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Conserved domains on  [gi|2462519910|ref|XP_054222194|]
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serine/threonine-protein phosphatase 2B catalytic subunit beta isoform isoform X6 [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 ...
 1-268 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: 624.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:cd07416    38 LLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSE 160
Cdd:cd07416   118 EYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLE 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 DFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNN 240
Cdd:cd07416   198 DFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNN 277

                         250       260
                  ....*....|....*....|....*...
gi 2462519910 241 KAAVLKYENNVMNIRQFNCSPHPYWLPN 268
Cdd:cd07416   278 KAAVLKYENNVMNIRQFNCSPHPYWLPN 305
 
Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 1-268 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: 624.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:cd07416    38 LLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSE 160
Cdd:cd07416   118 EYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLE 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 DFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNN 240
Cdd:cd07416   198 DFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNN 277

                         250       260
                  ....*....|....*....|....*...
gi 2462519910 241 KAAVLKYENNVMNIRQFNCSPHPYWLPN 268
Cdd:cd07416   278 KAAVLKYENNVMNIRQFNCSPHPYWLPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 1-252 2.31e-133

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: 384.64  E-value: 2.31e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910    1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:smart00156  23 LVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMN 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPse 160
Cdd:smart00156 103 EIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDP-- 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  161 dfgnEKSQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNN 240
Cdd:smart00156 181 ----DQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK------LVTIFSAPNYCDRFGN 249

                          250
                   ....*....|..
gi 2462519910  241 KAAVLKYENNVM 252
Cdd:smart00156 250 KAAVLKVDKDLK 261
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 1-252 2.46e-73

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 233.01  E-value: 2.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:PTZ00480   54 LLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASIN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSE 160
Cdd:PTZ00480  134 RIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDK 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 DFGNEKSQEhfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNN 240
Cdd:PTZ00480  214 DVQGWADNE-------RGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQ------LVTLFSAPNYCGEFDN 280

                         250
                  ....*....|..
gi 2462519910 241 KAAVLKYENNVM 252
Cdd:PTZ00480  281 AGSMMTIDESLM 292
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 7-114 3.16e-16

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: 74.56  E-value: 3.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   7 PITVCGDIH--GQFFDLMKLFEVGGSPANtRYLFL--GDYVDRGYFSiECVLYLWVLKILYpSTLFLLRGNHECRHLtEY 82
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGK-PDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYG-EC 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462519910  83 FTFKQEckIKYSERVYEACMEAFDSLPLAALL 114
Cdd:pfam00149  78 LRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
8-146 1.66e-03

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 39.13  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   8 ITVCGDIHGQFFDLMKLFE-VGGSPANtRYLFLGDYVDRGYFSIECVLYLWVLKILYpstlflLRGNHEcrhlteyftfk 86
Cdd:COG0622     2 IAVISDTHGNLPALEAVLEdLEREGVD-LIVHLGDLVGYGPDPPEVLDLLRELPIVA------VRGNHD----------- 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462519910  87 qeckikyservyEACMEAFDSLPLAALL---NQQFLCVHGGLSPEIHTLDDIRRLDR-FKEPPA 146
Cdd:COG0622    64 ------------GAVLRGLRSLPETLRLeleGVRILLVHGSPNEYLLPDTPAERLRAlAAEGDA 115
 
Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 1-268 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: 624.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:cd07416    38 LLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSE 160
Cdd:cd07416   118 EYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLE 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 DFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNN 240
Cdd:cd07416   198 DFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNN 277

                         250       260
                  ....*....|....*....|....*...
gi 2462519910 241 KAAVLKYENNVMNIRQFNCSPHPYWLPN 268
Cdd:cd07416   278 KAAVLKYENNVMNIRQFNCSPHPYWLPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 1-252 2.31e-133

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: 384.64  E-value: 2.31e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910    1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:smart00156  23 LVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMN 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPse 160
Cdd:smart00156 103 EIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDP-- 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  161 dfgnEKSQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNN 240
Cdd:smart00156 181 ----DQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK------LVTIFSAPNYCDRFGN 249

                          250
                   ....*....|..
gi 2462519910  241 KAAVLKYENNVM 252
Cdd:smart00156 250 KAAVLKVDKDLK 261
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 2-261 3.89e-108

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: 320.69  E-value: 3.89e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   2 IEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTE 81
Cdd:cd07415    38 QRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  82 YFTFKQECKIKY-SERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSE 160
Cdd:cd07415   118 VYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDD 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 DFGNEKSQehfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNN 240
Cdd:cd07415   198 REGWGISP--------RGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNK------LVTVWSAPNYCYRCGN 263

