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Conserved domains on  [gi|1091704803|emb|SCV04839|]
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LAMI_0H19790g1_1 [Lachancea mirantina]

Protein Classification

serine/threonine-protein phosphatase( domain architecture ID 10164812)

serine/threonine-protein phosphatase catalyzes the dephosphorylation of phosphoserine and phosphothreonine of specific target phosphoproteins; may be the catalytic subunit of a heterotrimeric enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 7-291 0e+00

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: 556.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   7 DHWLEKIKKCQSLTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTSGGFPDQiNYIFLGDYVDR 86
Cdd:cd07415     3 DQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDT-NYLFLGDYVDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  87 GYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYGSTTVWKYCCQVFDFLTLAAIIDGKILCVHGG 166
Cdd:cd07415    82 GYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 167 LSPEIRMLDQIRVLSRAQEVPHEGGFSDLLWSDPDNVEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFK 246
Cdd:cd07415   162 LSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQ 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1091704803 247 YHFSEKdVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVP 291
Cdd:cd07415   242 WMFNNK-LVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
 
Name Accession Description Interval E-value
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 7-291 0e+00

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: 556.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   7 DHWLEKIKKCQSLTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTSGGFPDQiNYIFLGDYVDR 86
Cdd:cd07415     3 DQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDT-NYLFLGDYVDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  87 GYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYGSTTVWKYCCQVFDFLTLAAIIDGKILCVHGG 166
Cdd:cd07415    82 GYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 167 LSPEIRMLDQIRVLSRAQEVPHEGGFSDLLWSDPDNVEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFK 246
Cdd:cd07415   162 LSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQ 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1091704803 247 YHFSEKdVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVP 291
Cdd:cd07415   242 WMFNNK-LVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 7-292 4.43e-162

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 453.50  E-value: 4.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   7 DHWLEKIKKCQSLTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTSGGFPDQiNYIFLGDYVDR 86
Cdd:PTZ00239    4 DRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNA-NYIFIGDFVDR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  87 GYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYGSTTVWKYCCQVFDFLTLAAIIDGKILCVHGG 166
Cdd:PTZ00239   83 GYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 167 LSPEIRMLDQIRVLSRAQEVPHEGGFSDLLWSDPDNVEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFK 246
Cdd:PTZ00239  163 LSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYK 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1091704803 247 YHFSEKDVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVPD 292
Cdd:PTZ00239  243 YWFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPE 288
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 19-291 1.32e-128

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: 367.31  E-value: 1.32e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   19 LTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTSGGFPDQiNYIFLGDYVDRGYYSLETFTLLM 98
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPET-NYVFLGDYVDRGPFSIEVILLLF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   99 CLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYGStTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEIRMLDQIR 178
Cdd:smart00156  80 ALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGE-RIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  179 VLSRAQEVPHEGGFSDLLWSDPDN-VEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFKYhFSEKDVVTV 257
Cdd:smart00156 159 KLKRPQEPPDDGLLIDLLWSDPDQpVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEF-FADGKLVTI 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1091704803  258 WSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVP 291
Cdd:smart00156 238 FSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 47-156 7.30e-19

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: 80.34  E-value: 7.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  47 PVTVCGDIH--GQFHDLLELFRtsGGFPDQINYIFL--GDYVDRGYYSlETFTLLMCLKVKYpSRLTLVRGNHESRqitq 122
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLK--KLLEEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD---- 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1091704803 123 vygfYEECLNKYGSTT----VWKYCCQVFDFLTLAAII 156
Cdd:pfam00149  74 ----YGECLRLYPYLGllarPWKRFLEVFNFLPLAGIL 107
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
50-166 3.19e-06

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 46.83  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  50 VCGDIHGQFHDL---LELFRTSGgfPDQInyIFLGDYVDRGYYSLETFTLLMCLKVKYpsrltlVRGNHEsrqitqvyGF 126
Cdd:COG0622     4 VISDTHGNLPALeavLEDLEREG--VDLI--VHLGDLVGYGPDPPEVLDLLRELPIVA------VRGNHD--------GA 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1091704803 127 YEECLNKYGSTtvwkyccQVFDfltlaaIIDGKILCVHGG 166
Cdd:COG0622    66 VLRGLRSLPET-------LRLE------LEGVRILLVHGS 92
 
Name Accession Description Interval E-value
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 7-291 0e+00

