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Conserved domains on  [gi|1491335861|gb|RLI96171|]
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MAG: phosphoesterase [Candidatus Altiarchaeales archaeon]

Protein Classification

metallophosphoesterase( domain architecture ID 10003657)

metallophosphoesterase contains 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
COG1407 COG1407
Metallophosphoesterase superfamily enzyme [General function prediction only];
17-238 4.29e-50

Metallophosphoesterase superfamily enzyme [General function prediction only];


:

Pssm-ID: 441017  Cd Length: 224  Bit Score: 163.51  E-value: 4.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  17 LYIEDEKTLLFGDMHLGYEEELNQMGYLIPRFQYDEIINHLTKVFSHIAPERVVICGDLKHEFGRISEQEWNEVMNFLSF 96
Cdd:COG1407    18 LYWPAERTLVVADLHLGKESAFRRRGIPLPPYDTRETLERLEALIERTGPDRLIILGDLFHDFGGPSRQEWEELERLLAL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  97 IERRvdDIVLIKGNHDTILGPIATKRNVKFFSNYYLSGrKIFITHghlipeDPDLYKAKIVIIGHDHPALGIRDEL-RVE 175
Cdd:COG1407    98 HAGV--EVILVRGNHDPGLPDLLEDLGGEVVDEELVLG-GLLFRH------EPEPEAADGEIAGHEHPAVRLRDRVgRSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491335861 176 KVKCFLlgkwRGKDLIQIPSLNFVTEGIDiIREKPLSPFMNQDlsHFRVYCIENDEIFDFGRI 238
Cdd:COG1407   169 RLPCFL----RDGRRLVLPAFGAFTGGLD-VNPPAFSPLLRRG--GAEAYLLDGTRLGPLARL 224
 
Name Accession Description Interval E-value
COG1407 COG1407
Metallophosphoesterase superfamily enzyme [General function prediction only];
17-238 4.29e-50

Metallophosphoesterase superfamily enzyme [General function prediction only];


Pssm-ID: 441017  Cd Length: 224  Bit Score: 163.51  E-value: 4.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  17 LYIEDEKTLLFGDMHLGYEEELNQMGYLIPRFQYDEIINHLTKVFSHIAPERVVICGDLKHEFGRISEQEWNEVMNFLSF 96
Cdd:COG1407    18 LYWPAERTLVVADLHLGKESAFRRRGIPLPPYDTRETLERLEALIERTGPDRLIILGDLFHDFGGPSRQEWEELERLLAL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  97 IERRvdDIVLIKGNHDTILGPIATKRNVKFFSNYYLSGrKIFITHghlipeDPDLYKAKIVIIGHDHPALGIRDEL-RVE 175
Cdd:COG1407    98 HAGV--EVILVRGNHDPGLPDLLEDLGGEVVDEELVLG-GLLFRH------EPEPEAADGEIAGHEHPAVRLRDRVgRSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491335861 176 KVKCFLlgkwRGKDLIQIPSLNFVTEGIDiIREKPLSPFMNQDlsHFRVYCIENDEIFDFGRI 238
Cdd:COG1407   169 RLPCFL----RDGRRLVLPAFGAFTGGLD-VNPPAFSPLLRRG--GAEAYLLDGTRLGPLARL 224
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 25-205 1.49e-49

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: 160.17  E-value: 1.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  25 LLFGDMHLGYEEELNQMGYLIPRFQYDEIINHLTKVFSHIAPERVVICGDLKHEFGRISEQEWNEVMNFlsFIERRVDDI 104
Cdd:cd07391     1 LVIADLHLGYEEELRRQGINLPRRQKERLLERLDRLLEELGPDRLVILGDLKHSFGRVSRQERREVPFF--RLLAKDVDV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861 105 VLIKGNHDTILGPIATKRNVKFFSnYYLSGrKIFITHGHlipEDPDLYKAKIVIIGHDHPALGIRDEL-RVEKVKCFLLG 183
Cdd:cd07391    79 ILIRGNHDGGLEEILSDVNVVVVE-GYLLG-GYLIFHGH---KEPDPLDAKLVIMGHEHPAIKLRDGVgASRKLPCFLRG 153

