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Conserved domains on  [gi|1278577275|gb|PJA90948|]
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MAG: hypothetical protein CO136_00075 [Candidatus Levybacteria bacterium CG_4_9_14_3_um_filter_36_7]

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 ...
 10-186 1.76e-11

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 cd07398:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 217  Bit Score: 61.22  E-value: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  10 LIFSDTHLGTEF---EEKKYDFLSRIISSVDHVIIAGDFYEGFVISFDEFIKSRWQGLFPLLKSKET----VYVYGNHDK 82
Cdd:cd07398     1 LFISDLHLGLRGcraDRLLDFLLVEELDEADALYLLGDIFDLWIGDDSVVWPGAHRALARLLRLADRgtevIYVPGNHDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  83 -----DKEDERVKLFSDLTTRQYvfhTNGKTFVVEHGDRFKPLLRLLKL-FGLEHSSYFTKFYEKTEKLLIRRIGPKIIQ 156
Cdd:cd07398    81 llgrfFAEALGAILLPEPAEHLE---LDGKRLLVLHGDQLDTDDRAYQWlRKLGRNPYLQLLFLNLPLNRRRRIAGLIRR 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1278577275 157 --------------AIYKVFNEDIKEKAKEEfqNGEILICGHTH 186
Cdd:cd07398   158 ssaaylkhkqkkalAIIDVFEEAVARLARHR--GVDGVICGHTH 199
 
Name Accession Description Interval E-value
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 10-186 1.76e-11

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: 61.22  E-value: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  10 LIFSDTHLGTEF---EEKKYDFLSRIISSVDHVIIAGDFYEGFVISFDEFIKSRWQGLFPLLKSKET----VYVYGNHDK 82
Cdd:cd07398     1 LFISDLHLGLRGcraDRLLDFLLVEELDEADALYLLGDIFDLWIGDDSVVWPGAHRALARLLRLADRgtevIYVPGNHDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  83 -----DKEDERVKLFSDLTTRQYvfhTNGKTFVVEHGDRFKPLLRLLKL-FGLEHSSYFTKFYEKTEKLLIRRIGPKIIQ 156
Cdd:cd07398    81 llgrfFAEALGAILLPEPAEHLE---LDGKRLLVLHGDQLDTDDRAYQWlRKLGRNPYLQLLFLNLPLNRRRRIAGLIRR 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1278577275 157 --------------AIYKVFNEDIKEKAKEEfqNGEILICGHTH 186
Cdd:cd07398   158 ssaaylkhkqkkalAIIDVFEEAVARLARHR--GVDGVICGHTH 199
LpxH COG2908
UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];
7-186 1.01e-08

UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442152 [Multi-domain]  Cd Length: 238  Bit Score: 53.65  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   7 VKILIFSDTHLGT----EFEEKKYDFLSRIISSVDHVIIAGDFYEGFVISfDEFIKSRWQGLFPLLKSK-----ETVYVY 77
Cdd:COG2908     1 MRTLFISDLHLGTpgpqAITAALLDFLRSIAHDADALYLLGDIFDFWIGD-DDVWPPGHNRVLQKLLELadkgtPVYYIP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  78 GNHD----KDKEDE-RVKLFSDlttrQYVFHTNGKTFVVEHGDRFKPLlrllklfglehssyfTKFYEKTEKLLIRR--- 149
Cdd:COG2908    80 GNHDfllgDYFAKElGATLLPD----PIHLTLDGKRFLLLHGDGLDTG---------------DKGYQLLRKLVRNPwlq 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1278577275 150 ---------IGPKIIQAIYK-----------VFNEDIKEKAKEEFQ--NGEILICGHTH 186
Cdd:COG2908   141 wlflglplwSRLALAAKLRRkskaanqdkavKIIDVFEQAVAELARerGVDGVIHGHTH 199
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 8-191 1.33e-08

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 52.31  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   8 KILIFSDTHLGTEFEEKkydFLSRIISSVDHVIIAGDFYEGFVIsfDEFIKsrwqgLFPLLksketvYVYGNHDKDKEDE 87
Cdd:pfam12850   2 RIGIISDTHDNLALPEA---ALERLKGVVDLIIHAGDIVAPEVL--EELLE-----LAPVL------AVRGNNDAAAEFA 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  88 RvklfsDLTTRQyVFHTNGKTFVVEHGDRFKpllrllklfglehssyftkfyektekllirrigpkiiqaiykvfnEDIK 167
Cdd:pfam12850  66 T-----DLPEEA-VLELGGVKILLTHGHGVK---------------------------------------------DALA 94

