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Conserved domains on  [gi|1822647201|ref|WP_165878083|]
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MULTISPECIES: metallophosphoesterase [unclassified Micromonospora]

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];
147-412 5.18e-94

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


:

Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 283.22  E-value: 5.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 147 AAIFAGLTATGVTGYGVRNAMGPPRLDRVRIPLAKLPRGMDGLRIATVSDIHLGPLRGRAHTERIVAMINRLDADLVAVV 226
Cdd:COG1408     1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 227 GDLVDGSVAELGEAAAPLRGLRSRYGSFFVTGNHEYYSGVEEWVPEVDRLGLRVLQNTRQEIRTPGGVLDLAGVNDVSAA 306
Cdd:COG1408    81 GDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYYAGLEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVDDPHAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 307 GTGlaapaDYAAALGDRDPGRPVVLLAHQPVAAVEAAKFGVDLQLSGHTHGGQIVPFNL-----LVNLEQPVVSGLGEVD 381
Cdd:COG1408   161 RFP-----DLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIgalltPVRLGRKYVAGLYREG 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1822647201 382 GTKVYVTNGAGFWGPPVRVGADPQITLVELR 412
Cdd:COG1408   236 GTQLYVSRGLGTSGPPVRFGCPPEITLITLK 266
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
147-412 5.18e-94

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 283.22  E-value: 5.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 147 AAIFAGLTATGVTGYGVRNAMGPPRLDRVRIPLAKLPRGMDGLRIATVSDIHLGPLRGRAHTERIVAMINRLDADLVAVV 226
Cdd:COG1408     1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 227 GDLVDGSVAELGEAAAPLRGLRSRYGSFFVTGNHEYYSGVEEWVPEVDRLGLRVLQNTRQEIRTPGGVLDLAGVNDVSAA 306
Cdd:COG1408    81 GDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYYAGLEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVDDPHAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 307 GTGlaapaDYAAALGDRDPGRPVVLLAHQPVAAVEAAKFGVDLQLSGHTHGGQIVPFNL-----LVNLEQPVVSGLGEVD 381
Cdd:COG1408   161 RFP-----DLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIgalltPVRLGRKYVAGLYREG 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1822647201 382 GTKVYVTNGAGFWGPPVRVGADPQITLVELR 412
Cdd:COG1408   236 GTQLYVSRGLGTSGPPVRFGCPPEITLITLK 266
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 188-411 2.59e-70

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: 221.00  E-value: 2.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 188 GLRIATVSDIHLGPLRGRAHTERIVAMINRLDADLVAVVGDLVDGSVAELGEAAAPLRGLRSRYGSFFVTGNHEYYSG-V 266
Cdd:cd07385     1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGdV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 267 EEWVPEVDRLGLRVLQNTRQEIRTPGGVLDLAGVNDVSAAGTGLaapaDYAAALGDRDPGRPVVLLAHQPVAAVEAAKFG 346
Cdd:cd07385    81 EVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGE----DLEKALKGLDENDPVILLAHNPDAAEEAQRPG 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822647201 347 VDLQLSGHTHGGQIVPFNLLVN--LEQPVVSGLGEV-DGTKVYVTNGAGFWGPPVRVGADPQITLVEL 411
Cdd:cd07385   157 VDLVLSGHTHGGQIFPPNYGVLskLGFPYDSGLYQIgGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 139-411 1.01e-15

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 76.81  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 139 RRLLLARGAAIFAGltatgvTGYGVRNAMGPPRLDRVRIPLAKLPRGMDGLRIATVSDIHLGPLRGRAHTERIVAMINRL 218
Cdd:PRK11340    6 RRLLQAAAATIATS------SGFGYMHYWEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 219 DADLVAVVGDLVDGS-VAELGEAAAPLRGLRSRYGSFFVTGNHEYYSGVEEwVPEVDRL----GLRVLQNTRQEIRTPGG 293
Cdd:PRK11340   80 KPDLILLGGDYVLFDmPLNFSAFSDVLSPLAECAPTFACFGNHDRPVGTEK-NHLIGETlksaGITVLFNQATVIATPNR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 294 VLDLAGVNDVSAagtglaapadyaaalGDRDPGR------PVVLLAHQPVAAVEAAKFGVDLQLSGHTHGGQI-VPF--- 363
Cdd:PRK11340  159 QFELVGTGDLWA---------------GQCKPPPaseanlPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLrVPLvge 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1822647201 364 NLLVNLEQPVVSGLGEVDGTKVYVTNGAGFWGpPVRVGADPQITLVEL 411
Cdd:PRK11340  224 PFAPVEDKRYVAGLNAFGERQIYTTRGVGSLY-GLRLNCRPEVTMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 189-263 3.05e-05

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: 42.97  E-value: 3.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822647201 189 LRIATVSDIHLGPlrGRAHTERIVAMINR-LDADLVAVVGDLVDGSVaeLGEAAAPLRGLRSRYGSFFVT-GNHEYY 263
Cdd:pfam00149   1 MRILVIGDLHLPG--QLDDLLELLKKLLEeGKPDLVLHAGDLVDRGP--PSEEVLELLERLIKYVPVYLVrGNHDFD 73
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
147-412 5.18e-94

