3',5'-cyclic-AMP phosphodiesterase [Ectopseudomonas oleovorans]
Protein Classification
phosphodiesterase( domain architecture ID 10164715)
phosphodiesterase of the metallophosphatase (MPP) superfamily, related to Enterobacter aerogenes glycerophosphodiesterase Q and Escherichia coli 3',5'-cyclic AMP phosphodiesterase CpdA
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| MPP_GpdQ | cd07402 | Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ... |
15-249 | 1.44e-95 | ||||
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: 280.70 E-value: 1.44e-95
|
||||||||
| Name | Accession | Description | Interval | E-value | |||||
| MPP_GpdQ | cd07402 | Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ... |
15-249 | 1.44e-95 | |||||
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: 280.70 E-value: 1.44e-95
|
|||||||||
| PRK11148 | PRK11148 | cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional |
6-271 | 5.65e-95 | |||||
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional Pssm-ID: 182997 [Multi-domain] Cd Length: 275 Bit Score: 280.67 E-value: 5.65e-95
|
|||||||||
| CpdA | COG1409 | 3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; |
13-259 | 1.86e-66 | |||||
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; Pssm-ID: 441019 [Multi-domain] Cd Length: 234 Bit Score: 206.47 E-value: 1.86e-66
|
|||||||||
| Metallophos | pfam00149 | Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ... |
15-94 | 1.39e-05 | |||||
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: 43.36 E-value: 1.39e-05
|
|||||||||
| sbcd | TIGR00619 | exonuclease SbcD; All proteins in this family for which functions are known are ... |
15-94 | 1.53e-03 | |||||
exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273178 [Multi-domain] Cd Length: 253 Bit Score: 38.94 E-value: 1.53e-03
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| MPP_GpdQ | cd07402 | Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ... |
15-249 | 1.44e-95 | |||||
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: 280.70 E-value: 1.44e-95
|
|||||||||
| PRK11148 | PRK11148 | cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional |
6-271 | 5.65e-95 | |||||
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional Pssm-ID: 182997 [Multi-domain] Cd Length: 275 Bit Score: 280.67 E-value: 5.65e-95
|
|||||||||
| CpdA | COG1409 | 3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; |
13-259 | 1.86e-66 | |||||
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; Pssm-ID: 441019 [Multi-domain] Cd Length: 234 Bit Score: 206.47 E-value: 1.86e-66
|
|||||||||
| COG2129 | COG2129 | Predicted phosphoesterase, related to the Icc protein [General function prediction only]; |
38-208 | 4.70e-09 | |||||
Predicted phosphoesterase, related to the Icc protein [General function prediction only]; Pssm-ID: 441732 [Multi-domain] Cd Length: 211 Bit Score: 55.02 E-value: 4.70e-09
|
|||||||||
| MPP_YkuE_C | cd07385 | Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ... |
15-201 | 5.76e-08 | |||||
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: 51.90 E-value: 5.76e-08
|
|||||||||
| MPP_1 | cd07400 | Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ... |
15-96 | 1.43e-06 | |||||
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain] Cd Length: 138 Bit Score: 46.52 E-value: 1.43e-06
|
|||||||||
| YaeI | COG1408 | Predicted phosphohydrolase, MPP superfamily [General function prediction only]; |
15-94 | 3.94e-06 | |||||
Predicted phosphohydrolase, MPP superfamily [General function prediction only]; Pssm-ID: 441018 [Multi-domain] Cd Length: 268 Bit Score: 47.10 E-value: 3.94e-06
|
|||||||||
| Metallophos | pfam00149 | Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ... |
15-94 | 1.39e-05 | |||||
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: 43.36 E-value: 1.39e-05
|
|||||||||
| MPP_superfamily | cd00838 | metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ... |
16-94 | 1.50e-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. Pssm-ID: 277317 [Multi-domain] Cd Length: 130 Bit Score: 43.41 E-value: 1.50e-05
|
|||||||||
| SbcD | COG0420 | DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; |
19-202 | 1.14e-04 | |||||
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; Pssm-ID: 440189 [Multi-domain] Cd Length: 250 Bit Score: 42.59 E-value: 1.14e-04
|
|||||||||
| MPP_Dcr2 | cd07383 | Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ... |
16-95 | 8.88e-04 | |||||
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain] Cd Length: 202 Bit Score: 39.58 E-value: 8.88e-04
|
|||||||||
| sbcd | TIGR00619 | exonuclease SbcD; All proteins in this family for which functions are known are ... |
15-94 | 1.53e-03 | |||||
exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273178 [Multi-domain] Cd Length: 253 Bit Score: 38.94 E-value: 1.53e-03
|
|||||||||
| MPP_Mre11_N | cd00840 | Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ... |
19-202 | 1.86e-03 | |||||
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 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: 277319 [Multi-domain] Cd Length: 186 Bit Score: 38.40 E-value: 1.86e-03
|
|||||||||
| Blast search parameters | ||||
|
