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Conserved domains on  [gi|62955371|ref|NP_001017701|]
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metallophosphoesterase 1 [Danio rerio]

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 ...
 55-314 6.13e-84

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: 252.38  E-value: 6.13e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  55 LFLSDTHLLGAIRGHWLDKLRREWQMERAFQTSMWLLNPEVVFILGDVFDEGKWSTSQDWEDDVRRFKRIFRHPVDTKLV 134
Cdd:cd08165   1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 135 VLVGNHDIGFHHEMTKQKLERFEQVFnvtsariltikgvnfllvnsvalhgdhcpicqhveeelqklshalncsiqgaqh 214
Cdd:cd08165  81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 215 ngqcknaarfapaapVLLQHYPLYRvsdamctgvdtapldeqyllfqerydvisknaskkLLWWFKPRLILSGHTHNGCE 294
Cdd:cd08165 107 ---------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACE 136

                       250       260
                ....*....|....*....|
gi 62955371 295 VLHEKLYPEISVPSFSWRNR 314
Cdd:cd08165 137 VLHYGGIPEISVPSFSWRNR 156
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 55-314 6.13e-84

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: 252.38  E-value: 6.13e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  55 LFLSDTHLLGAIRGHWLDKLRREWQMERAFQTSMWLLNPEVVFILGDVFDEGKWSTSQDWEDDVRRFKRIFRHPVDTKLV 134
Cdd:cd08165   1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 135 VLVGNHDIGFHHEMTKQKLERFEQVFnvtsariltikgvnfllvnsvalhgdhcpicqhveeelqklshalncsiqgaqh 214
Cdd:cd08165  81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 215 ngqcknaarfapaapVLLQHYPLYRvsdamctgvdtapldeqyllfqerydvisknaskkLLWWFKPRLILSGHTHNGCE 294
Cdd:cd08165 107 ---------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACE 136

                       250       260
                ....*....|....*....|
gi 62955371 295 VLHEKLYPEISVPSFSWRNR 314
Cdd:cd08165 137 VLHYGGIPEISVPSFSWRNR 156
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-330 2.70e-14

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 71.65  E-value: 2.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  52 LRALFLSDTHLLGAIRGHWLDKLRrewqmerAFQTSMWLLNPEVVFILGDVFDEGKwstsqdwEDDVRRFKRIFRhPVDT 131
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDGE-------PEEYAAAREILA-RLGV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 132 KLVVLVGNHDIGFHheMTKQKLERFEQVFNVTSARILTIKGVNFLLVNSVALHGDHCPICqhvEEELQKLSHALncsiqg 211
Cdd:COG1409  66 PVYVVPGNHDIRAA--MAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELG---PEQLAWLEEEL------ 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 212 aqhngqcknaaRFAPAAPVLL-QHYPLYRVSDAMctgvDTAPLDEQYLLFQ--ERYDVisknaskkllwwfkpRLILSGH 288
Cdd:COG1409 135 -----------AAAPAKPVIVfLHHPPYSTGSGS----DRIGLRNAEELLAllARYGV---------------DLVLSGH 184

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62955371 289 THNGcEVLHEKLYPEISVPSFSWRNRNNPSFVLGTFSQSEFQ 330
Cdd:COG1409 185 VHRY-ERTRRDGVPYIVAGSTGGQVRLPPGYRVIEVDGDGLT 225
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 52-189 3.51e-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: 45.67  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371    52 LRALFLSDTHLLGAIRG--HWLDKLRREwqmerafqtsmwlLNPEVVFILGDVFDEGKWStsQDWEDDVRRFKRIfrhpv 129
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDllELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS--EEVLELLERLIKY----- 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62955371   130 dTKLVVLVGNHDIGFHHemtkqkLERFEQVFNVTSARILTIKGVNFLLVNSVALHG-DHCP 189
Cdd:pfam00149  61 -VPVYLVRGNHDFDYGE------CLRLYPYLGLLARPWKRFLEVFNFLPLAGILSGhTHVP 114
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 55-314 6.13e-84

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: 252.38  E-value: 6.13e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  55 LFLSDTHLLGAIRGHWLDKLRREWQMERAFQTSMWLLNPEVVFILGDVFDEGKWSTSQDWEDDVRRFKRIFRHPVDTKLV 134
Cdd:cd08165   1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 135 VLVGNHDIGFHHEMTKQKLERFEQVFnvtsariltikgvnfllvnsvalhgdhcpicqhveeelqklshalncsiqgaqh 214
Cdd:cd08165  81 VVAGNHDIGFHYEMTTYKVHRFEKVF------------------------------------------------------ 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 215 ngqcknaarfapaapVLLQHYPLYRvsdamctgvdtapldeqyllfqerydvisknaskkLLWWFKPRLILSGHTHNGCE 294
Cdd:cd08165 107 ---------------ILLQHYPLYR-----------------------------------LLQWLKPRLVLSGHTHSACE 136

