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Conserved domains on  [gi|183603931|ref|NP_001116841|]
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serine/threonine-protein phosphatase 6 catalytic subunit isoform c [Homo sapiens]

Protein Classification

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

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

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

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 ...
 5-267 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: 505.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   5 DLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVD 62
Cdd:cd07415    1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQfydllelfriggdvpdtnylflGDYVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  63 RGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHG 142
Cdd:cd07415   81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 143 GLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGY 222
Cdd:cd07415  161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 183603931 223 KFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVP 267
Cdd:cd07415  241 QWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
 
Name Accession Description Interval E-value
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 5-267 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: 505.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   5 DLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVD 62
Cdd:cd07415    1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQfydllelfriggdvpdtnylflGDYVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  63 RGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHG 142
Cdd:cd07415   81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 143 GLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGY 222
Cdd:cd07415  161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 183603931 223 KFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVP 267
Cdd:cd07415  241 QWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 4-283 8.04e-156

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 436.55  E-value: 8.04e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   4 LDLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFV 61
Cdd:PTZ00239   1 MDIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQfydlqalfkeggdipnanyifiGDFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  62 DRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVH 141
Cdd:PTZ00239  81 DRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 142 GGLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEG 221
Cdd:PTZ00239 161 GGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEG 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 183603931 222 YKFMF-DEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVPDSERVIPPRTTTPYFL 283
Cdd:PTZ00239 241 YKYWFpDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKNVLPYFL 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 19-256 1.41e-117

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: 338.03  E-value: 1.41e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931    19 LPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVDRGYYSLETFTYLLA 76
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQfddllrlfdkngqppetnyvflGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931    77 LKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGnANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRT 156
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYG-ERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   157 IERNQEIPHKGAFCDLVWSDPED-VDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWS 235
Cdd:smart00156 160 LKRPQEPPDDGLLIDLLWSDPDQpVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFS 239

                          250       260
                   ....*....|....*....|..
gi 183603931   236 APNYCYRCGNIASIM-VFKDVN 256
Cdd:smart00156 240 APNYCDRFGNKAAVLkVDKDLK 261
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 47-133 2.68e-09

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: 53.76  E-value: 2.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   47 PVTVCGDIHGQ-------------------------GDFVDRGYYSlETFTYLLALKAKWpDRITLLRGNHESRqitqvy 101
Cdd:pfam00149   2 RILVIGDLHLPgqlddllellkklleegkpdlvlhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 183603931  102 gfYDECQTKYG----NANAWRYCTKVFDMLTVAALI 133
Cdd:pfam00149  74 --YGECLRLYPylglLARPWKRFLEVFNFLPLAGIL 107
 
Name Accession Description Interval E-value
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 5-267 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: 505.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   5 DLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVD 62
Cdd:cd07415    1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQfydllelfriggdvpdtnylflGDYVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  63 RGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHG 142
Cdd:cd07415   81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 143 GLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGY 222
Cdd:cd07415  161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 183603931 223 KFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVP 267
Cdd:cd07415  241 QWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 4-283 8.04e-156

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 436.55  E-value: 8.04e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   4 LDLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFV 61
Cdd:PTZ00239   1 MDIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQfydlqalfkeggdipnanyifiGDFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  62 DRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVH 141
Cdd:PTZ00239  81 DRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 142 GGLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEG 221
Cdd:PTZ00239 161 GGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEG 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 183603931 222 YKFMF-DEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVPDSERVIPPRTTTPYFL 283
Cdd:PTZ00239 241 YKYWFpDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKNVLPYFL 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 19-256 1.41e-117

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: 338.03  E-value: 1.41e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931    19 LPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVDRGYYSLETFTYLLA 76
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQfddllrlfdkngqppetnyvflGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931    77 LKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGnANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRT 156
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYG-ERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   157 IERNQEIPHKGAFCDLVWSDPED-VDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWS 235
Cdd:smart00156 160 LKRPQEPPDDGLLIDLLWSDPDQpVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFS 239

                          250       260
                   ....*....|....*....|..
gi 183603931   236 APNYCYRCGNIASIM-VFKDVN 256
Cdd:smart00156 240 APNYCDRFGNKAAVLkVDKDLK 261
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 19-250 3.46e-86

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: 259.19  E-value: 3.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  19 LPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVDRGYYSLETFTYLLA 76
Cdd:cd07414   23 LTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQyydllrlfeyggfppesnylflGDYVDRGKQSLETICLLLA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  77 LKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYgNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRT 156
Cdd:cd07414  103 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRR 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 157 IERNQEIPHKGAFCDLVWSDPE-DVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWS 235
Cdd:cd07414  182 IMRPTDVPDQGLLCDLLWSDPDkDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFS 261

