NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|86564684|ref|NP_001033531|]
View 

Calcineurin-like phosphoesterase domain-containing protein [Caenorhabditis elegans]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 11444094)

metallophosphatase family protein containing an active site consisting of two metal ions

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
117-176 5.94e-08

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 53.16  E-value: 5.94e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86564684 117 QRQALDALIGSM-DYKPAALIINGDLTDFGHLHQLHEFRKvWYDNFPIPLLLGLGNHDYDN 176
Cdd:COG1409  19 TAEVLAAALADInAPRPDFVVVTGDLTDDGEPEEYAAARE-ILARLGVPVYVVPGNHDIRA 78
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
117-176 5.94e-08

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 53.16  E-value: 5.94e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86564684 117 QRQALDALIGSM-DYKPAALIINGDLTDFGHLHQLHEFRKvWYDNFPIPLLLGLGNHDYDN 176
Cdd:COG1409  19 TAEVLAAALADInAPRPDFVVVTGDLTDDGEPEEYAAARE-ILARLGVPVYVVPGNHDIRA 78
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 111-174 3.72e-04

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 41.88  E-value: 3.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86564684 111 RFANRVQR-QALDALigsmdykPAALIINGDLTDFGHLHQLHEFRKVwYDNFPIPLLLGLGNHDY 174
Cdd:cd07402  25 RLAAAVAQvNALHPR-------PDLVVVTGDLSDDGSPESYERLREL-LAPLPAPVYWIPGNHDD 81
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
117-176 5.94e-08

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 53.16  E-value: 5.94e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86564684 117 QRQALDALIGSM-DYKPAALIINGDLTDFGHLHQLHEFRKvWYDNFPIPLLLGLGNHDYDN 176
Cdd:COG1409  19 TAEVLAAALADInAPRPDFVVVTGDLTDDGEPEEYAAARE-ILARLGVPVYVVPGNHDIRA 78
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
129-175 2.67e-04

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 41.92  E-value: 2.67e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 86564684 129 DYKPAALIINGDLTDFGHLHQLHEFRKvWYDNFPIPLLLGLGNHDYD 175
Cdd:COG2129  24 AEDADLVILAGDLTDFGTAEEAREVLE-ELAALGVPVLAVPGNHDDP 69
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 111-174 3.72e-04

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 41.88  E-value: 3.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86564684 111 RFANRVQR-QALDALigsmdykPAALIINGDLTDFGHLHQLHEFRKVwYDNFPIPLLLGLGNHDY 174
Cdd:cd07402  25 RLAAAVAQvNALHPR-------PDLVVVTGDLSDDGSPESYERLREL-LAPLPAPVYWIPGNHDD 81
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 130-173 1.11e-03

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: 38.79  E-value: 1.11e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 86564684 130 YKPAALIINGDLTDFGHLHQLHEFRKVWYDNFPIPLLLGLGNHD 173
Cdd:cd00838  25 EKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHD 68
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH