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Conserved domains on  [gi|568987032|ref|XP_006518770|]
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serine/threonine-protein phosphatase 2B catalytic subunit beta isoform isoform X1 [Mus musculus]

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

CATH:  3.60.21.10
EC:  3.1.3.16
Gene Ontology:  GO:0097720|GO:0033192|GO:0005509|GO:0005516|GO:0004722|GO:0046872|GO:0006470
PubMed:  30401537|9646865|25837850|29925267|18488168

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 ...
 50-354 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: 682.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  50 PRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV 129
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 130 DRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHG 209
Cdd:cd07416   81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 210 GLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRA 289
Cdd:cd07416  161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987032 290 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 354
Cdd:cd07416  241 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 305
 
Name Accession Description Interval E-value
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 50-354 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: 682.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  50 PRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV 129
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 130 DRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHG 209
Cdd:cd07416   81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 210 GLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRA 289
Cdd:cd07416  161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987032 290 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 354
Cdd:cd07416  241 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 67-338 8.01e-139

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: 401.98  E-value: 8.01e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032    67 EEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLK 146
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032   147 ILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDR 226
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032   227 FKEPPAFGPMCDLLWSDPsedfgnEKSQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQtt 306
Cdd:smart00156 163 PQEPPDDGLLIDLLWSDP------DQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK-- 233

                          250       260       270
                   ....*....|....*....|....*....|..
gi 568987032   307 gfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 338
Cdd:smart00156 234 ----LVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 60-347 6.78e-75

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 239.33  E-value: 6.78e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  60 VKEGRVDEEIALRIINEGAA-ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEC 138
Cdd:PTZ00239  10 LLNGGCLPERDLKLICERAKeIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVET 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 139 VLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHT 217
Cdd:PTZ00239  90 MEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 218 LDDIRRLDRFKEPPAFGPMCDLLWSDPSEdfgneksQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGY 297
Cdd:PTZ00239 170 IDQIRTIDRKIEIPHEGPFCDLMWSDPEE-------VEYWAVNS-RGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568987032 298 RMYRKSQttgfpSLITIFSAPNYLDVYNNKAAVLKYENNV-MNIRQFNCSP 347
Cdd:PTZ00239 242 KYWFPDQ-----NLVTVWSAPNYCYRCGNIASILCLDENLqQTWKTFKEVP 287
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 93-200 5.65e-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: 74.17  E-value: 5.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032   93 PITVCGDIH--GQFFDLMKLFEVGGSPANtRYLFL--GDYVDRGYFSiECVLYLWVLKILYpSTLFLLRGNHECRHLtEY 168
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGK-PDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYG-EC 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568987032  169 FTFKQEckIKYSERVYEACMEAFDSLPLAALL 200
Cdd:pfam00149  78 LRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
94-232 4.31e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 38.36  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  94 ITVCGDIHGQFFDLMKLFE-VGGSPANtRYLFLGDYVDRGYFSIECVLYLWVLKILYpstlflLRGNHEcrhlteyftfk 172
Cdd:COG0622    2 IAVISDTHGNLPALEAVLEdLEREGVD-LIVHLGDLVGYGPDPPEVLDLLRELPIVA------VRGNHD----------- 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987032 173 qeckikyservyEACMEAFDSLPLAALL---NQQFLCVHGGLSPEIHTLDDIRRLDR-FKEPPA 232
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 ...
 50-354 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: 682.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  50 PRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV 129
Cdd:cd07416    1 PRVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 130 DRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHG 209
Cdd:cd07416   81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 210 GLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRA 289
Cdd:cd07416  161 GLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987032 290 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 354
Cdd:cd07416  241 HEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPN 305
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 67-338 8.01e-139

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: 401.98  E-value: 8.01e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032    67 EEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLK 146
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032   147 ILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDR 226
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032   227 FKEPPAFGPMCDLLWSDPsedfgnEKSQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQtt 306
Cdd:smart00156 163 PQEPPDDGLLIDLLWSDP------DQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK-- 233

                          250       260       270
                   ....*....|....*....|....*....|..
gi 568987032   307 gfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 338
Cdd:smart00156 234 ----LVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 80-347 3.41e-109

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: 326.85  E-value: 3.41e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  80 ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGN 159
Cdd:cd07415   30 ILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 160 HECRHLTEYFTFKQECKIKY-SERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCD 238
Cdd:cd07415  110 HESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCD 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 239 LLWSDPSEDFGNEKSQehfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAP 318
Cdd:cd07415  190 LLWSDPDDREGWGISP--------RGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNK------LVTVWSAP 255