                         170       180
                  ....*....|....*....|....
gi 1278577275 168 EKAKEEFQNGEILICGHTHAQEAD 191
Cdd:pfam12850  95 RLLRRAEEGVAVVVYGHTHVPGVE 118
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 8-119 7.26e-07

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 47.37  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   8 KILIFSDTHLGTEFEEKKYDFLSRiISSVDHVIIAGDFYEGFVISFDEFIksrwqglfpllkSKETVYVYGNHDKDKEDe 87
Cdd:TIGR00040   2 KILVISDTHGPLRATELPVELFNL-ESNVDLVIHAGDLTSPFVLKEFEDL------------AAKVIAVRGNNDGERDE- 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1278577275  88 rvklfsdlTTRQYVFHTNGKTFVVEHGDRFKP 119
Cdd:TIGR00040  68 --------LPEEEIFEAEGIDFGLVHGDLVYP 91
 
Name Accession Description Interval E-value
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 10-186 1.76e-11

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: 61.22  E-value: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  10 LIFSDTHLGTEF---EEKKYDFLSRIISSVDHVIIAGDFYEGFVISFDEFIKSRWQGLFPLLKSKET----VYVYGNHDK 82
Cdd:cd07398     1 LFISDLHLGLRGcraDRLLDFLLVEELDEADALYLLGDIFDLWIGDDSVVWPGAHRALARLLRLADRgtevIYVPGNHDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  83 -----DKEDERVKLFSDLTTRQYvfhTNGKTFVVEHGDRFKPLLRLLKL-FGLEHSSYFTKFYEKTEKLLIRRIGPKIIQ 156
Cdd:cd07398    81 llgrfFAEALGAILLPEPAEHLE---LDGKRLLVLHGDQLDTDDRAYQWlRKLGRNPYLQLLFLNLPLNRRRRIAGLIRR 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1278577275 157 --------------AIYKVFNEDIKEKAKEEfqNGEILICGHTH 186
Cdd:cd07398   158 ssaaylkhkqkkalAIIDVFEEAVARLARHR--GVDGVICGHTH 199
LpxH COG2908
UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];
7-186 1.01e-08

UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442152 [Multi-domain]  Cd Length: 238  Bit Score: 53.65  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   7 VKILIFSDTHLGT----EFEEKKYDFLSRIISSVDHVIIAGDFYEGFVISfDEFIKSRWQGLFPLLKSK-----ETVYVY 77
Cdd:COG2908     1 MRTLFISDLHLGTpgpqAITAALLDFLRSIAHDADALYLLGDIFDFWIGD-DDVWPPGHNRVLQKLLELadkgtPVYYIP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  78 GNHD----KDKEDE-RVKLFSDlttrQYVFHTNGKTFVVEHGDRFKPLlrllklfglehssyfTKFYEKTEKLLIRR--- 149
Cdd:COG2908    80 GNHDfllgDYFAKElGATLLPD----PIHLTLDGKRFLLLHGDGLDTG---------------DKGYQLLRKLVRNPwlq 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1278577275 150 ---------IGPKIIQAIYK-----------VFNEDIKEKAKEEFQ--NGEILICGHTH 186
Cdd:COG2908   141 wlflglplwSRLALAAKLRRkskaanqdkavKIIDVFEQAVAELARerGVDGVIHGHTH 199
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 8-191 1.33e-08

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 52.31  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   8 KILIFSDTHLGTEFEEKkydFLSRIISSVDHVIIAGDFYEGFVIsfDEFIKsrwqgLFPLLksketvYVYGNHDKDKEDE 87
Cdd:pfam12850   2 RIGIISDTHDNLALPEA---ALERLKGVVDLIIHAGDIVAPEVL--EELLE-----LAPVL------AVRGNNDAAAEFA 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  88 RvklfsDLTTRQyVFHTNGKTFVVEHGDRFKpllrllklfglehssyftkfyektekllirrigpkiiqaiykvfnEDIK 167
Cdd:pfam12850  66 T-----DLPEEA-VLELGGVKILLTHGHGVK---------------------------------------------DALA 94

                         170       180
                  ....*....|....*....|....
gi 1278577275 168 EKAKEEFQNGEILICGHTHAQEAD 191
Cdd:pfam12850  95 RLLRRAEEGVAVVVYGHTHVPGVE 118
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
7-110 3.41e-08

