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Conserved domains on  [gi|1864720485|ref|WP_176902167|]
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MULTISPECIES: metallophosphoesterase [Streptomyces]

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];
178-430 3.91e-97

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


:

Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 291.70  E-value: 3.91e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 178 LGTVGYGTYGVLRGPRVKRVTVPLAKLPRSAHGFRIAVVSDIHLGPILGRAHTQRIVDTINRTQPDLIAVVGDLVDGTVA 257
Cdd:COG1408    10 LALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLVDGSVA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 258 DLGPAAEPLAGLTARHGAFFVTGNHEYFSGAAQWVDHVRELGLHPLENARVE----TAGFDLAGVNDIAGeseGQGPDFE 333
Cdd:COG1408    90 ELEALLELLKKLKAPLGVYAVLGNHDYYAGLEELRAALEEAGVRVLRNEAVTlergGDRLNLAGVDDPHA---GRFPDLE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 334 RALGDRDRARASVLLAHQPVVIDDAVAYGVDLQLSGHTHGGQLWPGNY-----LAELANPTVAGLERYGDTQLYVSRGAG 408
Cdd:COG1408   167 KALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIgalltPVRLGRKYVAGLYREGGTQLYVSRGLG 246

                         250       260
                  ....*....|....*....|..
gi 1864720485 409 AWGPPVRVGAPSDITVVQLASR 430
Cdd:COG1408   247 TSGPPVRFGCPPEITLITLKSA 268
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
178-430 3.91e-97

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 291.70  E-value: 3.91e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 178 LGTVGYGTYGVLRGPRVKRVTVPLAKLPRSAHGFRIAVVSDIHLGPILGRAHTQRIVDTINRTQPDLIAVVGDLVDGTVA 257
Cdd:COG1408    10 LALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLVDGSVA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 258 DLGPAAEPLAGLTARHGAFFVTGNHEYFSGAAQWVDHVRELGLHPLENARVE----TAGFDLAGVNDIAGeseGQGPDFE 333
Cdd:COG1408    90 ELEALLELLKKLKAPLGVYAVLGNHDYYAGLEELRAALEEAGVRVLRNEAVTlergGDRLNLAGVDDPHA---GRFPDLE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 334 RALGDRDRARASVLLAHQPVVIDDAVAYGVDLQLSGHTHGGQLWPGNY-----LAELANPTVAGLERYGDTQLYVSRGAG 408
Cdd:COG1408   167 KALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIgalltPVRLGRKYVAGLYREGGTQLYVSRGLG 246

                         250       260
                  ....*....|....*....|..
gi 1864720485 409 AWGPPVRVGAPSDITVVQLASR 430
Cdd:COG1408   247 TSGPPVRFGCPPEITLITLKSA 268
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 210-427 1.50e-74

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: 232.56  E-value: 1.50e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 210 GFRIAVVSDIHLGPILGRAHTQRIVDTINRTQPDLIAVVGDLVDGTVADLGPAAEPLAGLTARHGAFFVTGNHEYFSGA- 288
Cdd:cd07385     1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGDv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 289 AQWVDHVRELGLHPLENARVETAGFDLAGVNDIAGES--EGQGPDFERALGDRDRARASVLLAHQPVVIDDAVAYGVDLQ 366
Cdd:cd07385    81 EVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDdiGGHGEDLEKALKGLDENDPVILLAHNPDAAEEAQRPGVDLV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864720485 367 LSGHTHGGQLWPGNY--LAELANPTVAGLERYGDT-QLYVSRGAGAWGPPVRVGAPSDITVVQL 427
Cdd:cd07385   161 LSGHTHGGQIFPPNYgvLSKLGFPYDSGLYQIGGTtYLYVSRGLGTWGPPIRLGCPPEITLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 201-427 1.74e-13

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 70.26  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 201 LAKLPRSAHGFRIAVVSDIHLG-----PILGRAHTQRIvdtinRTQPDLIAVVGDLVDG-TVADLGPAAEPLAGLTARHG 274
Cdd:PRK11340   40 LAFFKDNAAPFKILFLADLHYSrfvplSLISDAIALGI-----EQKPDLILLGGDYVLFdMPLNFSAFSDVLSPLAECAP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 275 AFFVTGNHE--YFSGAAQWVDHV-RELGLHPLENARVETA----GFDLAGVNDI-AGESEGqgpdfERALgdrDRARASV 346
Cdd:PRK11340  115 TFACFGNHDrpVGTEKNHLIGETlKSAGITVLFNQATVIAtpnrQFELVGTGDLwAGQCKP-----PPAS---EANLPRL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 347 LLAHQPVVIDDAVAYGVDLQLSGHTHGGQL---WPGNYLAELANPT-VAGLERYGDTQLYVSRGAGAWGpPVRVGAPSDI 422
Cdd:PRK11340  187 VLAHNPDSKEVMRDEPWDLMLCGHTHGGQLrvpLVGEPFAPVEDKRyVAGLNAFGERQIYTTRGVGSLY-GLRLNCRPEV 265


