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Conserved domains on  [gi|578832192|ref|XP_006722411|]
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metallophosphoesterase 1 isoform X9 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 73-178 3.84e-70

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: 214.25  E-value: 3.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLK 152
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100
                 ....*....|....*....|....*.
gi 578832192 153 VVAGNHDIGFHYEMNTYKVERFEKVF 178
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 ...
 73-178 3.84e-70

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: 214.25  E-value: 3.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLK 152
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100
                 ....*....|....*....|....*.
gi 578832192 153 VVAGNHDIGFHYEMNTYKVERFEKVF 178
Cdd:cd08165   81 VVAGNHDIGFHYEMTTYKVHRFEKVF 106
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 70-186 2.12e-08

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: 51.45  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192   70 LKAMFLADTHLLGEF--LGHWLDKLRREwqmerafqtalwlLQPEVVFILGDIFDEGKWStpEAWADDVERFQKmfrhps 147
Cdd:pfam00149   1 MRILVIGDLHLPGQLddLLELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS--EEVLELLERLIK------ 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578832192  148 HVQLKVVAGNHDIGFH--------YEMNTYKVERFEKVFSSERLFSW 186
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGeclrlypyLGLLARPWKRFLEVFNFLPLAGI 106
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
75-197 1.68e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 51.23  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  75 LADTHLLGEFLGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDIFDEGkwsTPEAWaddvERFQKMFRhPSHVQLKVV 154
Cdd:COG1409    6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDG---EPEEY----AAAREILA-RLGVPVYVV 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578832192 155 AGNHDIGFHYEMNTYKVERFEKVFSSERLFSWKGINFVMVNSV 197
Cdd:COG1409   71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSN 113
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 73-178 3.84e-70

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: 214.25  E-value: 3.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  73 MFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLK 152
Cdd:cd08165    1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                         90       100
                 ....*....|....*....|....*.
gi 578832192 153 VVAGNHDIGFHYEMNTYKVERFEKVF 178
Cdd:cd08165   81 VVAGNHDIGFHYEMTTYKVHRFEKVF 106
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 73-178 6.41e-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: 145.18  E-value: 6.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  73 MFLADTHLLGEFLGHW-------LDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRH 145
Cdd:cd07384    1 LLIADPQILDETSYPPrpkpalrLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 578832192 146 PS-----HVQLKVVAGNHDIGFHYEMN-TYKVERFEKVF 178
Cdd:cd07384   81 KSpgslgSIPVIFIPGNHDIGYGGEAVfPEKVDRFEKYF 119
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 92-280 2.51e-17

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: 79.76  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  92 LRREW-QMERAfqtalwlLQPEVVFILGDIFDEGK-WSTpEAWADDVERFQKMFRhPSHVQLKV--VAGNHDIGFHYEMN 167
Cdd:cd08163   33 LRRNWrYLQKQ-------LKPDSTFFLGDLFDGGReWAD-EYWKKEYFRFNRIFD-PKPLRKMIesLPGNHDIGFGNGVK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192 168 TYKVERFEKVF-SSERLFSWKGINFVMVNSVALNgdgcgicSETEAELIEVSHRLNCSREQARgssrcgpGPLLPTsapV 246
Cdd:cd08163  104 LPVRQRFESYFgPTSRVIDVGNHTFVIVDTISLS-------NNDNPQVYQPAREFLHSFEAMK-------VNSKPR---I 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578832192 247 LLQHYPLYRRSDANCsgedaAPAEERDIPFKENY 280
Cdd:cd08163  167 LLTHVPLYRPPNTSC-----GPLREKKTPLPYGY 195
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 73-178 1.46e-09

uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; A functionally uncharacterized subgroup related to the metallophosphatase domain of Saccharomyces cerevisiae Cdc1, S. cerevisiae Ted1 and human MPPE1. Cdc1 is an endoplasmic reticulum-localized transmembrane lipid phosphatase and is a subunit of DNA polymerase delta. TED1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), acts together with Emp24p and Erv25p in cargo exit from the ER. The MPPE1 gene is a candidate susceptibility gene for Bipolar disorder. Proteins in this uncharacterized subgroup belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277373  Cd Length: 195  Bit Score: 56.68  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  73 MFLADTHLLGE----FLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSH 148
Cdd:cd08166    1 LLVADPQILGYenekFGLGEISRWDSDRYLAKTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPLKRG 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 578832192 149 VQLKVVAGNHDIGFHYEM-NTYKVERFEKVF 178
Cdd:cd08166   81 KNAIYIPGDNDIGGESEIiIESRVRRFNNYF 111
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 70-186 2.12e-08

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: 51.45  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192   70 LKAMFLADTHLLGEF--LGHWLDKLRREwqmerafqtalwlLQPEVVFILGDIFDEGKWStpEAWADDVERFQKmfrhps 147
Cdd:pfam00149   1 MRILVIGDLHLPGQLddLLELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS--EEVLELLERLIK------ 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578832192  148 HVQLKVVAGNHDIGFH--------YEMNTYKVERFEKVFSSERLFSW 186
Cdd:pfam00149  60 YVPVYLVRGNHDFDYGeclrlypyLGLLARPWKRFLEVFNFLPLAGI 106
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
75-197 1.68e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 51.23  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  75 LADTHLLGEFLGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDIFDEGkwsTPEAWaddvERFQKMFRhPSHVQLKVV 154
Cdd:COG1409    6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDG---EPEEY----AAAREILA-RLGVPVYVV 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578832192 155 AGNHDIGFHYEMNTYKVERFEKVFSSERLFSWKGINFVMVNSV 197
Cdd:COG1409   71 PGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSN 113
COG1407 COG1407
Metallophosphoesterase superfamily enzyme [General function prediction only];
71-161 4.90e-06

Metallophosphoesterase superfamily enzyme [General function prediction only];


Pssm-ID: 441017  Cd Length: 224  Bit Score: 46.79  E-value: 4.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  71 KAMFLADTHLlgEFLGHwldkLRRE------WQMERAFQ---TALWLLQPEVVFILGDIFDEGKWSTPEAWaDDVERFQK 141
Cdd:COG1407   24 RTLVVADLHL--GKESA----FRRRgiplppYDTRETLErleALIERTGPDRLIILGDLFHDFGGPSRQEW-EELERLLA 96

                         90       100
                 ....*....|....*....|
gi 578832192 142 MFRhpsHVQLKVVAGNHDIG 161
Cdd:COG1407   97 LHA---GVEVILVRGNHDPG 113
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 84-178 5.83e-06

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: 45.94  E-value: 5.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  84 FLGHwldklrrewqmerAFQTALWLLQPEVVFILGDIFDEgKWSTPEAWADDVERFQKMF-----------RHPS----- 147
Cdd:cd08164   31 FLGH-------------IYQMMQFRLKPTHVTVLGDLFSS-QWITDEEFEKRADRYKKRIfgrsdwqvgniSLAArtfen 96

                         90       100       110
                 ....*....|....*....|....*....|..
gi 578832192 148 -HVQLKVVAGNHDIGFHYEMNTYKVERFEKVF 178
Cdd:cd08164   97 gDILLINIAGNHDVGYAGESTEARISRFEQLF 128
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 74-164 8.01e-06

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: 44.57  E-value: 8.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  74 FLADTHLLGEFLGHWLDKLRREwqmerafqtalwLLQPEVVFILGDIFDEGKWstPEAWADDVERFQKMFrhpshVQLKV 153
Cdd:cd00838    2 VISDIHGNLEALEAVLEAALAK------------AEKPDLVICLGDLVDYGPD--PEEVELKALRLLLAG-----IPVYV 62

