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Conserved domains on  [gi|1267444762|ref|WP_098266215|]
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MULTISPECIES: metallophosphoesterase [Bacillus cereus group]

Protein Classification

metallophosphoesterase( domain architecture ID 10096151)

metallophosphoesterase contains 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_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-151 1.41e-38

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: 128.93  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   2 KALIVSDSHSSVKELQLLKEKYEGKVDVMIHCGDSE----LTPAHEELQGFRVVKGNCDY-------ANFQDEIVTV-VD 69
Cdd:cd00841     1 KIGVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVspfvLNALLELKAPLIAVRGNNDGevdqllgRPILPEFLTLeIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  70 GIRFVVVHGHRHNVKMTLqtlaYRAEEVDAQVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRvEKTFALLEMDEkhIDV 149
Cdd:cd00841    81 GLRILLTHGHLFGVLEAL----YLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEK--LEV 153


                  ..
gi 1267444762 150 RF 151
Cdd:cd00841   154 EI 155
 
Name Accession Description Interval E-value
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-151 1.41e-38

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: 128.93  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   2 KALIVSDSHSSVKELQLLKEKYEGKVDVMIHCGDSE----LTPAHEELQGFRVVKGNCDY-------ANFQDEIVTV-VD 69
Cdd:cd00841     1 KIGVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVspfvLNALLELKAPLIAVRGNNDGevdqllgRPILPEFLTLeIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  70 GIRFVVVHGHRHNVKMTLqtlaYRAEEVDAQVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRvEKTFALLEMDEkhIDV 149
Cdd:cd00841    81 GLRILLTHGHLFGVLEAL----YLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEK--LEV 153


                  ..
gi 1267444762 150 RF 151
Cdd:cd00841   154 EI 155
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-145 1.38e-35

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: 120.88  E-value: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   1 MKALIVSDSHSSVKELQLLKEKYEGKVDVMIHCGDS---ELTPAHEELQGFRVVKGNCDYAN-----FQDEIVTVVDGIR 72
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVVDLIIHAGDIvapEVLEELLELAPVLAVRGNNDAAAefatdLPEEAVLELGGVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267444762  73 FVVVHGHrhNVKMTLQTLAYRAEEVDAqVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRVEKTFALLEMDEK 145
Cdd:pfam12850  81 ILLTHGH--GVKDALARLLRRAEEGVA-VVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDDG 150
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-150 1.39e-32

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: 113.62  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   1 MKALIVSDSHSSVKELQLLKE--KYEGKVDVMIHCGDSE----LTPAHEELQGFRVVKGNCD--YANFQDEIVTVVDGIR 72
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVElfNLESNVDLVIHAGDLTspfvLKEFEDLAAKVIAVRGNNDgeRDELPEEEIFEAEGID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267444762  73 FVVVHGHRHNVKMTLQTLAYRAEEVDAQVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRVEKTFALLEMDEKHIDVR 150
Cdd:TIGR00040  81 FGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYAILDVDKDKVTAL 158
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-156 2.21e-32

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 113.86  E-value: 2.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   2 KALIVSDSHSSVKELQLLKEKYEG-KVDVMIHCGDSELTPAH-----EELQ--GFRVVKGNCDYA------NFQDEIVTV 67
Cdd:COG0622     1 KIAVISDTHGNLPALEAVLEDLEReGVDLIVHLGDLVGYGPDppevlDLLRelPIVAVRGNHDGAvlrglrSLPETLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  68 VDGIRFVVVHGHRHNV---KMTLQTLAYRAEEVDAQVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRVEKTFALLEMDE 144
Cdd:COG0622    81 LEGVRILLVHGSPNEYllpDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAILDIDD 160

                         170
                  ....*....|..
gi 1267444762 145 KHIDVRFETLDG 156
Cdd:COG0622   161 GEWSVEFVRVPY 172
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-159 6.25e-18

