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Conserved domains on  [gi|17544062|ref|NP_502041|]
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Serine/threonine-protein phosphatase [Caenorhabditis elegans]

Protein Classification

serine/threonine protein phosphatase( domain architecture ID 12191156)

protein phosphatase specific for serine and threonine, similar to Methanosarcina thermophila serine/threonine-protein phosphatase PP1-arch2 and Caenorhabditis elegans putative serine/threonine-protein phosphatase C23G10.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 36-360 1.10e-138

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: 395.43  E-value: 1.10e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062     36 FCAAELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqefealkdttvrsretgkrpqsep 115
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQP--------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    116 hstqpessndvkppvaapksvnkevttGYKRYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYG 195
Cdd:smart00156  54 ---------------------------PETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMNEIYG 106

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    196 FYREVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADPDPTEKG 275
Cdd:smart00156 107 FYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDPDQPVNG 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    276 YKPSARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAAVFSIDKKLKISINV 355
Cdd:smart00156 187 FGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQ 266


                   ....*
gi 17544062    356 FRPES 360
Cdd:smart00156 267 FKPGK 271
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 36-360 1.10e-138

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: 395.43  E-value: 1.10e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062     36 FCAAELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqefealkdttvrsretgkrpqsep 115
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQP--------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    116 hstqpessndvkppvaapksvnkevttGYKRYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYG 195
Cdd:smart00156  54 ---------------------------PETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMNEIYG 106

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    196 FYREVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADPDPTEKG 275
Cdd:smart00156 107 FYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDPDQPVNG 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    276 YKPSARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAAVFSIDKKLKISINV 355
Cdd:smart00156 187 FGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQ 266


                   ....*
gi 17544062    356 FRPES 360
Cdd:smart00156 267 FKPGK 271
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 39-358 2.77e-107

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: 316.59  E-value: 2.77e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  39 AELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqefealkdttvrsretgkrpqsephst 118
Cdd:cd07414  26 AEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFP------------------------------ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 119 qPESSndvkppvaapksvnkevttgykrYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYGFYR 198
Cdd:cd07414  76 -PESN-----------------------YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYD 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 199 EVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADPDPTEKGYKP 278
Cdd:cd07414 132 ECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGE 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 279 SARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAAVFSIDKKLKISINVFRP 358
Cdd:cd07414 212 NDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 16-358 2.96e-88

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 269.22  E-value: 2.96e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   16 VNKILEKIVFKWTHKTSMDL-FCAAELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqef 94
Cdd:PTZ00480  11 VDNIIERLLSVRGSKPGKNVnLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYP------ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   95 ealkdttvrsretgkrpqsephstqPESSndvkppvaapksvnkevttgykrYLFLGDYVDRGPFSMEVVILLTALKLAY 174
Cdd:PTZ00480  85 -------------------------PESN-----------------------YLFLGDYVDRGKQSLETICLLLAYKIKY 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  175 PDRIYLLRGNHESRSVNTSYGFYREVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLE 254
Cdd:PTZ00480 117 PENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTD 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  255 IPDVGVLTDLTWADPDPTEKGYKPSARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCG 334
Cdd:PTZ00480 197 VPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCG 276

                        330       340
                 ....*....|....*....|....
gi 17544062  335 QNDNTAAVFSIDKKLKISINVFRP 358
Cdd:PTZ00480 277 EFDNAGSMMTIDESLMCSFQILKP 300
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 64-225 2.05e-11

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: 60.30  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    64 PICVMGDIH--GQFDDLLAMLDMNgwplssqefealkdttvrsretgkrpqsephstQPESSNDVkppvaapksvnkevt 141
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKL---------------------------------LEEGKPDL--------------- 33

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   142 tgykrYLFLGDYVDRGPFSmEVVILLTALKLAYpDRIYLLRGNHESRSVNTsygFYREVNYRYDAQLYECFQNMFNVFPF 221
Cdd:pfam00149  34 -----VLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYGEC---LRLYPYLGLLARPWKRFLEVFNFLPL 103


                  ....
gi 17544062   222 CAVI 225
Cdd:pfam00149 104 AGIL 107
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 36-360 1.10e-138

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: 395.43  E-value: 1.10e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062     36 FCAAELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqefealkdttvrsretgkrpqsep 115
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQP--------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    116 hstqpessndvkppvaapksvnkevttGYKRYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYG 195
Cdd:smart00156  54 ---------------------------PETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMNEIYG 106

