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Conserved domains on  [gi|16130641|ref|NP_417214|]
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phosphoprotein phosphatase 2 [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

serine/threonine-protein phosphatase( domain architecture ID 10013389)

serine/threonine-protein phosphatase catalyzes the removal of phosphoryl groups from phosphorylated serines/threonines (and possibly tyrosines) in protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09968 PRK09968
protein-serine/threonine phosphatase;
1-218 4.76e-160

protein-serine/threonine phosphatase;


:

Pssm-ID: 182173  Cd Length: 218  Bit Score: 440.87  E-value: 4.76e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641    1 MPSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLLNQPWFTSVKGNHEA 80
Cdd:PRK09968   1 MPSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLLNQPWFISVKGNHEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641   81 MALEAFETGDGNMWLASGGDWFFDLNDSEQQEAIDLLLKFHHLPHIIEITNDNIKYAIAHADYPGSEYLFGKEIAESELL 160
Cdd:PRK09968  81 MALDAFETGDGNMWLASGGDWFFDLNDSEQQEATDLLLKFHHLPHIIEITNDNIKYVIAHADYPGDEYDFGKEIAESELL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130641  161 WPVDRVQKSLNGELQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPNSGRLSFYKIK 218
Cdd:PRK09968 161 WPVDRVQKSLNGELQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPKSGRLSFYKIK 218
 
Name Accession Description Interval E-value
PRK09968 PRK09968
protein-serine/threonine phosphatase;
1-218 4.76e-160

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 440.87  E-value: 4.76e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641    1 MPSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLLNQPWFTSVKGNHEA 80
Cdd:PRK09968   1 MPSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLLNQPWFISVKGNHEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641   81 MALEAFETGDGNMWLASGGDWFFDLNDSEQQEAIDLLLKFHHLPHIIEITNDNIKYAIAHADYPGSEYLFGKEIAESELL 160
Cdd:PRK09968  81 MALDAFETGDGNMWLASGGDWFFDLNDSEQQEATDLLLKFHHLPHIIEITNDNIKYVIAHADYPGDEYDFGKEIAESELL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130641  161 WPVDRVQKSLNGELQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPNSGRLSFYKIK 218
Cdd:PRK09968 161 WPVDRVQKSLNGELQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPKSGRLSFYKIK 218
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 15-218 1.44e-108

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: 310.02  E-value: 1.44e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  15 RHIWVVGDIHGEYQLLQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLLNQPWFTSVKGNHEAMALEAFETGDGNMW 94
Cdd:cd07424   1 GRDFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPWFHAVQGNHEQMAIDALRGGDDVMW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  95 LASGGDWFFDLNDSEQqeaIDLLLKFHHLPHIIEITNDNIKYAIAHADYPGSEYLFG---KEIAESELLWPVDRVQKSLn 171
Cdd:cd07424  81 RANGGGWFFDLPDEEA---KVLLEKLHHLPIAIEVESRNGKVGIVHADYPFDEYSFGfveKPEDEEEALWSRDRLQKSQ- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16130641 172 geLQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPNSGRLSFYKIK 218
Cdd:cd07424 157 --TQPVAGADAFIFGHTPVPEPLDLGNVYYIDTGGVFDGNLTLVKLQ 201
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-87 2.72e-10

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: 55.68  E-value: 2.72e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130641    16 HIWVVGDIHGEYQL--LQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL-----NQPWFTsVKGNHEAMALEAFE 87
Cdd:pfam00149   2 RILVIGDLHLPGQLddLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLerlikYVPVYL-VRGNHDFDYGECLR 79
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
19-187 7.74e-08

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 50.30  E-value: 7.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  19 VVGDIHGEYQLLQsRLhqLSFFPK--IDLLISVGDNIDRGPESLDVLRLLNQPWFTSVKGNHEAMALEafetgdgnmWLA 96
Cdd:COG0622   4 VISDTHGNLPALE-AV--LEDLERegVDLIVHLGDLVGYGPDPPEVLDLLRELPIVAVRGNHDGAVLR---------GLR 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  97 SggdwffdlndseqqeaidlllkfhhLPHIIEITNDNIKYAIAHADypGSEYLFGKEIAEsELLwpvdrvqkslngELQQ 176
Cdd:COG0622  72 S-------------------------LPETLRLELEGVRILLVHGS--PNEYLLPDTPAE-RLR------------ALAA 111