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 76.44  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   1 MKALIVSDSHSSVKELQLLKEKYE-GKVDVMIHCGD----------------SELTpahEELQGFRV----VKGNCD--- 56
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAqSGADWLVHLGDvlyhgprnplpegyapKKVA---ELLNAYADkiiaVRGNCDsev 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  57 ------YANFQDEIVTVVDGIRFVVVHGHRhnvkmtlqtlaYRAEEV----DAQVACFGHSHVLGAEFIDGVLFINPGSV 126
Cdd:PRK09453   78 dqmllhFPIMAPYQQVLLEGKRLFLTHGHL-----------YGPENLpalhDGDVLVYGHTHIPVAEKQGGIILFNPGSV 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1267444762 127 LLPRQRVEKTFALLEMDekhiDVRFETLDGQLV 159
Cdd:PRK09453  147 SLPKGGYPASYGILDDN----VLSVIDLEGGEV 175
 
Name Accession Description Interval E-value
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-151 1.41e-38

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: 128.93  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   2 KALIVSDSHSSVKELQLLKEKYEGKVDVMIHCGDSE----LTPAHEELQGFRVVKGNCDY-------ANFQDEIVTV-VD 69
Cdd:cd00841     1 KIGVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVspfvLNALLELKAPLIAVRGNNDGevdqllgRPILPEFLTLeIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  70 GIRFVVVHGHRHNVKMTLqtlaYRAEEVDAQVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRvEKTFALLEMDEkhIDV 149
Cdd:cd00841    81 GLRILLTHGHLFGVLEAL----YLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEK--LEV 153


                  ..
gi 1267444762 150 RF 151
Cdd:cd00841   154 EI 155
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-145 1.38e-35

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: 120.88  E-value: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   1 MKALIVSDSHSSVKELQLLKEKYEGKVDVMIHCGDS---ELTPAHEELQGFRVVKGNCDYAN-----FQDEIVTVVDGIR 72
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVVDLIIHAGDIvapEVLEELLELAPVLAVRGNNDAAAefatdLPEEAVLELGGVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267444762  73 FVVVHGHrhNVKMTLQTLAYRAEEVDAqVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRVEKTFALLEMDEK 145
Cdd:pfam12850  81 ILLTHGH--GVKDALARLLRRAEEGVA-VVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDDG 150
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-150 1.39e-32

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: 113.62  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   1 MKALIVSDSHSSVKELQLLKE--KYEGKVDVMIHCGDSE----LTPAHEELQGFRVVKGNCD--YANFQDEIVTVVDGIR 72
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVElfNLESNVDLVIHAGDLTspfvLKEFEDLAAKVIAVRGNNDgeRDELPEEEIFEAEGID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267444762  73 FVVVHGHRHNVKMTLQTLAYRAEEVDAQVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRVEKTFALLEMDEKHIDVR 150
Cdd:TIGR00040  81 FGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYAILDVDKDKVTAL 158
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-156 2.21e-32

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 113.86  E-value: 2.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   2 KALIVSDSHSSVKELQLLKEKYEG-KVDVMIHCGDSELTPAH-----EELQ--GFRVVKGNCDYA------NFQDEIVTV 67
Cdd:COG0622     1 KIAVISDTHGNLPALEAVLEDLEReGVDLIVHLGDLVGYGPDppevlDLLRelPIVAVRGNHDGAvlrglrSLPETLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  68 VDGIRFVVVHGHRHNV---KMTLQTLAYRAEEVDAQVACFGHSHVLGAEFIDGVLFINPGSVLLPRQRVEKTFALLEMDE 144
Cdd:COG0622    81 LEGVRILLVHGSPNEYllpDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAILDIDD 160

                         170
                  ....*....|..
gi 1267444762 145 KHIDVRFETLDG 156
Cdd:COG0622   161 GEWSVEFVRVPY 172
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-159 6.25e-18

