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Conserved domains on  [gi|489820678|ref|WP_003724482|]
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MULTISPECIES: metallophosphoesterase [Listeria]

Protein Classification

metallophosphoesterase( domain architecture ID 10003658)

metallophosphoesterase contains an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to Bacillus subtilis YkuE, which is specifically targeted by the Tat pathway to the cell wall

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0042578|GO:0016311
PubMed:  25837850|8003970

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
4-287 3.53e-86

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


:

Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 258.57  E-value: 3.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678   4 TGWGILGAVAAFTGYAYWS-TKHLTVTDYEIVSDKIPAEWDGATFVQLSDLHSASF--GLYNNPLLSIVNELAPDAVFLT 80
Cdd:COG1408    1 LALALLALGLALLAYGLYIePRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFigGERLERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  81 GDMIDGDESPYVAM-AVVRKLAKEFPVFYVSGNHEGRSAfYEDFKADMEKHHVTVLENERYFLKKDGAAIMVAGVRDPRF 159
Cdd:COG1408   81 GDLVDGSVAELEALlELLKKLKAPLGVYAVLGNHDYYAG-LEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVDDPHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 160 VRDDwaekelpkevweeaalkeALDDATANLSPDYFTILLAHRPEFWPLYQAYPIDLVLSGHAHGGQFRLPLTEGLFAPG 239
Cdd:COG1408  160 GRFP------------------DLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIGALLTPV 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 489820678 240 QgLMPKWTAGIHRAGGKALIVSRGLGNvTKLP-RLFNDPEIIRMTLRAK 287
Cdd:COG1408  222 R-LGRKYVAGLYREGGTQLYVSRGLGT-SGPPvRFGCPPEITLITLKSA 268
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
4-287 3.53e-86

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 258.57  E-value: 3.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678   4 TGWGILGAVAAFTGYAYWS-TKHLTVTDYEIVSDKIPAEWDGATFVQLSDLHSASF--GLYNNPLLSIVNELAPDAVFLT 80
Cdd:COG1408    1 LALALLALGLALLAYGLYIePRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFigGERLERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  81 GDMIDGDESPYVAM-AVVRKLAKEFPVFYVSGNHEGRSAfYEDFKADMEKHHVTVLENERYFLKKDGAAIMVAGVRDPRF 159
Cdd:COG1408   81 GDLVDGSVAELEALlELLKKLKAPLGVYAVLGNHDYYAG-LEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVDDPHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 160 VRDDwaekelpkevweeaalkeALDDATANLSPDYFTILLAHRPEFWPLYQAYPIDLVLSGHAHGGQFRLPLTEGLFAPG 239
Cdd:COG1408  160 GRFP------------------DLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIGALLTPV 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 489820678 240 QgLMPKWTAGIHRAGGKALIVSRGLGNvTKLP-RLFNDPEIIRMTLRAK 287
Cdd:COG1408  222 R-LGRKYVAGLYREGGTQLYVSRGLGT-SGPPvRFGCPPEITLITLKSA 268
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 44-284 3.95e-76

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: 231.40  E-value: 3.95e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  44 GATFVQLSDLHSASFGL--YNNPLLSIVNELAPDAVFLTGDMIDGDESPY-VAMAVVRKLAKEFPVFYVSGNHEGRSAFY 120
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGrtRLQKVVRKVNELNPDLIVITGDLVDGDVSVLrLLASPLSKLKAPLGVYFVLGNHDYYSGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 121 EDFKADMEKHHVTVLENERYFLKKDGAAIMVAGVrdprfvrddwaekelpkEVWEEAALKEALDDATANLSPDYFTILLA 200
Cdd:cd07385   81 EVWIAALEKAGITVLRNESVELSRDGATIGLAGS-----------------GVDDIGGHGEDLEKALKGLDENDPVILLA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 201 HRPEFWPLYQAYPIDLVLSGHAHGGQFRLPltegLFAPGQGLMPKWTAGIHR-AGGKALIVSRGLGNVTKLPRLFNDPEI 279
Cdd:cd07385  144 HNPDAAEEAQRPGVDLVLSGHTHGGQIFPP----NYGVLSKLGFPYDSGLYQiGGTTYLYVSRGLGTWGPPIRLGCPPEI 219