                       170
                ....*....|.
gi 16130641 177 INGADYFIFGH 187
Cdd:COG0622 112 EGDADVVVCGH 122
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 17-80 9.44e-05

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: 42.20  E-value: 9.44e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130641     17 IWVVGDIHGEYQLLQsRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL--------NQpwFTSVKGNHEA 80
Cdd:smart00156  30 VTVCGDIHGQFDDLL-RLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLfalkilypNR--IVLLRGNHES 98
 
Name Accession Description Interval E-value
PRK09968 PRK09968
protein-serine/threonine phosphatase;
1-218 4.76e-160

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 440.87  E-value: 4.76e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641    1 MPSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLLNQPWFTSVKGNHEA 80
Cdd:PRK09968   1 MPSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLLNQPWFISVKGNHEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641   81 MALEAFETGDGNMWLASGGDWFFDLNDSEQQEAIDLLLKFHHLPHIIEITNDNIKYAIAHADYPGSEYLFGKEIAESELL 160
Cdd:PRK09968  81 MALDAFETGDGNMWLASGGDWFFDLNDSEQQEATDLLLKFHHLPHIIEITNDNIKYVIAHADYPGDEYDFGKEIAESELL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130641  161 WPVDRVQKSLNGELQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPNSGRLSFYKIK 218
Cdd:PRK09968 161 WPVDRVQKSLNGELQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPKSGRLSFYKIK 218
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 15-218 1.44e-108

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: 310.02  E-value: 1.44e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  15 RHIWVVGDIHGEYQLLQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLLNQPWFTSVKGNHEAMALEAFETGDGNMW 94
Cdd:cd07424   1 GRDFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPWFHAVQGNHEQMAIDALRGGDDVMW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  95 LASGGDWFFDLNDSEQqeaIDLLLKFHHLPHIIEITNDNIKYAIAHADYPGSEYLFG---KEIAESELLWPVDRVQKSLn 171
Cdd:cd07424  81 RANGGGWFFDLPDEEA---KVLLEKLHHLPIAIEVESRNGKVGIVHADYPFDEYSFGfveKPEDEEEALWSRDRLQKSQ- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16130641 172 geLQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPNSGRLSFYKIK 218
Cdd:cd07424 157 --TQPVAGADAFIFGHTPVPEPLDLGNVYYIDTGGVFDGNLTLVKLQ 201
pphA PRK11439
protein-serine/threonine phosphatase;
2-218 2.95e-78

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 233.89  E-value: 2.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641    2 PSTRYQKINAHHYRHIWVVGDIHGEYQLLQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLLNQPWFTSVKGNHEAM 81
Cdd:PRK11439   4 PAPVYQRIAGHQWRHIWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEEHWVRAVRGNHEQM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641   82 ALEAFETGDGNMWLASGGDWFFDLNDSEQQEAIDLLLKFHHLPHIIEITNDNIKYAIAHADYPGSEYLFGKEIAESELLW 161
Cdd:PRK11439  84 ALDALASQQMSLWLMNGGDWFIALTDNQQKQAKTLLEKCQRLPFILEVHCRTGKHVIAHADYPADVYEWQKDVDLHQVLW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130641  162 PVDRVQKSLNGelQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPNSGRLSFYKIK 218
Cdd:PRK11439 164 SRSRLGERQKG--QGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 18-217 6.45e-15

