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Conserved domains on  [gi|488238197|ref|WP_002309405|]
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MULTISPECIES: metallophosphoesterase [Enterococcus]

Protein Classification

metallophosphoesterase( domain architecture ID 10096151)

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
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 4-154 6.32e-39

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: 129.70  E-value: 6.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197   4 LVVSDNHGDRDILVDLVDRYRSEVDIFFHCGDSELEASDP----LWDTFQVVQGNCDY-------GPGFEQKKVIQTGQD 72
Cdd:cd00841    3 GVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVSPFVLNalleLKAPLIAVRGNNDGevdqllgRPILPEFLTLEIGGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  73 TVFMTHGHLSNVRFGLTQlaieARAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGpiQIPSYALIESldDQISVQ 152
Cdd:cd00841   83 RILLTHGHLFGVLEALYL----AKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRG--GRPTYAILDI--EKLEVE 154


                 ..
gi 488238197 153 YY 154
Cdd:cd00841  155 II 156
 
Name Accession Description Interval E-value
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 4-154 6.32e-39

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: 129.70  E-value: 6.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197   4 LVVSDNHGDRDILVDLVDRYRSEVDIFFHCGDSELEASDP----LWDTFQVVQGNCDY-------GPGFEQKKVIQTGQD 72
Cdd:cd00841    3 GVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVSPFVLNalleLKAPLIAVRGNNDGevdqllgRPILPEFLTLEIGGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  73 TVFMTHGHLSNVRFGLTQlaieARAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGpiQIPSYALIESldDQISVQ 152
Cdd:cd00841   83 RILLTHGHLFGVLEALYL----AKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRG--GRPTYAILDI--EKLEVE 154


                 ..
gi 488238197 153 YY 154
Cdd:cd00841  155 II 156
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-147 2.75e-36

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: 122.81  E-value: 2.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197    1 MRYLVVSDNHGDRDILVDLVDRYRSEVDIFFHCGD-SELEASDPLWDTFQV--VQGNCDYGPGF----EQKKVIQTGQDT 73
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVVDLIIHAGDiVAPEVLEELLELAPVlaVRGNNDAAAEFatdlPEEAVLELGGVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488238197   74 VFMTHGHlsNVRFGLTQLAIEArAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGPIQiPSYALIESLDD 147
Cdd:pfam12850  81 ILLTHGH--GVKDALARLLRRA-EEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDP-PTYALLDIDDG 150
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-154 1.11e-25

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 96.91  E-value: 1.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197   2 RYLVVSDNHGDRDILVDLVDRYRSE-VDIFFHCGD--SELEASDPLWDTFQ-----VVQGNCDYG-----PGFEQKKVIQ 68
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEREgVDLIVHLGDlvGYGPDPPEVLDLLRelpivAVRGNHDGAvlrglRSLPETLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  69 TGQDTVFMTHGHLSNVRFGLT---QLAIEARAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGPiQIPSYALIESL 145
Cdd:COG0622   81 LEGVRILLVHGSPNEYLLPDTpaeRLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDG-DPASYAILDID 159


                 ....*....
gi 488238197 146 DDQISVQYY 154
Cdd:COG0622  160 DGEWSVEFV 168
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-151 1.24e-23

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: 90.89  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197    1 MRYLVVSDNHG-DR--DILVDLVDrYRSEVDIFFHCGDSE----LEASDPLWDTFQVVQGNCD-YGPGFEQKKVIQTGQD 72
Cdd:TIGR00040   1 MKILVISDTHGpLRatELPVELFN-LESNVDLVIHAGDLTspfvLKEFEDLAAKVIAVRGNNDgERDELPEEEIFEAEGI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488238197   73 TVFMTHGHLSNVRFGLTQLAIEARAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGPiQIPSYALIEslDDQISV 151
Cdd:TIGR00040  80 DFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNG-NTPSYAILD--VDKDKV 155
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-151 6.32e-13

