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Conserved domains on  [gi|1034604568|ref|XP_016881416|]
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metallophosphoesterase 1 isoform X3 [Homo sapiens]

Protein Classification

MPP_MPPE1 domain-containing protein( domain architecture ID 10169250)

MPP_MPPE1 domain-containing protein

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 ...
 73-307 3.61e-89

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: 265.48  E-value: 3.61e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLK 152
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 153 VVAGNHDIGFHYEMNTYKVERFEKVFsserlfswkginfvmvnsVALngdgcgicseteaelievshrlncsrEHYPLYR 232
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------ILL--------------------------QHYPLYR 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034604568 233 rsdancsgedaapaeerdipfkenydvlsreasqkLLWWLQPRLVLSGHTHSACEVHHGGRVPELSVPSFSWRNR 307
Cdd:cd08165   117 -----------------------------------LLQWLKPRLVLSGHTHSACEVLHYGGIPEISVPSFSWRNR 156
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 73-307 3.61e-89

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: 265.48  E-value: 3.61e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLK 152
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 153 VVAGNHDIGFHYEMNTYKVERFEKVFsserlfswkginfvmvnsVALngdgcgicseteaelievshrlncsrEHYPLYR 232
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------ILL--------------------------QHYPLYR 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034604568 233 rsdancsgedaapaeerdipfkenydvlsreasqkLLWWLQPRLVLSGHTHSACEVHHGGRVPELSVPSFSWRNR 307
Cdd:cd08165   117 -----------------------------------LLQWLKPRLVLSGHTHSACEVLHYGGIPEISVPSFSWRNR 156
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
75-312 1.10e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 69.72  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  75 LADTHLLGEFLGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDIFDEGkwsTPEAWaddvERFQKMFRhPSHVQLKVV 154
Cdd:COG1409     6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDG---EPEEY----AAAREILA-RLGVPVYVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 155 AGNHDIGFHYEMNTYKVERFEKVFSSERLFSWKGINFVMVNSVALNGDGCGICSETEAELIEV------SHRLNCSreHY 228
Cdd:COG1409    71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEElaaapaKPVIVFL--HH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 229 PLYrrsdANCSGEDAAPAEERDipfkENYDVLSReasqkllwwLQPRLVLSGHTHSACEVHHGGrVPELSVPSFSWRNRN 308
Cdd:COG1409   149 PPY----STGSGSDRIGLRNAE----ELLALLAR---------YGVDLVLSGHVHRYERTRRDG-VPYIVAGSTGGQVRL 210


                  ....
gi 1034604568 309 NPSF 312
Cdd:COG1409   211 PPGY 214
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 70-186 3.25e-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: 48.36  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  70 LKAMFLADTHLLGEF--LGHWLDKLRREwqmerafqtalwlLQPEVVFILGDIFDEGKWStpEAWADDVERFQKmfrhps 147
Cdd:pfam00149   1 MRILVIGDLHLPGQLddLLELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS--EEVLELLERLIK------ 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034604568 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 ...
 73-307 3.61e-89

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: 265.48  E-value: 3.61e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLK 152
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 153 VVAGNHDIGFHYEMNTYKVERFEKVFsserlfswkginfvmvnsVALngdgcgicseteaelievshrlncsrEHYPLYR 232
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------ILL--------------------------QHYPLYR 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034604568 233 rsdancsgedaapaeerdipfkenydvlsreasqkLLWWLQPRLVLSGHTHSACEVHHGGRVPELSVPSFSWRNR 307
Cdd:cd08165   117 -----------------------------------LLQWLKPRLVLSGHTHSACEVLHYGGIPEISVPSFSWRNR 156
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 73-307 9.75e-55

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: 177.93  E-value: 9.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  73 MFLADTHLLGEFLGHW-------LDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRH 145
Cdd:cd07384     1 LLIADPQILDETSYPPrpkpalrLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 146 PS-----HVQLKVVAGNHDIGFHYEMN-TYKVERFEKVFSserLFSwkginfvmvnsvalngdgcgicseteaelievsh 219
Cdd:cd07384    81 KSpgslgSIPVIFIPGNHDIGYGGEAVfPEKVDRFEKYFI---LLT---------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 220 rlncsreHYPLYRRSDAncsgedaapaeerdipfkenydvlsreasqkllwwLQPRLVLSGHTHSACEVHHG---GRVPE 296
Cdd:cd07384   124 -------HIPLYRLLDS-----------------------------------IKPVLILSGHDHDYCEVVHKsspGSVKE 161