                 ....*
gi 489820678 280 IRMTL 284
Cdd:cd07385  220 TLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 50-284 1.22e-20

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 88.75  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  50 LSDLHSASFGLYnnPLLSIVNELA----PDAVFLTGDMIDGD--ESPYVAMAVVRKLAKEFPVFYVSGNHEgRSAFYEDF 123
Cdd:PRK11340  55 LADLHYSRFVPL--SLISDAIALGieqkPDLILLGGDYVLFDmpLNFSAFSDVLSPLAECAPTFACFGNHD-RPVGTEKN 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 124 KA---DMEKHHVTVLENERYFLKKDGAAIMVAGVRDPrfvrddWAEKELPKEVWEEaalkealddatanlspDYFTILLA 200
Cdd:PRK11340 132 HLigeTLKSAGITVLFNQATVIATPNRQFELVGTGDL------WAGQCKPPPASEA----------------NLPRLVLA 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 201 HRPEFWPLYQAYPIDLVLSGHAHGGQFRLPLTEGLFAPGQGlmPKWTAGIHRAGGKALIVSRGLGNVTKLpRLFNDPEII 280
Cdd:PRK11340 190 HNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVED--KRYVAGLNAFGERQIYTTRGVGSLYGL-RLNCRPEVT 266


                 ....
gi 489820678 281 RMTL 284
Cdd:PRK11340 267 MLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 46-152 7.98e-08

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: 49.90  E-value: 7.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678   46 TFVQLSDLHsASFGLYNNPLL--SIVNELAPDAVFLTGDMIDGDESPYVAMAVVRKLAKEFPVFYVSGNHEGRSAFYEDF 123
Cdd:pfam00149   2 RILVIGDLH-LPGQLDDLLELlkKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGECLRL 80

                          90       100
                  ....*....|....*....|....*....
gi 489820678  124 KADMEKHHVTVLENERYFLKKDGAAIMVA 152
Cdd:pfam00149  81 YPYLGLLARPWKRFLEVFNFLPLAGILSG 109
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
4-287 3.53e-86

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 258.57  E-value: 3.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678   4 TGWGILGAVAAFTGYAYWS-TKHLTVTDYEIVSDKIPAEWDGATFVQLSDLHSASF--GLYNNPLLSIVNELAPDAVFLT 80
Cdd:COG1408    1 LALALLALGLALLAYGLYIePRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFigGERLERLVEKINALKPDLVVLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  81 GDMIDGDESPYVAM-AVVRKLAKEFPVFYVSGNHEGRSAfYEDFKADMEKHHVTVLENERYFLKKDGAAIMVAGVRDPRF 159
Cdd:COG1408   81 GDLVDGSVAELEALlELLKKLKAPLGVYAVLGNHDYYAG-LEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVDDPHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 160 VRDDwaekelpkevweeaalkeALDDATANLSPDYFTILLAHRPEFWPLYQAYPIDLVLSGHAHGGQFRLPLTEGLFAPG 239
Cdd:COG1408  160 GRFP------------------DLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIGALLTPV 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 489820678 240 QgLMPKWTAGIHRAGGKALIVSRGLGNvTKLP-RLFNDPEIIRMTLRAK 287
Cdd:COG1408  222 R-LGRKYVAGLYREGGTQLYVSRGLGT-SGPPvRFGCPPEITLITLKSA 268
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 44-284 3.95e-76

