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Conserved domains on  [gi|584593193|ref|NP_001276897|]
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serine/threonine-protein phosphatase 2B catalytic subunit beta isoform isoform d [Homo sapiens]

Protein Classification

serine/threonine-protein phosphatase 2B catalytic subunit( domain architecture ID 10164829)

serine/threonine-protein phosphatase 2B catalytic subunit is a calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 50-372 0e+00

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: 665.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  50 PRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV 129
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 130 DRGYFSIEhvlgtedisinphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAF 209
Cdd:cd07416   81 DRGYFSIE------------------CVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAF 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 210 DSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNY 289
Cdd:cd07416  143 DCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSY 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 290 PAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYW 369
Cdd:cd07416  223 RAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYW 302


                 ...
gi 584593193 370 LPN 372
Cdd:cd07416  303 LPN 305
 
Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 50-372 0e+00

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: 665.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  50 PRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV 129
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 130 DRGYFSIEhvlgtedisinphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAF 209
Cdd:cd07416   81 DRGYFSIE------------------CVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAF 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 210 DSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNY 289
Cdd:cd07416  143 DCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSY 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 290 PAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYW 369
Cdd:cd07416  223 RAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYW 302


                 ...
gi 584593193 370 LPN 372
Cdd:cd07416  303 LPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 67-356 8.49e-134

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


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 388.49  E-value: 8.49e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193    67 EEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEhvlgtedis 146
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIE--------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193   147 inphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVH 226
Cdd:smart00156  74 ---------VILLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMH 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193   227 GGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPsedfgnEKSQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIR 306
Cdd:smart00156 145 GGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDP------DQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIR 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 584593193   307 AHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 356
Cdd:smart00156 218 AHQVVDDGYEFFADGK------LVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 60-365 2.17e-70

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 227.01  E-value: 2.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  60 VKEGRVDEEIALRIINEGAA-ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEh 138
Cdd:PTZ00239  10 LLNGGCLPERDLKLICERAKeIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVE- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 139 vlgtedisinphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYEACMEAFDSLPLAAL 217
Cdd:PTZ00239  89 -----------------TMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAAL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 218 LNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEdfgneksQEHFSHNTvRGCSYFYNYPAVCEFLQ 297
Cdd:PTZ00239 152 IEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEE-------VEYWAVNS-RGAGYLFGAKVTKEFCR 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584593193 298 NNNLLSIIRAHEAQDAGYRMYRKSQttgfpSLITIFSAPNYLDVYNNKAAVLKYENNV-MNIRQFNCSP 365
Cdd:PTZ00239 224 LNDLTLICRAHQLVMEGYKYWFPDQ-----NLVTVWSAPNYCYRCGNIASILCLDENLqQTWKTFKEVP 287
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 93-218 4.46e-13

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: 65.70  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193   93 PITVCGDIH--GQFFDLMKLFEVGGSPANtRYLFL--GDYVDRGYFSiehvlgtedisinphnninECVLYLWVLKILYp 168
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGK-PDLVLhaGDLVDRGPPS-------------------EEVLELLERLIKY- 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 584593193  169 STLFLLRGNHECRHLtEYFTFKQEckIKYSERVYEACMEAFDSLPLAALL 218
Cdd:pfam00149  61 VPVYLVRGNHDFDYG-ECLRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
 
Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 50-372 0e+00

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: 665.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  50 PRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV 129
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 130 DRGYFSIEhvlgtedisinphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAF 209
Cdd:cd07416   81 DRGYFSIE------------------CVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAF 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 210 DSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNY 289
Cdd:cd07416  143 DCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSY 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 290 PAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYW 369
Cdd:cd07416  223 RAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYW 302


                 ...
gi 584593193 370 LPN 372
Cdd:cd07416  303 LPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 67-356 8.49e-134

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


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 388.49  E-value: 8.49e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193    67 EEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEhvlgtedis 146
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIE--------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193   147 inphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVH 226
Cdd:smart00156  74 ---------VILLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMH 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193   227 GGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPsedfgnEKSQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIR 306
Cdd:smart00156 145 GGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDP------DQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIR 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 584593193   307 AHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 356
Cdd:smart00156 218 AHQVVDDGYEFFADGK------LVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 80-365 3.38e-104

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: 313.37  E-value: 3.38e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  80 ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEhvlgtedisinphnnineCVLY 159
Cdd:cd07415   30 ILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVE------------------TFLL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 160 LWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDD 238
Cdd:cd07415   92 LLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQ 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 239 IRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQehfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMY 318
Cdd:cd07415  172 IRALDRFQEVPHEGPMCDLLWSDPDDREGWGISP--------RGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWM 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 584593193 319 RKSQttgfpsLITIFSAPNYLDVYNNKAAVLKY-ENNVMNIRQFNCSP 365
Cdd:cd07415  244 FNNK------LVTVWSAPNYCYRCGNVASILELdEHLNRSFKQFEAAP 285
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 52-367 1.18e-86

PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 269.51  E-value: 1.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  52 VDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAP----ITVCGDIHGQFFDLMKLFEVGGSPANT-RYLFLG 126
Cdd:cd07417   16 VKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETnPYLFNG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 127 DYVDRGYFSIEhvlgtedisinphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACM 206
Cdd:cd07417   96 DFVDRGSFSVE------------------VILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 207 EAFDSLPLAALLNQQFLCVHGGL-SPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQehfshntvRGCSY 285
Cdd:cd07417  158 EVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSK--------RGVGC 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 286 FYNyPAVCE-FLQNNNLLSIIRAHEAQDAGYRMYRKSqttgfpSLITIFSAPNYLDVYNNKAAVLKYENNVMNIR--QFN 362
Cdd:cd07417  230 QFG-PDVTKrFLEENNLDYIIRSHEVKDEGYEVEHDG------KCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKftQFE 302


                 ....*
gi 584593193 363 CSPHP 367
Cdd:cd07417  303 AVPHP 307
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 95-351 1.06e-83

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: 258.84  E-value: 1.06e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  95 TVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIehvlgtedisinphnninECVLYLWVLKILYPSTLFLL 174
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSV------------------EVIDLLLALKILYPDNVFLL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 175 RGNHECRHLTEYFTFKQE----CKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLdRFKEPPA 250
Cdd:cd00144   63 RGNHEFMLLNFLYGFYDErtlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPD 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 251 FGPMCDLLWSDPSEDFGneksqehFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRksqttgFPSLI 330
Cdd:cd00144  142 DQLVEDLLWSDPDESVG-------DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLH------GGKLI 208

                        250       260
                 ....*....|....*....|.
gi 584593193 331 TIFSAPNYLDVYNNKAAVLKY 351
Cdd:cd00144  209 TIFSAPNYCGKGGNKLAALVV 229
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 80-356 9.83e-79

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: 248.41  E-value: 9.83e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  80 ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEHVlgtedisinphnnineCVLY 159
Cdd:cd07414   38 IFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETI----------------CLLL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 160 LWvlKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDI 239
Cdd:cd07414  102 AY--KIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQI 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 240 RRLDRFKEPPAFGPMCDLLWSDPSEDFGNeksqehFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYR 319
Cdd:cd07414  180 RRIMRPTDVPDQGLLCDLLWSDPDKDVQG------WGEND-RGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFA 252

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 584593193 320 KSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 356
Cdd:cd07414  253 KRQ------LVTLFSAPNYCGEFDNAGAMMSVDETLM 283
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 60-365 2.17e-70

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 227.01  E-value: 2.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  60 VKEGRVDEEIALRIINEGAA-ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEh 138
Cdd:PTZ00239  10 LLNGGCLPERDLKLICERAKeIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVE- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 139 vlgtedisinphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYEACMEAFDSLPLAAL 217
Cdd:PTZ00239  89 -----------------TMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAAL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 218 LNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEdfgneksQEHFSHNTvRGCSYFYNYPAVCEFLQ 297
Cdd:PTZ00239 152 IEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEE-------VEYWAVNS-RGAGYLFGAKVTKEFCR 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584593193 298 NNNLLSIIRAHEAQDAGYRMYRKSQttgfpSLITIFSAPNYLDVYNNKAAVLKYENNV-MNIRQFNCSP 365
Cdd:PTZ00239 224 LNDLTLICRAHQLVMEGYKYWFPDQ-----NLVTVWSAPNYCYRCGNIASILCLDENLqQTWKTFKEVP 287
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 80-356 8.31e-69

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 223.38  E-value: 8.31e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  80 ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEHVlgtedisinphnnineCVLY 159
Cdd:PTZ00480  47 IFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETI----------------CLLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 160 LWvlKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDI 239
Cdd:PTZ00480 111 AY--KIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 240 RRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEhfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYR 319
Cdd:PTZ00480 189 RRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNE-------RGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFS 261

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 584593193 320 KSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 356
Cdd:PTZ00480 262 KRQ------LVTLFSAPNYCGEFDNAGSMMTIDESLM 292
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 65-355 2.27e-59

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 197.82  E-value: 2.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  65 VDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEhvlgted 144
Cdd:PTZ00244  25 IREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVE------- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 145 isinphnnineCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLC 224
Cdd:PTZ00244  98 -----------TITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIIC 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 225 VHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDF-GNEKSQehfshntvRGCSYFYNYPAVCEFLQNNNLLS 303
Cdd:PTZ00244 167 MHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVrGFLESD--------RGVSYLFGEDIVNDFLDMVDMDL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 584593193 304 IIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNV 355
Cdd:PTZ00244 239 IVRAHQVMERGYGFFASRQ------LVTVFSAPNYCGEFDNDAAVMNIDDKL 284
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 64-354 4.87e-58