                         170       180
                  ....*....|....*....|..
gi 1491335861 184 KWRGKDLIQIPSLNFVTEGIDI 205
Cdd:cd07391   154 EGEDGDVIVLPAFNPLTGGVDI 175
SbcD_rel_arch TIGR00024
putative phosphoesterase, SbcD/Mre11-related; Members of this uncharacterized family share a ...
 15-238 2.44e-46

putative phosphoesterase, SbcD/Mre11-related; Members of this uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11. SbcD is a subunit of the SbcCD nuclease of E. coli that can cleave DNA hairpins to unblock stalled DNA replication. All members of this family are archaeal. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129135  Cd Length: 225  Bit Score: 153.86  E-value: 2.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  15 LTLYIEDekTLLFGDMHLGYEEELNQMGYLIPRFQYDEIINHLTKVFSHIAPERVVICGDLKHEFGRisEQEWNEVMNFL 94
Cdd:TIGR00024  10 RVLIIGD--KAVIADLHLGFERHLDEQGVMVPGFQFREIIERALSIADKYGIEALIINGDLKHEFKK--GLEWRFIREFI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  95 SFIERrvdDIVLIKGNHDTilgpiatkrnvkFFSNYYLSGRKIF------ITHGHLIPEDPDLyKAKIVIIGHDHPALGI 168
Cdd:TIGR00024  86 EVTFR---DLILIRGNHDA------------LIPYIGLSGEESIrigkylIFHGHAVPDEEDL-DAKVLIFGHEHPAVKL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861 169 RDELRVEKVKCFLLGKWRGKDLIQIPSLNFVTEGIDIIREKPLSPFMNQDLSHFRVYCIENDEIFDFGRI 238
Cdd:TIGR00024 150 RDSAAGYKFPCFLLGEVEDKRVIVLPAFNPLCAGSDVLLDRPLSPILRKSLREFEVYAIEDFEIMLFGTL 219
PRK09453 PRK09453
phosphodiesterase; Provisional
 131-163 8.15e-06

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 44.85  E-value: 8.15e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1491335861 131 YLSGRKIFITHGHLIPED--PDLYKAKIVIIGHDH 163
Cdd:PRK09453   94 LLEGKRLFLTHGHLYGPEnlPALHDGDVLVYGHTH 128
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 23-163 3.34e-03

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: 36.42  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  23 KTLLFGDMHLGyeeelnqmgyliprFQYDEIINHLTKVFSHIAPERVVICGDLKHEfGRISEqewnEVMNFLSFIERRVD 102
Cdd:pfam00149   2 RILVIGDLHLP--------------GQLDDLLELLKKLLEEGKPDLVLHAGDLVDR-GPPSE----EVLELLERLIKYVP 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491335861 103 dIVLIKGNHDTILGPIATK-RNVKFFSNYYLSGRKIFithghlipedpDLYKAKIVIIGHDH 163
Cdd:pfam00149  63 -VYLVRGNHDFDYGECLRLyPYLGLLARPWKRFLEVF-----------NFLPLAGILSGHTH 112
 
Name Accession Description Interval E-value
COG1407 COG1407
Metallophosphoesterase superfamily enzyme [General function prediction only];
17-238 4.29e-50

Metallophosphoesterase superfamily enzyme [General function prediction only];


Pssm-ID: 441017  Cd Length: 224  Bit Score: 163.51  E-value: 4.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  17 LYIEDEKTLLFGDMHLGYEEELNQMGYLIPRFQYDEIINHLTKVFSHIAPERVVICGDLKHEFGRISEQEWNEVMNFLSF 96
Cdd:COG1407    18 LYWPAERTLVVADLHLGKESAFRRRGIPLPPYDTRETLERLEALIERTGPDRLIILGDLFHDFGGPSRQEWEELERLLAL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  97 IERRvdDIVLIKGNHDTILGPIATKRNVKFFSNYYLSGrKIFITHghlipeDPDLYKAKIVIIGHDHPALGIRDEL-RVE 175
Cdd:COG1407    98 HAGV--EVILVRGNHDPGLPDLLEDLGGEVVDEELVLG-GLLFRH------EPEPEAADGEIAGHEHPAVRLRDRVgRSL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491335861 176 KVKCFLlgkwRGKDLIQIPSLNFVTEGIDiIREKPLSPFMNQDlsHFRVYCIENDEIFDFGRI 238
Cdd:COG1407   169 RLPCFL----RDGRRLVLPAFGAFTGGLD-VNPPAFSPLLRRG--GAEAYLLDGTRLGPLARL 224
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 25-205 1.49e-49