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: 556.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   7 DHWLEKIKKCQSLTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTSGGFPDQiNYIFLGDYVDR 86
Cdd:cd07415     3 DQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDT-NYLFLGDYVDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  87 GYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYGSTTVWKYCCQVFDFLTLAAIIDGKILCVHGG 166
Cdd:cd07415    82 GYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 167 LSPEIRMLDQIRVLSRAQEVPHEGGFSDLLWSDPDNVEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFK 246
Cdd:cd07415   162 LSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQ 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1091704803 247 YHFSEKdVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVP 291
Cdd:cd07415   242 WMFNNK-LVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 7-292 4.43e-162

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 453.50  E-value: 4.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   7 DHWLEKIKKCQSLTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTSGGFPDQiNYIFLGDYVDR 86
Cdd:PTZ00239    4 DRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNA-NYIFIGDFVDR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  87 GYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYGSTTVWKYCCQVFDFLTLAAIIDGKILCVHGG 166
Cdd:PTZ00239   83 GYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 167 LSPEIRMLDQIRVLSRAQEVPHEGGFSDLLWSDPDNVEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFK 246
Cdd:PTZ00239  163 LSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYK 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1091704803 247 YHFSEKDVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVPD 292
Cdd:PTZ00239  243 YWFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPE 288
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 19-291 1.32e-128

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: 367.31  E-value: 1.32e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   19 LTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTSGGFPDQiNYIFLGDYVDRGYYSLETFTLLM 98
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPET-NYVFLGDYVDRGPFSIEVILLLF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   99 CLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYGStTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEIRMLDQIR 178
Cdd:smart00156  80 ALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGE-RIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  179 VLSRAQEVPHEGGFSDLLWSDPDN-VEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFKYhFSEKDVVTV 257
Cdd:smart00156 159 KLKRPQEPPDDGLLIDLLWSDPDQpVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEF-FADGKLVTI 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1091704803  258 WSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVP 291
Cdd:smart00156 238 FSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 12-286 2.72e-108

PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 (protein phosphatase type 1) is a serine/threonine phosphatase that regulates many cellular processes including: cell-cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling, through its interaction with at least 180 known targeting proteins. PP1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Also included here are the PPKL (PP1 and kelch-like) enzymes including the PPQ, PPZ1, and PPZ2 fungal phosphatases. These PPKLs have a large N-terminal kelch repeat in addition to a C-terminal phosphoesterase domain. The PPP (phosphoprotein phosphatase) family, to which PP1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 316.59  E-value: 2.72e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  12 KIKKCQSLTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFrTSGGFPDQINYIFLGDYVDRGYYSL 91
Cdd:cd07414    16 RPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLF-EYGGFPPESNYLFLGDYVDRGKQSL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  92 ETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYgSTTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEI 171
Cdd:cd07414    95 ETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 172 RMLDQIRVLSRAQEVPHEGGFSDLLWSDPD-NVEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFKYhFS 250
Cdd:cd07414   174 QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDkDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEF-FA 252

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1091704803 251 EKDVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKI 286
Cdd:cd07414   253 KRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQI 288
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 49-276 2.15e-92

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: 273.86  E-value: 2.15e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  49 TVCGDIHGQFHDLLELFRTsGGFPDQINYIFLGDYVDRGYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYE 128
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEK-LGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 129 ECLNK---YGSTTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEIRMLDQIRvLSRAQEVPHEGGFSDLLWSDPDN-VE 204
Cdd:cd00144    80 ERTLRclrKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIR-NIRPIENPDDQLVEDLLWSDPDEsVG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091704803 205 AWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFKYHFSEKdVVTVWSAPNYCYRCGNVASVMKV 276
Cdd:cd00144   159 DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGK-LITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 19-294 6.03e-92

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: 275.34  E-value: 6.03e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  19 LTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTsGGFPDQINYIFLGDYVDRGYYSLETFTLLM 98
Cdd:cd07416    16 LSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEV-GGSPANTRYLFLGDYVDRGYFSIECVLYLW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  99 CLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYgSTTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEIRMLDQIR 178
Cdd:cd07416    95 ALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 179 VLSRAQEVPHEGGFSDLLWSDPdnVEAWQVSP----------RGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFKYH 248
Cdd:cd07416   174 KLDRFREPPSYGPMCDLLWSDP--LEDFGNEKtqehfvhntvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMY 251

