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Conserved domains on  [gi|1751265990|ref|XP_030781654|]
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metallophosphoesterase 1 isoform X2 [Rhinopithecus roxellana]

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 ...
 73-329 6.06e-91

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: 270.87  E-value: 6.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSTPEAWADDVQRFQKMFRHPSHVQLK 152
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 153 VVAGNHDIGFHYEMNTYKVERFEKVFsserlfswkginfvmvnsvalngdgcgicseaeaelievshrlncsreargsrr 232
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 233 cgpgpllpisapVLLQHYPLYRrsdancsgddaappeerdipfkenydvlsreasqkLLWWLQPRLVLSGHTHSACEVHH 312
Cdd:cd08165   107 ------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACEVLH 139

                         250
                  ....*....|....*..
gi 1751265990 313 GGRVPELSVPSFSWRNR 329
Cdd:cd08165   140 YGGIPEISVPSFSWRNR 156
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 73-329 6.06e-91

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: 270.87  E-value: 6.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSTPEAWADDVQRFQKMFRHPSHVQLK 152
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 153 VVAGNHDIGFHYEMNTYKVERFEKVFsserlfswkginfvmvnsvalngdgcgicseaeaelievshrlncsreargsrr 232
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 233 cgpgpllpisapVLLQHYPLYRrsdancsgddaappeerdipfkenydvlsreasqkLLWWLQPRLVLSGHTHSACEVHH 312
Cdd:cd08165   107 ------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACEVLH 139

                         250
                  ....*....|....*..
gi 1751265990 313 GGRVPELSVPSFSWRNR 329
Cdd:cd08165   140 YGGIPEISVPSFSWRNR 156
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
75-334 3.87e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 74.34  E-value: 3.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  75 LADTHLLGEFLGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDVFDEGkwsTPEAWaddvQRFQKMFRhPSHVQLKVV 154
Cdd:COG1409     6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDG---EPEEY----AAAREILA-RLGVPVYVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 155 AGNHDIGFHYEMNTYKVERFEKVFSSERLFSWKGINFVMVNSvALNGDGCGICSEAEAELIEvsHRLncsREARGSRRcg 234
Cdd:COG1409    71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDS-NVPGRSSGELGPEQLAWLE--EEL---AAAPAKPV-- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 235 pgpllpisapVLLQHYPLYrrsdANCSGDDAAPPEERDipfkENYDVLSReasqkllwwLQPRLVLSGHTHSACEVHHGG 314
Cdd:COG1409   143 ----------IVFLHHPPY----STGSGSDRIGLRNAE----ELLALLAR---------YGVDLVLSGHVHRYERTRRDG 195

                         250       260
                  ....*....|....*....|
gi 1751265990 315 rVPELSVPSFSWRNRNNPSF 334
Cdd:COG1409   196 -VPYIVAGSTGGQVRLPPGY 214
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 70-186 1.14e-07

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: 49.90  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  70 LKAMFLADTHLLGEF--LGHWLDKLRREwqmerafqtalwlLQPEVVFILGDVFDEGKWStpEAWADDVQRFQKmfrhps 147
Cdd:pfam00149   1 MRILVIGDLHLPGQLddLLELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS--EEVLELLERLIK------ 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1751265990 148 HVQLKVVAGNHDIGFH--------YEMNTYKVERFEKVFSSERLFSW 186
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGeclrlypyLGLLARPWKRFLEVFNFLPLAGI 106
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 73-329 6.06e-91

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: 270.87  E-value: 6.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSTPEAWADDVQRFQKMFRHPSHVQLK 152
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 153 VVAGNHDIGFHYEMNTYKVERFEKVFsserlfswkginfvmvnsvalngdgcgicseaeaelievshrlncsreargsrr 232
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 233 cgpgpllpisapVLLQHYPLYRrsdancsgddaappeerdipfkenydvlsreasqkLLWWLQPRLVLSGHTHSACEVHH 312
Cdd:cd08165   107 ------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACEVLH 139

                         250
                  ....*....|....*..
gi 1751265990 313 GGRVPELSVPSFSWRNR 329
Cdd:cd08165   140 YGGIPEISVPSFSWRNR 156
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 73-329 1.12e-54

