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Conserved domains on  [gi|1002224581|ref|XP_015634025|]
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putative metallophosphoesterase At3g03305 [Oryza sativa Japonica Group]

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 ...
 42-261 8.17e-34

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 cd07401:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 254  Bit Score: 130.18  E-value: 8.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  42 WVVQLSDLHFSVHHPDRAYDFRRYVGPALAMVNPALVLITGDLTDGKSKDLLTMKQNEMEWieYRSKLKDVIESSKLPRS 121
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQDETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEW--QWKYYNILKESSVINKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 122 IFYDLRGNHDSFGVPSPGGDHDFYQKYSinAILRRHSRvqSITLENSGRKHLFVGFDSTMEIGLRGPTNLFGHPT----D 197
Cdd:cd07401    79 YLFDIRGNHDLFGIVSFDSQNNYYRKYS--NTGRDHSH--SFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDkkllD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002224581 198 KQLIELDQSLSqwdTDFnkaqvtKVAFGHFPmsFSTLTE-----SGKSIKDVFLKHSLAAYLCGHLHTR 261
Cdd:cd07401   155 RLEKELEKSKN---SKY------TIWFGHYP--HSLIISpsaksSSKTFKDLLKKYNVTAYLCGHLHPL 212
 
Name Accession Description Interval E-value
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 42-261 8.17e-34

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 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: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 130.18  E-value: 8.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  42 WVVQLSDLHFSVHHPDRAYDFRRYVGPALAMVNPALVLITGDLTDGKSKDLLTMKQNEMEWieYRSKLKDVIESSKLPRS 121
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQDETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEW--QWKYYNILKESSVINKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 122 IFYDLRGNHDSFGVPSPGGDHDFYQKYSinAILRRHSRvqSITLENSGRKHLFVGFDSTMEIGLRGPTNLFGHPT----D 197
Cdd:cd07401    79 YLFDIRGNHDLFGIVSFDSQNNYYRKYS--NTGRDHSH--SFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDkkllD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002224581 198 KQLIELDQSLSqwdTDFnkaqvtKVAFGHFPmsFSTLTE-----SGKSIKDVFLKHSLAAYLCGHLHTR 261
Cdd:cd07401   155 RLEKELEKSKN---SKY------TIWFGHYP--HSLIISpsaksSSKTFKDLLKKYNVTAYLCGHLHPL 212
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
43-295 2.39e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 70.11  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  43 VVQLSDLHFSvhhPDRAYDFRRYVGPALAMVN---PALVLITGDLTDGKSKDlltmkqnemEWIEYRSKLKDviesskLP 119
Cdd:COG1409     3 FAHISDLHLG---APDGSDTAEVLAAALADINaprPDFVVVTGDLTDDGEPE---------EYAAAREILAR------LG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 120 RSIFYdLRGNHDsfgvpSPGGDHDFYQKYsiNAILRRHSRVQSITLENsgrkHLFVGFDSTMeiglrgPTNLFGHPTDKQ 199
Cdd:COG1409    65 VPVYV-VPGNHD-----IRAAMAEAYREY--FGDLPPGGLYYSFDYGG----VRFIGLDSNV------PGRSSGELGPEQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 200 LIELDQSLSQWDTDFnkaqvtKVAFGHFPM------SFSTLTESGKSIKDVFLKHSLAAYLCGHLHtrfgknlkRYYHRS 273
Cdd:COG1409   127 LAWLEEELAAAPAKP------VIVFLHHPPystgsgSDRIGLRNAEELLALLARYGVDLVLSGHVH--------RYERTR 192

                         250       260
                  ....*....|....*....|....*
gi 1002224581 274 TEGSPLSEH---YYQFNMHQGYEIH 295
Cdd:COG1409   193 RDGVPYIVAgstGGQVRLPPGYRVI 217
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 43-132 1.08e-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: 39.50  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  43 VVQLSDLHFsvhhPDRAYDFRRYVGPALAMVNPALVLITGDLTDGKSKDLLTmkqneMEWIEYRSKLKDViessklprsi 122
Cdd:pfam00149   3 ILVIGDLHL----PGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEV-----LELLERLIKYVPV---------- 63