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: 70.86  E-value: 6.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  18 WVVGDIHGEYQLLQsRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL------NQPWFTSVKGNHEAMALEAFETGDG 91
Cdd:cd00144   1 IVVGDIHGCFDDLL-RLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLlalkilYPDNVFLLRGNHEFMLLNFLYGFYD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  92 NMWLASGGDWFFDLNDseqqeaiDLLLKFHHLPHIIEITNdniKYAIAHADYPGSEYL-----------FGKEIAESELL 160
Cdd:cd00144  80 ERTLRCLRKGGEELWR-------EFNEVFNYLPLAALVDG---KILCVHGGLSPDLTLldqirnirpieNPDDQLVEDLL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641 161 W-----------PVDRVQKSLNGELQ-----QINGADYFIFGHMMFDNIQTF---ANQIYIDTGS----PNSGRLSFYKI 217
Cdd:cd00144 150 WsdpdesvgdfeSSSRGGGYLFGEDAvdeflKKNGLKLIVRGHTPVEGGYEFlhgGKLITIFSAPnycgKGGNKLAALVV 229
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 17-79 1.13e-11

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: 62.18  E-value: 1.13e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130641  17 IWVVGDIHGEYQLLQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL--NQPWFTSVKGNHE 79
Cdd:cd07422   1 TYAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVksLGDSAVVVLGNHD 65
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
17-79 1.60e-11

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 62.11  E-value: 1.60e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130641   17 IWVVGDIHGEYQLLQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL--NQPWFTSVKGNHE 79
Cdd:PRK00166   3 TYAIGDIQGCYDELQRLLEKIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVksLGDSAVTVLGNHD 67
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-87 2.72e-10

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: 55.68  E-value: 2.72e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130641    16 HIWVVGDIHGEYQL--LQSRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL-----NQPWFTsVKGNHEAMALEAFE 87
Cdd:pfam00149   2 RILVIGDLHLPGQLddLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLerlikYVPVYL-VRGNHDFDYGECLR 79
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
19-187 7.74e-08

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 50.30  E-value: 7.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  19 VVGDIHGEYQLLQsRLhqLSFFPK--IDLLISVGDNIDRGPESLDVLRLLNQPWFTSVKGNHEAMALEafetgdgnmWLA 96
Cdd:COG0622   4 VISDTHGNLPALE-AV--LEDLERegVDLIVHLGDLVGYGPDPPEVLDLLRELPIVAVRGNHDGAVLR---------GLR 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  97 SggdwffdlndseqqeaidlllkfhhLPHIIEITNDNIKYAIAHADypGSEYLFGKEIAEsELLwpvdrvqkslngELQQ 176
Cdd:COG0622  72 S-------------------------LPETLRLELEGVRILLVHGS--PNEYLLPDTPAE-RLR------------ALAA 111

                       170
                ....*....|.
gi 16130641 177 INGADYFIFGH 187
Cdd:COG0622 112 EGDADVVVCGH 122
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
17-95 1.06e-07

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 50.40  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  17 IWVVGDIHGEYQLLqSRLHQLSFFPKIDLLISVGDNIDRGPES-----LDVLRLLNQPWFTsVKGNHEAMALEAFETGDG 91
Cdd:COG2129   2 ILAVSDLHGNFDLL-EKLLELARAEDADLVILAGDLTDFGTAEearevLEELAALGVPVLA-VPGNHDDPEVLDALEESG 79


                ....
gi 16130641  92 NMWL 95
Cdd:COG2129  80 VHNL 83
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 19-79 2.05e-06

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 46.74  E-value: 2.05e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130641  19 VVGDIHGEYQLLQSRLHQLSF-FPKIDL--------LISVGDNIDRGPESLDVLRLlnqpWFTSVK--------GNHE 79
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGYqKKEEGLyvhpegrkLVFLGDLVDRGPDSIDVLRL----VMNMVKagkalyvpGNHC 75
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 19-213 1.38e-05