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: 178.70  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  73 MFLADTHLLGEFLGHW-------LDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSTPEAWADDVQRFQKMFRH 145
Cdd:cd07384     1 LLIADPQILDETSYPPrpkpalrLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 146 PS-----HVQLKVVAGNHDIGFHYEMN-TYKVERFEKVFsserlfswkginfvmvnsvalngdgcgicseaeaelievsh 219
Cdd:cd07384    81 KSpgslgSIPVIFIPGNHDIGYGGEAVfPEKVDRFEKYF----------------------------------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 220 rlncsreargsrrcgpgpllpisapVLLQHYPLYRRSDAncsgddaappeerdipfkenydvlsreasqkllwwLQPRLV 299
Cdd:cd07384   120 -------------------------ILLTHIPLYRLLDS-----------------------------------IKPVLI 139

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1751265990 300 LSGHTHSACEVHHG---GRVPELSVPSFSWRNR 329
Cdd:cd07384   140 LSGHDHDYCEVVHKsspGSVKEITVKSFSWRMG 172
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 92-326 2.34e-24

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: 100.94  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  92 LRREW-QMERAfqtalwlLQPEVVFILGDVFDEGK-WSTpEAWADDVQRFQKMFRhPSHVQLKV--VAGNHDIGFHYEMN 167
Cdd:cd08163    33 LRRNWrYLQKQ-------LKPDSTFFLGDLFDGGReWAD-EYWKKEYFRFNRIFD-PKPLRKMIesLPGNHDIGFGNGVK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 168 TYKVERFEKVF-SSERLFSWKGINFVMVNSVALNgdgcgicSEAEAELIEVSHRLNCSREARGSrrcgpgPLLPisaPVL 246
Cdd:cd08163   104 LPVRQRFESYFgPTSRVIDVGNHTFVIVDTISLS-------NNDNPQVYQPAREFLHSFEAMKV------NSKP---RIL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 247 LQHYPLYRRSDANCsgddaAPPEERDIPFKENY-----DVLSREASQKLLWWLQPRLVLSGHTHSACEVHH-------GG 314
Cdd:cd08163   168 LTHVPLYRPPNTSC-----GPLREKKTPLPYGYgyqyqNVLEPSLSESILKAINPVAAFSGDDHDYCEVVHeyqfdgkEG 242

                         250
                  ....*....|..
gi 1751265990 315 RVPELSVPSFSW 326
Cdd:cd08163   243 SAREITVKSISM 254
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
75-334 3.87e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 74.34  E-value: 3.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  75 LADTHLLGEFLGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDVFDEGkwsTPEAWaddvQRFQKMFRhPSHVQLKVV 154
Cdd:COG1409     6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDG---EPEEY----AAAREILA-RLGVPVYVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 155 AGNHDIGFHYEMNTYKVERFEKVFSSERLFSWKGINFVMVNSvALNGDGCGICSEAEAELIEvsHRLncsREARGSRRcg 234
Cdd:COG1409    71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDS-NVPGRSSGELGPEQLAWLE--EEL---AAAPAKPV-- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 235 pgpllpisapVLLQHYPLYrrsdANCSGDDAAPPEERDipfkENYDVLSReasqkllwwLQPRLVLSGHTHSACEVHHGG 314
Cdd:COG1409   143 ----------IVFLHHPPY----STGSGSDRIGLRNAE----ELLALLAR---------YGVDLVLSGHVHRYERTRRDG 195

                         250       260
                  ....*....|....*....|
gi 1751265990 315 rVPELSVPSFSWRNRNNPSF 334
Cdd:COG1409   196 -VPYIVAGSTGGQVRLPPGY 214
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 73-178 2.58e-09

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: 56.68  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  73 MFLADTHLLGE----FLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSTPEAWADDVQRFQKMFRHPSH 148
Cdd:cd08166     1 LLVADPQILGYenekFGLGEISRWDSDRYLAKTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPLKRG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1751265990 149 VQLKVVAGNHDIGFHYEM-NTYKVERFEKVF 178
Cdd:cd08166    81 KNAIYIPGDNDIGGESEIiIESRVRRFNNYF 111
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 70-186 1.14e-07

