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Conserved domains on  [gi|4506027|ref|NP_002711|]
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serine/threonine-protein phosphatase 4 catalytic subunit isoform 1 [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 ...
 6-290 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: 654.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:cd07415   1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGY 245
Cdd:cd07415 161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 4506027  246 KWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
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 ...
 6-290 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: 654.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:cd07415   1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGY 245
Cdd:cd07415 161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 4506027  246 KWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:cd07415 241 QWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 6-307 2.91e-166

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 463.90  E-value: 2.91e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027     6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:PTZ00239  82 RGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGY 245
Cdd:PTZ00239 162 GLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506027   246 KWHFNETVL-TVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKpVADYFL 307
Cdd:PTZ00239 242 KYWFPDQNLvTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKN-VLPYFL 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 22-290 3.88e-138

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: 391.19  E-value: 3.88e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027      22 ESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALK 101
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027     102 VRYPDRITLIRGNHESRQITQVYGFYDECLRKYGsVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTID 181
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYG-ERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027     182 RKQEVPHDGPMCDLLWSDPEDTT-GWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAP 260
Cdd:smart00156 162 RPQEPPDDGLLIDLLWSDPDQPVnGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAP 241

                          250       260       270
                   ....*....|....*....|....*....|
gi 4506027     261 NYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:smart00156 242 NYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 48-156 3.08e-19

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 81.49  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027     48 PVTVCGDIH--GQFYDLKELFRVGGDVPETNY-LFMGDFVDRGFYSvETFLLLLALKVRYpDRITLIRGNHESRqitqvy 124
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLvLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 4506027    125 gfYDECLRKYG----SVTVWRYCTEIFDYLSLSAII 156
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 ...
 6-290 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: 654.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:cd07415   1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLAALIDGQIFCVHG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGY 245
Cdd:cd07415 161 GLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 4506027  246 KWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:cd07415 241 QWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 6-307 2.91e-166

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 463.90  E-value: 2.91e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027     6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:PTZ00239  82 RGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGY 245
Cdd:PTZ00239 162 GLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506027   246 KWHFNETVL-TVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKpVADYFL 307
Cdd:PTZ00239 242 KYWFPDQNLvTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKN-VLPYFL 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 22-290 3.88e-138

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: 391.19  E-value: 3.88e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027      22 ESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALK 101
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027     102 VRYPDRITLIRGNHESRQITQVYGFYDECLRKYGsVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTID 181
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYG-ERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027     182 RKQEVPHDGPMCDLLWSDPEDTT-GWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAP 260
Cdd:smart00156 162 RPQEPPDDGLLIDLLWSDPDQPVnGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAP 241

                          250       260       270
                   ....*....|....*....|....*....|
gi 4506027     261 NYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:smart00156 242 NYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 6-287 9.49e-116

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: 335.46  E-value: 9.49e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    6 DLDRQIEQL---------RRCELiKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETN 76
Cdd:cd07414   1 DIDSIIERLlevrgsrpgKNVQL-TEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   77 YLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYgSVTVWRYCTEIFDYLSLSAII 156
Cdd:cd07414  80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NIKLWKTFTDCFNCLPVAAIV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  157 DGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPE-DTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMIC 235
Cdd:cd07414 159 DEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDkDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLIC 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4506027  236 RAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFE 287
Cdd:cd07414 239 RAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 290
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 10-276 1.32e-101

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: 299.99  E-value: 1.32e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   10 QIEQLRRcELIKESEVKALCA-----KAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFV 84
Cdd:cd07416   2 RVDILKA-HFMREGRLSEEDAlriitEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   85 DRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYgSVTVWRYCTEIFDYLSLSAIIDGKIFCVH 164
Cdd:cd07416  81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYDACMEAFDCLPLAALMNQQFLCVH 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  165 GGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDP--EDTTGW------GVSPRGAGYLFGSDVVAQFNAANDIDMICR 236
Cdd:cd07416 160 GGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPleDFGNEKtqehfvHNTVRGCSYFYSYRAVCEFLQKNNLLSIIR 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 4506027  237 AHQLVMEGYKWH-FNET-----VLTVWSAPNYCYRCGNVAAILELD 276
Cdd:cd07416 240 AHEAQDAGYRMYrKSQTtgfpsLITIFSAPNYLDVYNNKAAVLKYE 285
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 50-275 9.99e-98

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: 287.35  E-value: 9.99e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   50 TVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDE 129
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  130 CLRK---YGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIdRKQEVPHDGPMCDLLWSDPEDTTG- 205
Cdd:cd00144  81 RTLRclrKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGd 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  206 WGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILEL 275
Cdd:cd00144 160 FESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 20-307 5.67e-97

