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Conserved domains on  [gi|2794475169|ref|WP_372380926|]
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metallophosphoesterase [Xanthomonas sp. NCPPB 1754]

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];
113-382 3.23e-68

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


:

Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 216.20  E-value: 3.23e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 113 IGLSLAVGIAVSFGTVGGPVVREEVIQVSGLPNGLDGLRIANIGDVHIGPFIKPADLAAAVDIVNARNVDLLAITGDLID 192
Cdd:COG1408     6 LALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLVD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 193 D-LDQLESTLDALERSEA-LPVLSILGNHDKYPNEAAVVAALKRRNprIEVLINSSMQVHPRGVPLRVAGVDyplaadgr 270
Cdd:COG1408    86 GsVAELEALLELLKKLKApLGVYAVLGNHDYYAGLEELRAALEEAG--VRVLRNEAVTLERGGDRLNLAGVD-------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 271 hmlprdeqDAAMHRFADL--AFAKVMPGEPLVVLSHHPEFFPIATARGAMLTLSSHTHGGQVRLFG-----RPVIVAYDY 343
Cdd:COG1408   156 --------DPHAGRFPDLekALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGigallTPVRLGRKY 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2794475169 344 MHGIYQEGSGYLDVSSGLGHW-LPLRIGVPREVSIITLRR 382
Cdd:COG1408   228 VAGLYREGGTQLYVSRGLGTSgPPVRFGCPPEITLITLKS 267
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
113-382 3.23e-68

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 216.20  E-value: 3.23e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 113 IGLSLAVGIAVSFGTVGGPVVREEVIQVSGLPNGLDGLRIANIGDVHIGPFIKPADLAAAVDIVNARNVDLLAITGDLID 192
Cdd:COG1408     6 LALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLVD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 193 D-LDQLESTLDALERSEA-LPVLSILGNHDKYPNEAAVVAALKRRNprIEVLINSSMQVHPRGVPLRVAGVDyplaadgr 270
Cdd:COG1408    86 GsVAELEALLELLKKLKApLGVYAVLGNHDYYAGLEELRAALEEAG--VRVLRNEAVTLERGGDRLNLAGVD-------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 271 hmlprdeqDAAMHRFADL--AFAKVMPGEPLVVLSHHPEFFPIATARGAMLTLSSHTHGGQVRLFG-----RPVIVAYDY 343
Cdd:COG1408   156 --------DPHAGRFPDLekALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGigallTPVRLGRKY 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2794475169 344 MHGIYQEGSGYLDVSSGLGHW-LPLRIGVPREVSIITLRR 382
Cdd:COG1408   228 VAGLYREGGTQLYVSRGLGTSgPPVRFGCPPEITLITLKS 267
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 149-380 2.42e-40

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: 142.42  E-value: 2.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 149 GLRIANIGDVHIGPFIKPADLAAAVDIVNARNVDLLAITGDLID-DLDQLESTLDALERSEA-LPVLSILGNHDKYP-NE 225
Cdd:cd07385     1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDgDVSVLRLLASPLSKLKApLGVYFVLGNHDYYSgDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 226 AAVVAALKRRNprIEVLINSSmqvhprgVPLRvaGVDYPLAADGrhmlpRDEQDAAMHRFAD-LAFAKVMPGEPLVVLSH 304
Cdd:cd07385    81 EVWIAALEKAG--ITVLRNES-------VELS--RDGATIGLAG-----SGVDDIGGHGEDLeKALKGLDENDPVILLAH 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 305 HPEFFPIATARGAMLTLSSHTHGGQVRLFGRPVIVAYD--YMHGIYQEGSG-YLDVSSGLGHW-LPLRIGVPREVSIITL 380
Cdd:cd07385   145 NPDAAEEAQRPGVDLVLSGHTHGGQIFPPNYGVLSKLGfpYDSGLYQIGGTtYLYVSRGLGTWgPPIRLGCPPEITLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 139-380 1.29e-14