                         250       260
                  ....*....|....*....|..
gi 2462519910 241 KAAVLKY-ENNVMNIRQFNCSP 261
Cdd:cd07415   264 VASILELdEHLNRSFKQFEAAP 285
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 9-247 2.41e-90

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: 273.48  E-value: 2.41e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   9 TVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQE 88
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  89 ----CKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLdRFKEPPAFGPMCDLLWSDPSEDFGn 164
Cdd:cd00144    81 rtlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVG- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 165 eksqehFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRksqttgFPSLITIFSAPNYLDVYNNKAAV 244
Cdd:cd00144   159 ------DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLH------GGKLITIFSAPNYCGKGGNKLAA 226


                  ...
gi 2462519910 245 LKY 247
Cdd:cd00144   227 LVV 229
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 1-263 3.22e-88

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: 271.05  E-value: 3.22e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAP----ITVCGDIHGQFFDLMKLFEVGGSPANT-RYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHE 75
Cdd:cd07417    51 LVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETnPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  76 CRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGL-SPEIHTLDDIRRLDRFKEPPAFGPMCDLL 154
Cdd:cd07417   131 TDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFRQPPDSGLMCELL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 155 WSDPSEDFGNEKSQehfshntvRGCSYFYNyPAVCE-FLQNNNLLSIIRAHEAQDAGYRMYRKSqttgfpSLITIFSAPN 233
Cdd:cd07417   211 WSDPQPQPGRGPSK--------RGVGCQFG-PDVTKrFLEENNLDYIIRSHEVKDEGYEVEHDG------KCITVFSAPN 275

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2462519910 234 YLDVYNNKAAVLKYENNVMNIR--QFNCSPHP 263
Cdd:cd07417   276 YCDQMGNKGAFIRFKGSDLKPKftQFEAVPHP 307
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 1-252 1.70e-83

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: 258.04  E-value: 1.70e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:cd07414    45 LLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASIN 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSE 160
Cdd:cd07414   125 RIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDK 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 DFGNeksqehFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNN 240
Cdd:cd07414   205 DVQG------WGEND-RGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQ------LVTLFSAPNYCGEFDN 271

                         250
                  ....*....|..
gi 2462519910 241 KAAVLKYENNVM 252
Cdd:cd07414   272 AGAMMSVDETLM 283
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 1-252 2.46e-73

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 233.01  E-value: 2.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:PTZ00480   54 LLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASIN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSE 160
Cdd:PTZ00480  134 RIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDK 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 DFGNEKSQEhfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNN 240
Cdd:PTZ00480  214 DVQGWADNE-------RGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQ------LVTLFSAPNYCGEFDN 280

                         250
                  ....*....|..
gi 2462519910 241 KAAVLKYENNVM 252
Cdd:PTZ00480  281 AGSMMTIDESLM 292
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 4-261 4.06e-73

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 231.63  E-value: 4.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   4 VEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYF 83
Cdd:PTZ00239   41 VRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVY 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  84 TFKQECKIKY-SERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEdf 162
Cdd:PTZ00239  121 GFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEE-- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 163 gneksQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpSLITIFSAPNYLDVYNNKA 242
Cdd:PTZ00239  199 -----VEYWAVNS-RGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFPDQ-----NLVTVWSAPNYCYRCGNIA 267

                         250       260
                  ....*....|....*....|
gi 2462519910 243 AVLKYENNV-MNIRQFNCSP 261
Cdd:PTZ00239  268 SILCLDENLqQTWKTFKEVP 287
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 1-251 6.20e-64

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 207.84  E-value: 6.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLT 80
Cdd:PTZ00244   47 LLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASIN 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  81 EYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSE 160
Cdd:PTZ00244  127 KMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPED 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 DF-GNEKSQehfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYN 239
Cdd:PTZ00244  207 EVrGFLESD--------RGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQ------LVTVFSAPNYCGEFD 272

                         250
                  ....*....|..
gi 2462519910 240 NKAAVLKYENNV 251
Cdd:PTZ00244  273 NDAAVMNIDDKL 284
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 1-250 1.64e-60