                       250       260
                ....*....|....*....|
gi 62955371 295 VLHEKLYPEISVPSFSWRNR 314
Cdd:cd08165 137 VLHYGGIPEISVPSFSWRNR 156
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 55-314 5.94e-43

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: 147.50  E-value: 5.94e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  55 LFLSDTHLLGAIRGHW-------LDKLRREWQMERAFQTSMWLLNPEVVFILGDVFDEGKWSTSQDWEDDVRRFKRIFRH 127
Cdd:cd07384   1 LLIADPQILDETSYPPrpkpalrLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 128 P-----VDTKLVVLVGNHDIGFHHEMTK-QKLERFEQVFnvtsariltikgvnfllvnsvalhgdhcpicqhveeelqkl 201
Cdd:cd07384  81 KspgslGSIPVIFIPGNHDIGYGGEAVFpEKVDRFEKYF----------------------------------------- 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 202 shalncsiqgaqhngqcknaarfapaapVLLQHYPLYRVSDAmctgvdtapldeqyllfqerydvisknaskkllwwFKP 281
Cdd:cd07384 120 ----------------------------ILLTHIPLYRLLDS-----------------------------------IKP 136

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 62955371 282 RLILSGHTHNGCEVLHEKLY---PEISVPSFSWRNR 314
Cdd:cd07384 137 VLILSGHDHDYCEVVHKSSPgsvKEITVKSFSWRMG 172
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 74-311 8.29e-25

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: 101.71  E-value: 8.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  74 LRREW-QMERAfqtsmwlLNPEVVFILGDVFDEGK-WSTSQdWEDDVRRFKRIFRHPVDTKLV-VLVGNHDIGFHHEMTK 150
Cdd:cd08163  33 LRRNWrYLQKQ-------LKPDSTFFLGDLFDGGReWADEY-WKKEYFRFNRIFDPKPLRKMIeSLPGNHDIGFGNGVKL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 151 QKLERFEQVFNVTSaRILTIKGVNFLLVNSVALHGDHCPICQHVEEELQKLshalncsiqgaqhngqcKNAARFAPAAPV 230
Cdd:cd08163 105 PVRQRFESYFGPTS-RVIDVGNHTFVIVDTISLSNNDNPQVYQPAREFLHS-----------------FEAMKVNSKPRI 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 231 LLQHYPLYRVSDAMCtgvdtAPLDEQYLLFQERY-----DVISKNASKKLLWWFKPRLILSGHTHNGCEVLHE------- 298
Cdd:cd08163 167 LLTHVPLYRPPNTSC-----GPLREKKTPLPYGYgyqyqNVLEPSLSESILKAINPVAAFSGDDHDYCEVVHEyqfdgke 241

                       250
                ....*....|...
gi 62955371 299 KLYPEISVPSFSW 311
Cdd:cd08163 242 GSAREITVKSISM 254
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-330 2.70e-14

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 71.65  E-value: 2.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  52 LRALFLSDTHLLGAIRGHWLDKLRrewqmerAFQTSMWLLNPEVVFILGDVFDEGKwstsqdwEDDVRRFKRIFRhPVDT 131
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDGE-------PEEYAAAREILA-RLGV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 132 KLVVLVGNHDIGFHheMTKQKLERFEQVFNVTSARILTIKGVNFLLVNSVALHGDHCPICqhvEEELQKLSHALncsiqg 211
Cdd:COG1409  66 PVYVVPGNHDIRAA--MAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELG---PEQLAWLEEEL------ 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 212 aqhngqcknaaRFAPAAPVLL-QHYPLYRVSDAMctgvDTAPLDEQYLLFQ--ERYDVisknaskkllwwfkpRLILSGH 288
Cdd:COG1409 135 -----------AAAPAKPVIVfLHHPPYSTGSGS----DRIGLRNAEELLAllARYGV---------------DLVLSGH 184

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62955371 289 THNGcEVLHEKLYPEISVPSFSWRNRNNPSFVLGTFSQSEFQ 330
Cdd:COG1409 185 VHRY-ERTRRDGVPYIVAGSTGGQVRLPPGYRVIEVDGDGLT 225
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 82-176 1.07e-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: 60.53  E-value: 1.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  82 RAFQTSMWLLNPEVVFILGDVFDEGKWSTSQDWEDDVRRFKRIFRHPVDTKLVVLVGNHDIGFHHEM-TKQKLERFEQVF 160
Cdd:cd08166  32 KTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPLKRGKNAIYIPGDNDIGGESEIiIESRVRRFNNYF 111