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 76.44  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   1 MKALIVSDSHSSVKELQLLKEKYE-GKVDVMIHCGD----------------SELTpahEELQGFRV----VKGNCD--- 56
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAqSGADWLVHLGDvlyhgprnplpegyapKKVA---ELLNAYADkiiaVRGNCDsev 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  57 ------YANFQDEIVTVVDGIRFVVVHGHRhnvkmtlqtlaYRAEEV----DAQVACFGHSHVLGAEFIDGVLFINPGSV 126
Cdd:PRK09453   78 dqmllhFPIMAPYQQVLLEGKRLFLTHGHL-----------YGPENLpalhDGDVLVYGHTHIPVAEKQGGIILFNPGSV 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1267444762 127 LLPRQRVEKTFALLEMDekhiDVRFETLDGQLV 159
Cdd:PRK09453  147 SLPKGGYPASYGILDDN----VLSVIDLEGGEV 175
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-147 5.38e-09

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 53.09  E-value: 5.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   2 KALIVSDSHSSVKEL-QLLKEKYEGKVDVMIHCGD-------SELTPAHEELQGFRV----VKGNCDYANFQDEI----- 64
Cdd:COG2129     1 KILAVSDLHGNFDLLeKLLELARAEDADLVILAGDltdfgtaEEAREVLEELAALGVpvlaVPGNHDDPEVLDALeesgv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  65 ------VTVVDGIRFVVVHGHRHN------------VKMTLQTLAYR--------------------------------- 93
Cdd:COG2129    81 hnlhgrVVEIGGLRIAGLGGSRPTpfgtpyeyteeeIEERLAKLREKdvdillthappygttldrvedgphvgskalrel 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1267444762  94 AEEVDAQVACFGHSHV-LGAEFIDGVLFINPGSvllprqRVEKTFALLEMDEKHI 147
Cdd:COG2129   161 IEEFQPKLVLHGHIHEsRGVDKIGGTRVVNPGS------LAEGYYALIDLEDRSV 209
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 48-126 7.25e-08

Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting protein 29), also known as vacuolar membrane protein Pep11, is a subunit of the retromer complex which is responsible for the retrieval of mannose-6-phosphate receptors (MPRs) from the endosomes for retrograde transport back to the Golgi. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer complex assembly as well as a phosphatase with specificity for the cytoplasmic tail of the MPR. The retromer includes the following 5 subunits: Vps35, Vps26, Vps29, and a dimer of the sorting nexins Vps5 (Snx1), and Vps17 (Snx2). Vps29 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: 163637 [Multi-domain]  Cd Length: 178  Bit Score: 49.51  E-value: 7.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762  48 FRVVKGNCD-YANFQDEIVTVVDGIRFVVVHGHRHNVKMTLQTLAYRAEEVDAQVACFGHSHVLGAEFIDGVLFINPGSV 126
Cdd:cd07394    55 VHIVRGDFDeNLNYPETKVITVGQFKIGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSA 134
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-124 6.11e-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: 40.71  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   4 LIVSDSHSSVKELQLLKEK---YEGKVDVMIHCGD---SELTPAHEELQGFR---------VVKGNCDyanfqdeivtvv 68
Cdd:cd00838     1 LVISDIHGNLEALEAVLEAalaKAEKPDLVICLGDlvdYGPDPEEVELKALRlllagipvyVVPGNHD------------ 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267444762  69 dgirFVVVHGHRHNVKMTL--------QTLAYRAEEVDAQVACFGHSHVLGAEFID--GVLFINPG 124
Cdd:cd00838    69 ----ILVTHGPPYDPLDEGspgedpgsEALLELLDKYGPDLVLSGHTHVPGRREVDkgGTLVVNPG 130
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 4-122 3.39e-03

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB 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: 277325 [Multi-domain]  Cd Length: 135  Bit Score: 35.68  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267444762   4 LIVSDSHSSVKELQLlkekyeGKVDVMIHCGD--SELTPahEELQGFR------------VVKGNCDYAnfQDEivtvvD 69
Cdd:cd07379     3 VCISDTHSRHPTISI------PDGDVLIHAGDftEGGTP--DEVKKFLdwlkslphphkiVIAGNHDLT--LDP-----E 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267444762  70 GIRFVVVHG--------HRHNVKMTLQTLAYRAEEVDAQVACFGHSH-VLGAEF----IDGVLFIN 122
Cdd:cd07379    68 GTDILVTHGppyghldlGSSGQRLGCEELLNTVQRVRPKLHVFGHIHeGYGIERvpdtDGETTFVN 133
 
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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