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 283.22  E-value: 5.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 147 AAIFAGLTATGVTGYGVRNAMGPPRLDRVRIPLAKLPRGMDGLRIATVSDIHLGPLRGRAHTERIVAMINRLDADLVAVV 226
Cdd:COG1408     1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 227 GDLVDGSVAELGEAAAPLRGLRSRYGSFFVTGNHEYYSGVEEWVPEVDRLGLRVLQNTRQEIRTPGGVLDLAGVNDVSAA 306
Cdd:COG1408    81 GDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYYAGLEELRAALEEAGVRVLRNEAVTLERGGDRLNLAGVDDPHAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 307 GTGlaapaDYAAALGDRDPGRPVVLLAHQPVAAVEAAKFGVDLQLSGHTHGGQIVPFNL-----LVNLEQPVVSGLGEVD 381
Cdd:COG1408   161 RFP-----DLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIgalltPVRLGRKYVAGLYREG 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1822647201 382 GTKVYVTNGAGFWGPPVRVGADPQITLVELR 412
Cdd:COG1408   236 GTQLYVSRGLGTSGPPVRFGCPPEITLITLK 266
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 188-411 2.59e-70

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: 221.00  E-value: 2.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 188 GLRIATVSDIHLGPLRGRAHTERIVAMINRLDADLVAVVGDLVDGSVAELGEAAAPLRGLRSRYGSFFVTGNHEYYSG-V 266
Cdd:cd07385     1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGdV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 267 EEWVPEVDRLGLRVLQNTRQEIRTPGGVLDLAGVNDVSAAGTGLaapaDYAAALGDRDPGRPVVLLAHQPVAAVEAAKFG 346
Cdd:cd07385    81 EVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGE----DLEKALKGLDENDPVILLAHNPDAAEEAQRPG 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822647201 347 VDLQLSGHTHGGQIVPFNLLVN--LEQPVVSGLGEV-DGTKVYVTNGAGFWGPPVRVGADPQITLVEL 411
Cdd:cd07385   157 VDLVLSGHTHGGQIFPPNYGVLskLGFPYDSGLYQIgGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 139-411 1.01e-15

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 76.81  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 139 RRLLLARGAAIFAGltatgvTGYGVRNAMGPPRLDRVRIPLAKLPRGMDGLRIATVSDIHLGPLRGRAHTERIVAMINRL 218
Cdd:PRK11340    6 RRLLQAAAATIATS------SGFGYMHYWEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 219 DADLVAVVGDLVDGS-VAELGEAAAPLRGLRSRYGSFFVTGNHEYYSGVEEwVPEVDRL----GLRVLQNTRQEIRTPGG 293
Cdd:PRK11340   80 KPDLILLGGDYVLFDmPLNFSAFSDVLSPLAECAPTFACFGNHDRPVGTEK-NHLIGETlksaGITVLFNQATVIATPNR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 294 VLDLAGVNDVSAagtglaapadyaaalGDRDPGR------PVVLLAHQPVAAVEAAKFGVDLQLSGHTHGGQI-VPF--- 363
Cdd:PRK11340  159 QFELVGTGDLWA---------------GQCKPPPaseanlPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLrVPLvge 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1822647201 364 NLLVNLEQPVVSGLGEVDGTKVYVTNGAGFWGpPVRVGADPQITLVEL 411
Cdd:PRK11340  224 PFAPVEDKRYVAGLNAFGERQIYTTRGVGSLY-GLRLNCRPEVTMLEL 270
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
189-356 3.10e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 74.73  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 189 LRIATVSDIHLGPLRG---RAHTERIVAMINRLDADLVAVVGDLV-DGSVAELGEAAAPLRGLRSRYgsFFVTGNHEYYS 264
Cdd:COG1409     1 FRFAHISDLHLGAPDGsdtAEVLAAALADINAPRPDFVVVTGDLTdDGEPEEYAAAREILARLGVPV--YVVPGNHDIRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 265 GVEEWVPEVdrLGLRVLQNTRQEIRTPGgvLDLAGVNDVSAAGTGLAAPADYAAALGD---RDPGRPVVLLAHQPVAAVE 341
Cdd:COG1409    79 AMAEAYREY--FGDLPPGGLYYSFDYGG--VRFIGLDSNVPGRSSGELGPEQLAWLEEelaAAPAKPVIVFLHHPPYSTG 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1822647201 342 A-----------------AKFGVDLQLSGHTH 356
Cdd:COG1409   155 SgsdriglrnaeellallARYGVDLVLSGHVH 186
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
190-358 5.10e-10

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 58.87  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 190 RIATVSDIHLGplrgRAHTERIVAMINRLDADLVAVVGDLVD-GSVAELGEAAAPLRGLRSRYgsFFVTGNHEYYsgveE 268
Cdd:COG2129     1 KILAVSDLHGN----FDLLEKLLELARAEDADLVILAGDLTDfGTAEEAREVLEELAALGVPV--LAVPGNHDDP----E 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 269 WVPEVDRLGLRVLQNTRQEIrtpGGVLdLAGVNDVSAA---GTGLAAPADYAAALGDRDPGRPVVLLAHQPV-------- 337
Cdd:COG2129    71 VLDALEESGVHNLHGRVVEI---GGLR-IAGLGGSRPTpfgTPYEYTEEEIEERLAKLREKDVDILLTHAPPygttldrv 146