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: 160.17  E-value: 1.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  25 LLFGDMHLGYEEELNQMGYLIPRFQYDEIINHLTKVFSHIAPERVVICGDLKHEFGRISEQEWNEVMNFlsFIERRVDDI 104
Cdd:cd07391     1 LVIADLHLGYEEELRRQGINLPRRQKERLLERLDRLLEELGPDRLVILGDLKHSFGRVSRQERREVPFF--RLLAKDVDV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861 105 VLIKGNHDTILGPIATKRNVKFFSnYYLSGrKIFITHGHlipEDPDLYKAKIVIIGHDHPALGIRDEL-RVEKVKCFLLG 183
Cdd:cd07391    79 ILIRGNHDGGLEEILSDVNVVVVE-GYLLG-GYLIFHGH---KEPDPLDAKLVIMGHEHPAIKLRDGVgASRKLPCFLRG 153

                         170       180
                  ....*....|....*....|..
gi 1491335861 184 KWRGKDLIQIPSLNFVTEGIDI 205
Cdd:cd07391   154 EGEDGDVIVLPAFNPLTGGVDI 175
SbcD_rel_arch TIGR00024
putative phosphoesterase, SbcD/Mre11-related; Members of this uncharacterized family share a ...
 15-238 2.44e-46

putative phosphoesterase, SbcD/Mre11-related; Members of this uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11. SbcD is a subunit of the SbcCD nuclease of E. coli that can cleave DNA hairpins to unblock stalled DNA replication. All members of this family are archaeal. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129135  Cd Length: 225  Bit Score: 153.86  E-value: 2.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  15 LTLYIEDekTLLFGDMHLGYEEELNQMGYLIPRFQYDEIINHLTKVFSHIAPERVVICGDLKHEFGRisEQEWNEVMNFL 94
Cdd:TIGR00024  10 RVLIIGD--KAVIADLHLGFERHLDEQGVMVPGFQFREIIERALSIADKYGIEALIINGDLKHEFKK--GLEWRFIREFI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  95 SFIERrvdDIVLIKGNHDTilgpiatkrnvkFFSNYYLSGRKIF------ITHGHLIPEDPDLyKAKIVIIGHDHPALGI 168
Cdd:TIGR00024  86 EVTFR---DLILIRGNHDA------------LIPYIGLSGEESIrigkylIFHGHAVPDEEDL-DAKVLIFGHEHPAVKL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861 169 RDELRVEKVKCFLLGKWRGKDLIQIPSLNFVTEGIDIIREKPLSPFMNQDLSHFRVYCIENDEIFDFGRI 238
Cdd:TIGR00024 150 RDSAAGYKFPCFLLGEVEDKRVIVLPAFNPLCAGSDVLLDRPLSPILRKSLREFEVYAIEDFEIMLFGTL 219
P_estr_lig_assc TIGR04123
metallophosphoesterase, DNA ligase-associated; Members of this protein family are an ...
 17-187 1.89e-14

metallophosphoesterase, DNA ligase-associated; Members of this protein family are an uncharacterized putative metallophosphoesterase associated with a DNA ligase, a helicase, and a putative exonuclease. It may play a role in DNA repair. Its system is present in about 12 % of prokaryotic reference genomes.