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: 49.90  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  70 LKAMFLADTHLLGEF--LGHWLDKLRREwqmerafqtalwlLQPEVVFILGDVFDEGKWStpEAWADDVQRFQKmfrhps 147
Cdd:pfam00149   1 MRILVIGDLHLPGQLddLLELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS--EEVLELLERLIK------ 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1751265990 148 HVQLKVVAGNHDIGFH--------YEMNTYKVERFEKVFSSERLFSW 186
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGeclrlypyLGLLARPWKRFLEVFNFLPLAGI 106
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 84-178 1.23e-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: 45.56  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  84 FLGHwldklrrewqmerAFQTALWLLQPEVVFILGDVFDEgKWSTPEAWADDVQRFQKMF-----------RHPS----- 147
Cdd:cd08164    31 FLGH-------------IYQMMQFRLKPTHVTVLGDLFSS-QWITDEEFEKRADRYKKRIfgrsdwqvgniSLAArtfen 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1751265990 148 -HVQLKVVAGNHDIGFHYEMNTYKVERFEKVF 178
Cdd:cd08164    97 gDILLINIAGNHDVGYAGESTEARISRFEQLF 128
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
76-159 2.73e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 45.29  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  76 ADTHLlgeflghwlDKLRREWQMERAFQTAL-WLL------QPEVVFILGDVFDegkwsTPEAWADDVQRFQKMFRHPSH 148
Cdd:COG0420     7 ADWHL---------GKPLHGASRREDQLAALdRLVdlaieeKVDAVLIAGDLFD-----SANPSPEAVRLLAEALRRLSE 72

                          90
                  ....*....|...
gi 1751265990 149 VQLKVV--AGNHD 159
Cdd:COG0420    73 AGIPVVliAGNHD 85
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 74-164 8.33e-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: 42.25  E-value: 8.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  74 FLADTHLLGEFLGHWLDKLRREwqmerafqtalwLLQPEVVFILGDVFDEGKWstPEAWADDVQRFQKMFrhpshVQLKV 153
Cdd:cd00838     2 VISDIHGNLEALEAVLEAALAK------------AEKPDLVICLGDLVDYGPD--PEEVELKALRLLLAG-----IPVYV 62

                          90
                  ....*....|..
gi 1751265990 154 VAGNHDIGF-HY 164
Cdd:cd00838    63 VPGNHDILVtHG 74
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 110-325 9.17e-05

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: 43.85  E-value: 9.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 110 QPEVVFILGDVFDEGKWstpEAWADD-VQRFQKMFRH-PSHVQLKVVAGNHDIGFHYEMNTykVERFEKVFSSERLFSW- 186
Cdd:cd07395    50 KPKFVVVCGDLVHAMPG---EEFREQqVSDLKDVLSKlDPDIPLVCVCGNHDVGNTPTPET--IQRYRDDFGDDYFSFWv 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990 187 KGINFVMVNSVALNGDGcGICSEAEAELIEVSHRLNCSREARGSRRcgpgpllpisapVLLQHYPLYRRSdancsgddaa 266
Cdd:cd07395   125 GGVFFIVLNSQLFKDPS-KVPELASAQDQWLEEQLQIARESDAKHV------------VVFQHIPLFLED---------- 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751265990 267 pPEERDipfkeNYDVLSREASQKLLWWL---QPRLVLSGHTHSacevHHGGRVPELSVPSFS 325
Cdd:cd07395   182 -PDEED-----DYFNIPKSVRRELLDKFkkaGVKAVFSGHYHR----NAGGRYRDLEMVVTS 233
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 73-159 1.95e-03

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: 39.26  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751265990  73 MFLADTHLLgeflghwLDKLRREWQMERAFQTalWLLQPEVVFILGDVFD---EGKWSTPEAWADDVQRFQKMFRHpsHV 149
Cdd:cd07398     1 LFISDLHLG-------LRGCRADRLLDFLLVE--ELDEADALYLLGDIFDlwiGDDSVVWPGAHRALARLLRLADR--GT 69

                          90
                  ....*....|
gi 1751265990 150 QLKVVAGNHD 159
Cdd:cd07398    70 EVIYVPGNHD 79
 
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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