                        250
                 ....*....|....*
gi 183603931 236 APNYCYRCGNIASIM 250
Cdd:cd07414  262 APNYCGEFDNAGAMM 276
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 49-252 1.81e-82

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: 247.67  E-value: 1.81e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  49 TVCGDIHGQ----------------------GDFVDRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDE 106
Cdd:cd00144    1 IVVGDIHGCfddllrlleklgfppedkylflGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 107 C---QTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRTIeRNQEIPHKGAFCDLVWSDP-EDVDT 182
Cdd:cd00144   81 RtlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPdESVGD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 183 WAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWSAPNYCYRCGNIASIMVF 252
Cdd:cd00144  160 FESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 19-252 4.92e-73

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: 226.03  E-value: 4.92e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  19 LPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVDRGYYSLETFTYLLA 76
Cdd:cd07416   16 LSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQfydllklfevggspantrylflGDYVDRGYFSIECVLYLWA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  77 LKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYgNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRT 156
Cdd:cd07416   96 LKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRK 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 157 IERNQEIPHKGAFCDLVWSDP-EDVDTWAISP-------RGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDE 228
Cdd:cd07416  175 LDRFREPPSYGPMCDLLWSDPlEDFGNEKTQEhfvhntvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKS 254

                        250       260       270
                 ....*....|....*....|....*....|
gi 183603931 229 K------LVTVWSAPNYCYRCGNIASIMVF 252
Cdd:cd07416  255 QttgfpsLITIFSAPNYLDVYNNKAAVLKY 284
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 19-254 7.76e-73

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 226.46  E-value: 7.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  19 LPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVDRGYYSLETFTYLLA 76
Cdd:PTZ00480  32 LTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQyfdllrlfeyggyppesnylflGDYVDRGKQSLETICLLLA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  77 LKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYgNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRT 156
Cdd:PTZ00480 112 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-TIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRR 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 157 IERNQEIPHKGAFCDLVWSDPE-DVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWS 235
Cdd:PTZ00480 191 IMRPTDVPDTGLLCDLLWSDPDkDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFS 270

                        250
                 ....*....|....*....
gi 183603931 236 APNYCYRCGNIASIMVFKD 254
Cdd:PTZ00480 271 APNYCGEFDNAGSMMTIDE 289
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 30-267 4.60e-70

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: 219.05  E-value: 4.60e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  30 YVCDLLLE--------ESNVQ---PVSTPVTVCGDIHGQ-----------------------GDFVDRGYYSLETFTYLL 75
Cdd:cd07417   33 YAYQILLQvkeilkklPSLVEitiPEGEKITVCGDTHGQfydllnifelnglpsetnpylfnGDFVDRGSFSVEVILTLF 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  76 ALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYgNANAWRYCTKVFDMLTVAALIDEQILCVHGGL-SPDIKTLDQI 154
Cdd:cd07417  113 AFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKY-NEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDI 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 155 RTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVW 234
Cdd:cd07417  192 RKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVF 271

                        250       260       270
                 ....*....|....*....|....*....|....
gi 183603931 235 SAPNYCYRCGNIASIMVFKDVN-TREPKLFRAVP 267
Cdd:cd07417  272 SAPNYCDQMGNKGAFIRFKGSDlKPKFTQFEAVP 305
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 21-254 1.20e-64

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 204.37  E-value: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  21 ENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ----------------------GDFVDRGYYSLETFTYLLALK 78
Cdd:PTZ00244  27 EEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQyydllrifekcgfppysnylflGDYVDRGKHSVETITLQFCYK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  79 AKWPDRITLLRGNHESRQITQVYGFYDECQTKYgNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRTIE 158
Cdd:PTZ00244 107 IVYPENFFLLRGNHECASINKMYGFFDDVKRRY-NIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIE 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 159 RNQEIPHKGAFCDLVWSDPED-VDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWSAP 237
Cdd:PTZ00244 186 RPCDVPDRGILCDLLWADPEDeVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAP 265