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 73.35  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 139 QVSGLPNGLDGLRIANIGDVHIGPFIKPADLAAAVDIVNARNVDLLAITGD--LIDDLDQLESTLDALER-SEALPVLSI 215
Cdd:PRK11340   39 RLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDyvLFDMPLNFSAFSDVLSPlAECAPTFAC 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 216 LGNHDK---YPNEAAVVAALKrrNPRIEVLINSSMQVHPRGVPLRVAGVDYPLAadGRHMLPRdEQDAAMhrfadlafak 292
Cdd:PRK11340  119 FGNHDRpvgTEKNHLIGETLK--SAGITVLFNQATVIATPNRQFELVGTGDLWA--GQCKPPP-ASEANL---------- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 293 vmpgePLVVLSHHPEFFPIATARGAMLTLSSHTHGGQVR--LFGRPVIVAYD--YMHGIYQEGSGYLDVSSGLGHWLPLR 368
Cdd:PRK11340  184 -----PRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRvpLVGEPFAPVEDkrYVAGLNAFGERQIYTTRGVGSLYGLR 258

                         250
                  ....*....|..
gi 2794475169 369 IGVPREVSIITL 380
Cdd:PRK11340  259 LNCRPEVTMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 150-227 7.79e-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: 50.29  E-value: 7.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 150 LRIANIGDVHIGPFIkpADLAAAVD-IVNARNVDLLAITGDLIDDLDQLESTLDALER-SEALPVLSILGNHDKYPNEAA 227
Cdd:pfam00149   1 MRILVIGDLHLPGQL--DDLLELLKkLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERlIKYVPVYLVRGNHDFDYGECL 78
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
113-382 3.23e-68

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 216.20  E-value: 3.23e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 113 IGLSLAVGIAVSFGTVGGPVVREEVIQVSGLPNGLDGLRIANIGDVHIGPFIKPADLAAAVDIVNARNVDLLAITGDLID 192
Cdd:COG1408     6 LALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLVD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 193 D-LDQLESTLDALERSEA-LPVLSILGNHDKYPNEAAVVAALKRRNprIEVLINSSMQVHPRGVPLRVAGVDyplaadgr 270
Cdd:COG1408    86 GsVAELEALLELLKKLKApLGVYAVLGNHDYYAGLEELRAALEEAG--VRVLRNEAVTLERGGDRLNLAGVD-------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 271 hmlprdeqDAAMHRFADL--AFAKVMPGEPLVVLSHHPEFFPIATARGAMLTLSSHTHGGQVRLFG-----RPVIVAYDY 343
Cdd:COG1408   156 --------DPHAGRFPDLekALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGigallTPVRLGRKY 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2794475169 344 MHGIYQEGSGYLDVSSGLGHW-LPLRIGVPREVSIITLRR 382
Cdd:COG1408   228 VAGLYREGGTQLYVSRGLGTSgPPVRFGCPPEITLITLKS 267
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 149-380 2.42e-40

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: 142.42  E-value: 2.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 149 GLRIANIGDVHIGPFIKPADLAAAVDIVNARNVDLLAITGDLID-DLDQLESTLDALERSEA-LPVLSILGNHDKYP-NE 225
Cdd:cd07385     1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDgDVSVLRLLASPLSKLKApLGVYFVLGNHDYYSgDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 226 AAVVAALKRRNprIEVLINSSmqvhprgVPLRvaGVDYPLAADGrhmlpRDEQDAAMHRFAD-LAFAKVMPGEPLVVLSH 304
Cdd:cd07385    81 EVWIAALEKAG--ITVLRNES-------VELS--RDGATIGLAG-----SGVDDIGGHGEDLeKALKGLDENDPVILLAH 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 305 HPEFFPIATARGAMLTLSSHTHGGQVRLFGRPVIVAYD--YMHGIYQEGSG-YLDVSSGLGHW-LPLRIGVPREVSIITL 380
Cdd:cd07385   145 NPDAAEEAQRPGVDLVLSGHTHGGQIFPPNYGVLSKLGfpYDSGLYQIGGTtYLYVSRGLGTWgPPIRLGCPPEITLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 139-380 1.29e-14

