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Conserved domains on  [gi|488242154|ref|WP_002313362|]
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MULTISPECIES: metallophosphoesterase family protein [Enterococcus]

Protein Classification

COG4186 family protein( domain architecture ID 10754707)

COG4186 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4186 COG4186
Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily ...
 1-189 4.37e-50

Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily [General function prediction only];


:

Pssm-ID: 443340  Cd Length: 167  Bit Score: 159.67  E-value: 4.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154   1 MNYFTSDMHFFHERLLGendFAPRLFANVDEMNQQLITSWNAVVKETDHVYHLGDLAMHPQYEKanadILELVSQLQGTI 80
Cdd:COG4186    1 MIYFTSDTHFGHANIIK---FCPRPFASVEEMDEALIANWNATVGPDDTVYHLGDFAFGGSAEE----AREILRRLNGRK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154  81 HLIKGNHDSRAFFRylekndpglsdGSPKFYFYDVGAIVKFDHQQYYLTHYPML--LGPNDTIRNLHGHIHHYSV--PIE 156
Cdd:COG4186   74 HLIRGNHDGKLLLR-----------LPAGFASVQDYAEIKLGGRRLLLCHYPLRtwNGADRGAWHLHGHVHGNRLlkPTR 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488242154 157 NVVNVGVDAPERdllkeklpfgTPLSEKQIKEI 189
Cdd:COG4186  143 RSINVGVDAWDY----------RPVSLEEILER 165
 
Name Accession Description Interval E-value
COG4186 COG4186
Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily ...
 1-189 4.37e-50

Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily [General function prediction only];


Pssm-ID: 443340  Cd Length: 167  Bit Score: 159.67  E-value: 4.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154   1 MNYFTSDMHFFHERLLGendFAPRLFANVDEMNQQLITSWNAVVKETDHVYHLGDLAMHPQYEKanadILELVSQLQGTI 80
Cdd:COG4186    1 MIYFTSDTHFGHANIIK---FCPRPFASVEEMDEALIANWNATVGPDDTVYHLGDFAFGGSAEE----AREILRRLNGRK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154  81 HLIKGNHDSRAFFRylekndpglsdGSPKFYFYDVGAIVKFDHQQYYLTHYPML--LGPNDTIRNLHGHIHHYSV--PIE 156
Cdd:COG4186   74 HLIRGNHDGKLLLR-----------LPAGFASVQDYAEIKLGGRRLLLCHYPLRtwNGADRGAWHLHGHVHGNRLlkPTR 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488242154 157 NVVNVGVDAPERdllkeklpfgTPLSEKQIKEI 189
Cdd:COG4186  143 RSINVGVDAWDY----------RPVSLEEILER 165
MPP_AQ1575 cd07390
Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes ...
 3-189 2.69e-42

Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to AQ1575, an uncharacterized Aquifex aeolicus protein. AQ1575 may play an accessory role in DNA repair, based on the close proximity of its gene to Holliday junction resolvasome genes. 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: 277336  Cd Length: 170  Bit Score: 139.80  E-value: 2.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154   3 YFTSDMHFFHERLLGendFAPRLFANVDEMNQQLITSWNAVVKETDHVYHLGDLAMHpqyEKANADILELVSQLQGTIHL 82
Cdd:cd07390    2 YFTSDTHFGHPNVIR---YTNRPFDNVEEMNKVIINNWNNTVGPDDIVYHLGDFALG---TNKANEALEILSLLNGHIHL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154  83 IKGNHDsraffryleknDPGLSDGSPKFYFYDVGAIVKFDHQQYYLTHYPML--LGPNDTIRNLHGHIHHYSVPIENVV- 159
Cdd:cd07390   76 IRGNHD-----------KSLLMYRPLFFESVQQYVRIEHGGRRFYLSHYPYRgpDSPDFDGWLIHGHVHSNSPDEGPFVy 144

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488242154 160 -----NVGVDAPERDllkeklpfgtPLSEKQIKEI 189
Cdd:cd07390  145 dprqiNVGVEAWDYR----------PVSLEEIEDL 169
 
Name Accession Description Interval E-value
COG4186 COG4186
Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily ...
 1-189 4.37e-50

Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily [General function prediction only];