                        90
                ....*....|....*.
gi 62955371 161 NVTSARILTIKGVNFL 176
Cdd:cd08166 112 IMLSHVPLLVEGYLLL 127
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 84-160 3.74e-09

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: 55.96  E-value: 3.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  84 FQTSMWLLNPEVVFILGDVFDEgKWSTSQDWEDDVRRFKRIF--RHPV---------------DTKLVVLVGNHDIGFHH 146
Cdd:cd08164  36 YQMMQFRLKPTHVTVLGDLFSS-QWITDEEFEKRADRYKKRIfgRSDWqvgnislaartfengDILLINIAGNHDVGYAG 114

                        90
                ....*....|....
gi 62955371 147 EMTKQKLERFEQVF 160
Cdd:cd08164 115 ESTEARISRFEQLF 128
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 55-188 2.14e-06

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: 48.12  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  55 LFLSDTHLL--GAIRGHWLDKLRREWqmerafqtsmwLLNPEVVFILGDVFDegKWSTSQDW-----EDDVRRFKRIFRH 127
Cdd:cd07398   1 LFISDLHLGlrGCRADRLLDFLLVEE-----------LDEADALYLLGDIFD--LWIGDDSVvwpgaHRALARLLRLADR 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62955371 128 PvdTKLVVLVGNHDigFHHEMTKQKLERFEQVFnvTSARILTIKGVNFLLvnsvaLHGDHC 188
Cdd:cd07398  68 G--TEVIYVPGNHD--FLLGRFFAEALGAILLP--EPAEHLELDGKRLLV-----LHGDQL 117
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 52-189 3.51e-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: 45.67  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371    52 LRALFLSDTHLLGAIRG--HWLDKLRREwqmerafqtsmwlLNPEVVFILGDVFDEGKWStsQDWEDDVRRFKRIfrhpv 129
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDllELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS--EEVLELLERLIKY----- 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62955371   130 dTKLVVLVGNHDIGFHHemtkqkLERFEQVFNVTSARILTIKGVNFLLVNSVALHG-DHCP 189
Cdd:pfam00149  61 -VPVYLVRGNHDFDYGE------CLRLYPYLGLLARPWKRFLEVFNFLPLAGILSGhTHVP 114
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 55-189 1.87e-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: 43.80  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  55 LFLSDTHLlgaiRGHWLDKLRREWQMERAfqtsmwllNPEVVFILGDVFDEGKWStsqdwEDDVRRFKRIFRHPVDTklV 134
Cdd:cd00838   1 LVISDIHG----NLEALEAVLEAALAKAE--------KPDLVICLGDLVDYGPDP-----EEVELKALRLLLAGIPV--Y 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62955371 135 VLVGNHDIGFHHEMTKQKLERFEQVFNVTSARILT-IKGVNFLLVnsvaLHG-DHCP 189
Cdd:cd00838  62 VVPGNHDILVTHGPPYDPLDEGSPGEDPGSEALLElLDKYGPDLV----LSGhTHVP 114
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
53-295 2.81e-05

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 44.62  E-value: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  53 RALFLSDTHLlgaiRGHWLDKLRREWQMERAfqtsmwllnpEVVFILGDVFDEGKWstsqdwEDDVRRFKRIFRHPVDTk 132
Cdd:COG2129   1 KILAVSDLHG----NFDLLEKLLELARAEDA----------DLVILAGDLTDFGTA------EEAREVLEELAALGVPV- 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 133 LVVLvGNHDigfhHEMTKQKLERFeqvfNVTSA--RILTIKGVNFLLVNSVALHGDHCPiCQHVEEELQKLSHALncsiq 210
Cdd:COG2129  60 LAVP-GNHD----DPEVLDALEES----GVHNLhgRVVEIGGLRIAGLGGSRPTPFGTP-YEYTEEEIEERLAKL----- 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 211 gaqhngqcknaarFAPAAPVLLQHYPlyrvsdamctgvdtaPLDEQYLLFQERYDVISKNAsKKLLWWFKPRLILSGHTH 290
Cdd:COG2129 125 -------------REKDVDILLTHAP---------------PYGTTLDRVEDGPHVGSKAL-RELIEEFQPKLVLHGHIH 175