                  ....*
gi 1864720485 423 TVVQL 427
Cdd:PRK11340  266 TMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 211-318 3.44e-09

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: 54.53  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 211 FRIAVVSDIHLGPilGRAHTQRIVDTINR-TQPDLIAVVGDLVDGTVADLGpAAEPLAGLTARHGAFFVTGNHEYFSGAA 289
Cdd:pfam00149   1 MRILVIGDLHLPG--QLDDLLELLKKLLEeGKPDLVLHAGDLVDRGPPSEE-VLELLERLIKYVPVYLVRGNHDFDYGEC 77

                          90       100
                  ....*....|....*....|....*....
gi 1864720485 290 QWVDHVRELGLHPLENARVETAGFDLAGV 318
Cdd:pfam00149  78 LRLYPYLGLLARPWKRFLEVFNFLPLAGI 106
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
178-430 3.91e-97

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 291.70  E-value: 3.91e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 178 LGTVGYGTYGVLRGPRVKRVTVPLAKLPRSAHGFRIAVVSDIHLGPILGRAHTQRIVDTINRTQPDLIAVVGDLVDGTVA 257
Cdd:COG1408    10 LALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLVDGSVA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 258 DLGPAAEPLAGLTARHGAFFVTGNHEYFSGAAQWVDHVRELGLHPLENARVE----TAGFDLAGVNDIAGeseGQGPDFE 333
Cdd:COG1408    90 ELEALLELLKKLKAPLGVYAVLGNHDYYAGLEELRAALEEAGVRVLRNEAVTlergGDRLNLAGVDDPHA---GRFPDLE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 334 RALGDRDRARASVLLAHQPVVIDDAVAYGVDLQLSGHTHGGQLWPGNY-----LAELANPTVAGLERYGDTQLYVSRGAG 408
Cdd:COG1408   167 KALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIgalltPVRLGRKYVAGLYREGGTQLYVSRGLG 246

                         250       260
                  ....*....|....*....|..
gi 1864720485 409 AWGPPVRVGAPSDITVVQLASR 430
Cdd:COG1408   247 TSGPPVRFGCPPEITLITLKSA 268
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 210-427 1.50e-74

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: 232.56  E-value: 1.50e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 210 GFRIAVVSDIHLGPILGRAHTQRIVDTINRTQPDLIAVVGDLVDGTVADLGPAAEPLAGLTARHGAFFVTGNHEYFSGA- 288
Cdd:cd07385     1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGDv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 289 AQWVDHVRELGLHPLENARVETAGFDLAGVNDIAGES--EGQGPDFERALGDRDRARASVLLAHQPVVIDDAVAYGVDLQ 366
Cdd:cd07385    81 EVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDdiGGHGEDLEKALKGLDENDPVILLAHNPDAAEEAQRPGVDLV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864720485 367 LSGHTHGGQLWPGNY--LAELANPTVAGLERYGDT-QLYVSRGAGAWGPPVRVGAPSDITVVQL 427
Cdd:cd07385   161 LSGHTHGGQIFPPNYgvLSKLGFPYDSGLYQIGGTtYLYVSRGLGTWGPPIRLGCPPEITLITL 224
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
211-392 1.19e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 75.88  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 211 FRIAVVSDIHLGPILG---RAHTQRIVDTINRTQPDLIAVVGDLV-DGTVADLGPAAEPLAGLTARhgAFFVTGNHEYFS 286
Cdd:COG1409     1 FRFAHISDLHLGAPDGsdtAEVLAAALADINAPRPDFVVVTGDLTdDGEPEEYAAAREILARLGVP--VYVVPGNHDIRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 287 G-AAQWVDHVRELGLHPLeNARVETAGFDLAGVND-IAGESEGQ-GPD----FERALgDRDRARASVLLAHQPVV----- 354
Cdd:COG1409    79 AmAEAYREYFGDLPPGGL-YYSFDYGGVRFIGLDSnVPGRSSGElGPEqlawLEEEL-AAAPAKPVIVFLHHPPYstgsg 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1864720485 355 -----IDDAVA-------YGVDLQLSGHTHGGQLWPGNYLAELANPTVAG 392
Cdd:COG1409   157 sdrigLRNAEEllallarYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGG 206
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
212-374 1.49e-14