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: 194.97  E-value: 4.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  64 RVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTR--------YLFLGDYVDRGYFS 135
Cdd:cd07419   20 FFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagdieyidYLFLGDYVDRGSHS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 136 IEHVlgtedisinphnnineCVLYlwVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSER------VYEACMEAF 209
Cdd:cd07419  100 LETI----------------CLLL--ALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirdgdsVWQRINRLF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 210 DSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGP-MCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYN 288
Cdd:cd07419  162 NWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPvVMDLLWSDPTENDSVLGLRPNAIDPRGTGLIVKFG 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584593193 289 YPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENN 354
Cdd:cd07419  242 PDRVMEFLEENDLQMIIRAHECVMDGFERFAQGH------LITLFSATNYCGTAGNAGAILVLGRD 301
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 80-367 3.15e-52

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: 181.54  E-value: 3.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  80 ILRREKTMIEVE----APITVCGDIHGQFFDLMKLFEVGGSPANTR-YLFLGDYVDRGYFSIEhvlgtedisinphnnin 154
Cdd:cd07418   50 ILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRfYVFNGDYVDRGAWGLE----------------- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 155 eCVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSER---VYEACMEAFDSLPLAALLNQQFLCVHGGL-- 229
Cdd:cd07418  113 -TFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKgkhVYRKCLGCFEGLPLASIIAGRVYTAHGGLfr 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 230 -------------------------SPEIHTLDDIRRLDR-FKEPPAFGPMC---DLLWSDPSEDFGneksqehFSHNTV 280
Cdd:cd07418  192 spslpkrkkqkgknrrvlllepeseSLKLGTLDDLMKARRsVLDPPGEGSNLipgDVLWSDPSLTPG-------LSPNKQ 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 281 RGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRM---------YRKSQTTGFPSLITIFSAPNYL------DVYNNK 345
Cdd:cd07418  265 RGIGLLWGPDCTEEFLEKNNLKLIIRSHEGPDAREKRpglagmnkgYTVDHDVESGKLITLFSAPDYPqfqateERYNNK 344

                        330       340
                 ....*....|....*....|..
gi 584593193 346 AAVLkyennVMNIRQFNCSPHP 367
Cdd:cd07418  345 GAYI-----ILQPPDFSDPQFH 361
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 71-356 5.35e-42

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: 151.79  E-value: 5.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  71 LRIINEGAAILR------REKTMIEVEapITVCGDIHGQFFDLMKLFEVGGSPANTR-YLFLGDYVDRGYFSIehvlgte 143
Cdd:cd07420   26 LLILREARKSLKqlpnisRVSTSYSKE--VTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSI------- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 144 disinphnninECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKY---SERVYEACMEAFDSLPLAALLNQ 220
Cdd:cd07420   97 -----------EILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYkdhGKKILRLLEDVFSWLPLATIIDN 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193 221 QFLCVHGGLSpEIHTLDDIRRLDRFK---EPPAFGPMCDLLWSDPsedfgneKSQEHFSHNTVRGCSYFYNYPAVCEFLQ 297
Cdd:cd07420  166 KVLVVHGGIS-DSTDLDLLDKIDRHKyvsTKTEWQQVVDILWSDP-------KATKGCKPNTFRGGGCYFGPDVTSQFLQ 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 584593193 298 NNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 356
Cdd:cd07420  238 KHGLSLLIRSHECKPEGYEFCHNNK------VITIFSASNYYEEGSNRGAYVKLGPQLT 290
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 93-218 4.46e-13

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: 65.70  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193   93 PITVCGDIH--GQFFDLMKLFEVGGSPANtRYLFL--GDYVDRGYFSiehvlgtedisinphnninECVLYLWVLKILYp 168
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGK-PDLVLhaGDLVDRGPPS-------------------EEVLELLERLIKY- 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 584593193  169 STLFLLRGNHECRHLtEYFTFKQEckIKYSERVYEACMEAFDSLPLAALL 218
Cdd:pfam00149  61 VPVYLVRGNHDFDYG-ECLRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 94-179 2.35e-04

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: 42.30  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584593193  94 ITVCGDIHGQFFDLM-KLFEVGGSPANTRYLFLGDYVDRGyfsiehvlgtedisinPHNninecvlyLWVLKILYPSTLF 172
Cdd:cd07424    3 DFVVGDIHGHFQRLQrALDAVGFDPARDRLISVGDLVDRG----------------PES--------LEVLELLKQPWFH 58


                 ....*..
gi 584593193 173 LLRGNHE 179
Cdd:cd07424   59 AVQGNHE 65
 
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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