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Conserved domains on  [gi|18405985|ref|NP_565974|]
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protein phosphatase 2A-3 [Arabidopsis thaliana]

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 ...
 13-297 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: 610.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  13 DLDEQISQLMQCKPLSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVD 92
Cdd:cd07415   1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  93 RGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWKIFTDLFDYFPLTALVESEIFCLHG 172
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 173 GLSPSIETLDNIRNFDRVQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGY 252
Cdd:cd07415 161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 18405985 253 NWAHEQKVVTIFSAPNYCYRCGNMASILEVDDCRNHTFIQFEPAP 297
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 ...
 13-297 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: 610.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  13 DLDEQISQLMQCKPLSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVD 92
Cdd:cd07415   1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  93 RGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWKIFTDLFDYFPLTALVESEIFCLHG 172
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 173 GLSPSIETLDNIRNFDRVQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGY 252
Cdd:cd07415 161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 18405985 253 NWAHEQKVVTIFSAPNYCYRCGNMASILEVDDCRNHTFIQFEPAP 297
Cdd:cd07415 241 QWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 13-313 3.77e-152

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 428.47  E-value: 3.77e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985   13 DLDEQISQLMQCKPLSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVD 92
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985   93 RGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWKIFTDLFDYFPLTALVESEIFCLHG 172
Cdd:PTZ00239  82 RGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  173 GLSPSIETLDNIRNFDRVQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGY 252
Cdd:PTZ00239 162 GLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18405985  253 N-WAHEQKVVTIFSAPNYCYRCGNMASILEVDDCRNHTFIQFEPAPRRGEPDVTRRTPDYFL 313
Cdd:PTZ00239 242 KyWFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKNVLPYFL 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 27-297 6.33e-152

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: 426.63  E-value: 6.33e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985     27 LSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVDRGYYSVETVTLLVA 106
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985    107 LKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGnANVWKIFTDLFDYFPLTALVESEIFCLHGGLSPSIETLDNIRN 186
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYG-ERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985    187 FDRVQEVPHEGPMCDLLWSDPDDRC-GWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGYNWAHEQKVVTIFS 265
Cdd:smart00156 160 LKRPQEPPDDGLLIDLLWSDPDQPVnGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFS 239

                          250       260       270
                   ....*....|....*....|....*....|..
gi 18405985    266 APNYCYRCGNMASILEVDDCRNHTFIQFEPAP 297
Cdd:smart00156 240 APNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 55-163 1.85e-17

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: 76.87  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985    55 PVTICGDIH--GQFHDLAELFRIGGmCPDTNYLFM--GDYVDRGYYSvETVTLLVALKMRYpQRITILRGNHESRqitqv 130
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD----- 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 18405985   131 ygfYDECLRKYG----NANVWKIFTDLFDYFPLTALV 163
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 ...
 13-297 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: 610.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  13 DLDEQISQLMQCKPLSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVD 92
Cdd:cd07415   1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  93 RGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWKIFTDLFDYFPLTALVESEIFCLHG 172
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 173 GLSPSIETLDNIRNFDRVQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGY 252
Cdd:cd07415 161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 18405985 253 NWAHEQKVVTIFSAPNYCYRCGNMASILEVDDCRNHTFIQFEPAP 297
Cdd:cd07415 241 QWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 13-313 3.77e-152

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 428.47  E-value: 3.77e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985   13 DLDEQISQLMQCKPLSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVD 92
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985   93 RGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWKIFTDLFDYFPLTALVESEIFCLHG 172
Cdd:PTZ00239  82 RGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  173 GLSPSIETLDNIRNFDRVQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGY 252
Cdd:PTZ00239 162 GLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18405985  253 N-WAHEQKVVTIFSAPNYCYRCGNMASILEVDDCRNHTFIQFEPAPRRGEPDVTRRTPDYFL 313
Cdd:PTZ00239 242 KyWFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKNVLPYFL 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 27-297 6.33e-152

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: 426.63  E-value: 6.33e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985     27 LSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVDRGYYSVETVTLLVA 106
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985    107 LKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGnANVWKIFTDLFDYFPLTALVESEIFCLHGGLSPSIETLDNIRN 186
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYG-ERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985    187 FDRVQEVPHEGPMCDLLWSDPDDRC-GWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGYNWAHEQKVVTIFS 265
Cdd:smart00156 160 LKRPQEPPDDGLLIDLLWSDPDQPVnGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFS 239

