISHRIFCC 194
Cdd:cd07419  98 HSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGedirdgDSVWQRINRLFNWLPLAALIEDKIICV 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 195 HGGLSPQLKELSNIESIARPTEVPETG-LLCDLLWSDPdrygfgwTSSDR--------------GVSYLYGRDVLEKFLQ 259
Cdd:cd07419 178 HGGIGRSINHIHQIENLKRPITMEAGSpVVMDLLWSDP-------TENDSvlglrpnaidprgtGLIVKFGPDRVMEFLE 250

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 17864626 260 KNDFDLVCRAHQVVEDGYEFFAKRQLVTVFSAPNYCGLYDNAGASMGVDKDLVI 313
Cdd:cd07419 251 ENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVV 304
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 64-303 4.02e-83

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: 254.49  E-value: 4.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  64 ARELFLDEPMLLNVPAP----IRVVGDIHGQFYDLLKILDQCGYP-PQTRYLFLGDYVDRGKNSVETITLLLALRVKFPK 138
Cdd:cd07417  41 VKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPsETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPN 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 139 HIYLLRGNHESQSVNRVYGFFDECKRRYTVKLWKTFVDCYNCMPVAAIISHRIFCCHGGL-SPQLKELSNIESIARPTEV 217
Cdd:cd07417 121 HFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFRQP 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 218 PETGLLCDLLWSDPDRYGfGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVFSAPNYCGL 297
Cdd:cd07417 201 PDSGLMCELLWSDPQPQP-GRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQ 279


                ....*.
gi 17864626 298 YDNAGA 303
Cdd:cd07417 280 MGNKGA 285
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 81-315 1.99e-56

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: 185.30  E-value: 1.99e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  81 IRVVGDIHGQFYDLLKILDQCGYP-PQTRYLFLGDYVDRGKNSVETITLLLALRVKFPKHIYLLRGNHESQSVNRVYGFF 159
Cdd:cd07420  53 VTICGDLHGKLDDLLLIFYKNGLPsPENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFT 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 160 DECKRRYTV---KLWKTFVDCYNCMPVAAIISHRIFCCHGGLSPQlKELSNIESIAR---PTEVPETGLLCDLLWSDPDR 233
Cdd:cd07420 133 KEVMQKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGISDS-TDLDLLDKIDRhkyVSTKTEWQQVVDILWSDPKA 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 234 YGFGWTSSDRGVSYLYGRDVLEKFLQKNDFDLVCRAHQVVEDGYEFFAKRQLVTVFSAPNYCGLYDNAGASMGVDKDLVI 313
Cdd:cd07420 212 TKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLTP 291


                ..
gi 17864626 314 SF 315
Cdd:cd07420 292 HF 293
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 55-294 3.70e-48

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: 166.13  E-value: 3.70e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  55 SEVNLLCTLARELFLDEPMLLNVP----APIRVVGDIHGQFYDLLKILDQCGYPPQTR-YLFLGDYVDRGKNSVETITLL 129
Cdd:cd07418  38 NVFDSLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRfYVFNGDYVDRGAWGLETFLLL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 130 LALRVKFPKHIYLLRGNHESQSVNRVYGFFDECKRRY---TVKLWKTFVDCYNCMPVAAIISHRIFCCHGGL--SPQL-- 202
Cdd:cd07418 118 LSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYgdkGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrSPSLpk 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626 203 ------KELSNIESIARPtEVPETGLLCDL----------------------LWSDPDRYGFGWTSSDRGVSYLYGRDVL 254
Cdd:cd07418 198 rkkqkgKNRRVLLLEPES-ESLKLGTLDDLmkarrsvldppgegsnlipgdvLWSDPSLTPGLSPNKQRGIGLLWGPDCT 276

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17864626 255 EKFLQKNDFDLVCRAHQvvedGYEFFAKR-------------------QLVTVFSAPNY 294
Cdd:cd07418 277 EEFLEKNNLKLIIRSHE----GPDAREKRpglagmnkgytvdhdvesgKLITLFSAPDY 331
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 80-188 1.83e-18

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: 79.56  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626    80 PIRVVGDIH--GQFYDLLKILDQCGyPPQTRYLFL--GDYVDRGKNSvETITLLLALRVKFpKHIYLLRGNHESqsvnrv 155
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDF------ 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 17864626   156 ygFFDECKRRY-----TVKLWKTFVDCYNCMPVAAIIS 188
Cdd:pfam00149  73 --DYGECLRLYpylglLARPWKRFLEVFNFLPLAGILS 108
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 81-157 2.79e-10

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: 58.87  E-value: 2.79e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17864626  81 IRVVGDIHGQFYDLLKILDQCGYPPQTRYLF-LGDYVDRGKNSVETITLLlalrvKFPkHIYLLRGNHESQSVNRVYG 157
Cdd:cd07424   3 DFVVGDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLEVLELL-----KQP-WFHAVQGNHEQMAIDALRG 74
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 44-75 2.17e-08

Serine-threonine protein phosphatase N-terminal domain; This family is often found at the N-terminus of Metallophos family, in serine-threonine protein phosphatases.


