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Conserved domains on  [gi|12654899|gb|AAH01294|]
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C17orf48 protein [Homo sapiens]

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 ...
 18-165 3.24e-61

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 cd07396:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 245  Bit Score: 191.01  E-value: 3.24e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654899  18 FSFGVIADVQFADLEDGFNFqGTRRRYYRHSLLHLQGAIEDWNNESsMPCCVLQLGDIIDGYNAQYnASKKSLELVMDMF 97
Cdd:cd07396   1 FSFGIIADIQYADIDDGKNL-GTRRRYYRNSLGVLERAVEEWNRES-NLAFVVQLGDIIDGYNAKD-RSKEALDAVLSIL 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12654899  98 KRLKVPVHHTWGNHEFYNFSREYLTHSKlntkfledqivhhpeTMPSEDYYAYHFVPFPKFRFILLDA 165
Cdd:cd07396  78 DRLKGPVHHVLGNHEFYNFPREYLNHLK---------------TLNGEDAYYYSFSPGPGFRFLVLDF 130
 
Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 18-165 3.24e-61

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 191.01  E-value: 3.24e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654899  18 FSFGVIADVQFADLEDGFNFqGTRRRYYRHSLLHLQGAIEDWNNESsMPCCVLQLGDIIDGYNAQYnASKKSLELVMDMF 97
Cdd:cd07396   1 FSFGIIADIQYADIDDGKNL-GTRRRYYRNSLGVLERAVEEWNRES-NLAFVVQLGDIIDGYNAKD-RSKEALDAVLSIL 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12654899  98 KRLKVPVHHTWGNHEFYNFSREYLTHSKlntkfledqivhhpeTMPSEDYYAYHFVPFPKFRFILLDA 165
Cdd:cd07396  78 DRLKGPVHHVLGNHEFYNFPREYLNHLK---------------TLNGEDAYYYSFSPGPGFRFLVLDF 130
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
18-164 4.65e-05

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 42.76  E-value: 4.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654899  18 FSFGVIADVQFADLEDgfnfqgtrrryyRHSLLHLQGAIEDWNNESsmPCCVLQLGDIIDgynaqyNASKKSLELVMDMF 97
Cdd:COG1409   1 FRFAHISDLHLGAPDG------------SDTAEVLAAALADINAPR--PDFVVVTGDLTD------DGEPEEYAAAREIL 60

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12654899  98 KRLKVPVHHTWGNHEFYN-FSREYLTHsklntkFledqivhhPETMPSEDYYAYHfvpFPKFRFILLD 164
Cdd:COG1409  61 ARLGVPVYVVPGNHDIRAaMAEAYREY------F--------GDLPPGGLYYSFD---YGGVRFIGLD 111
 
Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 18-165 3.24e-61

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 191.01  E-value: 3.24e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654899  18 FSFGVIADVQFADLEDGFNFqGTRRRYYRHSLLHLQGAIEDWNNESsMPCCVLQLGDIIDGYNAQYnASKKSLELVMDMF 97
Cdd:cd07396   1 FSFGIIADIQYADIDDGKNL-GTRRRYYRNSLGVLERAVEEWNRES-NLAFVVQLGDIIDGYNAKD-RSKEALDAVLSIL 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12654899  98 KRLKVPVHHTWGNHEFYNFSREYLTHSKlntkfledqivhhpeTMPSEDYYAYHFVPFPKFRFILLDA 165
Cdd:cd07396  78 DRLKGPVHHVLGNHEFYNFPREYLNHLK---------------TLNGEDAYYYSFSPGPGFRFLVLDF 130
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
18-164 4.65e-05

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 42.76  E-value: 4.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654899  18 FSFGVIADVQFADLEDgfnfqgtrrryyRHSLLHLQGAIEDWNNESsmPCCVLQLGDIIDgynaqyNASKKSLELVMDMF 97
Cdd:COG1409   1 FRFAHISDLHLGAPDG------------SDTAEVLAAALADINAPR--PDFVVVTGDLTD------DGEPEEYAAAREIL 60

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12654899  98 KRLKVPVHHTWGNHEFYN-FSREYLTHsklntkFledqivhhPETMPSEDYYAYHfvpFPKFRFILLD 164
Cdd:COG1409  61 ARLGVPVYVVPGNHDIRAaMAEAYREY------F--------GDLPPGGLYYSFD---YGGVRFIGLD 111
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 26-129 4.93e-05

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: 42.28  E-value: 4.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654899  26 VQFADLEDGfnfQGTRRRYYRHSllhlqgaiEDWNNESSM--------PCCVLQLGDIIDGYNAQYNASKKSLELVMDMF 97
Cdd:cd07383   6 LQFADLHFG---EGEWTCWEGCE--------ADLKTVEFIesvldeekPDLVVLTGDLITGENTADDNATSYLDKAVSPL 74

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 12654899  98 KRLKVPVHHTWGNHEFYNFSR----EYL--THSKLNTK 129
Cdd:cd07383  75 VERGIPWAATFGNHDGYDWIDpsqvEWFesTSAALKKK 112
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
69-136 3.06e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 37.30  E-value: 3.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12654899  69 VLQLGDIIDgynaqyNASKKSLELVMDMFKRLKVPVHHTWGNHEFYNFSREYlthSKLNTKFLEDQIV 136
Cdd:COG2129  30 VILAGDLTD------FGTAEEAREVLEELAALGVPVLAVPGNHDDPEVLDAL---EESGVHNLHGRVV 88
 
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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