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    196 FYREVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADPDPTEKG 275
Cdd:smart00156 107 FYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDPDQPVNG 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    276 YKPSARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAAVFSIDKKLKISINV 355
Cdd:smart00156 187 FGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQ 266


                   ....*
gi 17544062    356 FRPES 360
Cdd:smart00156 267 FKPGK 271
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 39-358 2.77e-107

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: 316.59  E-value: 2.77e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  39 AELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqefealkdttvrsretgkrpqsephst 118
Cdd:cd07414  26 AEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFP------------------------------ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 119 qPESSndvkppvaapksvnkevttgykrYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYGFYR 198
Cdd:cd07414  76 -PESN-----------------------YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYD 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 199 EVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADPDPTEKGYKP 278
Cdd:cd07414 132 ECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGE 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 279 SARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAAVFSIDKKLKISINVFRP 358
Cdd:cd07414 212 NDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 40-358 2.72e-92

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: 277.93  E-value: 2.72e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  40 ELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGwplssqefealkdttvrsretgkrpqsephstq 119
Cdd:cd07415  19 EVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGG--------------------------------- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 120 pessndvKPPvaapksvnkevttgYKRYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYGFYRE 199
Cdd:cd07415  66 -------DVP--------------DTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDE 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 200 VNYRY-DAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADPDPTEkGYKP 278
Cdd:cd07415 125 CLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDRE-GWGI 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 279 SARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAAVFSIDKKLKISINVFRP 358
Cdd:cd07415 204 SPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 16-358 2.96e-88

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 269.22  E-value: 2.96e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   16 VNKILEKIVFKWTHKTSMDL-FCAAELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqef 94
Cdd:PTZ00480  11 VDNIIERLLSVRGSKPGKNVnLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYP------ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   95 ealkdttvrsretgkrpqsephstqPESSndvkppvaapksvnkevttgykrYLFLGDYVDRGPFSMEVVILLTALKLAY 174
Cdd:PTZ00480  85 -------------------------PESN-----------------------YLFLGDYVDRGKQSLETICLLLAYKIKY 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  175 PDRIYLLRGNHESRSVNTSYGFYREVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLE 254
Cdd:PTZ00480 117 PENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTD 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  255 IPDVGVLTDLTWADPDPTEKGYKPSARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCG 334
Cdd:PTZ00480 197 VPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCG 276

                        330       340
                 ....*....|....*....|....
gi 17544062  335 QNDNTAAVFSIDKKLKISINVFRP 358
Cdd:PTZ00480 277 EFDNAGSMMTIDESLMCSFQILKP 300
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 49-352 5.18e-86

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 262.53  E-value: 5.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   49 RELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqefealkdttvrsretgkrpqsephstqpessndvkp 128
Cdd:PTZ00244  38 REIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFP---------------------------------------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  129 pvaapksvnkevttGYKRYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYGFYREVNYRYDAQL 208
Cdd:PTZ00244  78 --------------PYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  209 YECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADPDPTEKGYKPSARGASFVFG 288
Cdd:PTZ00244 144 FKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFG 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17544062  289 PPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAAVFSIDKKLKIS 352
Cdd:PTZ00244 224 EDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCS 287
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 66-342 6.89e-84

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: 254.60  E-value: 6.89e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  66 CVMGDIHGQFDDLLAMLDMNGWPlssqefealkdttvrsretgkrpqsephstqPEssndvkppvaapksvnkevttgyK 145
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFP-------------------------------PE-----------------------D 26

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 146 RYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYGFYREVN----YRYDAQLYECFQNMFNVFPF 221
Cdd:cd00144  27 KYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDERTlrclRKGGEELWREFNEVFNYLPL 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 222 CAVINNTIMCMHGGISEHLTSFNQFSvFKRPLEIPDVGVLTDLTWADPDPTEKGYKPSARGASFVFGPPALRAFLKKLDL 301
Cdd:cd00144 107 AALVDGKILCVHGGLSPDLTLLDQIR-NIRPIENPDDQLVEDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGL 185

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17544062 302 QMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAAV 342
Cdd:cd00144 186 KLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAA 226
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 39-355 3.44e-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: 242.60  E-value: 3.44e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  39 AELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPlssqefealkDTTvrsretgkrpqsephst 118
Cdd:cd07416  19 EDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSP----------ANT----------------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 119 qpessndvkppvaapksvnkevttgykRYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYGFYR 198
Cdd:cd07416  72 ---------------------------RYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQ 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 199 EVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADP------DPT 272
Cdd:cd07416 125 ECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPledfgnEKT 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 273 EKGYKP-SARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRR------LVTIFSAPNYCGQNDNTAAVfsi 345
Cdd:cd07416 205 QEHFVHnTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAV--- 281