Pssm-ID: 274996  Cd Length: 208  Bit Score: 69.89  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  17 LYIEDEKTLLFGDMHLGYEEELNQMGYLIPRFQYDEIINHLTKVFSHIAPERVVICGDLKHEFGRISEQEWNEVMNFLSF 96
Cdd:TIGR04123  16 LYWPAERLLVVADLHLGKAAHFRARGIPLPPYDTRATLERLAALIQRYQPRRLIVLGDLFHDRIGAERLTWEDFAAWRRL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  97 IERRvdDIVLIKGNHDTILGPIATKRNVKFFsNYYLSGRKIFiTHghlIPEDPDlykAKIVIIGHDHPALGIRDELRVEK 176
Cdd:TIGR04123  96 HAGR--DWVLIEGNHDRLAPDPPEDLGGEVV-DELRLGPLTF-RH---EPEPGP---GGFEIAGHLHPGARLRGRGRRLR 165

                         170
                  ....*....|.
gi 1491335861 177 VKCFLLGKWRG 187
Cdd:TIGR04123 166 LPCFAFDGNRL 176
PRK09453 PRK09453
phosphodiesterase; Provisional
 131-163 8.15e-06

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 44.85  E-value: 8.15e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1491335861 131 YLSGRKIFITHGHLIPED--PDLYKAKIVIIGHDH 163
Cdd:PRK09453   94 LLEGKRLFLTHGHLYGPEnlPALHDGDVLVYGHTH 128
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 50-163 1.87e-04

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain 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: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 40.72  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  50 YDEIINHLTKVFSHIApERVVICGDLkhefgrISEQEWNEVMNFlsfierrVDDIVLIKGNHDtilGPIATKRNVKFFSN 129
Cdd:cd00841    11 NLEAIEKALELFEDGV-DAVIHAGDF------VSPFVLNALLEL-------KAPLIAVRGNND---GEVDQLLGRPILPE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491335861 130 YY---LSGRKIFITHGHLIPEDPDLYKAK-----IVIIGHDH 163
Cdd:cd00841    74 FLtleIGGLRILLTHGHLFGVLEALYLAKeggadVVVFGHTH 115
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
57-163 3.74e-04

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 40.28  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  57 LTKVFSHIA---PERVVICGDLkHEFGRISeqewNEVMNFLsfierRVDDIVLIKGNHDTILgpIATKRNVKFFSNYYLS 133
Cdd:COG0622    15 LEAVLEDLEregVDLIVHLGDL-VGYGPDP----PEVLDLL-----RELPIVAVRGNHDGAV--LRGLRSLPETLRLELE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491335861 134 GRKIFITHGHL------------IPEDPDLYKAKIVIIGHDH 163
Cdd:COG0622    83 GVRILLVHGSPneyllpdtpaerLRALAAEGDADVVVCGHTH 124
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 32-163 1.46e-03

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: 38.57  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  32 LGYEEELNQMGYlIPRFQYDEII-NHLTKVFSHIAPERVVICGDLKHEFGRISEQEWNE-VMNFLS-FIERRVDDIVLIK 108
Cdd:cd08166     9 LGYENEKFGLGE-ISRWDSDRYLaKTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSyVQRFIGiFPLKRGKNAIYIP 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1491335861 109 GNHDtILG--PIATKRNVKFFSNYY--LSGRKIFITHGHLIPEDPDLYKAKIVIIGHDH 163
Cdd:cd08166    88 GDND-IGGesEIIIESRVRRFNNYFimLSHVPLLVEGYLLLKHVVVDLKPDLIFSGHDH 145
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 23-163 3.34e-03

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: 36.42  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491335861  23 KTLLFGDMHLGyeeelnqmgyliprFQYDEIINHLTKVFSHIAPERVVICGDLKHEfGRISEqewnEVMNFLSFIERRVD 102
Cdd:pfam00149   2 RILVIGDLHLP--------------GQLDDLLELLKKLLEEGKPDLVLHAGDLVDR-GPPSE----EVLELLERLIKYVP 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491335861 103 dIVLIKGNHDTILGPIATK-RNVKFFSNYYLSGRKIFithghlipedpDLYKAKIVIIGHDH 163
Cdd:pfam00149  63 -VYLVRGNHDFDYGECLRLyPYLGLLARPWKRFLEVF-----------NFLPLAGILSGHTH 112
 
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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