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Conserved domains on  [gi|1819555833|ref|WP_165243094|]
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metallophosphoesterase [Streptomyces coryli]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10005392)

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

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0016787|GO:0046872|GO:0042578
PubMed:  25837850|8003970
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-246 1.78e-33

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


:

Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 120.50  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833   2 RVHVVSDVHGNAGDLAKAGE-----GADALVCLGDLILFldyadhsrgifpdlfgtenatkivrlrteRRFDEARDfgrr 76
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLElaraeDADLVILAGDLTDF-----------------------------GTAEEARE---- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833  77 lwagldrdaaiesavrrqYTELFAAFPTPTYATYGNVDIPRLWPEYAHDGVTVLDGERVEIGGLVFGFVGGGLRTPMNTP 156
Cdd:COG2129    48 ------------------VLEELAALGVPVLAVPGNHDDPEVLDALEESGVHNLHGRVVEIGGLRIAGLGGSRPTPFGTP 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833 157 FEIDDDTYAAKVAAL--GDVDVLCSHIPPQIPELcyDVVARRFERGSEALLDAIHTVRPRYALFGHVHQPLAqRMRIGQT 234
Cdd:COG2129   110 YEYTEEEIEERLAKLreKDVDILLTHAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRG-VDKIGGT 186

                         250
                  ....*....|..
gi 1819555833 235 ECVNVGHFASRG 246
Cdd:COG2129   187 RVVNPGSLAEGY 198
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-246 1.78e-33

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 120.50  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833   2 RVHVVSDVHGNAGDLAKAGE-----GADALVCLGDLILFldyadhsrgifpdlfgtenatkivrlrteRRFDEARDfgrr 76
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLElaraeDADLVILAGDLTDF-----------------------------GTAEEARE---- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833  77 lwagldrdaaiesavrrqYTELFAAFPTPTYATYGNVDIPRLWPEYAHDGVTVLDGERVEIGGLVFGFVGGGLRTPMNTP 156
Cdd:COG2129    48 ------------------VLEELAALGVPVLAVPGNHDDPEVLDALEESGVHNLHGRVVEIGGLRIAGLGGSRPTPFGTP 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833 157 FEIDDDTYAAKVAAL--GDVDVLCSHIPPQIPELcyDVVARRFERGSEALLDAIHTVRPRYALFGHVHQPLAqRMRIGQT 234
Cdd:COG2129   110 YEYTEEEIEERLAKLreKDVDILLTHAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRG-VDKIGGT 186

                         250
                  ....*....|..
gi 1819555833 235 ECVNVGHFASRG 246
Cdd:COG2129   187 RVVNPGSLAEGY 198
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 97-240 3.08e-09

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. 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: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 55.01  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833  97 ELFAAFPTPTYATYGNVDIPRLwPEYAHDGVTVLDGERVEIGGLVFGFVGGGLRTPMNTPFEIDDDTYAAK----VAALG 172
Cdd:cd07392    47 NLLLAIGAPVLAVPGNCDTPEV-LGELNSAGLNIHGKVVEVGGYIFVGVGGSNPTPFNTPFEYSEEEIYSKlgllNVKLP 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819555833 173 DVDVLCSHIPPQIPELcyDVVARRFERGSEALLDAIHTVRPRYALFGHVHQPLAQRmRIGQTECVNVG 240
Cdd:cd07392   126 GRLILVTHAPPYGTAV--DRVSSGVHVGSKAIRKFIEEFQPLLCICGHIHESRGID-KIGNTLVVNPG 190
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-246 1.78e-33

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 120.50  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833   2 RVHVVSDVHGNAGDLAKAGE-----GADALVCLGDLILFldyadhsrgifpdlfgtenatkivrlrteRRFDEARDfgrr 76
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLElaraeDADLVILAGDLTDF-----------------------------GTAEEARE---- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833  77 lwagldrdaaiesavrrqYTELFAAFPTPTYATYGNVDIPRLWPEYAHDGVTVLDGERVEIGGLVFGFVGGGLRTPMNTP 156
Cdd:COG2129    48 ------------------VLEELAALGVPVLAVPGNHDDPEVLDALEESGVHNLHGRVVEIGGLRIAGLGGSRPTPFGTP 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833 157 FEIDDDTYAAKVAAL--GDVDVLCSHIPPQIPELcyDVVARRFERGSEALLDAIHTVRPRYALFGHVHQPLAqRMRIGQT 234
Cdd:COG2129   110 YEYTEEEIEERLAKLreKDVDILLTHAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRG-VDKIGGT 186

                         250
                  ....*....|..
gi 1819555833 235 ECVNVGHFASRG 246
Cdd:COG2129   187 RVVNPGSLAEGY 198
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 97-240 3.08e-09

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. 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: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 55.01  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833  97 ELFAAFPTPTYATYGNVDIPRLwPEYAHDGVTVLDGERVEIGGLVFGFVGGGLRTPMNTPFEIDDDTYAAK----VAALG 172
Cdd:cd07392    47 NLLLAIGAPVLAVPGNCDTPEV-LGELNSAGLNIHGKVVEVGGYIFVGVGGSNPTPFNTPFEYSEEEIYSKlgllNVKLP 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819555833 173 DVDVLCSHIPPQIPELcyDVVARRFERGSEALLDAIHTVRPRYALFGHVHQPLAQRmRIGQTECVNVG 240
Cdd:cd07392   126 GRLILVTHAPPYGTAV--DRVSSGVHVGSKAIRKFIEEFQPLLCICGHIHESRGID-KIGNTLVVNPG 190
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 172-238 5.04e-08

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB 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: 277325 [Multi-domain]  Cd Length: 135  Bit Score: 50.32  E-value: 5.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833 172 GDVDVLCSHIPPQIPelcYDVVARRFERGSEALLDAIHTVRPRYALFGHVHQP---LAQRMRIGQTECVN 238
Cdd:cd07379    67 EGTDILVTHGPPYGH---LDLGSSGQRLGCEELLNTVQRVRPKLHVFGHIHEGygiERVPDTDGETTFVN 133
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 168-240 6.84e-07

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: 47.26  E-value: 6.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819555833 168 VAALGDVDVLCSHIPPQIPELCYDvvaRRFERGSEALLDAIHTVRPRYALFGHVHQPLAQRMRIGQTECVNVG 240
Cdd:cd00838    61 YVVPGNHDILVTHGPPYDPLDEGS---PGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVVNPG 130
MPP_TTHA0053 cd07403
Thermus thermophilus TTHA0053 and related proteins, metallophosphatase domain; TTHA0053 is an ...
 173-238 1.88e-06

Thermus thermophilus TTHA0053 and related proteins, metallophosphatase domain; TTHA0053 is an uncharacterized Thermus thermophilus 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: 277348  Cd Length: 130  Bit Score: 45.96  E-value: 1.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819555833 173 DVDVLCSHIPPQIPELCYDVVarrfERGSEALLDAIHTVRPRYALFGHVH----QPLAQRMRIGQTECVN 238
Cdd:cd07403    56 GLDVLLTHAPPLGPSAGEDFA----HRGFRAFLLFIRLFRPRYLIHGHTHllgaNPERRHRTPGGTEVIN 121
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
5-33 3.33e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 37.59  E-value: 3.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1819555833   5 VVSDVHGNAGDLAKA-----GEGADALVCLGDLI 33
Cdd:COG0622     4 VISDTHGNLPALEAVledleREGVDLIVHLGDLV 37
 
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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