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Conserved domains on  [gi|215275681|sp|B1WC86|]
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RecName: Full=Metallophosphoesterase 1; AltName: Full=Post-GPI attachment to proteins factor 5

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10169250)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)| bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain; similar to Escherichia coli UshA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 70-327 9.99e-82

human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 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: 277372 [Multi-domain]  Cd Length: 156  Bit Score: 246.99  E-value: 9.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 150 VVIGNHDIGFHYQMSKYRINRFEKVFgserlfslkgvnfvmvnsvamegdgcticseaeaelreisrklncsqeqvqgss 229
Cdd:cd08165   81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 230 qcdheprlplsapVLLQHYPLYRasdancsgedaappeersvpfeekydvlsreasqkLLWWLRPRLILSGHTHSACEVL 309
Cdd:cd08165  107 -------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACEVL 138

                        250
                 ....*....|....*...
gi 215275681 310 HPGGAPEVSVPSFSWRNR 327
Cdd:cd08165  139 HYGGIPEISVPSFSWRNR 156
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 70-327 9.99e-82

human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 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: 277372 [Multi-domain]  Cd Length: 156  Bit Score: 246.99  E-value: 9.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 150 VVIGNHDIGFHYQMSKYRINRFEKVFgserlfslkgvnfvmvnsvamegdgcticseaeaelreisrklncsqeqvqgss 229
Cdd:cd08165   81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 230 qcdheprlplsapVLLQHYPLYRasdancsgedaappeersvpfeekydvlsreasqkLLWWLRPRLILSGHTHSACEVL 309
Cdd:cd08165  107 -------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACEVL 138

                        250
                 ....*....|....*...
gi 215275681 310 HPGGAPEVSVPSFSWRNR 327
Cdd:cd08165  139 HYGGIPEISVPSFSWRNR 156
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
72-332 1.71e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 69.33  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  72 LADTHLLGEIRGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQrmfrhgshVQLKVV 151
Cdd:COG1409    6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG--------VPVYVV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 152 IGNHDIGFHYQMSKYRINRFEKVFGSERLFSLKGVNFVMVNSVAMEGDGCTICSE----AEAELREISRKLNcsqeqvqg 227
Cdd:COG1409   71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEqlawLEEELAAAPAKPV-------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 228 ssqcdheprlplsapVLLQHYPLYrasdancsgedaappeeRSVPFEEKYDVLSREASQKLLWWLRPRLILSGHTHSAcE 307
Cdd:COG1409  143 ---------------IVFLHHPPY-----------------STGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRY-E 189

                        250       260
                 ....*....|....*....|....*
gi 215275681 308 VLHPGGAPEVSVPSFSWRNRNNPSF 332
Cdd:COG1409  190 RTRRDGVPYIVAGSTGGQVRLPPGY 214
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 67-167 6.17e-06

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: 44.90  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681   67 LKAMFLADTHLLGEIRG--HWLDKLRREwqmerafqtalwlLQPEVVFILGDVFDEGKWSsaqawaddlHRFQRMFRH-G 143
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDllELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS---------EEVLELLERlI 58

                          90       100
                  ....*....|....*....|....
gi 215275681  144 SHVQLKVVIGNHDIGFHYQMSKYR 167
Cdd:pfam00149  59 KYVPVYLVRGNHDFDYGECLRLYP 82
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 70-327 9.99e-82

human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 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: 277372 [Multi-domain]  Cd Length: 156  Bit Score: 246.99  E-value: 9.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 150 VVIGNHDIGFHYQMSKYRINRFEKVFgserlfslkgvnfvmvnsvamegdgcticseaeaelreisrklncsqeqvqgss 229
Cdd:cd08165   81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 230 qcdheprlplsapVLLQHYPLYRasdancsgedaappeersvpfeekydvlsreasqkLLWWLRPRLILSGHTHSACEVL 309
Cdd:cd08165  107 -------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACEVL 138

                        250
                 ....*....|....*...
gi 215275681 310 HPGGAPEVSVPSFSWRNR 327
Cdd:cd08165  139 HYGGIPEISVPSFSWRNR 156
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 70-327 4.74e-46