                ....*
gi 62955371 291 NGCEV 295
Cdd:COG2129 176 ESRGV 180
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 49-290 4.74e-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: 44.62  E-value: 4.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  49 HSPLRALFLSDTHLlGAIRGHWLDKLRREWQMERAF-QTSMWLLN-----PEVVFILGDVFDEGKWSTSQDweDDVRRFK 122
Cdd:cd07395   2 KGPFYFIQGADPQL-GLIKQNNIGNGGDEWDKEIELtEQAVQAINklnpkPKFVVVCGDLVHAMPGEEFRE--QQVSDLK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 123 RIFRHpVDTK--LVVLVGNHDIGfhHEMTKQKLERFEQVFNVTSARiLTIKGVNFLLVNSVaLHGDHcpicQHVEEELQK 200
Cdd:cd07395  79 DVLSK-LDPDipLVCVCGNHDVG--NTPTPETIQRYRDDFGDDYFS-FWVGGVFFIVLNSQ-LFKDP----SKVPELASA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 201 LSHALNCSIQGAqHNGQCKNAarfapaapVLLQHYPLYrvsdamctgVDTAPLDEQYllFQerydvISKNASKKLLWWFK 280
Cdd:cd07395 150 QDQWLEEQLQIA-RESDAKHV--------VVFQHIPLF---------LEDPDEEDDY--FN-----IPKSVRRELLDKFK 204

                       250
                ....*....|...
gi 62955371 281 P---RLILSGHTH 290
Cdd:cd07395 205 KagvKAVFSGHYH 217
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
55-141 2.96e-04

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 41.82  E-value: 2.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  55 LFLSDTHLlgairghwlDKLRREWQMERAFQTSM-WLL------NPEVVFILGDVFDegkwsTSQDWEDDVRRFKRIFR- 126
Cdd:COG0420   4 LHTADWHL---------GKPLHGASRREDQLAALdRLVdlaieeKVDAVLIAGDLFD-----SANPSPEAVRLLAEALRr 69

                        90
                ....*....|....*.
gi 62955371 127 -HPVDTKLVVLVGNHD 141
Cdd:COG0420  70 lSEAGIPVVLIAGNHD 85
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 91-143 1.27e-03

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277337  Cd Length: 175  Bit Score: 39.22  E-value: 1.27e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 62955371  91 LNPEVVFILGDVFDEGKWSTSQDWEDDVRRFKRifrhPVDTKLVVLVGNHDIG 143
Cdd:cd07391  40 LGPDRLVILGDLKHSFGRVSRQERREVPFFRLL----AKDVDVILIRGNHDGG 88
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 51-329 1.30e-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: 39.96  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  51 PLRALFLSDTHLLGAIRGHWLDKLRRewqMERAfqtsmwlLNPEVVFILGDVFDEGKWstsqdwedDVRRFKRIFR--HP 128
Cdd:cd07385   1 GLRIVQLSDIHLGPFVGRTRLQKVVR---KVNE-------LNPDLIVITGDLVDGDVS--------VLRLLASPLSklKA 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 129 VDTKLVVLvGNHDI-GFHHEMTKQKLERFEqvFNVTSARILTIKGVNFLLVNSVALHGDHCPICQHVEEELQKLShalnc 207
Cdd:cd07385  63 PLGVYFVL-GNHDYySGDVEVWIAALEKAG--ITVLRNESVELSRDGATIGLAGSGVDDIGGHGEDLEKALKGLD----- 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 208 siqgaqhngqcKNAARfapaapVLLQHYPLYRvsdamctgvdtapldEQYllfqERYDVisknaskkllwwfkpRLILSG 287
Cdd:cd07385 135 -----------ENDPV------ILLAHNPDAA---------------EEA----QRPGV---------------DLVLSG 163

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62955371 288 HTHNGcevlheklypEISVPSFSWRNRNNPSFVLGTFSQSEF 329
Cdd:cd07385 164 HTHGG----------QIFPPNYGVLSKLGFPYDSGLYQIGGT 195
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 57-291 1.68e-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: 39.57  E-value: 1.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371  57 LSDTHLLGAIRGHWL--DKLRRewqmeraFQTSMWLLN-----PEVVFILGDVFDEGkwstsqdWEDDVRRFKRIFrHPV 129
Cdd:cd07402   4 ISDTHLFAPGEGALLgvDTAAR-------LAAAVAQVNalhprPDLVVVTGDLSDDG-------SPESYERLRELL-APL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 130 DTKLVVLVGNHDigFHHEMtkqkLERFEQVFNVTSA---RILTIKGVNFLLVNSV---ALHGDHCpicqhvEEELQKLSH 203
Cdd:cd07402  69 PAPVYWIPGNHD--DRAAM----REALPEPPYDDNGpvqYVVDFGGWRLILLDTSvpgVHHGELS------DEQLDWLEA 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955371 204 ALncsiqgaqhngqcknaARfAPAAPVLL-QHYPLYRVSDamctgvdtAPLDEQYLLFQER-YDVISKNAskkllwwfKP 281
Cdd:cd07402 137 AL----------------AE-APDRPTLIfLHHPPFPLGI--------PWMDAIRLRNSQAlFAVLARHP--------QV 183

                       250
                ....*....|
gi 62955371 282 RLILSGHTHN 291
Cdd:cd07402 184 KAILCGHIHR 193
 
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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