Pssm-ID: 443340  Cd Length: 167  Bit Score: 159.67  E-value: 4.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154   1 MNYFTSDMHFFHERLLGendFAPRLFANVDEMNQQLITSWNAVVKETDHVYHLGDLAMHPQYEKanadILELVSQLQGTI 80
Cdd:COG4186    1 MIYFTSDTHFGHANIIK---FCPRPFASVEEMDEALIANWNATVGPDDTVYHLGDFAFGGSAEE----AREILRRLNGRK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154  81 HLIKGNHDSRAFFRylekndpglsdGSPKFYFYDVGAIVKFDHQQYYLTHYPML--LGPNDTIRNLHGHIHHYSV--PIE 156
Cdd:COG4186   74 HLIRGNHDGKLLLR-----------LPAGFASVQDYAEIKLGGRRLLLCHYPLRtwNGADRGAWHLHGHVHGNRLlkPTR 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488242154 157 NVVNVGVDAPERdllkeklpfgTPLSEKQIKEI 189
Cdd:COG4186  143 RSINVGVDAWDY----------RPVSLEEILER 165
MPP_AQ1575 cd07390
Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes ...
 3-189 2.69e-42

Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to AQ1575, an uncharacterized Aquifex aeolicus protein. AQ1575 may play an accessory role in DNA repair, based on the close proximity of its gene to Holliday junction resolvasome genes. 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: 277336  Cd Length: 170  Bit Score: 139.80  E-value: 2.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154   3 YFTSDMHFFHERLLGendFAPRLFANVDEMNQQLITSWNAVVKETDHVYHLGDLAMHpqyEKANADILELVSQLQGTIHL 82
Cdd:cd07390    2 YFTSDTHFGHPNVIR---YTNRPFDNVEEMNKVIINNWNNTVGPDDIVYHLGDFALG---TNKANEALEILSLLNGHIHL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154  83 IKGNHDsraffryleknDPGLSDGSPKFYFYDVGAIVKFDHQQYYLTHYPML--LGPNDTIRNLHGHIHHYSVPIENVV- 159
Cdd:cd07390   76 IRGNHD-----------KSLLMYRPLFFESVQQYVRIEHGGRRFYLSHYPYRgpDSPDFDGWLIHGHVHSNSPDEGPFVy 144

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488242154 160 -----NVGVDAPERDllkeklpfgtPLSEKQIKEI 189
Cdd:cd07390  145 dprqiNVGVEAWDYR----------PVSLEEIEDL 169
MPP_DR1119 cd07393
Deinococcus radiodurans DR1119 and related proteins, metallophosphatase domain; DR1119 is an ...
 34-88 7.36e-06

Deinococcus radiodurans DR1119 and related proteins, metallophosphatase domain; DR1119 is an uncharacterized Deinococcus radiodurans protein with a metallophosphatase domain. 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: 277339 [Multi-domain]  Cd Length: 238  Bit Score: 45.17  E-value: 7.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488242154  34 QQLITSWNAVVKETDHVYHLGDLAMHPQYEKANADiLELVSQLQGTIHLIKGNHD 88
Cdd:cd07393   30 SKLEENWNNVVSPEDIVLIPGDISWAMNLKEALKD-LTWINDLPGIKILLKGNHD 83
DR1119 COG1768
Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function ...
 36-88 4.44e-05

Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function prediction only];


Pssm-ID: 441374 [Multi-domain]  Cd Length: 230  Bit Score: 42.50  E-value: 4.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488242154  36 LITSWNAVVKETDHVYHLGDL--AMHPqyEKANADiLELVSQLQGTIHLIKGNHD 88
Cdd:COG1768   33 IAENWRETVGPDDTVLIPGDIswAMKL--EEALPD-LDWIDALPGRKVLIKGNHD 84
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
6-116 1.75e-04

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 40.83  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154   6 SDMHFFHERllgENDFAPRLFANVDEMNQQlitswnavvkETDHVYHLGDLAMH---PQYEKAnadiLELVSQLQGTIHL 82
Cdd:COG1409    7 SDLHLGAPD---GSDTAEVLAAALADINAP----------RPDFVVVTGDLTDDgepEEYAAA----REILARLGVPVYV 69

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488242154  83 IKGNHDSRAFFRYLEKNDPGLSDGSPKFYFYDVG 116
Cdd:COG1409   70 VPGNHDIRAAMAEAYREYFGDLPPGGLYYSFDYG 103
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
48-162 7.57e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 35.66  E-value: 7.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488242154  48 DHVYHLGDLAMHPQYEKANADILElvsqlQGTIHLIKGNHDsRAFFRYLEKndpglsdgspkfyfYDVGAIVKFDHQQYY 127
Cdd:COG0622   28 DLIVHLGDLVGYGPDPPEVLDLLR-----ELPIVAVRGNHD-GAVLRGLRS--------------LPETLRLELEGVRIL 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488242154 128 LTH-----YPMLLGPNDTIRNL----------HGHIHHYSV-PIEN--VVNVG 162
Cdd:COG0622   88 LVHgspneYLLPDTPAERLRALaaegdadvvvCGHTHIPFVrRVGGvlLVNPG 140
 
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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