                        250       260       270
                 ....*....|....*....|....*....|
gi 568987032 319 NYLDVYNNKAAVLKY-ENNVMNIRQFNCSP 347
Cdd:cd07415  256 NYCYRCGNVASILELdEHLNRSFKQFEAAP 285
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 52-349 2.90e-91

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: 282.22  E-value: 2.90e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  52 VDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAP----ITVCGDIHGQFFDLMKLFEVGGSPANT-RYLFLG 126
Cdd:cd07417   16 VKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETnPYLFNG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 127 DYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLC 206
Cdd:cd07417   96 DFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 207 VHGGL-SPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQehfshntvRGCSYFYNyPAVCE-FLQNNNLL 284
Cdd:cd07417  176 VHGGLfSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSK--------RGVGCQFG-PDVTKrFLEENNLD 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987032 285 SIIRAHEAQDAGYRMYRKSqttgfpSLITIFSAPNYLDVYNNKAAVLKYENNVMNIR--QFNCSPHP 349
Cdd:cd07417  247 YIIRSHEVKDEGYEVEHDG------KCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKftQFEAVPHP 307
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 95-333 5.61e-89

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: 273.09  E-value: 5.61e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  95 TVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQE 174
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 175 ----CKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLdRFKEPPAFGPMCDLLWSDPSEDFGn 250
Cdd:cd00144   81 rtlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVG- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 251 eksqehFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRksqttgFPSLITIFSAPNYLDVYNNKAAV 330
Cdd:cd00144  159 ------DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLH------GGKLITIFSAPNYCGKGGNKLAA 226


                 ...
gi 568987032 331 LKY 333
Cdd:cd00144  227 LVV 229
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 80-338 4.39e-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: 259.96  E-value: 4.39e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  80 ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGN 159
Cdd:cd07414   38 IFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGN 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 160 HECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDL 239
Cdd:cd07414  118 HECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDL 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 240 LWSDPSEDFGNeksqehFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPN 319
Cdd:cd07414  198 LWSDPDKDVQG------WGEND-RGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQ------LVTLFSAPN 264

                        250
                 ....*....|....*....
gi 568987032 320 YLDVYNNKAAVLKYENNVM 338
Cdd:cd07414  265 YCGEFDNAGAMMSVDETLM 283
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 60-347 6.78e-75

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 239.33  E-value: 6.78e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  60 VKEGRVDEEIALRIINEGAA-ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIEC 138
Cdd:PTZ00239  10 LLNGGCLPERDLKLICERAKeIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVET 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 139 VLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHT 217
Cdd:PTZ00239  90 MEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 218 LDDIRRLDRFKEPPAFGPMCDLLWSDPSEdfgneksQEHFSHNTvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGY 297
Cdd:PTZ00239 170 IDQIRTIDRKIEIPHEGPFCDLMWSDPEE-------VEYWAVNS-RGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568987032 298 RMYRKSQttgfpSLITIFSAPNYLDVYNNKAAVLKYENNV-MNIRQFNCSP 347
Cdd:PTZ00239 242 KYWFPDQ-----NLVTVWSAPNYCYRCGNIASILCLDENLqQTWKTFKEVP 287
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 80-338 1.24e-72

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 234.17  E-value: 1.24e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  80 ILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGN 159
Cdd:PTZ00480  47 IFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGN 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 160 HECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDL 239
Cdd:PTZ00480 127 HECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDL 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 240 LWSDPSEDFGNEKSQEhfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPN 319
Cdd:PTZ00480 207 LWSDPDKDVQGWADNE-------RGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQ------LVTLFSAPN 273

                        250
                 ....*....|....*....
gi 568987032 320 YLDVYNNKAAVLKYENNVM 338
Cdd:PTZ00480 274 YCGEFDNAGSMMTIDESLM 292
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 65-337 7.06e-64

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 210.15  E-value: 7.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  65 VDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWV 144
Cdd:PTZ00244  25 IREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFC 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 145 LKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRL 224
Cdd:PTZ00244 105 YKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 225 DRFKEPPAFGPMCDLLWSDPSEDF-GNEKSQehfshntvRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKS 303
Cdd:PTZ00244 185 ERPCDVPDRGILCDLLWADPEDEVrGFLESD--------RGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASR 256

                        250       260       270
                 ....*....|....*....|....*....|....
gi 568987032 304 QttgfpsLITIFSAPNYLDVYNNKAAVLKYENNV 337
Cdd:PTZ00244 257 Q------LVTVFSAPNYCGEFDNDAAVMNIDDKL 284
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 64-336 1.99e-62