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1091704803 249 FSEKD-----VVTVWSAPNYCYRCGNVASVMKVDEDLEpTFKIFSAVPDDY 294
Cdd:cd07416   252 RKSQTtgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM-NIRQFNCSPHPY 301
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 18-287 3.10e-86

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 261.52  E-value: 3.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  18 SLTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTsGGFPDQINYIFLGDYVDRGYYSLETFTLL 97
Cdd:PTZ00480   31 NLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEY-GGYPPESNYLFLGDYVDRGKQSLETICLL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  98 MCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYgSTTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEIRMLDQI 177
Cdd:PTZ00480  110 LAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-TIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 178 RVLSRAQEVPHEGGFSDLLWSDPD-NVEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFKYhFSEKDVVT 256
Cdd:PTZ00480  189 RRIMRPTDVPDTGLLCDLLWSDPDkDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEF-FSKRQLVT 267

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1091704803 257 VWSAPNYCYRCGNVASVMKVDEDLEPTFKIF 287
Cdd:PTZ00480  268 LFSAPNYCGEFDNAGSMMTIDESLMCSFQIL 298
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 31-291 8.95e-78

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: 239.47  E-value: 8.95e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  31 VKELLMEESNIQPVQTP----VTVCGDIHGQFHDLLELFRTSGgFPDQIN-YIFLGDYVDRGYYSLETFTLLMCLKVKYP 105
Cdd:cd07417    41 VKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNG-LPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLYP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 106 SRLTLVRGNHESRQITQVYGFYEECLNKYGSTTVwKYCCQVFDFLTLAAIIDGKILCVHGGL-SPEIRMLDQIRVLSRAQ 184
Cdd:cd07417   120 NHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMF-NLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 185 EVPHEGGFSDLLWSDPDNVEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFKYHFSEKdVVTVWSAPNYC 264
Cdd:cd07417   199 QPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGK-CITVFSAPNYC 277

                         250       260
                  ....*....|....*....|....*...
gi 1091704803 265 YRCGNVASVMKVDE-DLEPTFKIFSAVP 291
Cdd:cd07417   278 DQMGNKGAFIRFKGsDLKPKFTQFEAVP 305
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 19-290 3.80e-76

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 234.80  E-value: 3.80e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  19 LTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTSGgFPDQINYIFLGDYVDRGYYSLETFTLLM 98
Cdd:PTZ00244   25 IREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCG-FPPYSNYLFLGDYVDRGKHSVETITLQF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  99 CLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYgSTTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEIRMLDQIR 178
Cdd:PTZ00244  104 CYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRY-NIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 179 VLSRAQEVPHEGGFSDLLWSDPDN-VEAWQVSPRGAGWLFGSKVAREFNHVNGLSLIARAHQLVMEGFKYhFSEKDVVTV 257
Cdd:PTZ00244  183 EIERPCDVPDRGILCDLLWADPEDeVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGF-FASRQLVTV 261

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1091704803 258 WSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAV 290
Cdd:PTZ00244  262 FSAPNYCGEFDNDAAVMNIDDKLQCSFLIIPAR 294
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 6-288 6.99e-76

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 234.64  E-value: 6.99e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803   6 PDHWLEKIKKCQSLTEAEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELF-------RTSGGFPDQINYI 78
Cdd:cd07419     8 PRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFdeygspvTEEAGDIEYIDYL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  79 FLGDYVDRGYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYGS-----TTVWKYCCQVFDFLTLA 153
Cdd:cd07419    88 FLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdirdgDSVWQRINRLFNWLPLA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 154 AIIDGKILCVHGGLSPEIRMLDQIRVLSRAqeVPHEGG---FSDLLWSDP---DNVEAWQ---VSPRGAGWL--FGSKVA 222
Cdd:cd07419   168 ALIEDKIICVHGGIGRSINHIHQIENLKRP--ITMEAGspvVMDLLWSDPtenDSVLGLRpnaIDPRGTGLIvkFGPDRV 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091704803 223 REFNHVNGLSLIARAHQLVMEGFKyHFSEKDVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKIFS 288
Cdd:cd07419   246 MEFLEENDLQMIIRAHECVMDGFE-RFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIH 310
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 10-284 1.33e-48