                         90
                 ....*....|..
gi 578832192 154 VAGNHDIGF-HY 164
Cdd:cd00838   63 VPGNHDILVtHG 74
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
76-159 9.32e-06

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 46.06  E-value: 9.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  76 ADTHLlgeflghwlDKLRREWQMERAFQTAL-WLL------QPEVVFILGDIFDegkwsTPEAWADDVERFQKMFRHPSH 148
Cdd:COG0420    7 ADWHL---------GKPLHGASRREDQLAALdRLVdlaieeKVDAVLIAGDLFD-----SANPSPEAVRLLAEALRRLSE 72

                         90
                 ....*....|...
gi 578832192 149 VQLKVV--AGNHD 159
Cdd:COG0420   73 AGIPVVliAGNHD 85
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 110-197 5.53e-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: 40.77  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192 110 QPEVVFILGDIFDEGKWstpEAWADD-VERFQKMFRH-PSHVQLKVVAGNHDIGFHYEMNTykVERFEKVFSSERLFSW- 186
Cdd:cd07395   50 KPKFVVVCGDLVHAMPG---EEFREQqVSDLKDVLSKlDPDIPLVCVCGNHDVGNTPTPET--IQRYRDDFGDDYFSFWv 124

                         90
                 ....*....|.
gi 578832192 187 KGINFVMVNSV 197
Cdd:cd07395  125 GGVFFIVLNSQ 135
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 73-159 6.80e-04

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: 40.03  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  73 MFLADTHLLGEF--LGHWLDKLRREWqmerafqtalwLLQPEVVFILGDIFD---EGKWSTPEAWADDVERFQKMFRHps 147
Cdd:cd07398    1 LFISDLHLGLRGcrADRLLDFLLVEE-----------LDEADALYLLGDIFDlwiGDDSVVWPGAHRALARLLRLADR-- 67

                         90
                 ....*....|..
gi 578832192 148 HVQLKVVAGNHD 159
Cdd:cd07398   68 GTEVIYVPGNHD 79
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 73-160 3.25e-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: 38.02  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  73 MFL--ADTHLlGEFLGHWLDKLRREWQM-ERAFQTALwllQPEVVFIL--GDIFDEGKWStPEAwaddVERFQKMFR--H 145
Cdd:cd00840    1 RFLhtADWHL-GYPLYGLSRREEDFFKAfEEIVDLAI---EEKVDFVLiaGDLFDSNNPS-PEA----LKLAIEGLRrlC 71

                         90
                 ....*....|....*
gi 578832192 146 PSHVQLKVVAGNHDI 160
Cdd:cd00840   72 EAGIPVFVIAGNHDS 86
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 70-161 4.12e-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: 38.03  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  70 LKAMFLADTHLLG----EFLGHWLDKLRRewqmerafqtalwlLQPEVVFILGDIFDEGKWStpeawADDVERFQKMFRH 145
Cdd:cd07385    2 LRIVQLSDIHLGPfvgrTRLQKVVRKVNE--------------LNPDLIVITGDLVDGDVSV-----LRLLASPLSKLKA 62

                         90
                 ....*....|....*...
gi 578832192 146 PshvqLKV--VAGNHDIG 161
Cdd:cd07385   63 P----LGVyfVLGNHDYY 76
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 73-164 5.56e-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: 36.90  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832192  73 MFLADTHL-LGEFLG-HWLDKLRRewQMERAFQTALWLLQ---PEVVFILGDIFDEGKWSTPEAWaDDVERFqkmFRHPS 147
Cdd:cd07391    1 LVIADLHLgYEEELRrQGINLPRR--QKERLLERLDRLLEelgPDRLVILGDLKHSFGRVSRQER-REVPFF---RLLAK 74

                         90
                 ....*....|....*..
gi 578832192 148 HVQLKVVAGNHDIGFHY 164
Cdd:cd07391   75 DVDVILIRGNHDGGLEE 91
 
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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