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 288.87  E-value: 5.67e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    20 IKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLA 99
Cdd:PTZ00480  32 LTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   100 LKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYgSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRT 179
Cdd:PTZ00480 112 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-TIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRR 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   180 IDRKQEVPHDGPMCDLLWSDPE-DTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWS 258
Cdd:PTZ00480 191 IMRPTDVPDTGLLCDLLWSDPDkDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFS 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 4506027   259 APNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL 307
Cdd:PTZ00480 271 APNYCGEFDNAGSMMTIDESLMCSFQILKPAEQGQGASQQNKPGSAKFV 319
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 31-303 6.57e-93

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: 278.37  E-value: 6.57e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   31 KAREILVEESNVQRVDSP----VTVCGDIHGQFYDLKELFRVGGDVPETN-YLFMGDFVDRGFYSVETFLLLLALKVRYP 105
Cdd:cd07417  40 QVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLYP 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  106 DRITLIRGNHESRQITQVYGFYDECLRKYGSvTVWRYCTEIFDYLSLSAIIDGKIFCVHGGL-SPSIQTLDQIRTIDRKQ 184
Cdd:cd07417 120 NHFHLNRGNHETDNMNKIYGFEGEVKAKYNE-QMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFR 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  185 EVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCY 264
Cdd:cd07417 199 QPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCD 278

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4506027  265 RCGNVAAILELDEHLQK-DFIIFEAAPQetrgiPSKKPVA 303
Cdd:cd07417 279 QMGNKGAFIRFKGSDLKpKFTQFEAVPH-----PNVKPMA 313
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 19-289 1.07e-84

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 256.76  E-value: 1.07e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    19 LIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLL 98
Cdd:PTZ00244  24 LIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    99 ALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYgSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIR 178
Cdd:PTZ00244 104 CYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRY-NIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVN 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   179 TIDRKQEVPHDGPMCDLLWSDPED-TTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVW 257
Cdd:PTZ00244 183 EIERPCDVPDRGILCDLLWADPEDeVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVF 262

                        250       260       270
                 ....*....|....*....|....*....|..
gi 4506027   258 SAPNYCYRCGNVAAILELDEHLQKDFIIFEAA 289
Cdd:PTZ00244 263 SAPNYCGEFDNDAAVMNIDDKLQCSFLIIPAR 294
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 19-285 9.73e-82

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: 249.67  E-value: 9.73e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   19 LIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELF--------RVGGDVPETNYLFMGDFVDRGFYS 90
Cdd:cd07419  20 FFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFdeygspvtEEAGDIEYIDYLFLGDYVDRGSHS 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   91 VETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGS-----VTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:cd07419 100 LETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdirdgDSVWQRINRLFNWLPLAALIEDKIICVHG 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  166 GLSPSIQTLDQIRTIDRKQEVPHDGP-MCDLLWSDPEDTTGWGVS------PRGAGYL--FGSDVVAQFNAANDIDMICR 236
Cdd:cd07419 180 GIGRSINHIHQIENLKRPITMEAGSPvVMDLLWSDPTENDSVLGLrpnaidPRGTGLIvkFGPDRVMEFLEENDLQMIIR 259

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 4506027  237 AHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILeldeHLQKDFII 285
Cdd:cd07419 260 AHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAIL----VLGRDLVV 304
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 6-284 8.64e-57

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: 185.30  E-value: 8.64e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDS----PVTVCGDIHGQFYDLKELFRVGG-DVPETNYLFM 80
Cdd:cd07420   6 HIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGlPSPENPYVFN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   81 GDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYG--SVTVWRYCTEIFDYLSLSAIIDG 158
Cdd:cd07420  86 GDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKdhGKKILRLLEDVFSWLPLATIIDN 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  159 KIFCVHGGLSpSIQTLDQIRTIDR---KQEVPHDGPMCDLLWSDPEDTTG-WGVSPRGAGYLFGSDVVAQFNAANDIDMI 234
Cdd:cd07420 166 KVLVVHGGIS-DSTDLDLLDKIDRhkyVSTKTEWQQVVDILWSDPKATKGcKPNTFRGGGCYFGPDVTSQFLQKHGLSLL 244

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506027  235 CRAHQLVMEGYKWHFNETVLTVWSAPNYcYRCG-NVAAILELDEHLQKDFI 284
Cdd:cd07420 245 IRSHECKPEGYEFCHNNKVITIFSASNY-YEEGsNRGAYVKLGPQLTPHFV 294
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 23-288 2.97e-49

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: 168.05  E-value: 2.97e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   23 SEVKALCAKAREILVEESNVQRVD----SPVTVCGDIHGQFYDLKELFRVGGdVPETN--YLFMGDFVDRGFYSVETFLL 96
Cdd:cd07418  38 NVFDSLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAG-FPDQNrfYVFNGDYVDRGAWGLETFLL 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   97 LLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSV--TVWRYCTEIFDYLSLSAIIDGKIFCVHGGL------- 167
Cdd:cd07418 117 LLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKgkHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslp 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  168 --------------------SPSIQTLDQIRTIDRK-QEVPHDGPMC---DLLWSDPEDTTgwGVSP---RGAGYLFGSD 220
Cdd:cd07418 197 krkkqkgknrrvlllepeseSLKLGTLDDLMKARRSvLDPPGEGSNLipgDVLWSDPSLTP--GLSPnkqRGIGLLWGPD 274