                          90
                  ....*....|
gi 1002224581 123 fYDLRGNHDS 132
Cdd:pfam00149  64 -YLVRGNHDF 72
 
Name Accession Description Interval E-value
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 42-261 8.17e-34

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 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: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 130.18  E-value: 8.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  42 WVVQLSDLHFSVHHPDRAYDFRRYVGPALAMVNPALVLITGDLTDGKSKDLLTMKQNEMEWieYRSKLKDVIESSKLPRS 121
Cdd:cd07401     1 WFVHLTDIHVSSFHDPNRIQDETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEW--QWKYYNILKESSVINKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 122 IFYDLRGNHDSFGVPSPGGDHDFYQKYSinAILRRHSRvqSITLENSGRKHLFVGFDSTMEIGLRGPTNLFGHPT----D 197
Cdd:cd07401    79 YLFDIRGNHDLFGIVSFDSQNNYYRKYS--NTGRDHSH--SFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDkkllD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002224581 198 KQLIELDQSLSqwdTDFnkaqvtKVAFGHFPmsFSTLTE-----SGKSIKDVFLKHSLAAYLCGHLHTR 261
Cdd:cd07401   155 RLEKELEKSKN---SKY------TIWFGHYP--HSLIISpsaksSSKTFKDLLKKYNVTAYLCGHLHPL 212
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
43-295 2.39e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 70.11  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  43 VVQLSDLHFSvhhPDRAYDFRRYVGPALAMVN---PALVLITGDLTDGKSKDlltmkqnemEWIEYRSKLKDviesskLP 119
Cdd:COG1409     3 FAHISDLHLG---APDGSDTAEVLAAALADINaprPDFVVVTGDLTDDGEPE---------EYAAAREILAR------LG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 120 RSIFYdLRGNHDsfgvpSPGGDHDFYQKYsiNAILRRHSRVQSITLENsgrkHLFVGFDSTMeiglrgPTNLFGHPTDKQ 199
Cdd:COG1409    65 VPVYV-VPGNHD-----IRAAMAEAYREY--FGDLPPGGLYYSFDYGG----VRFIGLDSNV------PGRSSGELGPEQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 200 LIELDQSLSQWDTDFnkaqvtKVAFGHFPM------SFSTLTESGKSIKDVFLKHSLAAYLCGHLHtrfgknlkRYYHRS 273
Cdd:COG1409   127 LAWLEEELAAAPAKP------VIVFLHHPPystgsgSDRIGLRNAEELLALLARYGVDLVLSGHVH--------RYERTR 192

                         250       260
                  ....*....|....*....|....*
gi 1002224581 274 TEGSPLSEH---YYQFNMHQGYEIH 295
Cdd:COG1409   193 RDGVPYIVAgstGGQVRLPPGYRVI 217
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
43-134 3.38e-05

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 46.33  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  43 VVQLSDLHFsvhhpdRAYDFRRYVGPALAMVN---PALVLITGDLTDGKSKDLLtmkqnemEWIEYRSKLKdviesSKLP 119
Cdd:COG1408    45 IVQLSDLHL------GPFIGGERLERLVEKINalkPDLVVLTGDLVDGSVAELE-------ALLELLKKLK-----APLG 106

                          90
                  ....*....|....*
gi 1002224581 120 rsIFYDLrGNHDSFG 134
Cdd:COG1408   107 --VYAVL-GNHDYYA 118
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 43-178 5.20e-05