                         250
                  ....*....|.
gi 1034604568 297 LSVPSFSWRNR 307
Cdd:cd07384   162 ITVKSFSWRMG 172
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 92-304 2.29e-23

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: 97.48  E-value: 2.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  92 LRREW-QMERAfqtalwlLQPEVVFILGDIFDEGK-WSTpEAWADDVERFQKMFRhPSHVQLKV--VAGNHDIGFHYEMN 167
Cdd:cd08163    33 LRRNWrYLQKQ-------LKPDSTFFLGDLFDGGReWAD-EYWKKEYFRFNRIFD-PKPLRKMIesLPGNHDIGFGNGVK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 168 TYKVERFEKVF-SSERLFSWKGINFVMVNSVALNGDGCGICSETEAELIevsHRLNCSRE---------HYPLYRRSDAN 237
Cdd:cd08163   104 LPVRQRFESYFgPTSRVIDVGNHTFVIVDTISLSNNDNPQVYQPAREFL---HSFEAMKVnskprilltHVPLYRPPNTS 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604568 238 CsgedaAPAEERDIPFKENY-----DVLSREASQKLLWWLQPRLVLSGHTHSACEVHH-------GGRVPELSVPSFSW 304
Cdd:cd08163   181 C-----GPLREKKTPLPYGYgyqyqNVLEPSLSESILKAINPVAAFSGDDHDYCEVVHeyqfdgkEGSAREITVKSISM 254
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
75-312 1.10e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 69.72  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  75 LADTHLLGEFLGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDIFDEGkwsTPEAWaddvERFQKMFRhPSHVQLKVV 154
Cdd:COG1409     6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDG---EPEEY----AAAREILA-RLGVPVYVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 155 AGNHDIGFHYEMNTYKVERFEKVFSSERLFSWKGINFVMVNSVALNGDGCGICSETEAELIEV------SHRLNCSreHY 228
Cdd:COG1409    71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEElaaapaKPVIVFL--HH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 229 PLYrrsdANCSGEDAAPAEERDipfkENYDVLSReasqkllwwLQPRLVLSGHTHSACEVHHGGrVPELSVPSFSWRNRN 308
Cdd:COG1409   149 PPY----STGSGSDRIGLRNAE----ELLALLAR---------YGVDLVLSGHVHRYERTRRDG-VPYIVAGSTGGQVRL 210


                  ....
gi 1034604568 309 NPSF 312
Cdd:COG1409   211 PPGY 214
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 73-178 3.23e-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: 55.91  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  73 MFLADTHLLGE----FLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSH 148
Cdd:cd08166     1 LLVADPQILGYenekFGLGEISRWDSDRYLAKTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPLKRG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034604568 149 VQLKVVAGNHDIGFHYEM-NTYKVERFEKVF 178
Cdd:cd08166    81 KNAIYIPGDNDIGGESEIiIESRVRRFNNYF 111
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 70-186 3.25e-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: 48.36  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  70 LKAMFLADTHLLGEF--LGHWLDKLRREwqmerafqtalwlLQPEVVFILGDIFDEGKWStpEAWADDVERFQKmfrhps 147
Cdd:pfam00149   1 MRILVIGDLHLPGQLddLLELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS--EEVLELLERLIK------ 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034604568 148 HVQLKVVAGNHDIGFH--------YEMNTYKVERFEKVFSSERLFSW 186
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGeclrlypyLGLLARPWKRFLEVFNFLPLAGI 106
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 102-178 1.26e-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: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 102 FQTALWLLQPEVVFILGDIFDEgKWSTPEAWADDVERFQKMF-----------RHPS------HVQLKVVAGNHDIGFHY 164
Cdd:cd08164    36 YQMMQFRLKPTHVTVLGDLFSS-QWITDEEFEKRADRYKKRIfgrsdwqvgniSLAArtfengDILLINIAGNHDVGYAG 114