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 52.22  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   7 VKILIFSDTHLGTEFEEKK-----YDFLSRIIS-----SVDHVIIAGDFYEGFVISFD---EFIksrwQGLFPLLKSKET 73
Cdd:COG0420     1 MRFLHTADWHLGKPLHGASrredqLAALDRLVDlaieeKVDAVLIAGDLFDSANPSPEavrLLA----EALRRLSEAGIP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1278577275  74 VY-VYGNHDKDK---------EDERVKLFSDLTTRQYVFHTNGKTFV 110
Cdd:COG0420    77 VVlIAGNHDSPSrlsagspllENLGVHVFGSVEPEPVELEDGLGVAV 123
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 8-186 5.99e-08

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: 50.35  E-value: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   8 KILIFSDTHLGTEFEEKKYDFLSRiisSVDHVIIAGDFYEGFVisfdefiksrwqgLFPLLKSKETVY-VYGNHDkdkeD 86
Cdd:cd00841     1 KIGVISDTHGNLEAIEKALELFED---GVDAVIHAGDFVSPFV-------------LNALLELKAPLIaVRGNND----G 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  87 ERVKLFS-DLTTRQYVFHTNGKTFVVEHGDRFKPllrllklfglehssyftkfyektekllirrigpkiiqaiykvfnED 165
Cdd:cd00841    61 EVDQLLGrPILPEFLTLEIGGLRILLTHGHLFGV--------------------------------------------LE 96

                         170       180
                  ....*....|....*....|.
gi 1278577275 166 IKEKAKEEfqNGEILICGHTH 186
Cdd:cd00841    97 ALYLAKEG--GADVVVFGHTH 115
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
7-111 2.74e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 49.69  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   7 VKILIFSDTHLGTEFEEKKYDFLSRIISSV-----DHVIIAGDF-YEGFVISFDEFiKSRWQGLfpllkSKETVYVYGNH 80
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEVLAAALADInaprpDFVVVTGDLtDDGEPEEYAAA-REILARL-----GVPVYVVPGNH 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1278577275  81 D--KDKEDERVKLFSDLTT--RQYVFHTNGKTFVV 111
Cdd:COG1409    75 DirAAMAEAYREYFGDLPPggLYYSFDYGGVRFIG 109
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
8-186 4.63e-07

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 48.37  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   8 KILIFSDTHlgtefeeKKYDFLSRII-----SSVDHVIIAGDFyeGFVISFDEFIksrwqglFPLLKSKETVYVYGNHDk 82
Cdd:COG0622     1 KIAVISDTH-------GNLPALEAVLedlerEGVDLIVHLGDL--VGYGPDPPEV-------LDLLRELPIVAVRGNHD- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  83 dkeDERVKLFSDLTTRQyVFHTNGKTFVVEHGDRFkpllrllklfglehssyftkfyekteklliRRIGPkiiqaiyKVF 162
Cdd:COG0622    64 ---GAVLRGLRSLPETL-RLELEGVRILLVHGSPN------------------------------EYLLP-------DTP 102

                         170       180
                  ....*....|....*....|....
gi 1278577275 163 NEDIKEKAKEEfqNGEILICGHTH 186
Cdd:COG0622   103 AERLRALAAEG--DADVVVCGHTH 124
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 8-119 7.26e-07

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 47.37  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   8 KILIFSDTHLGTEFEEKKYDFLSRiISSVDHVIIAGDFYEGFVISFDEFIksrwqglfpllkSKETVYVYGNHDKDKEDe 87
Cdd:TIGR00040   2 KILVISDTHGPLRATELPVELFNL-ESNVDLVIHAGDLTSPFVLKEFEDL------------AAKVIAVRGNNDGERDE- 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1278577275  88 rvklfsdlTTRQYVFHTNGKTFVVEHGDRFKP 119
Cdd:TIGR00040  68 --------LPEEEIFEAEGIDFGLVHGDLVYP 91
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
7-81 8.68e-07

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 48.25  E-value: 8.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   7 VKILIFSDTHLGTEFEEKkydFLSRIISSV-----DHVIIAGDFYEGFVISFDEFIKsrwqgLFPLLKSKETVY-VYGNH 80
Cdd:COG1408    43 LRIVQLSDLHLGPFIGGE---RLERLVEKInalkpDLVVLTGDLVDGSVAELEALLE-----LLKKLKAPLGVYaVLGNH 114


