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Conserved domains on  [gi|15595741|ref|NP_249235|]
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hypothetical protein PA0544 [Pseudomonas aeruginosa PAO1]

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 ...
 3-232 2.10e-36

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 cd07404:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 201  Bit Score: 127.45  E-value: 2.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741   3 IRLLSDLHHEHFDGRRQLPEV----EADVVVLAGDIHSHLEGLHWARE----TFADSEIVYVAGNHEFYSSEMTDLTQAM 74
Cdd:cd07404   1 LQIASDLHLEVEQNLAKLKFFpkvpDADILILAGDIGRLTDAEAWDNFldlqSFQFEPVYYVPGNHEFYGGSLDITLDAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741  75 RNIARALE-IHFLENDEARIGPARFLGATLWTDFqlygadgyaPAHELALQSMpdfsCIDwfggDFTpeqsialhqasrd 153
Cdd:cd07404  81 RMAAQDLSnVHYLNNQEVVLDDVRILGCTLWSDF---------DPDGEDIVQR----KLN----DFR------------- 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741 154 wlaeqlarphdGPTLVVSHHAPSALS-IPPQFVGNPLSPAFASNLDELV--AQADYWLHGHVHDALDYRIGRARVLANPG 230
Cdd:cd07404 131 -----------GATVVVTHHAPSPRStSDNYADGLPKNAAFHVDLKDLIlaPPIDLWIHGHTHFNTDYSVGGTRVVSNQL 199


                ..
gi 15595741 231 GY 232
Cdd:cd07404 200 GY 201
 
Name Accession Description Interval E-value
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 3-232 2.10e-36

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. 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: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 127.45  E-value: 2.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741   3 IRLLSDLHHEHFDGRRQLPEV----EADVVVLAGDIHSHLEGLHWARE----TFADSEIVYVAGNHEFYSSEMTDLTQAM 74
Cdd:cd07404   1 LQIASDLHLEVEQNLAKLKFFpkvpDADILILAGDIGRLTDAEAWDNFldlqSFQFEPVYYVPGNHEFYGGSLDITLDAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741  75 RNIARALE-IHFLENDEARIGPARFLGATLWTDFqlygadgyaPAHELALQSMpdfsCIDwfggDFTpeqsialhqasrd 153
Cdd:cd07404  81 RMAAQDLSnVHYLNNQEVVLDDVRILGCTLWSDF---------DPDGEDIVQR----KLN----DFR------------- 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741 154 wlaeqlarphdGPTLVVSHHAPSALS-IPPQFVGNPLSPAFASNLDELV--AQADYWLHGHVHDALDYRIGRARVLANPG 230
Cdd:cd07404 131 -----------GATVVVTHHAPSPRStSDNYADGLPKNAAFHVDLKDLIlaPPIDLWIHGHTHFNTDYSVGGTRVVSNQL 199


                ..
gi 15595741 231 GY 232
Cdd:cd07404 200 GY 201
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-236 1.12e-20

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 86.61  E-value: 1.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741   2 KIRLLSDLHHEHFDGRRQLPEV---EADVVVLAGDI--HSHLEGLHWARETFA--DSEIVYVAGNHEFYSsemtdltqaM 74
Cdd:COG2129   1 KILAVSDLHGNFDLLEKLLELAraeDADLVILAGDLtdFGTAEEAREVLEELAalGVPVLAVPGNHDDPE---------V 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741  75 RNIARALEIHFLENDEARIGPARFLGATlwtdfqlygadgyapahelalqsmpdfscidwfGGDFTPEQSIalHQASRDW 154
Cdd:COG2129  72 LDALEESGVHNLHGRVVEIGGLRIAGLG---------------------------------GSRPTPFGTP--YEYTEEE 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741 155 LAEQLARPH-DGPTLVVSHHAPSALSIPPQFVGNPL-SPAFASNLDELvaQADYWLHGHVHDALDY-RIGRARVLaNPGG 231
Cdd:COG2129 117 IEERLAKLReKDVDILLTHAPPYGTTLDRVEDGPHVgSKALRELIEEF--QPKLVLHGHIHESRGVdKIGGTRVV-NPGS 193


                ....*
gi 15595741 232 YPHER 236
Cdd:COG2129 194 LAEGY 198
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-67 1.83e-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: 37.19  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595741     1 MKIRLLSDLH-HEHFDGRRQL-----PEVEADVVVLAGDIHSHLEGLHWARETFAD----SEIVYVAGNHEFYSSEM 67
Cdd:pfam00149   1 MRILVIGDLHlPGQLDDLLELlkkllEEGKPDLVLHAGDLVDRGPPSEEVLELLERlikyVPVYLVRGNHDFDYGEC 77
 
Name Accession Description Interval E-value
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 3-232 2.10e-36

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. 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: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 127.45  E-value: 2.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741   3 IRLLSDLHHEHFDGRRQLPEV----EADVVVLAGDIHSHLEGLHWARE----TFADSEIVYVAGNHEFYSSEMTDLTQAM 74
Cdd:cd07404   1 LQIASDLHLEVEQNLAKLKFFpkvpDADILILAGDIGRLTDAEAWDNFldlqSFQFEPVYYVPGNHEFYGGSLDITLDAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741  75 RNIARALE-IHFLENDEARIGPARFLGATLWTDFqlygadgyaPAHELALQSMpdfsCIDwfggDFTpeqsialhqasrd 153
Cdd:cd07404  81 RMAAQDLSnVHYLNNQEVVLDDVRILGCTLWSDF---------DPDGEDIVQR----KLN----DFR------------- 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741 154 wlaeqlarphdGPTLVVSHHAPSALS-IPPQFVGNPLSPAFASNLDELV--AQADYWLHGHVHDALDYRIGRARVLANPG 230
Cdd:cd07404 131 -----------GATVVVTHHAPSPRStSDNYADGLPKNAAFHVDLKDLIlaPPIDLWIHGHTHFNTDYSVGGTRVVSNQL 199