                       330
                ....*....|
gi 17544062 346 dkkLKISINV 355
Cdd:cd07416 282 ---LKYENNV 288
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 27-358 9.30e-75

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: 234.26  E-value: 9.30e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  27 WTHKTSMDL-FCAAELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLDMNGWPLSsqefEALKDTTvrsr 105
Cdd:cd07419  11 WKPPVERRFfFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVT----EEAGDIE---- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 106 etgkrpqsephstqpesSNDvkppvaapksvnkevttgykrYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNH 185
Cdd:cd07419  83 -----------------YID---------------------YLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNH 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 186 ESRSVNTSYGFYREVNYRY------DAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVG 259
Cdd:cd07419 125 EAADINALFGFREECIERLgedirdGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGS 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 260 -VLTDLTWADP---DPTEkGYKPSAR-----GASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAP 330
Cdd:cd07419 205 pVVMDLLWSDPtenDSVL-GLRPNAIdprgtGLIVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSAT 283

                       330       340
                ....*....|....*....|....*...
gi 17544062 331 NYCGQNDNTAAVFSIDKKLKISINVFRP 358
Cdd:cd07419 284 NYCGTAGNAGAILVLGRDLVVVPKLIHP 311
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 7-356 6.94e-73

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: 229.45  E-value: 6.94e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   7 EDQKNVRNFVNKILEKivFKwtHKTSMDLFCAAELaeLCHrARELIWSEPIFLKLEAP----ICVMGDIHGQFDDLLAML 82
Cdd:cd07417   7 EDGKVTLEFVKEMMEW--FK--DQKKLHKKYAYQI--LLQ-VKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  83 DMNGWPlssqefealkdttvrsretgkrpqSEPHstqpessndvkppvaapksvnkevttgykRYLFLGDYVDRGPFSME 162
Cdd:cd07417  80 ELNGLP------------------------SETN-----------------------------PYLFNGDFVDRGSFSVE 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 163 VVILLTALKLAYPDRIYLLRGNHESRSVNTSYGFYREVNYRYDAQLYECFQNMFNVFPFCAVINNTIMCMHGGI-SEHLT 241
Cdd:cd07417 107 VILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGV 186

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 242 SFNQFSVFKRPLEIPDVGVLTDLTWADPDPtEKGYKPSARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGR 321
Cdd:cd07417 187 TLDDIRKIDRFRQPPDSGLMCELLWSDPQP-QPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDG 265

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 17544062 322 RLVTIFSAPNYCGQNDNTAAVFSID-KKLKISINVF 356
Cdd:cd07417 266 KCITVFSAPNYCDQMGNKGAFIRFKgSDLKPKFTQF 301
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 40-360 2.84e-63

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 204.28  E-value: 2.84e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   40 ELAELCHRARELIWSEPIFLKLEAPICVMGDIHGQFDDLLAMLdmngwplssqefealkdttvrsRETGKRPQSEphstq 119
Cdd:PTZ00239  20 DLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALF----------------------KEGGDIPNAN----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  120 pessndvkppvaapksvnkevttgykrYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYGFYRE 199
Cdd:PTZ00239  73 ---------------------------YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEE 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  200 VNYRY-DAQLYECFQNMFNVFPFCAVINNTIMCMHGGISEHLTSFNQFSVFKRPLEIPDVGVLTDLTWADPDPTEKgYKP 278
Cdd:PTZ00239 126 ILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEY-WAV 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  279 SARGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEF-FDGRRLVTIFSAPNYCGQNDNTAAVFSIDKKLKISINVFR 357
Cdd:PTZ00239 205 NSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFK 284


                 ....*
gi 17544062  358 --PES 360
Cdd:PTZ00239 285 evPES 289
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 42-341 1.26e-48

