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Conserved domains on  [gi|2555850900|ref|WP_303678137|]
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metallophosphoesterase [Dehalococcoides mccartyi]

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 ...
 1171-1306 4.02e-12

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 cd07425:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 209  Bit Score: 67.32  E-value: 4.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2555850900 1171 VIGDLHGEYtDLLKDI--NTGydqpLIrgrsgDITSWkWNGKEQSLVQVGDIVDRGAHYEQIRSTFNRLADEAAQTGGNV 1248
Cdd:cd07425      2 AIGDLHGDL-DRLRTIlkLAG----VI-----DSNDR-WIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKAGGKV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2555850900 1249 TRLIGNHELAYLTG------EKIPGIDYSNAPTIRKGILDDISAGK----LKAAEAINGELYTHAGVS 1306
Cdd:cd07425     71 ILLLGNHELMNLCGdfryvhPRGLNEFGGVAKRRYALLSDGGYIGRylrtHPVVLVVNDILFVHGGLG 138
 
Name Accession Description Interval E-value
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 1171-1306 4.02e-12

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: 67.32  E-value: 4.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2555850900 1171 VIGDLHGEYtDLLKDI--NTGydqpLIrgrsgDITSWkWNGKEQSLVQVGDIVDRGAHYEQIRSTFNRLADEAAQTGGNV 1248
Cdd:cd07425      2 AIGDLHGDL-DRLRTIlkLAG----VI-----DSNDR-WIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKAGGKV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2555850900 1249 TRLIGNHELAYLTG------EKIPGIDYSNAPTIRKGILDDISAGK----LKAAEAINGELYTHAGVS 1306
Cdd:cd07425     71 ILLLGNHELMNLCGdfryvhPRGLNEFGGVAKRRYALLSDGGYIGRylrtHPVVLVVNDILFVHGGLG 138
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1170-1260 1.82e-03

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: 39.89  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2555850900 1170 TVIGDLH--GEYTDLLKDINTgydqpLIRGRSGDItswkwngkeqsLVQVGDIVDRGAHYEQIRSTFNRLADEAaqtggN 1247
Cdd:pfam00149    4 LVIGDLHlpGQLDDLLELLKK-----LLEEGKPDL-----------VLHAGDLVDRGPPSEEVLELLERLIKYV-----P 62

                           90
                   ....*....|...
gi 2555850900 1248 VTRLIGNHELAYL 1260
Cdd:pfam00149   63 VYLVRGNHDFDYG 75
 
Name Accession Description Interval E-value
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 1171-1306 4.02e-12

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: 67.32  E-value: 4.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2555850900 1171 VIGDLHGEYtDLLKDI--NTGydqpLIrgrsgDITSWkWNGKEQSLVQVGDIVDRGAHYEQIRSTFNRLADEAAQTGGNV 1248
Cdd:cd07425      2 AIGDLHGDL-DRLRTIlkLAG----VI-----DSNDR-WIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKAGGKV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2555850900 1249 TRLIGNHELAYLTG------EKIPGIDYSNAPTIRKGILDDISAGK----LKAAEAINGELYTHAGVS 1306
Cdd:cd07425     71 ILLLGNHELMNLCGdfryvhPRGLNEFGGVAKRRYALLSDGGYIGRylrtHPVVLVVNDILFVHGGLG 138
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 1170-1399 1.67e-07

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: 54.30  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2555850900 1170 TVIGDLHGEYTDLLKDINTGydqplirGRSGDITswkwngkeqsLVQVGDIVDRGahyEQIRSTFNRLADEAAQTGGNVT 1249
Cdd:cd00144      1 IVVGDIHGCFDDLLRLLEKL-------GFPPEDK----------YLFLGDYVDRG---PDSVEVIDLLLALKILYPDNVF 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2555850900 1250 RLIGNHELAYLTGEKIPGIDYSNAPTIRKG--ILDDISA--GKLKAAEAINGE-LYTHAGVSlekfPEWRGKDAAYIAAD 1324
Cdd:cd00144     61 LLRGNHEFMLLNFLYGFYDERTLRCLRKGGeeLWREFNEvfNYLPLAALVDGKiLCVHGGLS----PDLTLLDQIRNIRP 136

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2555850900 1325 INRRFNKALEQNKWIDHIFDKGSGERGYKGIGGPFWlrTKETSAEAINLGYK-QYFGHTPRPSGINEEAS-NAINVD 1399
Cdd:cd00144    137 IENPDDQLVEDLLWSDPDESVGDFESSSRGGGYLFG--EDAVDEFLKKNGLKlIVRGHTPVEGGYEFLHGgKLITIF 211
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 1202-1273 2.85e-04

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that belongs 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 44.63  E-value: 2.85e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2555850900 1202 ITSWKWNGKEQSLVQVGDIVDRGAHYEQIRSTFNRLADEAAQTGGNVTRLIGNHELAYLTGEKIPGIDYSNA 1273
Cdd:cd07396     38 VEEWNRESNLAFVVQLGDIIDGYNAKDRSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNG 109
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1170-1260 1.82e-03

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: 39.89  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2555850900 1170 TVIGDLH--GEYTDLLKDINTgydqpLIRGRSGDItswkwngkeqsLVQVGDIVDRGAHYEQIRSTFNRLADEAaqtggN 1247
Cdd:pfam00149    4 LVIGDLHlpGQLDDLLELLKK-----LLEEGKPDL-----------VLHAGDLVDRGPPSEEVLELLERLIKYV-----P 62

                           90
                   ....*....|...
gi 2555850900 1248 VTRLIGNHELAYL 1260
Cdd:pfam00149   63 VYLVRGNHDFDYG 75
 
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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