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: 206.91  E-value: 1.99e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  64 RVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTR--------YLFLGDYVDRGYFS 135
Cdd:cd07419   20 FFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagdieyidYLFLGDYVDRGSHS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 136 IECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSER------VYEACMEAFDSLPLAALLNQQFLCVHG 209
Cdd:cd07419  100 LETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirdgdsVWQRINRLFNWLPLAALIEDKIICVHG 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 210 GLSPEIHTLDDIRRLDRFKEPPAFGP-MCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIR 288
Cdd:cd07419  180 GIGRSINHIHQIENLKRPITMEAGSPvVMDLLWSDPTENDSVLGLRPNAIDPRGTGLIVKFGPDRVMEFLEENDLQMIIR 259

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568987032 289 AHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENN 336
Cdd:cd07419  260 AHECVMDGFERFAQGH------LITLFSATNYCGTAGNAGAILVLGRD 301
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 80-349 2.47e-56

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: 193.09  E-value: 2.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  80 ILRREKTMIEVE----APITVCGDIHGQFFDLMKLFEVGGSPANTR-YLFLGDYVDRGYFSIECVLYLWVLKILYPSTLF 154
Cdd:cd07418   50 ILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRfYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 155 LLRGNHECRHLTEYFTFKQECKIKYSER---VYEACMEAFDSLPLAALLNQQFLCVHGGL-------------------- 211
Cdd:cd07418  130 LLRGNHESKFCTSMYGFEQEVLTKYGDKgkhVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknrrvl 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 212 -------SPEIHTLDDIRRLDR-FKEPPAFGPMC---DLLWSDPSEDFGneksqehFSHNTVRGCSYFYNYPAVCEFLQN 280
Cdd:cd07418  210 llepeseSLKLGTLDDLMKARRsVLDPPGEGSNLipgDVLWSDPSLTPG-------LSPNKQRGIGLLWGPDCTEEFLEK 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 281 NNLLSIIRAHEAQDAGYRM---------YRKSQTTGFPSLITIFSAPNYL------DVYNNKAAVLkyennVMNIRQFNC 345
Cdd:cd07418  283 NNLKLIIRSHEGPDAREKRpglagmnkgYTVDHDVESGKLITLFSAPDYPqfqateERYNNKGAYI-----ILQPPDFSD 357


                 ....
gi 568987032 346 SPHP 349
Cdd:cd07418  358 PQFH 361
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 71-338 2.04e-46

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: 164.12  E-value: 2.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  71 LRIINEGAAILR------REKTMIEVEapITVCGDIHGQFFDLMKLFEVGGSPANTR-YLFLGDYVDRGYFSIECVLYLW 143
Cdd:cd07420   26 LLILREARKSLKqlpnisRVSTSYSKE--VTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 144 VLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKY---SERVYEACMEAFDSLPLAALLNQQFLCVHGGLSpEIHTLDD 220
Cdd:cd07420  104 AFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYkdhGKKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-DSTDLDL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 221 IRRLDRFK---EPPAFGPMCDLLWSDPsedfgneKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGY 297
Cdd:cd07420  183 LDKIDRHKyvsTKTEWQQVVDILWSDP-------KATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGY 255

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568987032 298 RMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 338
Cdd:cd07420  256 EFCHNNK------VITIFSASNYYEEGSNRGAYVKLGPQLT 290
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 93-200 5.65e-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: 74.17  E-value: 5.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032   93 PITVCGDIH--GQFFDLMKLFEVGGSPANtRYLFL--GDYVDRGYFSiECVLYLWVLKILYpSTLFLLRGNHECRHLtEY 168
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGK-PDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYG-EC 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568987032  169 FTFKQEckIKYSERVYEACMEAFDSLPLAALL 200
Cdd:pfam00149  78 LRLYPY--LGLLARPWKRFLEVFNFLPLAGIL 107
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 94-161 1.03e-06

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: 1.03e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987032  94 ITVCGDIHGQFFDLM-KLFEVGGSPANTRYLFLGDYVDRGYFSIECvlylwvLKILYPSTLFLLRGNHE 161
Cdd:cd07424    3 DFVVGDIHGHFQRLQrALDAVGFDPARDRLISVGDLVDRGPESLEV------LELLKQPWFHAVQGNHE 65
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 98-216 1.09e-05