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 164.12  E-value: 1.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  10 LEKIKKCQSLTEAEMKQLCEMVKELLMEESNIQPVQT----PVTVCGDIHGQFHDLLELFRTSGgFPDQIN-YIFLGDYV 84
Cdd:cd07420    11 IEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNG-LPSPENpYVFNGDFV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  85 DRGYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGFYEECLNKYG--STTVWKYCCQVFDFLTLAAIIDGKILC 162
Cdd:cd07420    90 DRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKdhGKKILRLLEDVFSWLPLATIIDNKVLV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 163 VHGGLSpEIRMLDQIRVLSRAQEVPHEGGFS---DLLWSDPDNVEA-WQVSPRGAGWLFGSKVAREFNHVNGLSLIARAH 238
Cdd:cd07420   170 VHGGIS-DSTDLDLLDKIDRHKYVSTKTEWQqvvDILWSDPKATKGcKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSH 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1091704803 239 QLVMEGFKYHFSEKdVVTVWSAPNYcYRCG-NVASVMKVDEDLEPTF 284
Cdd:cd07420   249 ECKPEGYEFCHNNK-VITIFSASNY-YEEGsNRGAYVKLGPQLTPHF 293
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 48-263 1.41e-47

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: 163.43  E-value: 1.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  48 VTVCGDIHGQFHDLLELFRTSGgFPDQIN-YIFLGDYVDRGYYSLETFTLLMCLKVKYPSRLTLVRGNHESRQITQVYGF 126
Cdd:cd07418    68 VVVVGDVHGQLHDVLFLLEDAG-FPDQNRfYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGF 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 127 YEECLNKYGST--TVWKYCCQVFDFLTLAAIIDGKILCVHGGL---------------------------SPEIRMLDQI 177
Cdd:cd07418   147 EQEVLTKYGDKgkHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknrrvlllepeseSLKLGTLDDL 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803 178 RVLSRAQEVPHEGGFS----DLLWSDPD-------NVEawqvspRGAGWLFGSKVAREFNHVNGLSLIARAHQ------- 239
Cdd:cd07418   227 MKARRSVLDPPGEGSNlipgDVLWSDPSltpglspNKQ------RGIGLLWGPDCTEEFLEKNNLKLIIRSHEgpdarek 300

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1091704803 240 -----LVMEGF--KYHFSEKDVVTVWSAPNY 263
Cdd:cd07418   301 rpglaGMNKGYtvDHDVESGKLITLFSAPDY 331
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 47-156 7.30e-19

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: 80.34  E-value: 7.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  47 PVTVCGDIH--GQFHDLLELFRtsGGFPDQINYIFL--GDYVDRGYYSlETFTLLMCLKVKYpSRLTLVRGNHESRqitq 122
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLK--KLLEEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD---- 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1091704803 123 vygfYEECLNKYGSTT----VWKYCCQVFDFLTLAAII 156
Cdd:pfam00149  74 ----YGECLRLYPYLGllarPWKRFLEVFNFLPLAGIL 107
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
50-166 3.19e-06

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 46.83  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  50 VCGDIHGQFHDL---LELFRTSGgfPDQInyIFLGDYVDRGYYSLETFTLLMCLKVKYpsrltlVRGNHEsrqitqvyGF 126
Cdd:COG0622     4 VISDTHGNLPALeavLEDLEREG--VDLI--VHLGDLVGYGPDPPEVLDLLRELPIVA------VRGNHD--------GA 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1091704803 127 YEECLNKYGSTtvwkyccQVFDfltlaaIIDGKILCVHGG 166
Cdd:COG0622    66 VLRGLRSLPET-------LRLE------LEGVRILLVHGS 92
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 52-116 3.69e-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: 47.12  E-value: 3.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091704803  52 GDIHGQFHDLLELFRTSG-GFPDQINY--------IFLGDYVDRGYYSLETFTLLMCLkVKYPSRLtLVRGNHE 116
Cdd:cd07423     4 GDVHGCYDELVELLEKLGyQKKEEGLYvhpegrklVFLGDLVDRGPDSIDVLRLVMNM-VKAGKAL-YVPGNHC 75
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 52-169 2.66e-05

