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Conserved domains on  [gi|1958743440|ref|XP_038952911|]
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metallophosphoesterase 1 isoform X6 [Rattus norvegicus]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 70-175 1.24e-62

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.


The actual alignment was detected with superfamily member cd08165:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 156  Bit Score: 193.06  E-value: 1.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100
                  ....*....|....*....|....*.
gi 1958743440 150 VVIGNHDIGFHYQMSKYRINRFEKVF 175
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF 106
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 70-175 1.24e-62

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: 193.06  E-value: 1.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100
                  ....*....|....*....|....*.
gi 1958743440 150 VVIGNHDIGFHYQMSKYRINRFEKVF 175
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF 106
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
72-217 1.28e-06

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  72 LADTHLLGEIRGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQrmfrhgshVQLKVV 151
Cdd:COG1409     6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG--------VPVYVV 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440 152 IGNHDIGFHYQMSKYRINRFEKVFGSERLFSLKGVNFVMVNSVAMEGDGCTICSE----AEAELREISRK 217
Cdd:COG1409    71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEqlawLEEELAAAPAK 140
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 67-167 2.09e-05

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: 42.59  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  67 LKAMFLADTHLLGEIRG--HWLDKLRREwqmerafqtalwlLQPEVVFILGDVFDEGKWSSAQAWAddlhrfqrMFRHGS 144
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDllELLKKLLEE-------------GKPDLVLHAGDLVDRGPPSEEVLEL--------LERLIK 59

                          90       100
                  ....*....|....*....|...
gi 1958743440 145 HVQLKVVIGNHDIGFHYQMSKYR 167
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGECLRLYP 82
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 70-175 1.24e-62

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: 193.06  E-value: 1.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100
                  ....*....|....*....|....*.
gi 1958743440 150 VVIGNHDIGFHYQMSKYRINRFEKVF 175
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFEKVF 106
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 70-175 5.95e-36

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: 125.15  E-value: 5.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  70 MFLADTHLLGEIRGHW-------LDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRH 142
Cdd:cd07384     1 LLIADPQILDETSYPPrpkpalrLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958743440 143 GS-----HVQLKVVIGNHDIGFHYQMSKY-RINRFEKVF 175
Cdd:cd07384    81 KSpgslgSIPVIFIPGNHDIGYGGEAVFPeKVDRFEKYF 119
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 61-197 6.74e-16

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: 74.75  E-value: 6.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  61 GRQEPVLK-AMFLADTHLlgeirghwldklRREW-QMERAfqtalwlLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQR 138
Cdd:cd08163    16 GRPWILNTlTEHFVDQYL------------RRNWrYLQKQ-------LKPDSTFFLGDLFDGGREWADEYWKKEYFRFNR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958743440 139 MFRHgSHVQLKVVI--GNHDIGFHYQMSKYRINRFEKVFG-SERLFSLKGVNFVMVNSVAME 197
Cdd:cd08163    77 IFDP-KPLRKMIESlpGNHDIGFGNGVKLPVRQRFESYFGpTSRVIDVGNHTFVIVDTISLS 137
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 70-175 3.55e-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: 57.45  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  70 MFLADTHLLGEIRGHWLDKLRREWQMER----AFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSH 145
Cdd:cd08166     1 LLVADPQILGYENEKFGLGEISRWDSDRylakTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPLKRG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958743440 146 VQLKVVIGNHDIGFHYQM-SKYRINRFEKVF 175
Cdd:cd08166    81 KNAIYIPGDNDIGGESEIiIESRVRRFNNYF 111
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
72-217 1.28e-06

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  72 LADTHLLGEIRGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQrmfrhgshVQLKVV 151
Cdd:COG1409     6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG--------VPVYVV 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440 152 IGNHDIGFHYQMSKYRINRFEKVFGSERLFSLKGVNFVMVNSVAMEGDGCTICSE----AEAELREISRK 217
Cdd:COG1409    71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEqlawLEEELAAAPAK 140
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 67-167 2.09e-05

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: 42.59  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  67 LKAMFLADTHLLGEIRG--HWLDKLRREwqmerafqtalwlLQPEVVFILGDVFDEGKWSSAQAWAddlhrfqrMFRHGS 144
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDllELLKKLLEE-------------GKPDLVLHAGDLVDRGPPSEEVLEL--------LERLIK 59

                          90       100
                  ....*....|....*....|...
gi 1958743440 145 HVQLKVVIGNHDIGFHYQMSKYR 167
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGECLRLYP 82
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 99-175 3.45e-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: 43.24  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  99 FQTALWLLQPEVVFILGDVF-------DEGKWSSAQAWA---------DDLHRFQRMFRHGSHVQLKVVIGNHDIGFHYQ 162
Cdd:cd08164    36 YQMMQFRLKPTHVTVLGDLFssqwitdEEFEKRADRYKKrifgrsdwqVGNISLAARTFENGDILLINIAGNHDVGYAGE 115

                          90
                  ....*....|...
gi 1958743440 163 MSKYRINRFEKVF 175
Cdd:cd08164   116 STEARISRFEQLF 128
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
73-156 4.56e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 43.36  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  73 ADTHLlgeirghwlDKLRREWQMERAFQTAL-WLL------QPEVVFILGDVFDegkwsSAQAWADDLHRFQRMFRHGSH 145
Cdd:COG0420     7 ADWHL---------GKPLHGASRREDQLAALdRLVdlaieeKVDAVLIAGDLFD-----SANPSPEAVRLLAEALRRLSE 72

                          90
                  ....*....|...
gi 1958743440 146 VQLKVVI--GNHD 156
Cdd:COG0420    73 AGIPVVLiaGNHD 85
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 70-233 3.99e-03

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: 37.68  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  70 MFLADTHLlGEIRGHWLDKLRREWQME-----RAFQTALWLL-QPEVVFILGDVFDEGKWSSAQAwaDDLHRFQRMFRH- 142
Cdd:cd07395     8 IQGADPQL-GLIKQNNIGNGGDEWDKEielteQAVQAINKLNpKPKFVVVCGDLVHAMPGEEFRE--QQVSDLKDVLSKl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440 143 GSHVQLKVVIGNHDIGFHYQMSKyrINRFEKVFGSERL-FSLKGVNFVMVNSVAMEGDGCTiCSEAEAELREISRKLNCS 221
Cdd:cd07395    85 DPDIPLVCVCGNHDVGNTPTPET--IQRYRDDFGDDYFsFWVGGVFFIVLNSQLFKDPSKV-PELASAQDQWLEEQLQIA 161

                         170
                  ....*....|..
gi 1958743440 222 QEVGDLCAQVFQ 233
Cdd:cd07395   162 RESDAKHVVVFQ 173
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 71-161 6.67e-03

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 35.71  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743440  71 FLADTHLlgeiRGHWLDKLRREWQMERAfqtalwllQPEVVFILGDVFDEGKWSSAQAWADDLHRFqrmfrhgSHVQLKV 150
Cdd:cd00838     2 VISDIHG----NLEALEAVLEAALAKAE--------KPDLVICLGDLVDYGPDPEEVELKALRLLL-------AGIPVYV 62

                          90
                  ....*....|..
gi 1958743440 151 VIGNHDIGF-HY 161
Cdd:cd00838    63 VPGNHDILVtHG 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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