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Conserved domains on  [gi|447083099|ref|WP_001160355|]
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MULTISPECIES: metallophosphoesterase [Enterobacterales]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 24-253 7.86e-08

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.


The actual alignment was detected with superfamily member cd07424:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 201  Bit Score: 51.93  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099  24 GRVFFLADPHGHYSTLCNLIHSIS-EPDEELIvFSTGNLFDYGPEPMELMTAINTGIFdgRSVRvfsaaGAGEEMLkkll 102
Cdd:cd07424    1 GRDFVVGDIHGHFQRLQRALDAVGfDPARDRL-ISVGDLVDRGPESLEVLELLKQPWF--HAVQ-----GNHEQMA---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099 103 pINKdrrtyYPSTFLNeRWCARGGRWHKQINRNYLEEEICKLlsTQLATVMKVLfKGNISIGICPSDYTDirqgfnNTYN 182
Cdd:cd07424   69 -IDA-----LRGGDDV-MWRANGGGWFFDLPDEEAKVLLEKL--HHLPIAIEVE-SRNGKVGIVHADYPF------DEYS 132

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447083099 183 ALLAFNqanvNIFQSQFLYG----MDHAVRPVNvsDVNLVVLGRNPVNSirkahglpltnlPVLIGNCLHINTGS 253
Cdd:cd07424  133 FGFVEK----PEDEEEALWSrdrlQKSQTQPVA--GADAFIFGHTPVPE------------PLDLGNVYYIDTGG 189
 
Name Accession Description Interval E-value
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 24-253 7.86e-08

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: 51.93  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099  24 GRVFFLADPHGHYSTLCNLIHSIS-EPDEELIvFSTGNLFDYGPEPMELMTAINTGIFdgRSVRvfsaaGAGEEMLkkll 102
Cdd:cd07424    1 GRDFVVGDIHGHFQRLQRALDAVGfDPARDRL-ISVGDLVDRGPESLEVLELLKQPWF--HAVQ-----GNHEQMA---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099 103 pINKdrrtyYPSTFLNeRWCARGGRWHKQINRNYLEEEICKLlsTQLATVMKVLfKGNISIGICPSDYTDirqgfnNTYN 182
Cdd:cd07424   69 -IDA-----LRGGDDV-MWRANGGGWFFDLPDEEAKVLLEKL--HHLPIAIEVE-SRNGKVGIVHADYPF------DEYS 132

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447083099 183 ALLAFNqanvNIFQSQFLYG----MDHAVRPVNvsDVNLVVLGRNPVNSirkahglpltnlPVLIGNCLHINTGS 253
Cdd:cd07424  133 FGFVEK----PEDEEEALWSrdrlQKSQTQPVA--GADAFIFGHTPVPE------------PLDLGNVYYIDTGG 189
PRK09968 PRK09968
protein-serine/threonine phosphatase;
9-172 8.24e-04

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 40.26  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099   9 MASEHVQTIDLTNFSgRVFFLADPHGHYSTLCNLIHSIS-EPDEELIVfSTGNLFDYGPEPMELMTAINTGIFdgrsvrv 87
Cdd:PRK09968   1 MPSTRYQKINAHHYR-HIWVVGDIHGEYQLLQSRLHQLSfCPETDLLI-SVGDNIDRGPESLNVLRLLNQPWF------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099  88 FSAAGAGEEMLKKLLpinkdrrtyypSTFLNERWCARGGRWHKQINRNYLEEEICKLLS-TQLATVMKVLfKGNISIGIC 166
Cdd:PRK09968  72 ISVKGNHEAMALDAF-----------ETGDGNMWLASGGDWFFDLNDSEQQEATDLLLKfHHLPHIIEIT-NDNIKYVIA 139


                 ....*.
gi 447083099 167 PSDYTD 172
Cdd:PRK09968 140 HADYPG 145
 
Name Accession Description Interval E-value
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 24-253 7.86e-08

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: 51.93  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099  24 GRVFFLADPHGHYSTLCNLIHSIS-EPDEELIvFSTGNLFDYGPEPMELMTAINTGIFdgRSVRvfsaaGAGEEMLkkll 102
Cdd:cd07424    1 GRDFVVGDIHGHFQRLQRALDAVGfDPARDRL-ISVGDLVDRGPESLEVLELLKQPWF--HAVQ-----GNHEQMA---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099 103 pINKdrrtyYPSTFLNeRWCARGGRWHKQINRNYLEEEICKLlsTQLATVMKVLfKGNISIGICPSDYTDirqgfnNTYN 182
Cdd:cd07424   69 -IDA-----LRGGDDV-MWRANGGGWFFDLPDEEAKVLLEKL--HHLPIAIEVE-SRNGKVGIVHADYPF------DEYS 132

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447083099 183 ALLAFNqanvNIFQSQFLYG----MDHAVRPVNvsDVNLVVLGRNPVNSirkahglpltnlPVLIGNCLHINTGS 253
Cdd:cd07424  133 FGFVEK----PEDEEEALWSrdrlQKSQTQPVA--GADAFIFGHTPVPE------------PLDLGNVYYIDTGG 189
PRK09968 PRK09968
protein-serine/threonine phosphatase;
9-172 8.24e-04

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 40.26  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099   9 MASEHVQTIDLTNFSgRVFFLADPHGHYSTLCNLIHSIS-EPDEELIVfSTGNLFDYGPEPMELMTAINTGIFdgrsvrv 87
Cdd:PRK09968   1 MPSTRYQKINAHHYR-HIWVVGDIHGEYQLLQSRLHQLSfCPETDLLI-SVGDNIDRGPESLNVLRLLNQPWF------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083099  88 FSAAGAGEEMLKKLLpinkdrrtyypSTFLNERWCARGGRWHKQINRNYLEEEICKLLS-TQLATVMKVLfKGNISIGIC 166
Cdd:PRK09968  72 ISVKGNHEAMALDAF-----------ETGDGNMWLASGGDWFFDLNDSEQQEATDLLLKfHHLPHIIEIT-NDNIKYVIA 139


                 ....*.
gi 447083099 167 PSDYTD 172
Cdd:PRK09968 140 HADYPG 145
 
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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