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: 231.40  E-value: 3.95e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  44 GATFVQLSDLHSASFGL--YNNPLLSIVNELAPDAVFLTGDMIDGDESPY-VAMAVVRKLAKEFPVFYVSGNHEGRSAFY 120
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGrtRLQKVVRKVNELNPDLIVITGDLVDGDVSVLrLLASPLSKLKAPLGVYFVLGNHDYYSGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 121 EDFKADMEKHHVTVLENERYFLKKDGAAIMVAGVrdprfvrddwaekelpkEVWEEAALKEALDDATANLSPDYFTILLA 200
Cdd:cd07385   81 EVWIAALEKAGITVLRNESVELSRDGATIGLAGS-----------------GVDDIGGHGEDLEKALKGLDENDPVILLA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 201 HRPEFWPLYQAYPIDLVLSGHAHGGQFRLPltegLFAPGQGLMPKWTAGIHR-AGGKALIVSRGLGNVTKLPRLFNDPEI 279
Cdd:cd07385  144 HNPDAAEEAQRPGVDLVLSGHTHGGQIFPP----NYGVLSKLGFPYDSGLYQiGGTTYLYVSRGLGTWGPPIRLGCPPEI 219


                 ....*
gi 489820678 280 IRMTL 284
Cdd:cd07385  220 TLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 50-284 1.22e-20

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 88.75  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  50 LSDLHSASFGLYnnPLLSIVNELA----PDAVFLTGDMIDGD--ESPYVAMAVVRKLAKEFPVFYVSGNHEgRSAFYEDF 123
Cdd:PRK11340  55 LADLHYSRFVPL--SLISDAIALGieqkPDLILLGGDYVLFDmpLNFSAFSDVLSPLAECAPTFACFGNHD-RPVGTEKN 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 124 KA---DMEKHHVTVLENERYFLKKDGAAIMVAGVRDPrfvrddWAEKELPKEVWEEaalkealddatanlspDYFTILLA 200
Cdd:PRK11340 132 HLigeTLKSAGITVLFNQATVIATPNRQFELVGTGDL------WAGQCKPPPASEA----------------NLPRLVLA 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 201 HRPEFWPLYQAYPIDLVLSGHAHGGQFRLPLTEGLFAPGQGlmPKWTAGIHRAGGKALIVSRGLGNVTKLpRLFNDPEII 280
Cdd:PRK11340 190 HNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVED--KRYVAGLNAFGERQIYTTRGVGSLYGL-RLNCRPEVT 266


                 ....
gi 489820678 281 RMTL 284
Cdd:PRK11340 267 MLEL 270
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
46-223 4.14e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 75.50  E-value: 4.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  46 TFVQLSDLHSASFGLYNNP-----LLSIVNELAPDAVFLTGDMI-DGDESPY-VAMAVVRKLakEFPVFYVSGNHEGRSA 118
Cdd:COG1409    2 RFAHISDLHLGAPDGSDTAevlaaALADINAPRPDFVVVTGDLTdDGEPEEYaAAREILARL--GVPVYVVPGNHDIRAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 119 FYEDFKADMEKHHvtvlENERYFLKKDGAAimvagvrdpRFV-----RDDWAEKELPKEvwEEAALKEALDDAtanlsPD 193
Cdd:COG1409   80 MAEAYREYFGDLP----PGGLYYSFDYGGV---------RFIgldsnVPGRSSGELGPE--QLAWLEEELAAA-----PA 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489820678 194 YFTILLAHRP-----------------EFWPLYQAYPIDLVLSGHAH 223
Cdd:COG1409  140 KPVIVFLHHPpystgsgsdriglrnaeELLALLARYGVDLVLSGHVH 186
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
50-225 1.89e-13

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 67.73  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  50 LSDLHSASFGLYnnPLLSIVNELAPDAVFLTGDMIDGDESPYvAMAVVRKLAK-EFPVFYVSGNHEgrsafYEDFKADME 128
Cdd:COG2129    5 VSDLHGNFDLLE--KLLELARAEDADLVILAGDLTDFGTAEE-AREVLEELAAlGVPVLAVPGNHD-----DPEVLDALE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 129 KHHVTVLENERYFLKKdgaaIMVAGVRDPRFvrDDWAEkelPKEvWEEAALKEALddatANLSPDYFTILLAH------- 201
Cdd:COG2129   77 ESGVHNLHGRVVEIGG----LRIAGLGGSRP--TPFGT---PYE-YTEEEIEERL----AKLREKDVDILLTHappygtt 142

