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Conserved domains on  [gi|499244349|ref|WP_010941889|]
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metallophosphoesterase family protein [Geobacter sulfurreducens]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10582454)

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

CATH:  3.60.21.10
Gene Ontology:  GO:0046872|GO:0042578
PubMed:  25837850
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-146 2.78e-31

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


:

Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 109.71  E-value: 2.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349    1 MKIVVLSDTHGNQRLALSILDLHEDA-GHVVHLGDeLQDADFLEDATG-KTIIKVQGNCD----CSPAHPREVSLELAGR 74
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVvDLIIHAGD-IVAPEVLEELLElAPVLAVRGNNDaaaeFATDLPEEAVLELGGV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499244349   75 RFLLTHGDiyHVKSGLERLRERAAAVDAAVvLFGHTHVACIETTDGILYVNPG--CLKRGAGNLTYAVVTLTDG 146
Cdd:pfam12850  80 KILLTHGH--GVKDALARLLRRAEEGVAVV-VYGHTHVPGVERIGGVLFVNPGsvGGPRFGDPPTYALLDIDDG 150
 
Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-146 2.78e-31

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 109.71  E-value: 2.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349    1 MKIVVLSDTHGNQRLALSILDLHEDA-GHVVHLGDeLQDADFLEDATG-KTIIKVQGNCD----CSPAHPREVSLELAGR 74
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVvDLIIHAGD-IVAPEVLEELLElAPVLAVRGNNDaaaeFATDLPEEAVLELGGV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499244349   75 RFLLTHGDiyHVKSGLERLRERAAAVDAAVvLFGHTHVACIETTDGILYVNPG--CLKRGAGNLTYAVVTLTDG 146
Cdd:pfam12850  80 KILLTHGH--GVKDALARLLRRAEEGVAVV-VYGHTHVPGVERIGGVLFVNPGsvGGPRFGDPPTYALLDIDDG 150
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-145 1.01e-26

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain 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: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 98.11  E-value: 1.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   2 KIVVLSDTHGNQRLALSILDLHED-AGHVVHLGDELqdADFLEDATGKTIIK---VQGNCD-------CSPAHPREVSLE 70
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALELFEDgVDAVIHAGDFV--SPFVLNALLELKAPliaVRGNNDgevdqllGRPILPEFLTLE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499244349  71 LAGRRFLLTHGDIYHVKSGLERLRERAAAVDaavvLFGHTHVACIETTDGILYVNPG--CLKRGAGNlTYAVVTLTD 145
Cdd:cd00841   79 IGGLRILLTHGHLFGVLEALYLAKEGGADVV----VFGHTHVPVIERVGGTLLLNPGsvSGPRGGRP-TYAILDIEK 150
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-153 2.73e-26

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 97.68  E-value: 2.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   2 KIVVLSDTHGNQRLALSILDLHEDAG--HVVHLGD----ELQDADFLEDATGKTIIKVQGNCD-----CSPAHPREVSLE 70
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEREGvdLIVHLGDlvgyGPDPPEVLDLLRELPIVAVRGNHDgavlrGLRSLPETLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349  71 LAGRRFLLTHGDIYHV---KSGLERLRERAAAVDAAVVLFGHTHVACIETTDGILYVNPG--CLKRGAGNLTYAVVTLTD 145
Cdd:COG0622   81 LEGVRILLVHGSPNEYllpDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGsvGQPRDGDPASYAILDIDD 160


                 ....*...
gi 499244349 146 GSITAEIL 153
Cdd:COG0622  161 GEWSVEFV 168
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-151 6.15e-24

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 91.28  E-value: 6.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349    1 MKIVVLSDTHGNQR---LALSILDLHEDAGHVVHLGD--ELQDADFLEDATGKTIIkVQGNCDcSPAH--PREVSLELAG 73
Cdd:TIGR00040   1 MKILVISDTHGPLRateLPVELFNLESNVDLVIHAGDltSPFVLKEFEDLAAKVIA-VRGNND-GERDelPEEEIFEAEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   74 RRFLLTHGDIYHVKSGLERLRERAAAVDAAVVLFGHTHVACIETTDGILYVNPG--CLKRGAGNLTYAVVTLTDGSITAE 151
Cdd:TIGR00040  79 IDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGslTGPRNGNTPSYAILDVDKDKVTAL 158
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-141 8.12e-19

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 78.37  E-value: 8.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   1 MKIVVLSDTHG---NQRLALSILDlHEDAGHVVHLGDEL---------------QDADFLeDATGKTIIKVQGNCDCS-- 60
Cdd:PRK09453   1 MKLMFASDTHGslpATEKALELFA-QSGADWLVHLGDVLyhgprnplpegyapkKVAELL-NAYADKIIAVRGNCDSEvd 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349  61 ------PAHPREVSLELAGRRFLLTHGDIYHvKSGLERLREraaavdAAVVLFGHTHVACIETTDGILYVNPG--CLKRG 132
Cdd:PRK09453  79 qmllhfPIMAPYQQVLLEGKRLFLTHGHLYG-PENLPALHD------GDVLVYGHTHIPVAEKQGGIILFNPGsvSLPKG 151


                 ....*....
gi 499244349 133 AGNLTYAVV 141
Cdd:PRK09453 152 GYPASYGIL 160
 
Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-146 2.78e-31

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 109.71  E-value: 2.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349    1 MKIVVLSDTHGNQRLALSILDLHEDA-GHVVHLGDeLQDADFLEDATG-KTIIKVQGNCD----CSPAHPREVSLELAGR 74
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVvDLIIHAGD-IVAPEVLEELLElAPVLAVRGNNDaaaeFATDLPEEAVLELGGV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499244349   75 RFLLTHGDiyHVKSGLERLRERAAAVDAAVvLFGHTHVACIETTDGILYVNPG--CLKRGAGNLTYAVVTLTDG 146
Cdd:pfam12850  80 KILLTHGH--GVKDALARLLRRAEEGVAVV-VYGHTHVPGVERIGGVLFVNPGsvGGPRFGDPPTYALLDIDDG 150
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-145 1.01e-26