Pssm-ID: 465300 [Multi-domain]  Cd Length: 48  Bit Score: 49.80  E-value: 2.17e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 17864626    44 RSKMQRLPLLESEVNLLCTLARELFLDEPMLL 75
Cdd:pfam16891  14 KPGGKQVQLSEAEIRALCRKAREIFLSQPMLL 45
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 83-160 6.00e-08

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: 52.52  E-value: 6.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  83 VVGDIHGQFYDLLKILDQCGY----------PPQTRYLFLGDYVDRGKNSVETITLLLALRVKfpKHIYLLRGNHEsqsv 152
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGYqkkeeglyvhPEGRKLVFLGDLVDRGPDSIDVLRLVMNMVKA--GKALYVPGNHC---- 75


                ....*...
gi 17864626 153 NRVYGFFD 160
Cdd:cd07423  76 NKLYRYLK 83
PHA02239 PHA02239
putative protein phosphatase
 81-174 7.40e-08

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 52.30  E-value: 7.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626   81 IRVVGDIHGQFYDLLKILDQCG--YPPQTRYLFLGDYVDRGKNSVETITLLLALRVKfPKHIYLLRGNHES------QSV 152
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKINneRKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSN-DDNVVTLLGNHDDefynimENV 81

                         90       100
                 ....*....|....*....|...
gi 17864626  153 NRVyGFFD-ECKRRYTVKLWKTF 174
Cdd:PHA02239  82 DRL-SIYDiEWLSRYCIETLNSY 103
pphA PRK11439
protein-serine/threonine phosphatase;
81-148 2.41e-07

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 50.92  E-value: 2.41e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17864626   81 IRVVGDIHGQFYDLLKILDQCGYPPQTRYLF-LGDYVDRGKNSVETITLLLAlrvkfpKHIYLLRGNHE 148
Cdd:PRK11439  19 IWLVGDIHGCFEQLMRKLRHCRFDPWRDLLIsVGDLIDRGPQSLRCLQLLEE------HWVRAVRGNHE 81
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 83-159 1.02e-06

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 49.32  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626   83 VVGDIHGQFYDLLKILDQCGY---------PPQTRYLFLGDYVDRGKNSVETITLLLALRVKfpKHIYLLRGNHesqsVN 153
Cdd:PRK13625   5 IIGDIHGCYQEFQALTEKLGYnwssglpvhPDQRKLAFVGDLTDRGPHSLRMIEIVWELVEK--KAAYYVPGNH----CN 78


                 ....*.
gi 17864626  154 RVYGFF 159
Cdd:PRK13625  79 KLYRFF 84
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 83-148 4.87e-06

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.


Pssm-ID: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 47.15  E-value: 4.87e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864626  83 VVGDIHGQFYDLLKILDQCGYPPQTRYL-FLGDYVDRGKNSVETITLLLALRvkfpKHIYLLRGNHE 148
Cdd:cd07422   3 AIGDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLETLRFVKSLG----DSAVVVLGNHD 65
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 83-148 7.53e-06

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: 44.95  E-value: 7.53e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17864626  83 VVGDIHGQFYDLLKILD--QCGYPPQTRYLFLGDYVDRGKNSVETITLLLALRVKFPKhIYLLRGNHE 148
Cdd:cd00838   2 VISDIHGNLEALEAVLEaaLAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIP-VYVVPGNHD 68
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 84-148 9.18e-06

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: 46.73  E-value: 9.18e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864626  84 VGDIHGQFYDLLKILD--QCGYPPQ----TRYLFLGDYVDRGKNSVETITLLLALRVKFPK--HIYLLrGNHE 148
Cdd:cd07421   7 VGDIHGYISKLNNLWLnlQSALGPSdfasALVIFLGDYCDRGPETRKVIDFLISLPEKHPKqrHVFLC-GNHD 78
PRK09968 PRK09968
protein-serine/threonine phosphatase;
81-153 1.18e-05

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 45.65  E-value: 1.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17864626   81 IRVVGDIHGQFYDLLKILDQCGYPPQTRYLF-LGDYVDRGKNSVETITLLlalrvKFPKHIYlLRGNHESQSVN 153
Cdd:PRK09968  17 IWVVGDIHGEYQLLQSRLHQLSFCPETDLLIsVGDNIDRGPESLNVLRLL-----NQPWFIS-VKGNHEAMALD 84
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 83-200 1.23e-05

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: 45.37  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864626  83 VVGDIHGQFYDLLKIL--------DQCGYPPQTRYLFLGDYVDRGKNSVETITLLLALRVKFPK---HIYLLRGNHESQS 151
Cdd:cd07425   2 AIGDLHGDLDRLRTILklagvidsNDRWIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKaggKVILLLGNHELMN 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17864626 152 V---------NRVYGFFDECKRRYtvKLWK--TFVDCY-NCMPVAAIISHRIFcCHGGLSP 200
Cdd:cd07425  82 LcgdfryvhpRGLNEFGGVAKRRY--ALLSdgGYIGRYlRTHPVVLVVNDILF-VHGGLGP 139
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
83-148 1.59e-05

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 45.93  E-value: 1.59e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864626   83 VVGDIHGQFYDLLKILDQCGYPPQTRYL-FLGDYVDRGKNSVETITLLLALRvkfpKHIYLLRGNHE 148
Cdd:PRK00166   5 AIGDIQGCYDELQRLLEKIDFDPAKDTLwLVGDLVNRGPDSLEVLRFVKSLG----DSAVTVLGNHD 67
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
81-156 2.11e-04

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 41.92  E-value: 2.11e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864626  81 IRVVGDIHGQFYDLLKILDQCGYPPQTRYLFLGDYVDRGKnsVETITLLLALRVKFPKHIYLLRGNHESQSVNRVY 156
Cdd:COG2129   2 ILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGT--AEEAREVLEELAALGVPVLAVPGNHDDPEVLDAL 75
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 83-148 1.27e-03

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 39.46  E-value: 1.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17864626  83 VVGDIHGQFYDLLKILDQCGYP--------PQTRYLFLGDYVDRGKNSVETITLLLALrVKFPKHIYLLrGNHE 148
Cdd:cd07413   3 LIGDVHGCAHTLDRLLDLLGYRlqggvwrhPRRQALFVGDLIDRGPRIREVLHRVHAM-VDAGEALCVM-GNHE 74
 
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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