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Conserved domains on  [gi|34364933|emb|CAE45887|]
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hypothetical 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 ...
 29-153 7.42e-60

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 cd07395:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 263  Bit Score: 186.76  E-value: 7.42e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933  29 WKGPFYFILGADPQFGLIRAWSTGdcdNGGDEWEQEIRLTEQAVQAINKLNPKPKFFVLCGDLIHAMP------------ 96
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPgeefreqqvsdl 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933     --------------------------------------------------------------------------------
Cdd:cd07395  78 kdvlskldpdiplvcvcgnhdvgntptpetiqryrddfgddyfsfwvggvffivlnsqlfkdpskvpelasaqdqwleeq 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933  97 -------------------------------------------------GVRVVFSGHYHRNAGGTYQNLDMVVSSAIGC 127
Cdd:cd07395 158 lqiaresdakhvvvfqhiplfledpdeeddyfnipksvrrelldkfkkaGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 34364933 128 QLGRDPHGLRVVVVTAEKIVHRYYSL 153
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 29-153 7.42e-60

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: 186.76  E-value: 7.42e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933  29 WKGPFYFILGADPQFGLIRAWSTGdcdNGGDEWEQEIRLTEQAVQAINKLNPKPKFFVLCGDLIHAMP------------ 96
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPgeefreqqvsdl 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933     --------------------------------------------------------------------------------
Cdd:cd07395  78 kdvlskldpdiplvcvcgnhdvgntptpetiqryrddfgddyfsfwvggvffivlnsqlfkdpskvpelasaqdqwleeq 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933  97 -------------------------------------------------GVRVVFSGHYHRNAGGTYQNLDMVVSSAIGC 127
Cdd:cd07395 158 lqiaresdakhvvvfqhiplfledpdeeddyfnipksvrrelldkfkkaGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 34364933 128 QLGRDPHGLRVVVVTAEKIVHRYYSL 153
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
97-155 6.48e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 47.38  E-value: 6.48e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34364933  97 GVRVVFSGHYHRNAGGTYQNLDMVVSSAIGCQLgRDPHGLRVVVVTAEKIVHRYYSLDE 155
Cdd:COG1409 176 GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV-RLPPGYRVIEVDGDGLTVEVRRVDG 233
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 29-153 7.42e-60

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: 186.76  E-value: 7.42e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933  29 WKGPFYFILGADPQFGLIRAWSTGdcdNGGDEWEQEIRLTEQAVQAINKLNPKPKFFVLCGDLIHAMP------------ 96
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPgeefreqqvsdl 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933     --------------------------------------------------------------------------------
Cdd:cd07395  78 kdvlskldpdiplvcvcgnhdvgntptpetiqryrddfgddyfsfwvggvffivlnsqlfkdpskvpelasaqdqwleeq 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364933  97 -------------------------------------------------GVRVVFSGHYHRNAGGTYQNLDMVVSSAIGC 127
Cdd:cd07395 158 lqiaresdakhvvvfqhiplfledpdeeddyfnipksvrrelldkfkkaGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 34364933 128 QLGRDPHGLRVVVVTAEKIVHRYYSL 153
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
97-155 6.48e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 47.38  E-value: 6.48e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34364933  97 GVRVVFSGHYHRNAGGTYQNLDMVVSSAIGCQLgRDPHGLRVVVVTAEKIVHRYYSLDE 155
Cdd:COG1409 176 GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV-RLPPGYRVIEVDGDGLTVEVRRVDG 233
 
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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