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 63.34  E-value: 6.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197   1 MRYLVVSDNHGDRDILVDLVDRYR-SEVDIFFHCGDsEL---------EASDP---------LWDTFQVVQGNCDYG--- 58
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAqSGADWLVHLGD-VLyhgprnplpEGYAPkkvaellnaYADKIIAVRGNCDSEvdq 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  59 -----PGFEQKKVIQTGQDTVFMTHGHLsnvrFGLTQLAieaRAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGP 133
Cdd:PRK09453  80 mllhfPIMAPYQQVLLEGKRLFLTHGHL----YGPENLP---ALHDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGG 152

                        170
                 ....*....|....*...
gi 488238197 134 iQIPSYALIEslDDQISV 151
Cdd:PRK09453 153 -YPASYGILD--DNVLSV 167
 
Name Accession Description Interval E-value
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 4-154 6.32e-39

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: 129.70  E-value: 6.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197   4 LVVSDNHGDRDILVDLVDRYRSEVDIFFHCGDSELEASDP----LWDTFQVVQGNCDY-------GPGFEQKKVIQTGQD 72
Cdd:cd00841    3 GVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVSPFVLNalleLKAPLIAVRGNNDGevdqllgRPILPEFLTLEIGGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  73 TVFMTHGHLSNVRFGLTQlaieARAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGpiQIPSYALIESldDQISVQ 152
Cdd:cd00841   83 RILLTHGHLFGVLEALYL----AKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRG--GRPTYAILDI--EKLEVE 154


                 ..
gi 488238197 153 YY 154
Cdd:cd00841  155 II 156
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-147 2.75e-36

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: 122.81  E-value: 2.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197    1 MRYLVVSDNHGDRDILVDLVDRYRSEVDIFFHCGD-SELEASDPLWDTFQV--VQGNCDYGPGF----EQKKVIQTGQDT 73
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVVDLIIHAGDiVAPEVLEELLELAPVlaVRGNNDAAAEFatdlPEEAVLELGGVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488238197   74 VFMTHGHlsNVRFGLTQLAIEArAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGPIQiPSYALIESLDD 147
Cdd:pfam12850  81 ILLTHGH--GVKDALARLLRRA-EEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDP-PTYALLDIDDG 150
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-154 1.11e-25

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 96.91  E-value: 1.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197   2 RYLVVSDNHGDRDILVDLVDRYRSE-VDIFFHCGD--SELEASDPLWDTFQ-----VVQGNCDYG-----PGFEQKKVIQ 68
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEREgVDLIVHLGDlvGYGPDPPEVLDLLRelpivAVRGNHDGAvlrglRSLPETLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  69 TGQDTVFMTHGHLSNVRFGLT---QLAIEARAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGPiQIPSYALIESL 145
Cdd:COG0622   81 LEGVRILLVHGSPNEYLLPDTpaeRLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDG-DPASYAILDID 159


                 ....*....
gi 488238197 146 DDQISVQYY 154
Cdd:COG0622  160 DGEWSVEFV 168
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-151 1.24e-23

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: 90.89  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197    1 MRYLVVSDNHG-DR--DILVDLVDrYRSEVDIFFHCGDSE----LEASDPLWDTFQVVQGNCD-YGPGFEQKKVIQTGQD 72
Cdd:TIGR00040   1 MKILVISDTHGpLRatELPVELFN-LESNVDLVIHAGDLTspfvLKEFEDLAAKVIAVRGNNDgERDELPEEEIFEAEGI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488238197   73 TVFMTHGHLSNVRFGLTQLAIEARAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGPiQIPSYALIEslDDQISV 151
Cdd:TIGR00040  80 DFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNG-NTPSYAILD--VDKDKV 155
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-151 6.32e-13

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 63.34  E-value: 6.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197   1 MRYLVVSDNHGDRDILVDLVDRYR-SEVDIFFHCGDsEL---------EASDP---------LWDTFQVVQGNCDYG--- 58
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAqSGADWLVHLGD-VLyhgprnplpEGYAPkkvaellnaYADKIIAVRGNCDSEvdq 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  59 -----PGFEQKKVIQTGQDTVFMTHGHLsnvrFGLTQLAieaRAANADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGP 133
Cdd:PRK09453  80 mllhfPIMAPYQQVLLEGKRLFLTHGHL----YGPENLP---ALHDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGG 152