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 73.35  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 139 QVSGLPNGLDGLRIANIGDVHIGPFIKPADLAAAVDIVNARNVDLLAITGD--LIDDLDQLESTLDALER-SEALPVLSI 215
Cdd:PRK11340   39 RLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDyvLFDMPLNFSAFSDVLSPlAECAPTFAC 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 216 LGNHDK---YPNEAAVVAALKrrNPRIEVLINSSMQVHPRGVPLRVAGVDYPLAadGRHMLPRdEQDAAMhrfadlafak 292
Cdd:PRK11340  119 FGNHDRpvgTEKNHLIGETLK--SAGITVLFNQATVIATPNRQFELVGTGDLWA--GQCKPPP-ASEANL---------- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 293 vmpgePLVVLSHHPEFFPIATARGAMLTLSSHTHGGQVR--LFGRPVIVAYD--YMHGIYQEGSGYLDVSSGLGHWLPLR 368
Cdd:PRK11340  184 -----PRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRvpLVGEPFAPVEDkrYVAGLNAFGERQIYTTRGVGSLYGLR 258

                         250
                  ....*....|..
gi 2794475169 369 IGVPREVSIITL 380
Cdd:PRK11340  259 LNCRPEVTMLEL 270
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
150-340 1.46e-13

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 69.72  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 150 LRIANIGDVHIGP---FIKPADLAAAVDIVNARNVDLLAITGDLIDD--LDQLESTLDALERSEAlPVLSILGNHDKY-P 223
Cdd:COG1409     1 FRFAHISDLHLGApdgSDTAEVLAAALADINAPRPDFVVVTGDLTDDgePEEYAAAREILARLGV-PVYVVPGNHDIRaA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 224 NEAAVVAALKRRNPrievliNSSMQVHPRGvPLRVAGVD--YPLAADGRhmLPRDEQDAAMHRFADLafakvmPGEPLVV 301
Cdd:COG1409    80 MAEAYREYFGDLPP------GGLYYSFDYG-GVRFIGLDsnVPGRSSGE--LGPEQLAWLEEELAAA------PAKPVIV 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2794475169 302 LSHHP-----------------EFFPIATARGAMLTLSSHTH-GGQVRLFGRPVIVA 340
Cdd:COG1409   145 FLHHPpystgsgsdriglrnaeELLALLARYGVDLVLSGHVHrYERTRRDGVPYIVA 201
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
151-305 5.81e-10

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 59.16  E-value: 5.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 151 RIANIGDVHIG-PFIKP---AD----LAAAVDIVNARNVDLLAITGDLID----DLDQLESTLDALER--SEALPVLSIL 216
Cdd:COG0420     2 RFLHTADWHLGkPLHGAsrrEDqlaaLDRLVDLAIEEKVDAVLIAGDLFDsanpSPEAVRLLAEALRRlsEAGIPVVLIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 217 GNHDkYPNEAAVVAALkRRNPRIEVL--INSSMQVHPRGVPLRVAGVDYplaadgrhmLPRDEQDAAMHRFADLAfAKVM 294
Cdd:COG0420    82 GNHD-SPSRLSAGSPL-LENLGVHVFgsVEPEPVELEDGLGVAVYGLPY---------LRPSDEEALRDLLERLP-RALD 149

                         170
                  ....*....|.
gi 2794475169 295 PGEPLVVLSHH 305
Cdd:COG0420   150 PGGPNILLLHG 160
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
151-306 1.47e-09