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain 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: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 98.11  E-value: 1.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   2 KIVVLSDTHGNQRLALSILDLHED-AGHVVHLGDELqdADFLEDATGKTIIK---VQGNCD-------CSPAHPREVSLE 70
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALELFEDgVDAVIHAGDFV--SPFVLNALLELKAPliaVRGNNDgevdqllGRPILPEFLTLE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499244349  71 LAGRRFLLTHGDIYHVKSGLERLRERAAAVDaavvLFGHTHVACIETTDGILYVNPG--CLKRGAGNlTYAVVTLTD 145
Cdd:cd00841   79 IGGLRILLTHGHLFGVLEALYLAKEGGADVV----VFGHTHVPVIERVGGTLLLNPGsvSGPRGGRP-TYAILDIEK 150
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-153 2.73e-26

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 97.68  E-value: 2.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   2 KIVVLSDTHGNQRLALSILDLHEDAG--HVVHLGD----ELQDADFLEDATGKTIIKVQGNCD-----CSPAHPREVSLE 70
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEREGvdLIVHLGDlvgyGPDPPEVLDLLRELPIVAVRGNHDgavlrGLRSLPETLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349  71 LAGRRFLLTHGDIYHV---KSGLERLRERAAAVDAAVVLFGHTHVACIETTDGILYVNPG--CLKRGAGNLTYAVVTLTD 145
Cdd:COG0622   81 LEGVRILLVHGSPNEYllpDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGsvGQPRDGDPASYAILDIDD 160


                 ....*...
gi 499244349 146 GSITAEIL 153
Cdd:COG0622  161 GEWSVEFV 168
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-151 6.15e-24

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 91.28  E-value: 6.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349    1 MKIVVLSDTHGNQR---LALSILDLHEDAGHVVHLGD--ELQDADFLEDATGKTIIkVQGNCDcSPAH--PREVSLELAG 73
Cdd:TIGR00040   1 MKILVISDTHGPLRateLPVELFNLESNVDLVIHAGDltSPFVLKEFEDLAAKVIA-VRGNND-GERDelPEEEIFEAEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   74 RRFLLTHGDIYHVKSGLERLRERAAAVDAAVVLFGHTHVACIETTDGILYVNPG--CLKRGAGNLTYAVVTLTDGSITAE 151
Cdd:TIGR00040  79 IDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGslTGPRNGNTPSYAILDVDKDKVTAL 158
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-141 8.12e-19

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 78.37  E-value: 8.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   1 MKIVVLSDTHG---NQRLALSILDlHEDAGHVVHLGDEL---------------QDADFLeDATGKTIIKVQGNCDCS-- 60
Cdd:PRK09453   1 MKLMFASDTHGslpATEKALELFA-QSGADWLVHLGDVLyhgprnplpegyapkKVAELL-NAYADKIIAVRGNCDSEvd 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349  61 ------PAHPREVSLELAGRRFLLTHGDIYHvKSGLERLREraaavdAAVVLFGHTHVACIETTDGILYVNPG--CLKRG 132
Cdd:PRK09453  79 qmllhfPIMAPYQQVLLEGKRLFLTHGHLYG-PENLPALHD------GDVLVYGHTHIPVAEKQGGIILFNPGsvSLPKG 151


                 ....*....
gi 499244349 133 AGNLTYAVV 141
Cdd:PRK09453 152 GYPASYGIL 160
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-148 1.22e-04

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 40.38  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   2 KIVVLSDTHGNQRLALSILDL--HEDAGHVVHLGD------ELQDADFLE--DATGKTIIKVQGNCDcSPAHPREV---- 67
Cdd:COG2129    1 KILAVSDLHGNFDLLEKLLELarAEDADLVILAGDltdfgtAEEAREVLEelAALGVPVLAVPGNHD-DPEVLDALeesg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349  68 -------SLELAGRRF------------------------------------LLTH-----------GDIYHVksGLERL 93
Cdd:COG2129   80 vhnlhgrVVEIGGLRIaglggsrptpfgtpyeyteeeieerlaklrekdvdiLLTHappygttldrvEDGPHV--GSKAL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499244349  94 RERAAAVDAAVVLFGHTHVAC-IETTDGILYVNPGCLKRGagnlTYAVVTLTDGSI 148
Cdd:COG2129  158 RELIEEFQPKLVLHGHIHESRgVDKIGGTRVVNPGSLAEG----YYALIDLEDRSV 209
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-127 8.06e-04

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: 37.63  E-value: 8.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499244349   4 VVLSDTHGN----QRLALSILDLHEDAGHVVHLGD---------ELQDADFLEDATGKTIIKVQGNCDcspahprevsle 70
Cdd:cd00838    1 LVISDIHGNlealEAVLEAALAKAEKPDLVICLGDlvdygpdpeEVELKALRLLLAGIPVYVVPGNHD------------ 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499244349  71 lagrrFLLTHGDIYHVKSGLERLRERAAAVDAAVV--------LFGHTHVACIETTD--GILYVNPG 127
Cdd:cd00838   69 -----ILVTHGPPYDPLDEGSPGEDPGSEALLELLdkygpdlvLSGHTHVPGRREVDkgGTLVVNPG 130
 
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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