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1822647201 338 --------AAVEAA--KFGVDLQLSGHTHGG 358
Cdd:COG2129   147 edgphvgsKALRELieEFQPKLVLHGHIHES 177
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 191-260 1.50e-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: 1.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822647201 191 IATVSDIHLGPLRGRAHTER-IVAMINRLDADLVAVVGDLVD-GSVAELGEAAAPLRGLRSrYGSFFVTGNH 260
Cdd:cd07400     1 IAHISDLHFGEERKPEVLELnLLDEINALKPDLVVVTGDLTQrARPAEFEEAREFLDALEP-EPVVVVPGNH 71
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
190-362 6.56e-07

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 50.30  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 190 RIATVSDIHLG-PLRGRAHTE-------RIVAMINRLDADLVAVVGDLVDG---SVAELGEAAAPLRGLRSRYGSFFVT- 257
Cdd:COG0420     2 RFLHTADWHLGkPLHGASRREdqlaaldRLVDLAIEEKVDAVLIAGDLFDSanpSPEAVRLLAEALRRLSEAGIPVVLIa 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 258 GNHEYYSGVEEWVPEVDRLGLRVLQNTRQEIRT--PGGVLDLAGVNDVSAAGTGlAAPADYAAALGDRDPGRPVVLLAHQ 335
Cdd:COG0420    82 GNHDSPSRLSAGSPLLENLGVHVFGSVEPEPVEleDGLGVAVYGLPYLRPSDEE-ALRDLLERLPRALDPGGPNILLLHG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1822647201 336 --------------PVAAVEAAKFGVDLQLSGHTHGGQIVP 362
Cdd:COG0420   161 fvagasgsrdiyvaPVPLSALPAAGFDYVALGHIHRPQVLG 201
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 189-263 3.05e-05

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: 42.97  E-value: 3.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822647201 189 LRIATVSDIHLGPlrGRAHTERIVAMINR-LDADLVAVVGDLVDGSVaeLGEAAAPLRGLRSRYGSFFVT-GNHEYY 263
Cdd:pfam00149   1 MRILVIGDLHLPG--QLDDLLELLKKLLEeGKPDLVLHAGDLVDRGP--PSEEVLELLERLIKYVPVYLVrGNHDFD 73
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 191-260 9.46e-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: 9.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 191 IATVSDIHLGP--------LRGRAHTERIVAMINRL--DADLVAVVGDLVD-GSVAELGEAAAPLRGLRSRYgsFFVTGN 259
Cdd:cd07402     1 IAQISDTHLFApgegallgVDTAARLAAAVAQVNALhpRPDLVVVTGDLSDdGSPESYERLRELLAPLPAPV--YWIPGN 78


                  .
gi 1822647201 260 H 260
Cdd:cd07402    79 H 79
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 194-261 8.53e-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: 39.17  E-value: 8.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822647201 194 VSDIHLGPLRGRAHTERIVamINRLDADLVAVVGDLVDGSVAELGEAAAPLRGLRSRYGSFFVTGNHE 261
Cdd:cd00838     3 ISDIHGNLEALEAVLEAAL--AKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHD 68
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 190-266 3.66e-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: 38.40  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 190 RIATVSDIHLG-PLRGRAHT--------ERIVAMINRLDADLVAVVGDLVDG---SVAELGEAAAPLRGLRSRYGSFFVT 257
Cdd:cd00840     1 RFLHTADWHLGyPLYGLSRReedffkafEEIVDLAIEEKVDFVLIAGDLFDSnnpSPEALKLAIEGLRRLCEAGIPVFVI 80

                          90
                  ....*....|
gi 1822647201 258 -GNHEYYSGV 266
Cdd:cd00840    81 aGNHDSPARV 90
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 194-265 5.70e-03

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: 38.11  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822647201 194 VSDIHLGPLRGRAHTERIVAMINRLD-ADLVAVVGDLVDGSVAELG-------EAAAPLRGLRSRyGS--FFVTGNHEYY 263
Cdd:cd07398     3 ISDLHLGLRGCRADRLLDFLLVEELDeADALYLLGDIFDLWIGDDSvvwpgahRALARLLRLADR-GTevIYVPGNHDFL 81


                  ..
gi 1822647201 264 SG 265
Cdd:cd07398    82 LG 83
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
190-263 8.23e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 37.20  E-value: 8.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822647201 190 RIATVSDIHlgplrGRAH-TERIVAMINRLDADLVAVVGDLVDGSVAELgEAAAPLRGLRSRygsfFVTGNHEYY 263
Cdd:COG0622     1 KIAVISDTH-----GNLPaLEAVLEDLEREGVDLIVHLGDLVGYGPDPP-EVLDLLRELPIV----AVRGNHDGA 65
 
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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