                ..
gi 15595741 231 GY 232
Cdd:cd07404 200 GY 201
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-236 1.12e-20

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 86.61  E-value: 1.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741   2 KIRLLSDLHHEHFDGRRQLPEV---EADVVVLAGDI--HSHLEGLHWARETFA--DSEIVYVAGNHEFYSsemtdltqaM 74
Cdd:COG2129   1 KILAVSDLHGNFDLLEKLLELAraeDADLVILAGDLtdFGTAEEAREVLEELAalGVPVLAVPGNHDDPE---------V 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741  75 RNIARALEIHFLENDEARIGPARFLGATlwtdfqlygadgyapahelalqsmpdfscidwfGGDFTPEQSIalHQASRDW 154
Cdd:COG2129  72 LDALEESGVHNLHGRVVEIGGLRIAGLG---------------------------------GSRPTPFGTP--YEYTEEE 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741 155 LAEQLARPH-DGPTLVVSHHAPSALSIPPQFVGNPL-SPAFASNLDELvaQADYWLHGHVHDALDY-RIGRARVLaNPGG 231
Cdd:COG2129 117 IEERLAKLReKDVDILLTHAPPYGTTLDRVEDGPHVgSKALRELIEEF--QPKLVLHGHIHESRGVdKIGGTRVV-NPGS 193


                ....*
gi 15595741 232 YPHER 236
Cdd:COG2129 194 LAEGY 198
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-240 9.97e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 73.96  E-value: 9.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741   1 MKIRLLSDLHHEHFDGRRQLPEVEA----------DVVVLAGDI--HSHLEGLHWARETFADSEI--VYVAGNHEFYSSE 66
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLAAaladinaprpDFVVVTGDLtdDGEPEEYAAAREILARLGVpvYVVPGNHDIRAAM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741  67 MTDLTQAMRNIARA-LEIHFlendeaRIGPARFLGatlwtdfqlygadgyapahelaLQSmpdfSCIDWFGGDFTPEQsi 145
Cdd:COG1409  81 AEAYREYFGDLPPGgLYYSF------DYGGVRFIG----------------------LDS----NVPGRSSGELGPEQ-- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741 146 alhqasRDWLAEQLARPHDGPTLVVSHHAPSALSIPPQFVGNPLSPAFASNLDElvAQADYWLHGHVHDALDYRIGRARV 225
Cdd:COG1409 127 ------LAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEELLALLAR--YGVDLVLSGHVHRYERTRRDGVPY 198

                       250
                ....*....|....*..
gi 15595741 226 LANP--GGYPHERGGFR 240
Cdd:COG1409 199 IVAGstGGQVRLPPGYR 215
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
1-128 4.23e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 55.57  E-value: 4.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741   1 MKIRLLSDLHHEHFDGRRQLPEV-------EADVVVLAGD-IHSHLEGLHWARETFAD----SEIVYVAGNHEFYSSemt 68
Cdd:COG1408  43 LRIVQLSDLHLGPFIGGERLERLvekinalKPDLVVLTGDlVDGSVAELEALLELLKKlkapLGVYAVLGNHDYYAG--- 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595741  69 dlTQAMRNIARALEIHFLENDEARIGPArflGATLWtdfqLYGAD----GYAPAHELALQSMPD 128
Cdd:COG1408 120 --LEELRAALEEAGVRVLRNEAVTLERG---GDRLN----LAGVDdphaGRFPDLEKALAGVPP 174
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 2-94 4.76e-06

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: 46.12  E-value: 4.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741   2 KIRLLSDLHHEHFDGRRQLPEV-------EADVVVLAGDIhshLEGLHWARETFADS--------EIVYVAGNHEFYSSE 66
Cdd:cd07385   3 RIVQLSDIHLGPFVGRTRLQKVvrkvnelNPDLIVITGDL---VDGDVSVLRLLASPlsklkaplGVYFVLGNHDYYSGD 79

                        90       100
                ....*....|....*....|....*...
gi 15595741  67 MTDLTQAMRNIaralEIHFLENDEARIG 94
Cdd:cd07385  80 VEVWIAALEKA----GITVLRNESVELS 103
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 153-230 1.83e-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: 41.49  E-value: 1.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595741 153 DWLAEQLARPHDGPTLVVSHHAPSALSIPPqFVGNPLspAFASNLDELVA---QADYWLHGHVHDALDYRIGRARVLANP 229
Cdd:cd07402 132 DWLEAALAEAPDRPTLIFLHHPPFPLGIPW-MDAIRL--RNSQALFAVLArhpQVKAILCGHIHRPISGSFRGIPFSTAP 208


                .
gi 15595741 230 G 230
Cdd:cd07402 209 S 209
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-67 1.83e-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: 37.19  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595741     1 MKIRLLSDLH-HEHFDGRRQL-----PEVEADVVVLAGDIHSHLEGLHWARETFAD----SEIVYVAGNHEFYSSEM 67
Cdd:pfam00149   1 MRILVIGDLHlPGQLDDLLELlkkllEEGKPDLVLHAGDLVDRGPPSEEVLELLERlikyVPVYLVRGNHDFDYGEC 77
 
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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