                          90
                  ....*....|....
gi 1034604568 165 EMNTYKVERFEKVF 178
Cdd:cd08164   115 ESTEARISRFEQLF 128
COG1407 COG1407
Metallophosphoesterase superfamily enzyme [General function prediction only];
71-161 1.30e-05

Metallophosphoesterase superfamily enzyme [General function prediction only];


Pssm-ID: 441017  Cd Length: 224  Bit Score: 45.64  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  71 KAMFLADTHLlgEFLGHwldkLRRE------WQMERAFQ---TALWLLQPEVVFILGDIFDEGKWSTPEAWaDDVERFQK 141
Cdd:COG1407    24 RTLVVADLHL--GKESA----FRRRgiplppYDTRETLErleALIERTGPDRLIILGDLFHDFGGPSRQEW-EELERLLA 96

                          90       100
                  ....*....|....*....|
gi 1034604568 142 MFRhpsHVQLKVVAGNHDIG 161
Cdd:COG1407    97 LHA---GVEVILVRGNHDPG 113
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
76-159 2.23e-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: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  76 ADTHLlgeflghwlDKLRREWQMERAFQTAL-WLL------QPEVVFILGDIFDegkwsTPEAWADDVERFQKMFRHPSH 148
Cdd:COG0420     7 ADWHL---------GKPLHGASRREDQLAALdRLVdlaieeKVDAVLIAGDLFD-----SANPSPEAVRLLAEALRRLSE 72

                          90
                  ....*....|...
gi 1034604568 149 VQLKVV--AGNHD 159
Cdd:COG0420    73 AGIPVVliAGNHD 85
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 74-164 7.51e-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: 7.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  74 FLADTHLLGEFLGHWLDKLRREwqmerafqtalwLLQPEVVFILGDIFDEGKWstPEAWADDVERFQKMFrhpshVQLKV 153
Cdd:cd00838     2 VISDIHGNLEALEAVLEAALAK------------AEKPDLVICLGDLVDYGPD--PEEVELKALRLLLAG-----IPVYV 62

                          90
                  ....*....|..
gi 1034604568 154 VAGNHDIGF-HY 164
Cdd:cd00838    63 VPGNHDILVtHG 74
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 110-303 3.25e-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: 41.92  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 110 QPEVVFILGDIFDEGKWstpEAWADD-VERFQKMFRH-PSHVQLKVVAGNHDIGFHYEMNTykVERFEKVFSSERLFSW- 186
Cdd:cd07395    50 KPKFVVVCGDLVHAMPG---EEFREQqVSDLKDVLSKlDPDIPLVCVCGNHDVGNTPTPET--IQRYRDDFGDDYFSFWv 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 187 KGINFVMVNSVAL-NGDGCGICSETE----AELIEVSHRLNCSR----EHYPLYRRSdancsgedaaPAEErdipfkENY 257
Cdd:cd07395   125 GGVFFIVLNSQLFkDPSKVPELASAQdqwlEEQLQIARESDAKHvvvfQHIPLFLED----------PDEE------DDY 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034604568 258 DVLSREASQKLLWWL---QPRLVLSGHTHSacevHHGGRVPELSVPSFS 303
Cdd:cd07395   189 FNIPKSVRRELLDKFkkaGVKAVFSGHYHR----NAGGRYRDLEMVVTS 233
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 96-284 3.68e-04

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 41.90  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  96 WQMERAFQTALWLLQ----PEVVFILGDI---FDEGKWSTPEAWADDVERFQkmfrhpSHVQLKVVAGNHDIGFHYEMNT 168
Cdd:cd00839    15 QNTNNSTNTLDHLEKelgnYDAIIHVGDIayaDGYNNGSRWDTFMRQIEPLA------SYVPYMVAPGNHEADYNGSTSK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 169 YK-----VERFEKVFSSERLF--SWK--GINFVMVNSVALNGDGcGICSET----EAELIEVshrlNCSRE-------HY 228
Cdd:cd00839    89 IKffmpgRGMPPSPSGSTENLwySFDvgPVHFISLSTETDFLKG-DNISPQydwlEADLAKV----DRSRTpwiivmgHR 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034604568 229 PLYrrsdanCSGEDAApaeerDIPFKENYdvlsREASQKLLWWLQPRLVLSGHTHS 284
Cdd:cd00839   164 PMY------CSNDDDA-----DCIEGEKM----REALEDLFYKYGVDLVLSGHVHA 204
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 73-159 2.74e-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: 38.88  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  73 MFLADTHLLgeflghwLDKLRREWQMERAFQTalWLLQPEVVFILGDIFD---EGKWSTPEAWADDVERFQKMFRHpsHV 149
Cdd:cd07398     1 LFISDLHLG-------LRGCRADRLLDFLLVE--ELDEADALYLLGDIFDlwiGDDSVVWPGAHRALARLLRLADR--GT 69