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  221 VVAQFNAANDIDMICRAHQ------------LVMEGYKWHFNETV---LTVWSAPNYCY------RCGNVAA--ILELDE 277
Cdd:cd07418 275 CTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYTVDHDVESgklITLFSAPDYPQfqateeRYNNKGAyiILQPPD 354

                       330
                ....*....|.
gi 4506027  278 HLQKDFIIFEA 288
Cdd:cd07418 355 FSDPQFHTFEA 365
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 48-156 3.08e-19

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 81.49  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027     48 PVTVCGDIH--GQFYDLKELFRVGGDVPETNY-LFMGDFVDRGFYSvETFLLLLALKVRYpDRITLIRGNHESRqitqvy 124
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLvLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 4506027    125 gfYDECLRKYG----SVTVWRYCTEIFDYLSLSAII 156
Cdd:pfam00149  74 --YGECLRLYPylglLARPWKRFLEVFNFLPLAGIL 107
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 51-116 3.13e-05

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 43.02  E-value: 3.13e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4506027   51 VCGDIHGQFYDLKELFR--VGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRyPDRITLIRGNHE 116
Cdd:cd00838   2 VISDIHGNLEALEAVLEaaLAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLA-GIPVYVVPGNHD 68
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 49-116 3.25e-05

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: 44.80  E-value: 3.25e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4506027   49 VTVC-GDIHGQFYDLKELFR-----VGGDVPETNY-LFMGDFVDRGFYSVETFLLLLALKVRYPD-RITLIRGNHE 116
Cdd:cd07421   3 VVICvGDIHGYISKLNNLWLnlqsaLGPSDFASALvIFLGDYCDRGPETRKVIDFLISLPEKHPKqRHVFLCGNHD 78
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 51-135 2.27e-04

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


Pssm-ID: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 41.53  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   51 VCGDIHGQFYDL-KELFRVGGDvPETNYLF-MGDFVDRGFYSVETFLLLLALKVRYpdritlIRGNHESRQITQVYGFYD 128
Cdd:cd07424   5 VVGDIHGHFQRLqRALDAVGFD-PARDRLIsVGDLVDRGPESLEVLELLKQPWFHA------VQGNHEQMAIDALRGGDD 77


                ....*..
gi 4506027  129 ECLRKYG 135
Cdd:cd07424  78 VMWRANG 84
PHA02239 PHA02239
putative protein phosphatase
 49-150 1.58e-03

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 39.21  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027    49 VTVCGDIHGQFydlKELFRVGGDV-----PETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIrGNHES---RQI 120
Cdd:PHA02239   3 IYVVPDIHGEY---QKLLTIMDKInnerkPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHDDefyNIM 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 4506027   121 TQV--YGFYD---------ECLRKYGSVTVWRYCTEIFDYL 150
Cdd:PHA02239  79 ENVdrLSIYDiewlsryciETLNSYGVSTVTLKYSSVEENL 119
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 53-116 2.17e-03

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


Pssm-ID: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 39.06  E-value: 2.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4506027   53 GDIHGQFYDLKELF-RVGGDvPETNYL-FMGDFVDRGFYSVETFLLLLALKvrypDRITLIRGNHE 116
Cdd:cd07422   5 GDIQGCYDELQRLLeKINFD-PAKDRLwLVGDLVNRGPDSLETLRFVKSLG----DSAVVVLGNHD 65
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 53-169 2.87e-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: 38.43  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027   53 GDIHGQFYDLKELFRVGGDVPETNY--------LFMGDFVDRGFYSVETFLLLLALK---VRYPDRITLIRGNHESRQI- 120
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGVIDSNDRwiggdtvvVQTGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELMNLc 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506027  121 --------TQVYGFYDECLRKYgsvTVWRYCTEIFDYLSLS---AIIDGKIFcVHGGLSP 169
Cdd:cd07425  84 gdfryvhpRGLNEFGGVAKRRY---ALLSDGGYIGRYLRTHpvvLVVNDILF-VHGGLGP 139
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 20-41 2.95e-03

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


Pssm-ID: 465300 [Multi-domain]  Cd Length: 48  Bit Score: 35.16  E-value: 2.95e-03
                          10        20
                  ....*....|....*....|..
gi 4506027     20 IKESEVKALCAKAREILVEESN 41
Cdd:pfam16891  22 LSEAEIRALCRKAREIFLSQPM 43
 
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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