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Conserved domains on  [gi|516388891|ref|WP_017778567|]
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MULTISPECIES: phosphodiesterase [Aeromonas]

Protein Classification

metallophosphoesterase( domain architecture ID 10013241)

metallophosphoesterase contains an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to Escherichia coli YfcE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-180 2.72e-97

phosphodiesterase; Provisional


:

Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 279.06  E-value: 2.72e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   1 MKIAILSDLHGSLSALEQVLDQLAPWQPDHYLLLGDLLNHGPRNPVPPGYAPAAVAERLNGLASRIMAVRGNCDSEVDQM 80
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNPLPEGYAPKKVAELLNAYADKIIAVRGNCDSEVDQM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891  81 LLDFPITAPYNQLLVDGRRWFVSHGHLYRPAEVP-LPAGSLFISGHTHLPVLQREGELVLMNPGSICFPRGNLAASYGRY 159
Cdd:PRK09453  81 LLHFPIMAPYQQVLLEGKRLFLTHGHLYGPENLPaLHDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGYPASYGIL 160

                        170       180
                 ....*....|....*....|.
gi 516388891 160 EDGVLGIHACADSEVLLRLAL 180
Cdd:PRK09453 161 DDNVLSVIDLEGGEVIAQVAI 181
 
Name Accession Description Interval E-value
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-180 2.72e-97

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 279.06  E-value: 2.72e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   1 MKIAILSDLHGSLSALEQVLDQLAPWQPDHYLLLGDLLNHGPRNPVPPGYAPAAVAERLNGLASRIMAVRGNCDSEVDQM 80
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNPLPEGYAPKKVAELLNAYADKIIAVRGNCDSEVDQM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891  81 LLDFPITAPYNQLLVDGRRWFVSHGHLYRPAEVP-LPAGSLFISGHTHLPVLQREGELVLMNPGSICFPRGNLAASYGRY 159
Cdd:PRK09453  81 LLHFPIMAPYQQVLLEGKRLFLTHGHLYGPENLPaLHDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGYPASYGIL 160

                        170       180
                 ....*....|....*....|.
gi 516388891 160 EDGVLGIHACADSEVLLRLAL 180
Cdd:PRK09453 161 DDNVLSVIDLEGGEVIAQVAI 181
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-160 9.84e-47

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: 150.11  E-value: 9.84e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   2 KIAILSDLHGSLSALEQVLDQLAPwQPDHYLLLGDLLNHGPRNPvppgyapaavaerLNGLASRIMAVRGNCDSEVDQML 81
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALELFED-GVDAVIHAGDFVSPFVLNA-------------LLELKAPLIAVRGNNDGEVDQLL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891  82 lDFPITAPYNQLLVDGRRWFVSHGHLYRPAEVPLPA----GSLFISGHTHLPVLQREGELVLMNPGSICFPRGnLAASYG 157
Cdd:cd00841   67 -GRPILPEFLTLEIGGLRILLTHGHLFGVLEALYLAkeggADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRG-GRPTYA 144


                 ...
gi 516388891 158 RYE 160
Cdd:cd00841  145 ILD 147
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-160 6.69e-46

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 148.91  E-value: 6.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   2 KIAILSDLHGSLSALEQVLDQLAPWQPDHYLLLGDLLNHGPRnpvppgyaPAAVAERLNGLasRIMAVRGNCDSEVDQML 81
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPD--------PPEVLDLLREL--PIVAVRGNHDGAVLRGL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891  82 LDFPITApynQLLVDGRRWFVSHGHLYRP-----------AEVPLPAGSLFISGHTHLPVLQREGELVLMNPGSICFPRG 150
Cdd:COG0622   71 RSLPETL---RLELEGVRILLVHGSPNEYllpdtpaerlrALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRD 147

                        170
                 ....*....|
gi 516388891 151 NLAASYGRYE 160
Cdd:COG0622  148 GDPASYAILD 157
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-160 3.13e-26

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: 97.38  E-value: 3.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891    1 MKIAILSDLHGSLSALEQVLDQLAPwQPDHYLLLGDLLNhgprnpvppgyapAAVAERLNGLAsRIMAVRGNCDSEVdQM 80
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKG-VVDLIIHAGDIVA-------------PEVLEELLELA-PVLAVRGNNDAAA-EF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   81 LLDFPITAPynqLLVDGRRWFVSHGHLYRPAEVPL-----PAGSLFISGHTHLPVLQREGELVLMNPGSICFPRGNLAAS 155
Cdd:pfam12850  65 ATDLPEEAV---LELGGVKILLTHGHGVKDALARLlrraeEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPT 141