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: 166.04  E-value: 1.26e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  42 AELCHRARELIWSEPIFLKL------EAPICvmGDIHGQFDDLLAMLDMNGWPLSSqefealkdttvrsretgkRPqsep 115
Cdd:cd07420  26 LLILREARKSLKQLPNISRVstsyskEVTIC--GDLHGKLDDLLLIFYKNGLPSPE------------------NP---- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 116 hstqpessndvkppvaapksvnkevttgykrYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTSYG 195
Cdd:cd07420  82 -------------------------------YVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYG 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 196 FYREVNYRYD---AQLYECFQNMFNVFPFCAVINNTIMCMHGGISEhLTSFNQFSVFKR------PLEIPDVgvlTDLTW 266
Cdd:cd07420 131 FTKEVMQKYKdhgKKILRLLEDVFSWLPLATIIDNKVLVVHGGISD-STDLDLLDKIDRhkyvstKTEWQQV---VDILW 206

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17544062 267 ADPDPTeKGYKPSA-RGASFVFGPPALRAFLKKLDLQMVIRGHQVVEDGYEFFDGRRLVTIFSAPNYCGQNDNTAA 341
Cdd:cd07420 207 SDPKAT-KGCKPNTfRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGA 281
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 38-332 6.29e-32

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: 123.76  E-value: 6.29e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062  38 AAELAELCHRARELIWSEPIFLKLE----APICVMGDIHGQFDDLLAMLDMNGWPlssqefealkdttvrsretgkrpqs 113
Cdd:cd07418  37 VNVFDSLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFP------------------------- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 114 ephstqpessndvkppvaapksvnkevtTGYKRYLFLGDYVDRGPFSMEVVILLTALKLAYPDRIYLLRGNHESRSVNTS 193
Cdd:cd07418  92 ----------------------------DQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSM 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 194 YGFYREVNYRYD---AQLY----ECFQNMfnvfPFCAVINNTIMCMHGGIsehltsFNQFSVFKRPL------------- 253
Cdd:cd07418 144 YGFEQEVLTKYGdkgKHVYrkclGCFEGL----PLASIIAGRVYTAHGGL------FRSPSLPKRKKqkgknrrvlllep 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 254 --EIPDVGVLTDLT----------------------WADPDPTEKGYKPSARGASFVFGPPALRAFLKKLDLQMVIRGHQ 309
Cdd:cd07418 214 esESLKLGTLDDLMkarrsvldppgegsnlipgdvlWSDPSLTPGLSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHE 293

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 17544062 310 ------------VVEDGYEF---FDGRRLVTIFSAPNY 332
Cdd:cd07418 294 gpdarekrpglaGMNKGYTVdhdVESGKLITLFSAPDY 331
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 64-225 2.05e-11

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: 60.30  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062    64 PICVMGDIH--GQFDDLLAMLDMNgwplssqefealkdttvrsretgkrpqsephstQPESSNDVkppvaapksvnkevt 141
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKL---------------------------------LEEGKPDL--------------- 33

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062   142 tgykrYLFLGDYVDRGPFSmEVVILLTALKLAYpDRIYLLRGNHESRSVNTsygFYREVNYRYDAQLYECFQNMFNVFPF 221
Cdd:pfam00149  34 -----VLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYGEC---LRLYPYLGLLARPWKRFLEVFNFLPL 103


                  ....
gi 17544062   222 CAVI 225
Cdd:pfam00149 104 AGIL 107
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 150-237 6.61e-07

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: 49.60  E-value: 6.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544062 150 LGDYVDRGPFSMEVVILLTALK---LAYPDRIYLLRGNHES-------RSVNTSY--GFYREVNYRYDAQLYECF-QNMF 216
Cdd:cd07425  39 TGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELmnlcgdfRYVHPRGlnEFGGVAKRRYALLSDGGYiGRYL 118

                        90       100
                ....*....|....*....|.
gi 17544062 217 NVFPFCAVINNTIMcMHGGIS 237
Cdd:cd07425 119 RTHPVVLVVNDILF-VHGGLG 138
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 148-186 1.98e-04

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: 42.88  E-value: 1.98e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 17544062 148 LFLGDYVDRGPFSMEVVILLTALKLAYPDRIY-LLRGNHE 186
Cdd:cd07421  39 IFLGDYCDRGPETRKVIDFLISLPEKHPKQRHvFLCGNHD 78
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 143-209 9.72e-04

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: 38.79  E-value: 9.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17544062 143 GYKRYLFLGDYVDRGPFSMEVVILLTALKLAyPDRIYLLRGNHEsrSVNTSYGFYREVNYRYDAQLY 209
Cdd:cd00838  26 KPDLVICLGDLVDYGPDPEEVELKALRLLLA-GIPVYVVPGNHD--ILVTHGPPYDPLDEGSPGEDP 89
 
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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