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 72.35  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 212 RIAVVSDIHLGpilgRAHTQRIVDTINRTQPDLIAVVGDLVD-GTVADLGPAAEPLAGLTARhgAFFVTGNHEYFSgaaq 290
Cdd:COG2129     1 KILAVSDLHGN----FDLLEKLLELARAEDADLVILAGDLTDfGTAEEAREVLEELAALGVP--VLAVPGNHDDPE---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 291 WVDHVRELGLHPLENARVETAGFDLAGV-----NDIAGESEGQGPDFERALGDRDRARASVLLAHQPV------------ 353
Cdd:COG2129    71 VLDALEESGVHNLHGRVVEIGGLRIAGLggsrpTPFGTPYEYTEEEIEERLAKLREKDVDILLTHAPPygttldrvedgp 150

                         170       180
                  ....*....|....*....|....*..
gi 1864720485 354 -----VIDDAV-AYGVDLQLSGHTHGG 374
Cdd:COG2129   151 hvgskALRELIeEFQPKLVLHGHIHES 177
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 201-427 1.74e-13

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 70.26  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 201 LAKLPRSAHGFRIAVVSDIHLG-----PILGRAHTQRIvdtinRTQPDLIAVVGDLVDG-TVADLGPAAEPLAGLTARHG 274
Cdd:PRK11340   40 LAFFKDNAAPFKILFLADLHYSrfvplSLISDAIALGI-----EQKPDLILLGGDYVLFdMPLNFSAFSDVLSPLAECAP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 275 AFFVTGNHE--YFSGAAQWVDHV-RELGLHPLENARVETA----GFDLAGVNDI-AGESEGqgpdfERALgdrDRARASV 346
Cdd:PRK11340  115 TFACFGNHDrpVGTEKNHLIGETlKSAGITVLFNQATVIAtpnrQFELVGTGDLwAGQCKP-----PPAS---EANLPRL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 347 LLAHQPVVIDDAVAYGVDLQLSGHTHGGQL---WPGNYLAELANPT-VAGLERYGDTQLYVSRGAGAWGpPVRVGAPSDI 422
Cdd:PRK11340  187 VLAHNPDSKEVMRDEPWDLMLCGHTHGGQLrvpLVGEPFAPVEDKRyVAGLNAFGERQIYTTRGVGSLY-GLRLNCRPEV 265


                  ....*
gi 1864720485 423 TVVQL 427
Cdd:PRK11340  266 TMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 211-318 3.44e-09

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: 54.53  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 211 FRIAVVSDIHLGPilGRAHTQRIVDTINR-TQPDLIAVVGDLVDGTVADLGpAAEPLAGLTARHGAFFVTGNHEYFSGAA 289
Cdd:pfam00149   1 MRILVIGDLHLPG--QLDDLLELLKKLLEeGKPDLVLHAGDLVDRGPPSEE-VLELLERLIKYVPVYLVRGNHDFDYGEC 77

                          90       100
                  ....*....|....*....|....*....
gi 1864720485 290 QWVDHVRELGLHPLENARVETAGFDLAGV 318
Cdd:pfam00149  78 LRLYPYLGLLARPWKRFLEVFNFLPLAGI 106
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
211-380 1.62e-08

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 55.30  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 211 FRIAVVSDIHLGPILGRAHTQ--------RIVDTINRTQPDLIAVVGDLVDG---TVADLGPAAEPLAGLTARHGAFFVT 279
Cdd:COG0420     1 MRFLHTADWHLGKPLHGASRRedqlaaldRLVDLAIEEKVDAVLIAGDLFDSanpSPEAVRLLAEALRRLSEAGIPVVLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 280 -GNHEYFSGAAQWVDHVRELGLHPLENARVETagFDLAGVNDIA---------GESEGQGPDFERALGDRDRARASVLLA 349
Cdd:COG0420    81 aGNHDSPSRLSAGSPLLENLGVHVFGSVEPEP--VELEDGLGVAvyglpylrpSDEEALRDLLERLPRALDPGGPNILLL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1864720485 350 HQ--------------PVVIDDAVAYGVDLQLSGHTHGGQLWPGN 380
Cdd:COG0420   159 HGfvagasgsrdiyvaPVPLSALPAAGFDYVALGHIHRPQVLGGD 203
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
212-398 2.79e-07

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 50.30  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 212 RIAVVSDIHlgpilGRAH-TQRIVDTINRTQPDLIAVVGDLVDGtvadlGPAAEPLAGLTARHGAFFVTGNHEYFsgaaq 290
Cdd:COG0622     1 KIAVISDTH-----GNLPaLEAVLEDLEREGVDLIVHLGDLVGY-----GPDPPEVLDLLRELPIVAVRGNHDGA----- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 291 WVDHVRELGLHplenARVETAGFDLAGVNdiagesegqGPDFERALGDRDRARasvllahqpvVIDDAVAYGVDLQLSGH 370
Cdd:COG0622    66 VLRGLRSLPET----LRLELEGVRILLVH---------GSPNEYLLPDTPAER----------LRALAAEGDADVVVCGH 122