                  ....*
gi 516388891  156 YGRYE 160
Cdd:pfam12850 142 YALLD 146
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-166 2.31e-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: 92.82  E-value: 2.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891    1 MKIAILSDLHGSLSALE---QVLDQLApwQPDHYLLLGDLLnhgprnpvppgyaPAAVAERLNGLASRIMAVRGNCDSEV 77
Cdd:TIGR00040   1 MKILVISDTHGPLRATElpvELFNLES--NVDLVIHAGDLT-------------SPFVLKEFEDLAAKVIAVRGNNDGER 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   78 DQMLLDFPITAPYNQLLVDGRRWFVSHGHLYRPAEVPLPAG-SLFISGHTHLPVLQREGELVLMNPGSICFPRGNLAASY 156
Cdd:TIGR00040  66 DELPEEEIFEAEGIDFGLVHGDLVYPRGDLLVLEYLAKELGvDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSY 145

                         170
                  ....*....|
gi 516388891  157 GRYEDGVLGI 166
Cdd:TIGR00040 146 AILDVDKDKV 155
 
Name Accession Description Interval E-value
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-180 2.72e-97

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 279.06  E-value: 2.72e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   1 MKIAILSDLHGSLSALEQVLDQLAPWQPDHYLLLGDLLNHGPRNPVPPGYAPAAVAERLNGLASRIMAVRGNCDSEVDQM 80
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNPLPEGYAPKKVAELLNAYADKIIAVRGNCDSEVDQM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891  81 LLDFPITAPYNQLLVDGRRWFVSHGHLYRPAEVP-LPAGSLFISGHTHLPVLQREGELVLMNPGSICFPRGNLAASYGRY 159
Cdd:PRK09453  81 LLHFPIMAPYQQVLLEGKRLFLTHGHLYGPENLPaLHDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGYPASYGIL 160

                        170       180
                 ....*....|....*....|.
gi 516388891 160 EDGVLGIHACADSEVLLRLAL 180
Cdd:PRK09453 161 DDNVLSVIDLEGGEVIAQVAI 181
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-160 9.84e-47

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: 150.11  E-value: 9.84e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   2 KIAILSDLHGSLSALEQVLDQLAPwQPDHYLLLGDLLNHGPRNPvppgyapaavaerLNGLASRIMAVRGNCDSEVDQML 81
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALELFED-GVDAVIHAGDFVSPFVLNA-------------LLELKAPLIAVRGNNDGEVDQLL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891  82 lDFPITAPYNQLLVDGRRWFVSHGHLYRPAEVPLPA----GSLFISGHTHLPVLQREGELVLMNPGSICFPRGnLAASYG 157
Cdd:cd00841   67 -GRPILPEFLTLEIGGLRILLTHGHLFGVLEALYLAkeggADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRG-GRPTYA 144


                 ...
gi 516388891 158 RYE 160
Cdd:cd00841  145 ILD 147
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-160 6.69e-46

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 148.91  E-value: 6.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   2 KIAILSDLHGSLSALEQVLDQLAPWQPDHYLLLGDLLNHGPRnpvppgyaPAAVAERLNGLasRIMAVRGNCDSEVDQML 81
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPD--------PPEVLDLLREL--PIVAVRGNHDGAVLRGL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891  82 LDFPITApynQLLVDGRRWFVSHGHLYRP-----------AEVPLPAGSLFISGHTHLPVLQREGELVLMNPGSICFPRG 150
Cdd:COG0622   71 RSLPETL---RLELEGVRILLVHGSPNEYllpdtpaerlrALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRD 147

                        170
                 ....*....|
gi 516388891 151 NLAASYGRYE 160
Cdd:COG0622  148 GDPASYAILD 157
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-160 3.13e-26

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: 97.38  E-value: 3.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891    1 MKIAILSDLHGSLSALEQVLDQLAPwQPDHYLLLGDLLNhgprnpvppgyapAAVAERLNGLAsRIMAVRGNCDSEVdQM 80
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKG-VVDLIIHAGDIVA-------------PEVLEELLELA-PVLAVRGNNDAAA-EF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   81 LLDFPITAPynqLLVDGRRWFVSHGHLYRPAEVPL-----PAGSLFISGHTHLPVLQREGELVLMNPGSICFPRGNLAAS 155
Cdd:pfam12850  65 ATDLPEEAV---LELGGVKILLTHGHGVKDALARLlrraeEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPT 141


                  ....*
gi 516388891  156 YGRYE 160
Cdd:pfam12850 142 YALLD 146
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-166 2.31e-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: 92.82  E-value: 2.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891    1 MKIAILSDLHGSLSALE---QVLDQLApwQPDHYLLLGDLLnhgprnpvppgyaPAAVAERLNGLASRIMAVRGNCDSEV 77
Cdd:TIGR00040   1 MKILVISDTHGPLRATElpvELFNLES--NVDLVIHAGDLT-------------SPFVLKEFEDLAAKVIAVRGNNDGER 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   78 DQMLLDFPITAPYNQLLVDGRRWFVSHGHLYRPAEVPLPAG-SLFISGHTHLPVLQREGELVLMNPGSICFPRGNLAASY 156
Cdd:TIGR00040  66 DELPEEEIFEAEGIDFGLVHGDLVYPRGDLLVLEYLAKELGvDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSY 145

                         170
                  ....*....|
gi 516388891  157 GRYEDGVLGI 166
Cdd:TIGR00040 146 AILDVDKDKV 155
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-129 2.06e-11

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: 57.99  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891    1 MKIAILSDLH--GSLSALEQVLDQLAP-WQPDHYLLLGDLLNHGPRnpvppgyaPAAVAERLNGLAS--RIMAVRGNCDS 75
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEeGKPDLVLHAGDLVDRGPP--------SEEVLELLERLIKyvPVYLVRGNHDF 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 516388891   76 EVDQMLLDFPITAPYNQLLVDGRRWFvshghlyrpaeVPLPAGSLfISGHTHLP 129
Cdd:pfam00149  73 DYGECLRLYPYLGLLARPWKRFLEVF-----------NFLPLAGI-LSGHTHVP 114
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-98 2.37e-10

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 56.95  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   2 KIAILSDLHGSLSALEQVLDQLAPWQPDHYLLLGDLLNHGPRNPVppgyapAAVAERLNGLASRIMAVRGNCDS-EVDQM 80
Cdd:COG2129    1 KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEA------REVLEELAALGVPVLAVPGNHDDpEVLDA 74

                         90
                 ....*....|....*...
gi 516388891  81 LldfpitAPYNQLLVDGR 98
Cdd:COG2129   75 L------EESGVHNLHGR 86
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-72 3.69e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 48.53  E-value: 3.69e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516388891   1 MKIAILSDLH-------GSLSALEQVLDQLAPWQPDHYLLLGDLLNHGPrnpvPPGYapAAVAERLNGLASRIMAVRGN 72
Cdd:COG1409    1 FRFAHISDLHlgapdgsDTAEVLAAALADINAPRPDFVVVTGDLTDDGE----PEEY--AAAREILARLGVPVYVVPGN 73
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-143 3.83e-06

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: 44.18  E-value: 3.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   4 AILSDLHGSLSALEQVLDQLAPW--QPDHYLLLGDLLNHGPRNPVPPGYAPAAVAERLNglasrIMAVRGNCDsevdqml 81
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKaeKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIP-----VYVVPGNHD------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891  82 ldfpitapynqllvdgrrWFVSHGHLYRPAEVPLPAGS----------------LFISGHTHLP--VLQREGELVLMNPG 143
Cdd:cd00838   69 ------------------ILVTHGPPYDPLDEGSPGEDpgseallelldkygpdLVLSGHTHVPgrREVDKGGTLVVNPG 130
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 5-44 2.20e-04

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs 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: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 40.43  E-value: 2.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 516388891   5 ILSDLHGSLSALEQVLDQLAPWQPDHYLLLGDLLNHGPRN 44
Cdd:cd00144    2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDS 41
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 6-108 6.60e-04

Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an Escherichia coli UDP-2,3-diacylglucosamine hydrolase thought to catalyze the fourth step of lipid A biosynthesis, in which a precursor UDP-2,3-diacylglucosamine is hydrolyzed to yield 2,3-diacylglucosamine 1-phosphate and UMP. YbbF 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: 277343 [Multi-domain]  Cd Length: 217  Bit Score: 38.88  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516388891   6 LSDLH-----GSLSALEQVLDQLAPWQPDHYLLLGDLLN--HGPRNPVPPGYAPAAvaERLNGLASR---IMAVRGNCDS 75
Cdd:cd07398    3 ISDLHlglrgCRADRLLDFLLVEELDEADALYLLGDIFDlwIGDDSVVWPGAHRAL--ARLLRLADRgteVIYVPGNHDF 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 516388891  76 EVDQM----LLDFPITAPYNQLLVDGRRWFVSHGHLY 108
Cdd:cd07398   81 LLGRFfaeaLGAILLPEPAEHLELDGKRLLVLHGDQL 117
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 3-74 7.81e-03

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. 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: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 35.75  E-value: 7.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516388891   3 IAILSDLHGSLSALEQVldQLAPWQPDHYLLLGDLLNHGPRNPVPPgyapaaVAERLNGLASRIMAVRGNCD 74
Cdd:cd07392    1 ILAISDVHGDVPKLKKI--KLKAEEADAVIVAGDITHFGPGEEAIE------ALNLLLAIGAPVLAVPGNCD 64
 
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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