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 44.69  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641   19 VVGDIHGEYQLLQSRLHQLSFFPKIDL--------LISVGDNIDRGPESLDVLR----LLNQPWFTSVKGNHeAMALEAF 86
Cdd:PRK13625   5 IIGDIHGCYQEFQALTEKLGYNWSSGLpvhpdqrkLAFVGDLTDRGPHSLRMIEivweLVEKKAAYYVPGNH-CNKLYRF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641   87 ETGDgNMWLASGGDW----FFDLNDSEQQEAIDLLLKFHH---LPHIIeitnDNIKYAIAHA----DYPGSE-------Y 148
Cdd:PRK13625  84 FLGR-NVTIAHGLETtvaeYEALPSHKQNMIKEKFITLYEqapLYHIL----DEGRLVVAHAgirqDYIGRQdkkvqtfV 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130641  149 LFGKEIAESellWPVDR-VQKSLngeLQQINGADYFIFGHMMFDNIQTFANQIYIDTGSPNSGRLS 213
Cdd:PRK13625 159 LYGDITGEK---HPDGSpVRRDW---AKEYKGTAWIVYGHTPVKEPRFVNHTVNIDTGCVFGGRLT 218
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 19-136 1.95e-05

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 42.64  E-value: 1.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  19 VVGDIHGEYQLLQSRL-HQLSFFPKIDLLISVGDNIDRGPESLDV------LRLLNQPWFtSVKGNHEAMALEAFETGDG 91
Cdd:cd00838   2 VISDIHGNLEALEAVLeAALAKAEKPDLVICLGDLVDYGPDPEEVelkalrLLLAGIPVY-VVPGNHDILVTHGPPYDPL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 16130641  92 NMWLASGGDWFFDLNDSEQQEAIDLLLKFH-HLPHIIEITNDNIKY 136
Cdd:cd00838  81 DEGSPGEDPGSEALLELLDKYGPDLVLSGHtHVPGRREVDKGGTLV 126
PHA02239 PHA02239
putative protein phosphatase
 17-79 3.72e-05

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 43.44  E-value: 3.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130641   17 IWVVGDIHGEYQLLQSRLHQLSFFPKI-DLLISVGDNIDRGPESLDVLR-----LLNQPWFTSVKGNHE 79
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKINNERKPeETIVFLGDYVDRGKRSKDVVNyifdlMSNDDNVVTLLGNHD 71
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 17-80 9.44e-05

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: 42.20  E-value: 9.44e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130641     17 IWVVGDIHGEYQLLQsRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL--------NQpwFTSVKGNHEA 80
Cdd:smart00156  30 VTVCGDIHGQFDDLL-RLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLfalkilypNR--IVLLRGNHES 98
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 17-79 2.52e-04

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: 41.17  E-value: 2.52e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130641  17 IWVVGDIHGEY-QLLqsRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL---------NqpwFTSVKGNHE 79
Cdd:cd07414  52 LKICGDIHGQYyDLL--RLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLlaykikypeN---FFLLRGNHE 119
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 19-84 1.18e-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: 38.82  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  19 VVGDIHGEYQllqsRLHQLSFFPKI-----------DLLISVGDNIDRGPESLDVLRLLNQPW---------FTSVKGNH 78
Cdd:cd07425   2 AIGDLHGDLD----RLRTILKLAGVidsndrwiggdTVVVQTGDILDRGDDEIEILKLLEKLKrqarkaggkVILLLGNH 77


                ....*.
gi 16130641  79 EAMALE 84
Cdd:cd07425  78 ELMNLC 83
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 19-88 3.44e-03

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. 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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 37.53  E-value: 3.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130641  19 VVGDIHGEYQLLQSRLHQLSF--------FPKIDLLIsVGDNIDRGPESLDVLR----LLNQPWFTSVKGNHEAMALeAF 86
Cdd:cd07413   3 LIGDVHGCAHTLDRLLDLLGYrlqggvwrHPRRQALF-VGDLIDRGPRIREVLHrvhaMVDAGEALCVMGNHEFNAL-AW 80


                ..
gi 16130641  87 ET 88
Cdd:cd07413  81 HT 82
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 19-83 4.61e-03

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 37.33  E-value: 4.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130641   19 VVGDIHGEY-QLLqsRLHQLSFFPKIDLLISVGDNIDRGPESLDVLRLL-----NQPW-FTSVKGNHEAMAL 83
Cdd:PTZ00480  63 ICGDVHGQYfDLL--RLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLlaykiKYPEnFFLLRGNHECASI 132
 
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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