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1864720485 371 TH-------GGQLwpgnylaeLANPTVAGLERYGD 398
Cdd:COG0622   123 THipfvrrvGGVL--------LVNPGSVGQPRDGD 149
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 213-390 3.25e-05

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: 43.44  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 213 IAVVSDIHLGPILGRAHTQR-IVDTINRTQPDLIAVVGDLVD-GTVADLGPAAEPLAGLTArHGAFFVTGNHEYFSgaaq 290
Cdd:cd07400     1 IAHISDLHFGEERKPEVLELnLLDEINALKPDLVVVTGDLTQrARPAEFEEAREFLDALEP-EPVVVVPGNHDAIV---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 291 wVDHvrelglHPLenarvetagfdlagvndiagesegqgpdfeRALGDRDRARASVLLAHQpvVIDDAVAYGVDLQLSGH 370
Cdd:cd07400    76 -ALH------HPL------------------------------LPPPDTGRERNVLLDAGD--ALKLLKELGVDLVLHGH 116

                         170       180
                  ....*....|....*....|
gi 1864720485 371 THGGQLWPgnylAELANPTV 390
Cdd:cd07400   117 KHVPAVWN----LGLLNGIV 132
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 214-285 3.03e-04

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: 40.71  E-value: 3.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864720485 214 AVVSDIHLGPILGRAHTQRIVdtINRTQPDLIAVVGDLVDGTVADLGPAAEPLAGLTARHGAFFVTGNHEYF 285
Cdd:cd00838     1 LVISDIHGNLEALEAVLEAAL--AKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHDIL 70
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 215-312 3.26e-04

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: 41.96  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 215 VVSDIHLGPILGRAHTQRIVDTIN-RTQPDLIAVVGDLVDGTVADLGPAAEP-------LAGLTARHGA-FFVTGNHEYF 285
Cdd:cd07398     2 FISDLHLGLRGCRADRLLDFLLVEeLDEADALYLLGDIFDLWIGDDSVVWPGahralarLLRLADRGTEvIYVPGNHDFL 81

                          90       100
                  ....*....|....*....|....*...
gi 1864720485 286 SGaaqwVDHVRELGLHPL-ENARVETAG 312
Cdd:cd07398    82 LG----RFFAEALGAILLpEPAEHLELD 105
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 213-282 7.36e-04

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: 41.11  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 213 IAVVSDIHLGP-----ILG---RAHTQRIVDTINR--TQPDLIAVVGDLVD-GTVADLGPAAEPLAGLTARhgAFFVTGN 281
Cdd:cd07402     1 IAQISDTHLFApgegaLLGvdtAARLAAAVAQVNAlhPRPDLVVVTGDLSDdGSPESYERLRELLAPLPAP--VYWIPGN 78


                  .
gi 1864720485 282 H 282
Cdd:cd07402    79 H 79
LpxH COG2908
UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];
211-312 8.19e-04

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


Pssm-ID: 442152 [Multi-domain]  Cd Length: 238  Bit Score: 40.94  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 211 FRIAVVSDIHLGPILGRAHTQRIVDTINRT--QPDLIAVVGDLVDG-------------TVADLgpaaepLAGLtARHGA 275
Cdd:COG2908     1 MRTLFISDLHLGTPGPQAITAALLDFLRSIahDADALYLLGDIFDFwigdddvwppghnRVLQK------LLEL-ADKGT 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1864720485 276 --FFVTGNH-----EYFSgaaqwvdhvRELGLHPLENARVETAG 312
Cdd:COG2908    74 pvYYIPGNHdfllgDYFA---------KELGATLLPDPIHLTLD 108
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 212-375 8.89e-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: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 212 RIAVVSDIHLG------PILGRAHTQ---RIVDTINRTQPDLIAVVGDLVDG---TVADLGPAAEPLAGLTARHGAFFVT 279
Cdd:cd00840     1 RFLHTADWHLGyplyglSRREEDFFKafeEIVDLAIEEKVDFVLIAGDLFDSnnpSPEALKLAIEGLRRLCEAGIPVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864720485 280 -GNHEYFSGAAqwvdhvrelgLHPLENARVETAGFDLAGVNDIAGESEGQGPdferalgdrdraraSVLLAHQ------- 351
Cdd:cd00840    81 aGNHDSPARVA----------IYGLPYLRDERLERLFEDLELRPRLLKPDWF--------------NILLLHQgvdgagp 136

                         170       180
                  ....*....|....*....|....*....
gi 1864720485 352 -----PVVIDDAVAYGVDLQLSGHTHGGQ 375
Cdd:cd00840   137 sdserPIVPEDLLPDGFDYVALGHIHKPQ 165
 
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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