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 57.33  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 151 RIANIGDVHiGPFikpADLAAAVDIVNARNVDLLAITGDLID--DLDQLESTLDALeRSEALPVLSILGNHDKYpneaAV 228
Cdd:COG2129     1 KILAVSDLH-GNF---DLLEKLLELARAEDADLVILAGDLTDfgTAEEAREVLEEL-AALGVPVLAVPGNHDDP----EV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 229 VAALKRRNprIEVLINSSMQVHprgvPLRVAGVDY--PLAADGRHMLPRDEQDAAMhrfadlafAKVMPGEPLVVLSHHP 306
Cdd:COG2129    72 LDALEESG--VHNLHGRVVEIG----GLRIAGLGGsrPTPFGTPYEYTEEEIEERL--------AKLREKDVDILLTHAP 137
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 150-227 7.79e-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: 50.29  E-value: 7.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 150 LRIANIGDVHIGPFIkpADLAAAVD-IVNARNVDLLAITGDLIDDLDQLESTLDALER-SEALPVLSILGNHDKYPNEAA 227
Cdd:pfam00149   1 MRILVIGDLHLPGQL--DDLLELLKkLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERlIKYVPVYLVRGNHDFDYGECL 78
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 152-220 1.20e-07

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: 50.37  E-value: 1.20e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794475169 152 IANIGDVHIGPFIKPADLAA-AVDIVNARNVDLLAITGDLID--DLDQLESTLDALERSEALPVLSILGNHD 220
Cdd:cd07400     1 IAHISDLHFGEERKPEVLELnLLDEINALKPDLVVVTGDLTQraRPAEFEEAREFLDALEPEPVVVVPGNHD 72
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 151-339 1.94e-07

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: 50.73  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 151 RIANIGDVHIGPFIKPAD---------LAAAVDIVNARNVDLLAITGDLIDD----LDQLESTLDALER--SEALPVLSI 215
Cdd:cd00840     1 RFLHTADWHLGYPLYGLSrreedffkaFEEIVDLAIEEKVDFVLIAGDLFDSnnpsPEALKLAIEGLRRlcEAGIPVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 216 LGNHDkypneaavvaalkrrnprievlinssmqvHPRGVplRVAGVDYplaadgrhmlPRDEQDAAMHRFADLAFAKVMP 295
Cdd:cd00840    81 AGNHD-----------------------------SPARV--AIYGLPY----------LRDERLERLFEDLELRPRLLKP 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2794475169 296 GEPLVVLSH-----HPEFFPIATARGAMLTLSS-------HTHGGQVRLFGRPVIV 339
Cdd:cd00840   120 DWFNILLLHqgvdgAGPSDSERPIVPEDLLPDGfdyvalgHIHKPQIIEGGGPPIV 175
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 155-220 2.46e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 43.41  E-value: 2.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2794475169 155 IGDVHIGPFIKPADLAAAVdiVNARNVDLLAITGDLIDDLDQLESTLDALERSEAL--PVLSILGNHD 220
Cdd:cd00838     3 ISDIHGNLEALEAVLEAAL--AKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAgiPVYVVPGNHD 68
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 152-308 9.70e-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: 43.42  E-value: 9.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 152 IANIGDVHIGP-------FIKPAD-LAAAVDIVNARN--VDLLAITGDLIDD-----LDQLESTLDALerseALPVLSIL 216
Cdd:cd07402     1 IAQISDTHLFApgegallGVDTAArLAAAVAQVNALHprPDLVVVTGDLSDDgspesYERLRELLAPL----PAPVYWIP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794475169 217 GNHDKypneaaVVAALKRRNPRIEVLINSSMQVHPRGvPLRVAGVD--YPLAADGRHmlprDEQDAAMHRfADLAFAkvm 294
Cdd:cd07402    77 GNHDD------RAAMREALPEPPYDDNGPVQYVVDFG-GWRLILLDtsVPGVHHGEL----SDEQLDWLE-AALAEA--- 141

                         170
                  ....*....|....
gi 2794475169 295 PGEPLVVLSHHPEF 308
Cdd:cd07402   142 PDRPTLIFLHHPPF 155
 
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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