                          250       260       270
                   ....*....|....*....|....*....|..
gi 18405985    266 APNYCYRCGNMASILEVDDCRNHTFIQFEPAP 297
Cdd:smart00156 240 APNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 13-295 3.66e-114

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: 331.61  E-value: 3.66e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  13 DLDEQISQLMQCK--------PLSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNY 84
Cdd:cd07414   1 DIDSIIERLLEVRgsrpgknvQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  85 LFMGDYVDRGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYgNANVWKIFTDLFDYFPLTALVE 164
Cdd:cd07414  81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NIKLWKTFTDCFNCLPVAAIVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 165 SEIFCLHGGLSPSIETLDNIRNFDRVQEVPHEGPMCDLLWSDPD-DRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIAR 243
Cdd:cd07414 160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDkDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 18405985 244 AHQLVMDGYNWAHEQKVVTIFSAPNYCYRCGNMASILEVDDCRNHTFIQFEP 295
Cdd:cd07414 240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 57-282 2.23e-97

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: 286.57  E-value: 2.23e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  57 TICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVDRGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDE 136
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 137 CLRK---YGNANVWKIFTDLFDYFPLTALVESEIFCLHGGLSPSIETLDNIRNFdRVQEVPHEGPMCDLLWSDPDDRCG- 212
Cdd:cd00144  81 RTLRclrKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGd 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 213 WGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGYNWAHEQKVVTIFSAPNYCYRCGNMASILEV 282
Cdd:cd00144 160 FESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 27-297 5.82e-97

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: 288.44  E-value: 5.82e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  27 LSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVDRGYYSVETVTLLVA 106
Cdd:cd07416  16 LSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 107 LKMRYPQRITILRGNHESRQITQVYGFYDECLRKYgNANVWKIFTDLFDYFPLTALVESEIFCLHGGLSPSIETLDNIRN 186
Cdd:cd07416  96 LKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRK 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 187 FDRVQEVPHEGPMCDLLWSDP--DDRCGW------GISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGYN-WAHE 257
Cdd:cd07416 175 LDRFREPPSYGPMCDLLWSDPleDFGNEKtqehfvHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRmYRKS 254

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 18405985 258 QK-----VVTIFSAPNYCYRCGNMASILEVDDcRNHTFIQFEPAP 297
Cdd:cd07416 255 QTtgfpsLITIFSAPNYLDVYNNKAAVLKYEN-NVMNIRQFNCSP 298
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 12-296 3.14e-95

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 284.63  E-value: 3.14e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985   12 IDLDEQISQLMQC---KP-----LSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTN 83
Cdd:PTZ00480   9 IDVDNIIERLLSVrgsKPgknvnLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985   84 YLFMGDYVDRGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYgNANVWKIFTDLFDYFPLTALV 163
Cdd:PTZ00480  89 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-TIKLWKTFTDCFNCLPVAALI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  164 ESEIFCLHGGLSPSIETLDNIRNFDRVQEVPHEGPMCDLLWSDPD-DRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIA 242
Cdd:PTZ00480 168 DEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDkDVQGWADNERGVSYVFSQEIVQVFLKKHELDLIC 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18405985  243 RAHQLVMDGYNWAHEQKVVTIFSAPNYCYRCGNMASILEVDDCRNHTFIQFEPA 296
Cdd:PTZ00480 248 RAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPA 301
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 38-304 9.54e-90

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: 270.28  E-value: 9.54e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  38 KAKEILMDESNVQPVKSP----VTICGDIHGQFHDLAELFRIGGMCPDTN-YLFMGDYVDRGYYSVETVTLLVALKMRYP 112
Cdd:cd07417  40 QVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLYP 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 113 QRITILRGNHESRQITQVYGFYDECLRKYgNANVWKIFTDLFDYFPLTALVESEIFCLHGGLsPSIE--TLDNIRNFDRV 190
Cdd:cd07417 120 NHFHLNRGNHETDNMNKIYGFEGEVKAKY-NEQMFNLFSEVFNWLPLAHLINGKVLVVHGGL-FSDDgvTLDDIRKIDRF 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 191 QEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGYNWAHEQKVVTIFSAPNYC 270
Cdd:cd07417 198 RQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYC 277

                       250       260       270
                ....*....|....*....|....*....|....*
gi 18405985 271 YRCGNMASILEVD-DCRNHTFIQFEPAPrrgEPDV 304
Cdd:cd07417 278 DQMGNKGAFIRFKgSDLKPKFTQFEAVP---HPNV 309
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 27-284 1.97e-82