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489820678 202 --RPEFWP---------LYQAYPIDLVLSGHAHGG 225
Cdd:COG2129  143 ldRVEDGPhvgskalreLIEEFQPKLVLHGHIHES 177
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
65-226 4.89e-09

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 55.69  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  65 LLSIVNELAPDAVFLTGDMIDGDESPYVAMA----VVRKLAKE-FPVFYVSGNHE--GRSAFYEDFkadMEKHHVTVL-- 135
Cdd:COG0420   31 LVDLAIEEKVDAVLIAGDLFDSANPSPEAVRllaeALRRLSEAgIPVVLIAGNHDspSRLSAGSPL---LENLGVHVFgs 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 136 ENERYFLKKDGAAIMVAGVrdprfvrdDWAEKelpkevWEEAALKEALDDATANLSPDYFTILLAH-----RPEFWPLYQ 210
Cdd:COG0420  108 VEPEPVELEDGLGVAVYGL--------PYLRP------SDEEALRDLLERLPRALDPGGPNILLLHgfvagASGSRDIYV 173

                        170       180
                 ....*....|....*....|....*
gi 489820678 211 AY---------PIDLVLSGHAHGGQ 226
Cdd:COG0420  174 APvplsalpaaGFDYVALGHIHRPQ 198
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 48-114 6.66e-08

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: 50.34  E-value: 6.66e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489820678  48 VQLSDLHSASFGLYNNPLLSIVNELAPDAVFLTGDMID-GDESPYVAMAVVRKLAKEFPVFYVSGNHE 114
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLVDyGPDPEEVELKALRLLLAGIPVYVVPGNHD 68
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 46-152 7.98e-08

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: 49.90  E-value: 7.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678   46 TFVQLSDLHsASFGLYNNPLL--SIVNELAPDAVFLTGDMIDGDESPYVAMAVVRKLAKEFPVFYVSGNHEGRSAFYEDF 123
Cdd:pfam00149   2 RILVIGDLH-LPGQLDDLLELlkKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGECLRL 80

                          90       100
                  ....*....|....*....|....*....
gi 489820678  124 KADMEKHHVTVLENERYFLKKDGAAIMVA 152
Cdd:pfam00149  81 YPYLGLLARPWKRFLEVFNFLPLAGILSG 109
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 48-113 2.05e-06

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: 46.13  E-value: 2.05e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489820678  48 VQLSDLHsasFGLYNNP------LLSIVNELAPDAVFLTGDMID-GDESPYV-AMAVVRKLAKEfPVFYVSGNH 113
Cdd:cd07400    2 AHISDLH---FGEERKPevlelnLLDEINALKPDLVVVTGDLTQrARPAEFEeAREFLDALEPE-PVVVVPGNH 71
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 47-223 4.84e-05

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 43.81  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  47 FVQLSDLHSASFG----LYNNPL------LSIVNEL--APDAVFLTGDMIDGDESPyvAMAVVRKLAKEF--PVFYVSGN 112
Cdd:cd07402    1 IAQISDTHLFAPGegalLGVDTAarlaaaVAQVNALhpRPDLVVVTGDLSDDGSPE--SYERLRELLAPLpaPVYWIPGN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 113 HEGRSAFYEDFK----ADMEK-HHVTVLENERyFLKKDgaaIMVAGVRDPRFVRDDWAekelpkevWEEAALKEALDDAT 187
Cdd:cd07402   79 HDDRAAMREALPeppyDDNGPvQYVVDFGGWR-LILLD---TSVPGVHHGELSDEQLD--------WLEAALAEAPDRPT 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489820678 188 --------ANL-SPDYFTILLAHRPEFWPLYQAYP-IDLVLSGHAH 223
Cdd:cd07402  147 liflhhppFPLgIPWMDAIRLRNSQALFAVLARHPqVKAILCGHIH 192
MPP_UshA_N_like cd00845
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes ...
 46-223 6.04e-04

Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277323 [Multi-domain]  Cd Length: 255  Bit Score: 40.37  E-value: 6.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  46 TFVQLSDLHSASFGLYNNP------LLSIVNEL---APDAVFL-TGDMIDG----------------DESPYVAMAV--- 96
Cdd:cd00845    2 TILHTNDLHGHLDPHSNGGiggaarLAGLVKQIraeNPNTLLLdAGDNFQGsplstltdgeavidlmNALGYDAATVgnh 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  97 --------VRKLAKEFPVFYVSGN--HEGRSAFYEDFKAdmekHHVtvleneryfLKKDGAAIMVAGVRDP---RFVRDD 163
Cdd:cd00845   82 efdygldqLEELLKQAKFPWLSANvyEDGTGTGEPGAKP----YTI---------ITVDGVKVGVIGLTTPdtpTVTPPE 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489820678 164 WAEK-ELPKEVWEEAALKEALDDATANLspdyfTILLAH--RPEFWPLYQAYP-IDLVLSGHAH 223
Cdd:cd00845  149 GNRGvEFPDPAEAIAEAAEELKAEGVDV-----IIALSHlgIDTDERLAAAVKgIDVILGGHSH 207
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 50-142 1.09e-03

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. 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: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 39.24  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  50 LSDLHsASFGLYNNPLLSIVNELAPDAVFLTGDMIDGDESPYVAMAVVRKLAKEFPVFYVSGNHE--GRSAFYEDFKADM 127
Cdd:cd07404    4 ASDLH-LEVEQNLAKLKFFPKVPDADILILAGDIGRLTDAEAWDNFLDLQSFQFEPVYYVPGNHEfyGGSLDITLDALRM 82

                         90
                 ....*....|....*...
gi 489820678 128 EKH---HVTVLENERYFL 142
Cdd:cd07404   83 AAQdlsNVHYLNNQEVVL 100
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 44-239 4.48e-03

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: 37.25  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  44 GATFVQLSDLHSASFGLYNNpLLSIVNELAPDAVFLTGDMIDgDESP-----YVAMAVVRKLAKE-FPVFYVSGNHEgrs 117
Cdd:cd00840   11 GYPLYGLSRREEDFFKAFEE-IVDLAIEEKVDFVLIAGDLFD-SNNPspealKLAIEGLRRLCEAgIPVFVIAGNHD--- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 118 afyedfkadmekhhvtvleneryflkkDGAAIMVAGVRdprfvrddWAEKELPKEVWEEAALKEALDDatanlsPDYFTI 197
Cdd:cd00840   86 ---------------------------SPARVAIYGLP--------YLRDERLERLFEDLELRPRLLK------PDWFNI 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489820678 198 LLAH------------RPEFWPLYQAYPIDLVLSGHAHGGQFRLPLTEGLFAPG 239
Cdd:cd00840  125 LLLHqgvdgagpsdseRPIVPEDLLPDGFDYVALGHIHKPQIIEGGGPPIVYPG 178
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 68-223 5.53e-03

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: 37.68  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678  68 IVNELAPDAVF--LTGDMIDG-----DESPYVA--MAVVRKLAKEFPVFYVSGNH--------EGRSAFYEDFKADmekh 130
Cdd:cd07395   43 AINKLNPKPKFvvVCGDLVHAmpgeeFREQQVSdlKDVLSKLDPDIPLVCVCGNHdvgntptpETIQRYRDDFGDD---- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820678 131 hvtvlenerYFlkkdgaAIMVAGVR----DPRFVRDDWAEKELPKE--VWEEAALKEA-LDDA--------------TAN 189
Cdd:cd07395  119 ---------YF------SFWVGGVFfivlNSQLFKDPSKVPELASAqdQWLEEQLQIArESDAkhvvvfqhiplfleDPD 183

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489820678 190 LSPDYFTILLAHRPEFWPLYQAYPIDLVLSGHAH 223
Cdd:cd07395  184 EEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYH 217
 
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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