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: 45.35  E-value: 5.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  43 VVQLSDLHFsvhhpdRAYDFRRYVGPALAMVN---PALVLITGDLTDGKSKDLLTMkqnemewIEYRSKLKdviesSKLP 119
Cdd:cd07385     4 IVQLSDIHL------GPFVGRTRLQKVVRKVNelnPDLIVITGDLVDGDVSVLRLL-------ASPLSKLK-----APLG 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002224581 120 rsIFYDLrGNHdsfgvpspggDHDFYQKYSINAILRRHS----RVQSITLENSGRKHLFVGFD 178
Cdd:cd07385    66 --VYFVL-GNH----------DYYSGDVEVWIAALEKAGitvlRNESVELSRDGATIGLAGSG 115
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 43-132 1.08e-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: 39.50  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  43 VVQLSDLHFsvhhPDRAYDFRRYVGPALAMVNPALVLITGDLTDGKSKDLLTmkqneMEWIEYRSKLKDViessklprsi 122
Cdd:pfam00149   3 ILVIGDLHL----PGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEV-----LELLERLIKYVPV---------- 63

                          90
                  ....*....|
gi 1002224581 123 fYDLRGNHDS 132
Cdd:pfam00149  64 -YLVRGNHDF 72
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 43-289 1.50e-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: 40.72  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  43 VVQLSDLHFSVhhPDRAYDF----RRYVGPALAMVN-----PALVLITGDLTDGKSKDlltmkqnemewiEYRsKLKDVI 113
Cdd:cd07402     1 IAQISDTHLFA--PGEGALLgvdtAARLAAAVAQVNalhprPDLVVVTGDLSDDGSPE------------SYE-RLRELL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 114 ESSKLPrsiFYDLRGNHDSFGVPSPGgdhdFYQKYSINailrrHSRVQSITLENSGRkhlFVGFDSTMeiglrgPTNLFG 193
Cdd:cd07402    66 APLPAP---VYWIPGNHDDRAAMREA----LPEPPYDD-----NGPVQYVVDFGGWR---LILLDTSV------PGVHHG 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581 194 HPTDKQLIELDQSLSQWDTDFnkaqvTKVAFGH--FPMSFSTLTESGksikdvfLKHS------LAAY------LCGHLH 259
Cdd:cd07402   125 ELSDEQLDWLEAALAEAPDRP-----TLIFLHHppFPLGIPWMDAIR-------LRNSqalfavLARHpqvkaiLCGHIH 192

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1002224581 260 trfgknlkRYYHRSTEGSPLS---EHYYQFNMH 289
Cdd:cd07402   193 --------RPISGSFRGIPFStapSTCHQFALD 217
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 43-138 2.80e-03

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 39.58  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  43 VVQLSDLHFSVHHPDRAYDFR------RYVGPALAMVNPALVLITGDLTDGKSkdllTMKQNemewieYRSKLKDVIE-- 114
Cdd:cd07383     5 ILQFADLHFGEGEWTCWEGCEadlktvEFIESVLDEEKPDLVVLTGDLITGEN----TADDN------ATSYLDKAVSpl 74

                          90       100
                  ....*....|....*....|....*
gi 1002224581 115 -SSKLPRSIFYdlrGNHDSFGVPSP 138
Cdd:cd07383    75 vERGIPWAATF---GNHDGYDWIDP 96
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 44-143 5.78e-03

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 37.66  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002224581  44 VQLSDLHFSvhhpdRAYDFRRYVGPALAMVN---PALVLITGDLTDGKSkdlltmkqnEMEWIEYRSKLkDVIESSKLpr 120
Cdd:cd07400     2 AHISDLHFG-----EERKPEVLELNLLDEINalkPDLVVVTGDLTQRAR---------PAEFEEAREFL-DALEPEPV-- 64

                          90       100
                  ....*....|....*....|....*....
gi 1002224581 121 sifYDLRGNHDSFGV------PSPGGDHD 143
Cdd:cd07400    65 ---VVVPGNHDAIVAlhhpllPPPDTGRE 90
 
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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