                  .
gi 1278577275  81 D 81
Cdd:COG1408   115 D 115
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 8-81 3.11e-06

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: 46.50  E-value: 3.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278577275   8 KILIFSDTHLGTEFEEKKYDFLSRII--SSVDHVIIAGDFYEGFVISFDEFIKsrwqgLFPLLKSKETVY-VYGNHD 81
Cdd:cd07385     3 RIVQLSDIHLGPFVGRTRLQKVVRKVneLNPDLIVITGDLVDGDVSVLRLLAS-----PLSKLKAPLGVYfVLGNHD 74
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 10-81 8.70e-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: 43.80  E-value: 8.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278577275  10 LIFSDTHLGTEFEEKKYDFLSRIISSVDHVIIAGDF-YEGFVISFDEFIKSRWqglfpLLKSKETVYVYGNHD 81
Cdd:cd00838     1 LVISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLvDYGPDPEEVELKALRL-----LLAGIPVYVVPGNHD 68
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 8-109 1.40e-05

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: 42.97  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   8 KILIFSDTHLGTEFE--EKKYDFLsRIISSVDHVIIAGDFYEGFVISfdefikSRWQGLFPLLKSKETVY-VYGNHDkDK 84
Cdd:pfam00149   2 RILVIGDLHLPGQLDdlLELLKKL-LEEGKPDLVLHAGDLVDRGPPS------EEVLELLERLIKYVPVYlVRGNHD-FD 73

                          90       100
                  ....*....|....*....|....*
gi 1278577275  85 EDERVKLFSDLTTRQYVFHTNGKTF 109
Cdd:pfam00149  74 YGECLRLYPYLGLLARPWKRFLEVF 98
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
8-81 1.42e-05

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 44.24  E-value: 1.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278577275   8 KILIFSDTHLgtefEEKKYDFLSRIISS--VDHVIIAGDF-YEGFVISFDEFIksRWQGLFPllksKETVYVYGNHD 81
Cdd:COG2129     1 KILAVSDLHG----NFDLLEKLLELARAedADLVILAGDLtDFGTAEEAREVL--EELAALG----VPVLAVPGNHD 67
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 8-81 5.64e-04

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: 39.56  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   8 KILIFSDTHLGTEF------EEKKYDFLSRIIS-----SVDHVIIAGDFYEGFVISFDEFIKSRwQGLFPLLKSKETVYV 76
Cdd:cd00840     1 RFLHTADWHLGYPLyglsrrEEDFFKAFEEIVDlaieeKVDFVLIAGDLFDSNNPSPEALKLAI-EGLRRLCEAGIPVFV 79


                  ....*.
gi 1278577275  77 -YGNHD 81
Cdd:cd00840    80 iAGNHD 85
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 9-81 4.82e-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: 36.12  E-value: 4.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278577275   9 ILIFSDTHLGTEFEEK--KYDFLSRIIS-SVDHVIIAGDFYEGfvISFDEFIKSRwqGLFPLLKSKETVYVYGNHD 81
Cdd:cd07400     1 IAHISDLHFGEERKPEvlELNLLDEINAlKPDLVVVTGDLTQR--ARPAEFEEAR--EFLDALEPEPVVVVPGNHD 72
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 10-81 6.78e-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: 36.13  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275  10 LIFSDTHLGTE----------FEEKKYDFLSRIIS-----SVDHVIIAGDFYEGF-VISFDEFiksRWQGLFPLLKSKET 73
Cdd:cd07391     1 LVIADLHLGYEeelrrqginlPRRQKERLLERLDRlleelGPDRLVILGDLKHSFgRVSRQER---REVPFFRLLAKDVD 77


                  ....*....
gi 1278577275  74 VYVY-GNHD 81
Cdd:cd07391    78 VILIrGNHD 86
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 6-84 6.98e-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: 36.50  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278577275   6 TVKILIFSDTHLG----TEFEEKKYD-----FLSRIISS--VDHVIIAGDFYEGFVISFDEFIKSRWQGLFPLLKSKET- 73
Cdd:cd07383     2 KFKILQFADLHFGegewTCWEGCEADlktveFIESVLDEekPDLVVLTGDLITGENTADDNATSYLDKAVSPLVERGIPw 81

                          90
                  ....*....|.
gi 1278577275  74 VYVYGNHDKDK 84
Cdd:cd07383    82 AATFGNHDGYD 92
 
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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