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


Pssm-ID: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 44.21  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  52 GDIHGQFHDLLELFRTSGGFPDQINYIF-------LGDYVDRGYYSLETFTLLMCLK---VKYPSRLTLVRGNHESRQIT 121
Cdd:cd07425     4 GDLHGDLDRLRTILKLAGVIDSNDRWIGgdtvvvqTGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELMNLC 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091704803 122 -----------QVYGFYEECLNKYGS--TTVWKYccqVFDFLTLAAIIDgkILCVHGGLSP 169
Cdd:cd07425    84 gdfryvhprglNEFGGVAKRRYALLSdgGYIGRY---LRTHPVVLVVND--ILFVHGGLGP 139
pphA PRK11439
protein-serine/threonine phosphatase;
48-116 7.18e-05

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 43.21  E-value: 7.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091704803  48 VTVCGDIHGQFHDLLELFRTSGGFPDQINYIFLGDYVDRGYYSLETFTLLMClkvkypSRLTLVRGNHE 116
Cdd:PRK11439   19 IWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEE------HWVRAVRGNHE 81
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 50-116 1.55e-04

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


Pssm-ID: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 41.92  E-value: 1.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091704803  50 VCGDIHGQFHDLLELFRTSGGFPDQINYIFLGDYVDRGYYSLETFTLLmclkvKYPsRLTLVRGNHE 116
Cdd:cd07424     5 VVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELL-----KQP-WFHAVQGNHE 65
PHA02239 PHA02239
putative protein phosphatase
 48-150 1.75e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 42.29  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091704803  48 VTVCGDIHGQFHDLLELFrtsggfpDQIN--------YIFLGDYVDRGYYSLETFTLLMCLKVKYPSRLTLVrGNHES-- 117
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIM-------DKINnerkpeetIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHDDef 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1091704803 118 -RQITQV--YGFYE---------ECLNKYGSTTVWKYCCQVFDFL 150
Cdd:PHA02239   75 yNIMENVdrLSIYDiewlsryciETLNSYGVSTVTLKYSSVEENL 119
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 52-116 1.79e-04

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: 42.15  E-value: 1.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091704803  52 GDIHGQFHDLLELFrtsggfpDQINY-------IFLGDYVDRGYYSLETFTLLMCLKvkypSRLTLVRGNHE 116
Cdd:cd07422     5 GDIQGCYDELQRLL-------EKINFdpakdrlWLVGDLVNRGPDSLETLRFVKSLG----DSAVVVLGNHD 65
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 48-116 2.04e-04

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


Pssm-ID: 163664  Cd Length: 304  Bit Score: 42.49  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091704803  48 VTVC-GDIHGQFHDLLELFRT--SGGFPDQIN---YIFLGDYVDRGYYSLETFTLLMCLKVKYPS-RLTLVRGNHE 116
Cdd:cd07421     3 VVICvGDIHGYISKLNNLWLNlqSALGPSDFAsalVIFLGDYCDRGPETRKVIDFLISLPEKHPKqRHVFLCGNHD 78
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 50-116 3.16e-04

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 39.94  E-value: 3.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091704803  50 VCGDIHGQFHDLLELFRT----SGGfPDQInyIFLGDYVDRGYYSLETFtLLMCLKVKYPSRLTLVRGNHE 116
Cdd:cd00838     2 VISDIHGNLEALEAVLEAalakAEK-PDLV--ICLGDLVDYGPDPEEVE-LKALRLLLAGIPVYVVPGNHD 68
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
52-116 8.08e-04

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 8.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091704803  52 GDIHGQFHDLLELFrtsggfpDQINY-------IFLGDYVDRGYYSLETFTLLMCLKvkypSRLTLVRGNHE 116
Cdd:PRK00166    7 GDIQGCYDELQRLL-------EKIDFdpakdtlWLVGDLVNRGPDSLEVLRFVKSLG----DSAVTVLGNHD 67
PRK09968 PRK09968
protein-serine/threonine phosphatase;
50-117 1.11e-03

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 39.49  E-value: 1.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091704803  50 VCGDIHGQFHDLLELFRTSGGFPDQINYIFLGDYVDRGYYSLETFTLLmclkvkYPSRLTLVRGNHES 117
Cdd:PRK09968   19 VVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLL------NQPWFISVKGNHEA 80
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 12-64 6.41e-03

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


Pssm-ID: 465300 [Multi-domain]  Cd Length: 48  Bit Score: 34.00  E-value: 6.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1091704803  12 KIKKCQsLTEAEMKQLCEMVKELLMEesniQPVqtpvtvcgdihgqfhdLLEL 64
Cdd:pfam16891  16 GGKQVQ-LSEAEIRALCRKAREIFLS----QPM----------------LLEL 47
 
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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