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 250.98  E-value: 1.97e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985   27 LSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVDRGYYSVETVTLLVA 106
Cdd:PTZ00244  25 IREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFC 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  107 LKMRYPQRITILRGNHESRQITQVYGFYDECLRKYgNANVWKIFTDLFDYFPLTALVESEIFCLHGGLSPSIETLDNIRN 186
Cdd:PTZ00244 105 YKIVYPENFFLLRGNHECASINKMYGFFDDVKRRY-NIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNE 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  187 FDRVQEVPHEGPMCDLLWSDPDDRC-GWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGYNWAHEQKVVTIFS 265
Cdd:PTZ00244 184 IERPCDVPDRGILCDLLWADPEDEVrGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFS 263

                        250
                 ....*....|....*....
gi 18405985  266 APNYCYRCGNMASILEVDD 284
Cdd:PTZ00244 264 APNYCGEFDNDAAVMNIDD 282
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 26-280 2.79e-78

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: 240.81  E-value: 2.79e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  26 PLSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGmCPDTN---------YLFMGDYVDRGYY 96
Cdd:cd07419  20 FFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYG-SPVTEeagdieyidYLFLGDYVDRGSH 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  97 SVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGNA-----NVWKIFTDLFDYFPLTALVESEIFCLH 171
Cdd:cd07419  99 SLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirdgdSVWQRINRLFNWLPLAALIEDKIICVH 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 172 GGLSPSIETLDNIRNFDRVQEVPHEGP-MCDLLWSDP---DDRCGW---GISPRGAG--YTFGQDISEQFNHTNNLKLIA 242
Cdd:cd07419 179 GGIGRSINHIHQIENLKRPITMEAGSPvVMDLLWSDPtenDSVLGLrpnAIDPRGTGliVKFGPDRVMEFLEENDLQMII 258

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 18405985 243 RAHQLVMDGYNWAHEQKVVTIFSAPNYCYRCGNMASIL 280
Cdd:cd07419 259 RAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAIL 296
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 13-269 1.35e-55

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: 182.22  E-value: 1.35e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  13 DLDEQISQLMQCKPLSEQQVRALCEKAKEILMDESNVQPVKS----PVTICGDIHGQFHDLAELFRIGGM-CPDTNYLFM 87
Cdd:cd07420   6 HIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLpSPENPYVFN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  88 GDYVDRGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYG--NANVWKIFTDLFDYFPLTALVES 165
Cdd:cd07420  86 GDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKdhGKKILRLLEDVFSWLPLATIIDN 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 166 EIFCLHGGLSPSIEtLDNIRNFDR--VQEVPHE-GPMCDLLWSDPDDRCG-WGISPRGAGYTFGQDISEQFNHTNNLKLI 241
Cdd:cd07420 166 KVLVVHGGISDSTD-LDLLDKIDRhkYVSTKTEwQQVVDILWSDPKATKGcKPNTFRGGGCYFGPDVTSQFLQKHGLSLL 244

                       250       260
                ....*....|....*....|....*...
gi 18405985 242 ARAHQLVMDGYNWAHEQKVVTIFSAPNY 269
Cdd:cd07420 245 IRSHECKPEGYEFCHNNKVITIFSASNY 272
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 19-298 1.16e-52

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 176.91  E-value: 1.16e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  19 SQLMQCKPLSEQQVRALCekAKEILMDESNVQPV----KSPVTICGDIHGQFHDLAELFRIGGM-CPDTNYLFMGDYVDR 93
Cdd:cd07418  29 SELPSVLPVNVFDSLVLT--AHKILHREPNCVRIdvedVCEVVVVGDVHGQLHDVLFLLEDAGFpDQNRFYVFNGDYVDR 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  94 GYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGN--ANVWKIFTDLFDYFPLTALVESEIFCLH 171
Cdd:cd07418 107 GAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDkgKHVYRKCLGCFEGLPLASIIAGRVYTAH 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 172 GGL---------------------------SPSIETLDNIRNFDR-VQEVPHEGPMC---DLLWSDPDDRCgwGISP--- 217
Cdd:cd07418 187 GGLfrspslpkrkkqkgknrrvlllepeseSLKLGTLDDLMKARRsVLDPPGEGSNLipgDVLWSDPSLTP--GLSPnkq 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 218 RGAGYTFGQDISEQFNHTNNLKLIARAHQ------------LVMDGYNWAHE---QKVVTIFSAPNYCY------RCGNM 276
Cdd:cd07418 265 RGIGLLWGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYTVDHDvesGKLITLFSAPDYPQfqateeRYNNK 344