                          90
                  ....*....|
gi 1034604568 150 QLKVVAGNHD 159
Cdd:cd07398    70 EVIYVPGNHD 79
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 75-301 3.23e-03

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 38.80  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  75 LADTHLLGEFLGHWL--DKLRRewqmeraFQTALWLL-----QPEVVFILGDIFDEGkwsTPEAWaddvERFQKM---FR 144
Cdd:cd07402     4 ISDTHLFAPGEGALLgvDTAAR-------LAAAVAQVnalhpRPDLVVVTGDLSDDG---SPESY----ERLRELlapLP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 145 HPSHvqlkVVAGNHDigfhyemntyKVERFEKVFSS---------ERLFSWKGINFVMVNSVaLNGDGCGICSETEAELI 215
Cdd:cd07402    70 APVY----WIPGNHD----------DRAAMREALPEppyddngpvQYVVDFGGWRLILLDTS-VPGVHHGELSDEQLDWL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 216 EvsHRLNCSRE--------HYPLyrrsDANCSGEDAAPAEERDipfkENYDVLSREAsqkllwwlQPRLVLSGHTHSACE 287
Cdd:cd07402   135 E--AALAEAPDrptliflhHPPF----PLGIPWMDAIRLRNSQ----ALFAVLARHP--------QVKAILCGHIHRPIS 196

                         250
                  ....*....|....
gi 1034604568 288 VHHGGRvPELSVPS 301
Cdd:cd07402   197 GSFRGI-PFSTAPS 209
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 70-315 5.76e-03

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE 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: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 37.64  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  70 LKAMFLADTHLLG----EFLGHWLDKLRRewqmerafqtalwlLQPEVVFILGDIFDEGKWStpeawADDVERFQKMFRH 145
Cdd:cd07385     2 LRIVQLSDIHLGPfvgrTRLQKVVRKVNE--------------LNPDLIVITGDLVDGDVSV-----LRLLASPLSKLKA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 146 PshvqLKV--VAGNHDIGfhyemnTYKVERFEKVFSSErlfswkGINfVMVN-SVALNGDGCGICSETeaelIEVSHRLN 222
Cdd:cd07385    63 P----LGVyfVLGNHDYY------SGDVEVWIAALEKA------GIT-VLRNeSVELSRDGATIGLAG----SGVDDIGG 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568 223 csreHYPLYRRSDANCSGEDA------APAEERDIpfkENYDVlsreasqkllwwlqpRLVLSGHThsacevhHGGRVPe 296
Cdd:cd07385   122 ----HGEDLEKALKGLDENDPvillahNPDAAEEA---QRPGV---------------DLVLSGHT-------HGGQIF- 171

                         250
                  ....*....|....*....
gi 1034604568 297 lsVPSFSWRNRNNPSFIMG 315
Cdd:cd07385   172 --PPNYGVLSKLGFPYDSG 188
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 73-160 7.37e-03

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 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: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 37.25  E-value: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604568  73 MFL--ADTHLlGEFLGHWLDKLRREWQM-ERAFQTALwllQPEVVFIL--GDIFDEGKWStPEAwaddVERFQKMFR--H 145
Cdd:cd00840     1 RFLhtADWHL-GYPLYGLSRREEDFFKAfEEIVDLAI---EEKVDFVLiaGDLFDSNNPS-PEA----LKLAIEGLRrlC 71

                          90
                  ....*....|....*
gi 1034604568 146 PSHVQLKVVAGNHDI 160
Cdd:cd00840    72 EAGIPVFVIAGNHDS 86
 
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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