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Conserved domains on  [gi|497580624|ref|WP_009894808|]
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metallophosphoesterase [Clostridioides difficile]

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 ...
 148-276 8.46e-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.


The actual alignment was detected with superfamily member cd07391:

Pssm-ID: 472684  Cd Length: 175  Bit Score: 43.07  E-value: 8.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497580624 148 MLISDIHYGLEIinAFNRYNSEIFKIRIQYLKDKIIEYSKLHKINRLhvMLLGDLisghihnsirLENRENIVEQIIEVS 227
Cdd:cd07391    1 LVIADLHLGYEE--ELRRQGINLPRRQKERLLERLDRLLEELGPDRL--VILGDL----------KHSFGRVSRQERREV 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497580624 228 EILsefiyELSKEIDKIIVysVGGNHDRILP--KKDENLDKDNfTLLIDEY 276
Cdd:cd07391   67 PFF-----RLLAKDVDVIL--IRGNHDGGLEeiLSDVNVVVVE-GYLLGGY 109
 
Name Accession Description Interval E-value
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 148-276 8.46e-05

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family 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: 277337  Cd Length: 175  Bit Score: 43.07  E-value: 8.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497580624 148 MLISDIHYGLEIinAFNRYNSEIFKIRIQYLKDKIIEYSKLHKINRLhvMLLGDLisghihnsirLENRENIVEQIIEVS 227
Cdd:cd07391    1 LVIADLHLGYEE--ELRRQGINLPRRQKERLLERLDRLLEELGPDRL--VILGDL----------KHSFGRVSRQERREV 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497580624 228 EILsefiyELSKEIDKIIVysVGGNHDRILP--KKDENLDKDNfTLLIDEY 276
Cdd:cd07391   67 PFF-----RLLAKDVDVIL--IRGNHDGGLEeiLSDVNVVVVE-GYLLGGY 109
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
147-282 1.08e-04

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 43.63  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497580624 147 IMLISDIHYGLEIINAFNRynseifkiriqylkdKIIEysklhKINRLH---VMLLGDLISGHihnsirlenreniVEQI 223
Cdd:COG1408   45 IVQLSDLHLGPFIGGERLE---------------RLVE-----KINALKpdlVVLTGDLVDGS-------------VAEL 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497580624 224 IEVSEILSEFiyelsKEIDKiiVYSVGGNHDRILPKKD--ENLDKDNFTLLIDEYIKLRIK 282
Cdd:COG1408   92 EALLELLKKL-----KAPLG--VYAVLGNHDYYAGLEElrAALEEAGVRVLRNEAVTLERG 145
 
Name Accession Description Interval E-value
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 148-276 8.46e-05

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family 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: 277337  Cd Length: 175  Bit Score: 43.07  E-value: 8.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497580624 148 MLISDIHYGLEIinAFNRYNSEIFKIRIQYLKDKIIEYSKLHKINRLhvMLLGDLisghihnsirLENRENIVEQIIEVS 227
Cdd:cd07391    1 LVIADLHLGYEE--ELRRQGINLPRRQKERLLERLDRLLEELGPDRL--VILGDL----------KHSFGRVSRQERREV 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497580624 228 EILsefiyELSKEIDKIIVysVGGNHDRILP--KKDENLDKDNfTLLIDEY 276
Cdd:cd07391   67 PFF-----RLLAKDVDVIL--IRGNHDGGLEeiLSDVNVVVVE-GYLLGGY 109
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 147-282 1.04e-04

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE 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: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 43.42  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497580624 147 IMLISDIHYGLeiinafnrYNSEIFkiriqylKDKIIEysklhKINRLH---VMLLGDLISGHihnsirlenreniVEQI 223
Cdd:cd07385    4 IVQLSDIHLGP--------FVGRTR-------LQKVVR-----KVNELNpdlIVITGDLVDGD-------------VSVL 50

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497580624 224 IEVSEILSEFIYELSkeidkiiVYSVGGNHD---RILPKKDENLDKDNFTLLIDEYIKLRIK 282
Cdd:cd07385   51 RLLASPLSKLKAPLG-------VYFVLGNHDyysGDVEVWIAALEKAGITVLRNESVELSRD 105
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
147-282 1.08e-04

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 43.63  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497580624 147 IMLISDIHYGLEIINAFNRynseifkiriqylkdKIIEysklhKINRLH---VMLLGDLISGHihnsirlenreniVEQI 223
Cdd:COG1408   45 IVQLSDLHLGPFIGGERLE---------------RLVE-----KINALKpdlVVLTGDLVDGS-------------VAEL 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497580624 224 IEVSEILSEFiyelsKEIDKiiVYSVGGNHDRILPKKD--ENLDKDNFTLLIDEYIKLRIK 282
Cdd:COG1408   92 EALLELLKKL-----KAPLG--VYAVLGNHDYYAGLEElrAALEEAGVRVLRNEAVTLERG 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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