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: 199.59  E-value: 1.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   1 MIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTR--------YLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRG 72
Cdd:cd07419    43 VLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagdieyidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  73 NHECRHLTEYFTFKQECKIKYSER------VYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPA 146
Cdd:cd07419   123 NHEAADINALFGFREECIERLGEDirdgdsVWQRINRLFNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 147 FGP-MCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsL 225
Cdd:cd07419   203 GSPvVMDLLWSDPTENDSVLGLRPNAIDPRGTGLIVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGH------L 276

                         250       260
                  ....*....|....*....|....*
gi 2462519910 226 ITIFSAPNYLDVYNNKAAVLKYENN 250
Cdd:cd07419   277 ITLFSATNYCGTAGNAGAILVLGRD 301
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 8-263 1.26e-54

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: 186.16  E-value: 1.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   8 ITVCGDIHGQFFDLMKLFEVGGSPANTR-YLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFK 86
Cdd:cd07418    68 VVVVGDVHGQLHDVLFLLEDAGFPDQNRfYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  87 QECKIKYSER---VYEACMEAFDSLPLAALLNQQFLCVHGGL---------------------------SPEIHTLDDIR 136
Cdd:cd07418   148 QEVLTKYGDKgkhVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknrrvlllepeseSLKLGTLDDLM 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 137 RLDR-FKEPPAFGPMC---DLLWSDPSEDFGneksqehFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYR 212
Cdd:cd07418   228 KARRsVLDPPGEGSNLipgDVLWSDPSLTPG-------LSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEGPDAREK 300

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462519910 213 M---------YRKSQTTGFPSLITIFSAPNYL------DVYNNKAAVLkyennVMNIRQFNCSPHP 263
Cdd:cd07418   301 RpglagmnkgYTVDHDVESGKLITLFSAPDYPqfqateERYNNKGAYI-----ILQPPDFSDPQFH 361
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 8-252 4.90e-47

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: 163.73  E-value: 4.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   8 ITVCGDIHGQFFDLMKLFEVGGSPANTR-YLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFK 86
Cdd:cd07420    53 VTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFT 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  87 QECKIKY---SERVYEACMEAFDSLPLAALLNQQFLCVHGGLSpEIHTLDDIRRLDRFK---EPPAFGPMCDLLWSDPse 160
Cdd:cd07420   133 KEVMQKYkdhGKKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-DSTDLDLLDKIDRHKyvsTKTEWQQVVDILWSDP-- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910 161 dfgneKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNN 240
Cdd:cd07420   210 -----KATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNK------VITIFSASNYYEEGSN 278

                         250
                  ....*....|..
gi 2462519910 241 KAAVLKYENNVM 252
Cdd:cd07420   279 RGAYVKLGPQLT 290
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 7-114 3.16e-16

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: 74.56  E-value: 3.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   7 PITVCGDIH--GQFFDLMKLFEVGGSPANtRYLFL--GDYVDRGYFSiECVLYLWVLKILYpSTLFLLRGNHECRHLtEY 82
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGK-PDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYG-EC 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462519910  83 FTFKQEckIKYSERVYEACMEAFDSLPLAALL 114
Cdd:pfam00149  78 LRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 8-75 7.91e-07

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


Pssm-ID: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 49.62  E-value: 7.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462519910   8 ITVCGDIHGQFFDLM-KLFEVGGSPANTRYLFLGDYVDRGYFSIECvlylwvLKILYPSTLFLLRGNHE 75
Cdd:cd07424     3 DFVVGDIHGHFQRLQrALDAVGFDPARDRLISVGDLVDRGPESLEV------LELLKQPWFHAVQGNHE 65
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 12-130 5.59e-06

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 47.51  E-value: 5.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  12 GDIHGQFFDLMKLFEVGG----------SPANTRYLFLGDYVDRGYFSIECVLYlwVLKILYPSTLFLLRGNHE---CRH 78
Cdd:cd07423     4 GDVHGCYDELVELLEKLGyqkkeeglyvHPEGRKLVFLGDLVDRGPDSIDVLRL--VMNMVKAGKALYVPGNHCnklYRY 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462519910  79 L---------------TEYFTFKQECKIKYSERVyeacMEAFDSLPLAALLNQ-QFLCVHGGLSPEIH 130
Cdd:cd07423    82 LkgrnvqlahglettvEELEALSKEERPEFRERF----AEFLESLPSHLVLDGgRLVVAHAGIKEEMI 145
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 10-75 4.25e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 43.02  E-value: 4.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462519910  10 VCGDIHGQFFDLMKLF--EVGGSPANTRYLFLGDYVDRGYFSiECVLYLWVLKILYPSTLFLLRGNHE 75
Cdd:cd00838     2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDP-EEVELKALRLLLAGIPVYVVPGNHD 68
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 12-128 4.77e-05

Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and PrpA/PrpB. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 44.84  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  12 GDIHGQFFDLMKLFE-VGGSPANTRYLFLGDYVDRGYFSIECVLYlwvLKILYPSTLFLLrGNHECRHLTEYFTFKqecK 90
Cdd:cd07422     5 GDIQGCYDELQRLLEkINFDPAKDRLWLVGDLVNRGPDSLETLRF---VKSLGDSAVVVL-GNHDLHLLAVAAGIK---K 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462519910  91 IKYSERVYEAcMEAFDSLPLAALLNQQ----------FLCVHGGLSPE 128
Cdd:cd07422    78 LKKKDTLDEI-LEAPDRDELLDWLRHQpllhrddelgIVMVHAGIPPQ 124
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 12-127 1.31e-04

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: 43.06  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  12 GDIHGQFFDLMKLFEVGG-SPANTRYLF-------LGDYVDRGYFSIEcVLYLwvLKILYP------STLFLLRGNHECR 77
Cdd:cd07425     4 GDLHGDLDRLRTILKLAGvIDSNDRWIGgdtvvvqTGDILDRGDDEIE-ILKL--LEKLKRqarkagGKVILLLGNHELM 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462519910  78 HL---------TEYFTFKQECKIKYSER---VYEACMeaFDSLPLAALLNqQFLCVHGGLSP 127
Cdd:cd07425    81 NLcgdfryvhpRGLNEFGGVAKRRYALLsdgGYIGRY--LRTHPVVLVVN-DILFVHGGLGP 139
PHA02239 PHA02239
putative protein phosphatase
 8-107 1.37e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 43.06  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   8 ITVCGDIHGQFFDLMKLFEV---GGSPANTrYLFLGDYVDRGYFSIECVLYLWVLkILYPSTLFLLRGNHEcrhlTEYFT 84
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMDKinnERKPEET-IVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHD----DEFYN 76

                          90       100
                  ....*....|....*....|....*.
gi 2462519910  85 FKQECK---IKYSERVYEACMEAFDS 107
Cdd:PHA02239   77 IMENVDrlsIYDIEWLSRYCIETLNS 102
pphA PRK11439
protein-serine/threonine phosphatase;
8-75 2.99e-04

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 42.06  E-value: 2.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462519910   8 ITVCGDIHGQFFDLM-KLFEVGGSPANTRYLFLGDYVDRGYFSIECvlylwvLKILYPSTLFLLRGNHE 75
Cdd:PRK11439   19 IWLVGDIHGCFEQLMrKLRHCRFDPWRDLLISVGDLIDRGPQSLRC------LQLLEEHWVRAVRGNHE 81
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
8-146 1.66e-03

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 39.13  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910   8 ITVCGDIHGQFFDLMKLFE-VGGSPANtRYLFLGDYVDRGYFSIECVLYLWVLKILYpstlflLRGNHEcrhlteyftfk 86
Cdd:COG0622     2 IAVISDTHGNLPALEAVLEdLEREGVD-LIVHLGDLVGYGPDPPEVLDLLRELPIVA------VRGNHD----------- 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462519910  87 qeckikyservyEACMEAFDSLPLAALL---NQQFLCVHGGLSPEIHTLDDIRRLDR-FKEPPA 146
Cdd:COG0622    64 ------------GAVLRGLRSLPETLRLeleGVRILLVHGSPNEYLLPDTPAERLRAlAAEGDA 115
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 10-140 2.54e-03

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 39.30  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  10 VCGDIHGQFFDLMKLFEVGG---------SPANTRYLFLGDYVDRGYFSIECVLYLWVL----KILYpstlflLRGNHeC 76
Cdd:PRK13625    5 IIGDIHGCYQEFQALTEKLGynwssglpvHPDQRKLAFVGDLTDRGPHSLRMIEIVWELvekkAAYY------VPGNH-C 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519910  77 RHLTEYF------------TFKQECK---IKYSERVYEACMEAFDSLPLAALL-NQQFLCVHGGLSPeihtlDDIRRLDR 140
Cdd:PRK13625   78 NKLYRFFlgrnvtiahgleTTVAEYEalpSHKQNMIKEKFITLYEQAPLYHILdEGRLVVAHAGIRQ-----DYIGRQDK 152
 
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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