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. This group also contains Saccharomyces cerevisiae TED1 (Trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), which acts together with Emp24p and Erv25p in cargo exit from the ER, and human MPPE1. The human MPPE1 gene is a candidate susceptibility gene for bipolar disorder. These proteins 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: 277330 [Multi-domain]  Cd Length: 172  Bit Score: 155.97  E-value: 4.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  70 MFLADTHLLGEIRGHW-------LDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRH 142
Cdd:cd07384    1 LLIADPQILDETSYPPrpkpalrLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 143 GS-----HVQLKVVIGNHDIGFHYQMSKY-RINRFEKVFgserlfslkgvnfvmvnsvamegdgcticseaeaelreisr 216
Cdd:cd07384   81 KSpgslgSIPVIFIPGNHDIGYGGEAVFPeKVDRFEKYF----------------------------------------- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 217 klncsqeqvqgssqcdheprlplsapVLLQHYPLYRasdancsgedaappeersvpfeekydvlsreasqkLLWWLRPRL 296
Cdd:cd07384  120 --------------------------ILLTHIPLYR-----------------------------------LLDSIKPVL 138

                        250       260       270
                 ....*....|....*....|....*....|....
gi 215275681 297 ILSGHTHSACEVLH---PGGAPEVSVPSFSWRNR 327
Cdd:cd07384  139 ILSGHDHDYCEVVHkssPGSVKEITVKSFSWRMG 172
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 61-324 4.22e-27

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. Cdc1 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: 277370  Cd Length: 257  Bit Score: 108.26  E-value: 4.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  61 GRQEPVLK-AMFLADTHLlgeirghwldklRREW-QMERAfqtalwlLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQR 138
Cdd:cd08163   16 GRPWILNTlTEHFVDQYL------------RRNWrYLQKQ-------LKPDSTFFLGDLFDGGREWADEYWKKEYFRFNR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 139 MFRHgSHVQLKVVI--GNHDIGFHYQMSKYRINRFEKVFG-SERLFSLKGVNFVMVNSVAMEgdgcticseaeaelreis 215
Cdd:cd08163   77 IFDP-KPLRKMIESlpGNHDIGFGNGVKLPVRQRFESYFGpTSRVIDVGNHTFVIVDTISLS------------------ 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 216 rklNCSQEQV-QGSSQCDHE---PRLPLSAPVLLQHYPLYRASDANCsgedaAPPEERSVPFEEKY-----DVLSREASQ 286
Cdd:cd08163  138 ---NNDNPQVyQPAREFLHSfeaMKVNSKPRILLTHVPLYRPPNTSC-----GPLREKKTPLPYGYgyqyqNVLEPSLSE 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 215275681 287 KLLWWLRPRLILSGHTHSACEVLHP-------GGAPEVSVPSFSW 324
Cdd:cd08163  210 SILKAINPVAAFSGDDHDYCEVVHEyqfdgkeGSAREITVKSISM 254
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
72-332 1.71e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 69.33  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  72 LADTHLLGEIRGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQrmfrhgshVQLKVV 151
Cdd:COG1409    6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG--------VPVYVV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 152 IGNHDIGFHYQMSKYRINRFEKVFGSERLFSLKGVNFVMVNSVAMEGDGCTICSE----AEAELREISRKLNcsqeqvqg 227
Cdd:COG1409   71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEqlawLEEELAAAPAKPV-------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 228 ssqcdheprlplsapVLLQHYPLYrasdancsgedaappeeRSVPFEEKYDVLSREASQKLLWWLRPRLILSGHTHSAcE 307
Cdd:COG1409  143 ---------------IVFLHHPPY-----------------STGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRY-E 189

                        250       260
                 ....*....|....*....|....*
gi 215275681 308 VLHPGGAPEVSVPSFSWRNRNNPSF 332
Cdd:COG1409  190 RTRRDGVPYIVAGSTGGQVRLPPGY 214
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 70-175 6.60e-10

uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; A functionally uncharacterized subgroup related to the metallophosphatase domain of Saccharomyces cerevisiae Cdc1, S. cerevisiae Ted1 and human MPPE1. Cdc1 is an endoplasmic reticulum-localized transmembrane lipid phosphatase and is a subunit of DNA polymerase delta. TED1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), acts together with Emp24p and Erv25p in cargo exit from the ER. The MPPE1 gene is a candidate susceptibility gene for Bipolar disorder. Proteins in this uncharacterized subgroup 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: 277373  Cd Length: 195  Bit Score: 58.22  E-value: 6.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  70 MFLADTHLLGEIRGHWLDKLRREWQMER----AFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSH 145
Cdd:cd08166    1 LLVADPQILGYENEKFGLGEISRWDSDRylakTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPLKRG 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 215275681 146 VQLKVVIGNHDIGFHYQM-SKYRINRFEKVF 175
Cdd:cd08166   81 KNAIYIPGDNDIGGESEIiIESRVRRFNNYF 111
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 67-167 6.17e-06

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: 44.90  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681   67 LKAMFLADTHLLGEIRG--HWLDKLRREwqmerafqtalwlLQPEVVFILGDVFDEGKWSsaqawaddlHRFQRMFRH-G 143
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDllELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS---------EEVLELLERlI 58

                          90       100
                  ....*....|....*....|....
gi 215275681  144 SHVQLKVVIGNHDIGFHYQMSKYR 167
Cdd:pfam00149  59 KYVPVYLVRGNHDFDYGECLRLYP 82
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 99-175 2.71e-05

Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces cerevisiae Ted1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1) is a metallophosphatase domain-containing protein which acts together with Emp24p and Erv25p in cargo exit from the ER. Ted1 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: 277371  Cd Length: 193  Bit Score: 44.78  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  99 FQTALWLLQPEVVFILGDVFdegkwsSAQaWADD------LHRFQRMFRHGS-----------------HVQLKVVIGNH 155
Cdd:cd08164   36 YQMMQFRLKPTHVTVLGDLF------SSQ-WITDeefekrADRYKKRIFGRSdwqvgnislaartfengDILLINIAGNH 108

                         90       100
                 ....*....|....*....|
gi 215275681 156 DIGFHYQMSKYRINRFEKVF 175
Cdd:cd08164  109 DVGYAGESTEARISRFEQLF 128
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
73-156 6.02e-05

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 44.13  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  73 ADTHLlgeirghwlDKLRREWQMERAFQTAL-WLL------QPEVVFILGDVFDegkwsSAQAWADDLHRFQRMFRHGSH 145
Cdd:COG0420    7 ADWHL---------GKPLHGASRREDQLAALdRLVdlaieeKVDAVLIAGDLFD-----SANPSPEAVRLLAEALRRLSE 72

                         90
                 ....*....|...
gi 215275681 146 VQLKVVI--GNHD 156
Cdd:COG0420   73 AGIPVVLiaGNHD 85
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 70-251 1.69e-04

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 43.08  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  70 MFLADTHLlGEIRGHWLDKLRREWQME-----RAFQTALWLL-QPEVVFILGDVFDE---GKWSSAQAwaDDlhrFQRMF 140
Cdd:cd07395    8 IQGADPQL-GLIKQNNIGNGGDEWDKEielteQAVQAINKLNpKPKFVVVCGDLVHAmpgEEFREQQV--SD---LKDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681 141 RH-GSHVQLKVVIGNHDIGFHYQMSKyrINRFEKVFGSERL-FSLKGVNFVMVNSVAMEGDGCTiCSEAEAELREISRKL 218
Cdd:cd07395   82 SKlDPDIPLVCVCGNHDVGNTPTPET--IQRYRDDFGDDYFsFWVGGVFFIVLNSQLFKDPSKV-PELASAQDQWLEEQL 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 215275681 219 ncsqeQVQGSSQCDHEprlplsapVLLQHYPLY 251
Cdd:cd07395  159 -----QIARESDAKHV--------VVFQHIPLF 178
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 71-161 2.99e-03

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: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215275681  71 FLADTHLlgeiRGHWLDKLRREWQMERAfqtalwllQPEVVFILGDVFDEGKWSSAQAWADDLHRFqrmfrhgSHVQLKV 150
Cdd:cd00838    2 VISDIHG----NLEALEAVLEAALAKAE--------KPDLVICLGDLVDYGPDPEEVELKALRLLL-------AGIPVYV 62

                         90
                 ....*....|..
gi 215275681 151 VIGNHDIGF-HY 161
Cdd:cd00838   63 VPGNHDILVtHG 74
 
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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