                        250
                 ....*....|....*..
gi 183603931 238 NYCYRCGNIASIMVFKD 254
Cdd:PTZ00244 266 NYCGEFDNDAAVMNIDD 282
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 19-262 8.75e-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: 197.66  E-value: 8.75e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  19 LPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQ------------------------------GDFVDRGYYSL 68
Cdd:cd07419   21 FDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQfgdlmrlfdeygspvteeagdieyidylflGDYVDRGSHSL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  69 ETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNA-----NAWRYCTKVFDMLTVAALIDEQILCVHGG 143
Cdd:cd07419  101 ETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirdgdSVWQRINRLFNWLPLAALIEDKIICVHGG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 144 LSPDIKTLDQIRTIERNQEIPHKG-AFCDLVWSDPEDVDTW------AISPRGAGWL--FGAKVTNEFVHINNLKLICRA 214
Cdd:cd07419  181 IGRSINHIHQIENLKRPITMEAGSpVVMDLLWSDPTENDSVlglrpnAIDPRGTGLIvkFGPDRVMEFLEENDLQMIIRA 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 183603931 215 HQLVHEGYKFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKL 262
Cdd:cd07419  261 HECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKL 308
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 30-239 2.67e-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: 157.19  E-value: 2.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  30 YVCDLLLEES-------NVQPVST----PVTVCGDIHGQ-----------------------GDFVDRGYYSLETFTYLL 75
Cdd:cd07420   24 YVLLILREARkslkqlpNISRVSTsyskEVTICGDLHGKlddlllifyknglpspenpyvfnGDFVDRGKRSIEILMILF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  76 ALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYG--NANAWRYCTKVFDMLTVAALIDEQILCVHGGLSpDIKTLDQ 153
Cdd:cd07420  104 AFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKdhGKKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-DSTDLDL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 154 IRTIERNQEIPHKGAF---CDLVWSDPEDVD-TWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEK 229
Cdd:cd07420  183 LDKIDRHKYVSTKTEWqqvVDILWSDPKATKgCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNK 262

                        250
                 ....*....|
gi 183603931 230 LVTVWSAPNY 239
Cdd:cd07420  263 VITIFSASNY 272
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 8-282 3.76e-41

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: 145.71  E-value: 3.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   8 KYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPV----STPVTVCGDIHGQ-----------------------GDF 60
Cdd:cd07418   24 RNLPPSELPSVLPVNVFDSLVLTAHKILHREPNCVRIdvedVCEVVVVGDVHGQlhdvlflledagfpdqnrfyvfnGDY 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  61 VDRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGN--ANAWRYCTKVFDMLTVAALIDEQIL 138
Cdd:cd07418  104 VDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDkgKHVYRKCLGCFEGLPLASIIAGRVY 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 139 CVHGGL---------------------------SPDIKTLDQIRTIERN-QEIPHKGAFC---DLVWSDPEDVDtwAISP 187
Cdd:cd07418  184 TAHGGLfrspslpkrkkqkgknrrvlllepeseSLKLGTLDDLMKARRSvLDPPGEGSNLipgDVLWSDPSLTP--GLSP 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931 188 ---RGAGWLFGAKVTNEFVHINNLKLICRAHQ------------LVHEGYKFMFD---EKLVTVWSAPNYCY------RC 243
Cdd:cd07418  262 nkqRGIGLLWGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYTVDHDvesGKLITLFSAPDYPQfqateeRY 341

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 183603931 244 GNIASIMVFKDVNTREPKLfravPDSERVIPPRTTTPYF 282
Cdd:cd07418  342 NNKGAYIILQPPDFSDPQF----HTFEAVKPRPKANPYY 376
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 47-133 2.68e-09

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: 53.76  E-value: 2.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931   47 PVTVCGDIHGQ-------------------------GDFVDRGYYSlETFTYLLALKAKWpDRITLLRGNHESRqitqvy 101
Cdd:pfam00149   2 RILVIGDLHLPgqlddllellkklleegkpdlvlhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 183603931  102 gfYDECQTKYG----NANAWRYCTKVFDMLTVAALI 133
Cdd:pfam00149  74 --YGECLRLYPylglLARPWKRFLEVFNFLPLAGIL 107
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 58-146 9.62e-03

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: 36.51  E-value: 9.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183603931  58 GDFVDRGYYSLETFTYLLALK---AKWPDRITLLRGNHESRQITQVYGFYD--ECQTKYGNANAWR--------YCTKVF 124
Cdd:cd07425   40 GDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELMNLCGDFRYVHprGLNEFGGVAKRRYallsdggyIGRYLR 119

                         90       100
                 ....*....|....*....|..
gi 183603931 125 DMLTVAALIDeqILCVHGGLSP 146
Cdd:cd07425  120 THPVVLVVND--ILFVHGGLGP 139
 
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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