                        170
                 ....*....|....*...
gi 488238197 134 iQIPSYALIEslDDQISV 151
Cdd:PRK09453 153 -YPASYGILD--DNVLSV 167
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 48-154 1.15e-11

Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting protein 29), also known as vacuolar membrane protein Pep11, is a subunit of the retromer complex which is responsible for the retrieval of mannose-6-phosphate receptors (MPRs) from the endosomes for retrograde transport back to the Golgi. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer complex assembly as well as a phosphatase with specificity for the cytoplasmic tail of the MPR. The retromer includes the following 5 subunits: Vps35, Vps26, Vps29, and a dimer of the sorting nexins Vps5 (Snx1), and Vps17 (Snx2). Vps29 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: 163637 [Multi-domain]  Cd Length: 178  Bit Score: 59.91  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  48 FQVVQGNCDYGPGFEQKKVIQTGQDTVFMTHGHLSNVRFGLTQLAIEARAANADMVFFGHTHQIGC-EMDQKiLFLNPGS 126
Cdd:cd07394   55 VHIVRGDFDENLNYPETKVITVGQFKIGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAfEHEGK-FFINPGS 133

                         90       100       110
                 ....*....|....*....|....*....|.
gi 488238197 127 ISQPRGPIQ---IPSYALIESLDDQISVQYY 154
Cdd:cd07394  134 ATGAFSPLDpnvIPSFVLMDIQGSTVVTYVY 164
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-125 1.75e-07

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: 47.65  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197   4 LVVSDNHGDRD---ILVDLVDRYRSEVDIFFHCGD-----SELEASDPLWDTFQ-------VVQGNCDygpgfeqkkviq 68
Cdd:cd00838    1 LVISDIHGNLEaleAVLEAALAKAEKPDLVICLGDlvdygPDPEEVELKALRLLlagipvyVVPGNHD------------ 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488238197  69 tgqdtVFMTHGHLSNVRFGLTQLAIEARAA--------NADMVFFGHTH--QIGCEMDQKILFLNPG 125
Cdd:cd00838   69 -----ILVTHGPPYDPLDEGSPGEDPGSEAllelldkyGPDLVLSGHTHvpGRREVDKGGTLVVNPG 130
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
73-154 2.43e-04

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 40.06  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197  73 TVFMTHGHLSNVRFGLTQLAIEARAA--------NADMVFFGHTHQIGCEMDQKILFLNPGSISQPRGPiqIPSYALIES 144
Cdd:COG1409  142 VIVFLHHPPYSTGSGSDRIGLRNAEEllallaryGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL--PPGYRVIEV 219

                         90
                 ....*....|
gi 488238197 145 LDDQISVQYY 154
Cdd:COG1409  220 DGDGLTVEVR 229
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-110 1.75e-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: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238197    1 MRYLVVSDNH--GDRDILVDLVDRYRSE--VDIFFHCGD-------SE--LEASDPLWDTFQV--VQGNCDYGPGFEQKK 65
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEEgkPDLVLHAGDlvdrgppSEevLELLERLIKYVPVylVRGNHDFDYGECLRL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 488238197   66 VIQTGQDTvfMTHGHLSNVRFGLTQLAIearaanadmvFFGHTHQ 110
Cdd:pfam00149  81 YPYLGLLA--RPWKRFLEVFNFLPLAGI----------LSGHTHV 113
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
4-57 6.13e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 35.76  E-value: 6.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488238197   4 LVVSDNHGDRDILVDLVDRYRSE-VDIFFHCGD----SELEASDPLWDTFQ-------VVQGNCDY 57
Cdd:COG2129    3 LAVSDLHGNFDLLEKLLELARAEdADLVILAGDltdfGTAEEAREVLEELAalgvpvlAVPGNHDD 68
 
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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