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: 46.74  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  98 GDIHGQFFDLMKLFEVGG----------SPANTRYLFLGDYVDRGYFSIECVLYlwVLKILYPSTLFLLRGNHE---CRH 164
Cdd:cd07423    4 GDVHGCYDELVELLEKLGyqkkeeglyvHPEGRKLVFLGDLVDRGPDSIDVLRL--VMNMVKAGKALYVPGNHCnklYRY 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987032 165 L---------------TEYFTFKQECKIKYSERVyeacMEAFDSLPLAALLNQ-QFLCVHGGLSPEIH 216
Cdd:cd07423   82 LkgrnvqlahglettvEELEALSKEERPEFRERF----AEFLESLPSHLVLDGgRLVVAHAGIKEEMI 145
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 98-214 6.35e-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: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  98 GDIHGQFFDLMKLFE-VGGSPANTRYLFLGDYVDRGYFSIECVLYlwvLKILYPSTLFLLrGNHECRHLTEYFTFKqecK 176
Cdd:cd07422    5 GDIQGCYDELQRLLEkINFDPAKDRLWLVGDLVNRGPDSLETLRF---VKSLGDSAVVVL-GNHDLHLLAVAAGIK---K 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568987032 177 IKYSERVYEAcMEAFDSLPLAALLNQQ----------FLCVHGGLSPE 214
Cdd:cd07422   78 LKKKDTLDEI-LEAPDRDELLDWLRHQpllhrddelgIVMVHAGIPPQ 124
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 96-161 7.42e-05

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 42.64  E-value: 7.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987032  96 VCGDIHGQFFDLMKLF--EVGGSPANTRYLFLGDYVDRGYFSiECVLYLWVLKILYPSTLFLLRGNHE 161
Cdd:cd00838    2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDP-EEVELKALRLLLAGIPVYVVPGNHD 68
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 98-213 1.72e-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: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  98 GDIHGQFFDLMKLFEVGG-SPANTRYLF-------LGDYVDRGYFSIEcVLYLwvLKILYP------STLFLLRGNHECR 163
Cdd:cd07425    4 GDLHGDLDRLRTILKLAGvIDSNDRWIGgdtvvvqTGDILDRGDDEIE-ILKL--LEKLKRqarkagGKVILLLGNHELM 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987032 164 HL---------TEYFTFKQECKIKYSER---VYEACMeaFDSLPLAALLNqQFLCVHGGLSP 213
Cdd:cd07425   81 NLcgdfryvhpRGLNEFGGVAKRRYALLsdgGYIGRY--LRTHPVVLVVN-DILFVHGGLGP 139
PHA02239 PHA02239
putative protein phosphatase
 94-193 1.79e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 43.06  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  94 ITVCGDIHGQFFDLMKLFEV---GGSPANTrYLFLGDYVDRGYFSIECVLYLWVLkILYPSTLFLLRGNHEcrhlTEYFT 170
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKinnERKPEET-IVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHD----DEFYN 76

                         90       100
                 ....*....|....*....|....*.
gi 568987032 171 FKQECK---IKYSERVYEACMEAFDS 193
Cdd:PHA02239  77 IMENVDrlsIYDIEWLSRYCIETLNS 102
pphA PRK11439
protein-serine/threonine phosphatase;
94-161 3.74e-04

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 42.06  E-value: 3.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987032  94 ITVCGDIHGQFFDLM-KLFEVGGSPANTRYLFLGDYVDRGYFSIECvlylwvLKILYPSTLFLLRGNHE 161
Cdd:PRK11439  19 IWLVGDIHGCFEQLMrKLRHCRFDPWRDLLISVGDLIDRGPQSLRC------LQLLEEHWVRAVRGNHE 81
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
94-232 4.31e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 38.36  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  94 ITVCGDIHGQFFDLMKLFE-VGGSPANtRYLFLGDYVDRGYFSIECVLYLWVLKILYpstlflLRGNHEcrhlteyftfk 172
Cdd:COG0622    2 IAVISDTHGNLPALEAVLEdLEREGVD-LIVHLGDLVGYGPDPPEVLDLLRELPIVA------VRGNHD----------- 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987032 173 qeckikyservyEACMEAFDSLPLAALL---NQQFLCVHGGLSPEIHTLDDIRRLDR-FKEPPA 232
Cdd:COG0622   64 ------------GAVLRGLRSLPETLRLeleGVRILLVHGSPNEYLLPDTPAERLRAlAAEGDA 115
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 96-226 4.60e-03

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 38.92  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032  96 VCGDIHGQFFDLMKLFEVGG---------SPANTRYLFLGDYVDRGYFSIECVLYLWVL----KILYpstlflLRGNHeC 162
Cdd:PRK13625   5 IIGDIHGCYQEFQALTEKLGynwssglpvHPDQRKLAFVGDLTDRGPHSLRMIEIVWELvekkAAYY------VPGNH-C 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987032 163 RHLTEYF------------TFKQECK---IKYSERVYEACMEAFDSLPLAALL-NQQFLCVHGGLSPeihtlDDIRRLDR 226
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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