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Conserved domains on  [gi|503052671|ref|WP_013287647|]
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metallophosphoesterase [Micromonospora aurantiaca]

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

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List of domain hits

 Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
219-472 1.14e-15

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


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 76.65  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 219 LLHVTDPHYATGrfrsehqwrleteDGATRPTMVDAISDALARDQrsVGAVLVTGDLTYVAHRDEFAAARAglfkltnGL 298
Cdd:COG1409    3 FAHISDLHLGAP-------------DGSDTAEVLAAALADINAPR--PDFVVVTGDLTDDGEPEEYAAARE-------IL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 299 LGLGMEhLVVIPGNHDIAWTRGDsyeygapvevapaaataNYREFFRALYGYPasphlsmaRRFIFPGGNlVDIAAVNSS 378
Cdd:COG1409   61 ARLGVP-VYVVPGNHDIRAAMAE-----------------AYREYFGDLPPGG--------LYYSFDYGG-VRFIGLDSN 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 379 sleqgqsflagmgrVQESAYREVTSA-LAW-----SNPGSALRVLALHHHLAltEDLESPDEYATgfgiaIDAPRIQRLA 452
Cdd:COG1409  114 --------------VPGRSSGELGPEqLAWleeelAAAPAKPVIVFLHHPPY--STGSGSDRIGL-----RNAEELLALL 172

                        250       260
                 ....*....|....*....|
gi 503052671 453 ARDGVHLAVHGHKHRAFVWR 472
Cdd:COG1409  173 ARYGVDLVLSGHVHRYERTR 192
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
219-472 1.14e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 76.65  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 219 LLHVTDPHYATGrfrsehqwrleteDGATRPTMVDAISDALARDQrsVGAVLVTGDLTYVAHRDEFAAARAglfkltnGL 298
Cdd:COG1409    3 FAHISDLHLGAP-------------DGSDTAEVLAAALADINAPR--PDFVVVTGDLTDDGEPEEYAAARE-------IL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 299 LGLGMEhLVVIPGNHDIAWTRGDsyeygapvevapaaataNYREFFRALYGYPasphlsmaRRFIFPGGNlVDIAAVNSS 378
Cdd:COG1409   61 ARLGVP-VYVVPGNHDIRAAMAE-----------------AYREYFGDLPPGG--------LYYSFDYGG-VRFIGLDSN 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 379 sleqgqsflagmgrVQESAYREVTSA-LAW-----SNPGSALRVLALHHHLAltEDLESPDEYATgfgiaIDAPRIQRLA 452
Cdd:COG1409  114 --------------VPGRSSGELGPEqLAWleeelAAAPAKPVIVFLHHPPY--STGSGSDRIGL-----RNAEELLALL 172

                        250       260
                 ....*....|....*....|
gi 503052671 453 ARDGVHLAVHGHKHRAFVWR 472
Cdd:COG1409  173 ARYGVDLVLSGHVHRYERTR 192
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 219-315 1.45e-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: 47.67  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 219 LLHVTDPHYATGRFRSEHQWRLETEDGATRPTMVdaisdalardqrsvgavLVTGDLTYVAHRDEFAAARAglFkltngL 298
Cdd:cd07400    1 IAHISDLHFGEERKPEVLELNLLDEINALKPDLV-----------------VVTGDLTQRARPAEFEEARE--F-----L 56

                         90
                 ....*....|....*..
gi 503052671 299 LGLGMEHLVVIPGNHDI 315
Cdd:cd07400   57 DALEPEPVVVVPGNHDA 73
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
219-472 1.14e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 76.65  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 219 LLHVTDPHYATGrfrsehqwrleteDGATRPTMVDAISDALARDQrsVGAVLVTGDLTYVAHRDEFAAARAglfkltnGL 298
Cdd:COG1409    3 FAHISDLHLGAP-------------DGSDTAEVLAAALADINAPR--PDFVVVTGDLTDDGEPEEYAAARE-------IL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 299 LGLGMEhLVVIPGNHDIAWTRGDsyeygapvevapaaataNYREFFRALYGYPasphlsmaRRFIFPGGNlVDIAAVNSS 378
Cdd:COG1409   61 ARLGVP-VYVVPGNHDIRAAMAE-----------------AYREYFGDLPPGG--------LYYSFDYGG-VRFIGLDSN 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 379 sleqgqsflagmgrVQESAYREVTSA-LAW-----SNPGSALRVLALHHHLAltEDLESPDEYATgfgiaIDAPRIQRLA 452
Cdd:COG1409  114 --------------VPGRSSGELGPEqLAWleeelAAAPAKPVIVFLHHPPY--STGSGSDRIGL-----RNAEELLALL 172

                        250       260
                 ....*....|....*....|
gi 503052671 453 ARDGVHLAVHGHKHRAFVWR 472
Cdd:COG1409  173 ARYGVDLVLSGHVHRYERTR 192
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 219-315 1.45e-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: 47.67  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 219 LLHVTDPHYATGRFRSEHQWRLETEDGATRPTMVdaisdalardqrsvgavLVTGDLTYVAHRDEFAAARAglFkltngL 298
Cdd:cd07400    1 IAHISDLHFGEERKPEVLELNLLDEINALKPDLV-----------------VVTGDLTQRARPAEFEEARE--F-----L 56

                         90
                 ....*....|....*..
gi 503052671 299 LGLGMEHLVVIPGNHDI 315
Cdd:cd07400   57 DALEPEPVVVVPGNHDA 73
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 219-314 1.07e-03

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: 40.72  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503052671 219 LLHVTDPHyatgrFRSEHQWRLETEDGATRptmVDAISDALARDQRSVGAVLVTGDLTYVAHRDEFAAARAGLFKLTNGL 298
Cdd:cd07402    1 IAQISDTH-----LFAPGEGALLGVDTAAR---LAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPV 72

                         90
                 ....*....|....*.
gi 503052671 299 LglgmehlvVIPGNHD 314
Cdd:cd07402   73 Y--------WIPGNHD 80
 
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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