                       330       340
                ....*....|....*....|....*..
gi 18405985 277 AS--ILEVDDCRN---HTFIQFEPAPR 298
Cdd:cd07418 345 GAyiILQPPDFSDpqfHTFEAVKPRPK 371
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 55-163 1.85e-17

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: 76.87  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985    55 PVTICGDIH--GQFHDLAELFRIGGmCPDTNYLFM--GDYVDRGYYSvETVTLLVALKMRYpQRITILRGNHESRqitqv 130
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD----- 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 18405985   131 ygfYDECLRKYG----NANVWKIFTDLFDYFPLTALV 163
Cdd:pfam00149  74 ---YGECLRLYPylglLARPWKRFLEVFNFLPLAGIL 107
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 56-123 5.73e-07

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: 50.19  E-value: 5.73e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18405985  56 VTIC-GDIHGQFHDLAELFRIGGMCPDTN------YLFMGDYVDRGYYSVETVTLLVALKMRYP-QRITILRGNHE 123
Cdd:cd07421   3 VVICvGDIHGYISKLNNLWLNLQSALGPSdfasalVIFLGDYCDRGPETRKVIDFLISLPEKHPkQRHVFLCGNHD 78
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 58-123 1.09e-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: 41.48  E-value: 1.09e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405985  58 ICGDIHGQFHDLAELFR--IGGMCPDTNYLFMGDYVDRGYYSVETVTLLVALKMRyPQRITILRGNHE 123
Cdd:cd00838   2 VISDIHGNLEALEAVLEaaLAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLA-GIPVYVVPGNHD 68
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 14-52 1.31e-04

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: 39.01  E-value: 1.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 18405985    14 LDEQISQLMQCK--------PLSEQQVRALCEKAKEILMDesnvQPV 52
Cdd:pfam16891   1 LDDIIERLLEVRgkpggkqvQLSEAEIRALCRKAREIFLS----QPM 43
PHA02239 PHA02239
putative protein phosphatase
 61-141 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 18405985   61 DIHGQFHDLAELFR--IGGMCPDTNYLFMGDYVDRGYYSVETVTLLVALkMRYPQRITILRGNHES---RQITQV--YGF 133
Cdd:PHA02239   8 DIHGEYQKLLTIMDkiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHDDefyNIMENVdrLSI 86


                 ....*....
gi 18405985  134 YD-ECLRKY 141
Cdd:PHA02239  87 YDiEWLSRY 95
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 60-176 4.39e-04

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


Pssm-ID: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 40.74  E-value: 4.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  60 GDIHGQFHDLAELFRIGGMCP--------DTNYLFMGDYVDRGYYSVETVTLLVALK---MRYPQRITILRGNHESRQI- 127
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGVIDsndrwiggDTVVVQTGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELMNLc 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985 128 --------TQVYGFYDECLRKYgnaNVWKIFTDLFDYF---PLTALVESEIFClHGGLSP 176
Cdd:cd07425  84 gdfryvhpRGLNEFGGVAKRRY---ALLSDGGYIGRYLrthPVVLVVNDILFV-HGGLGP 139
PRK09968 PRK09968
protein-serine/threonine phosphatase;
60-124 2.52e-03

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 38.72  E-value: 2.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18405985   60 GDIHGQFHDLAELFRIGGMCPDTNYLF-MGDYVDRGYYSVETVTLLvalkmRYPQRITIlRGNHES 124
Cdd:PRK09968  21 GDIHGEYQLLQSRLHQLSFCPETDLLIsVGDNIDRGPESLNVLRLL-----NQPWFISV-KGNHEA 80
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 58-123 3.99e-03

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: 37.88  E-value: 3.99e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405985  58 ICGDIHGQFHDLAELF-RIGGMCPDTNY---------LFMGDYVDRGYYSVETVTLLvalkMRYPQRITIL--RGNHE 123
Cdd:cd07423   2 IIGDVHGCYDELVELLeKLGYQKKEEGLyvhpegrklVFLGDLVDRGPDSIDVLRLV----MNMVKAGKALyvPGNHC 75
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 60-142 4.43e-03

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: 37.68  E-value: 4.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405985  60 GDIHGQFHDLAELFRIGGMCPDTNYLF-MGDYVDRGYYSVEtvtLLVALKMRYpqrITILRGNHESRQITQVYGFYDECL 138
Cdd:cd07424   7 GDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLE---VLELLKQPW---FHAVQGNHEQMAIDALRGGDDVMW 80


                ....
gi 18405985 139 RKYG 142
Cdd:cd07424  81 RANG 84
 
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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