NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|317008614|ref|NP_001186931|]
View 

transmembrane protein with metallophosphoesterase domain [Mus musculus]

Protein Classification

metallophosphoesterase( domain architecture ID 10164616)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 206-443 2.28e-97

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: 291.49  E-value: 2.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 206 NLKIVLLSDIHLGPTVGRTKMEMFVRMVNRLEPDITVIVGDLSDSEASVLRTAVAPLGQLHSRLGTYFVTGNHEYYTSDV 285
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 286 SNWFTLLESLHVRPLHNENVKISapgdpdsagRDREWVCLAGVDDieadiLHYSGHGMDLDKALEGCSPDDATILLAHQP 365
Cdd:cd07385   81 EVWIAALEKAGITVLRNESVELS---------RDGATIGLAGSGV-----DDIGGHGEDLEKALKGLDENDPVILLAHNP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 366 LAAKRAlqARPDINLILSGHTHAGQIFPWNVGA--YLLNPFFAGLYQVGKATFVYVSPGTAYYGIPMRLGSRAEITELIL 443
Cdd:cd07385  147 DAAEEA--QRPGVDLVLSGHTHGGQIFPPNYGVlsKLGFPYDSGLYQIGGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
 
Name Accession Description Interval E-value
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 206-443 2.28e-97

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: 291.49  E-value: 2.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 206 NLKIVLLSDIHLGPTVGRTKMEMFVRMVNRLEPDITVIVGDLSDSEASVLRTAVAPLGQLHSRLGTYFVTGNHEYYTSDV 285
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 286 SNWFTLLESLHVRPLHNENVKISapgdpdsagRDREWVCLAGVDDieadiLHYSGHGMDLDKALEGCSPDDATILLAHQP 365
Cdd:cd07385   81 EVWIAALEKAGITVLRNESVELS---------RDGATIGLAGSGV-----DDIGGHGEDLEKALKGLDENDPVILLAHNP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 366 LAAKRAlqARPDINLILSGHTHAGQIFPWNVGA--YLLNPFFAGLYQVGKATFVYVSPGTAYYGIPMRLGSRAEITELIL 443
Cdd:cd07385  147 DAAEEA--QRPGVDLVLSGHTHGGQIFPPNYGVlsKLGFPYDSGLYQIGGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
167-443 2.79e-88

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 269.74  E-value: 2.79e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 167 ALAVAVTAVLSTIGLLNAAQPPVVKTVEVPIHQLPASMDNLKIVLLSDIHLGPTVGRTKMEMFVRMVNRLEPDITVIVGD 246
Cdd:COG1408    3 LALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 247 LSDSEASVLRTAVAPLGQLHSRLGTYFVTGNHEYYtSDVSNWFTLLESLHVRPLHNENVKISAPGDPdsagrdrewVCLA 326
Cdd:COG1408   83 LVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYY-AGLEELRAALEEAGVRVLRNEAVTLERGGDR---------LNLA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 327 GVDDieadilHYSGHGMDLDKALEGCSPDDATILLAHQPLAAKRALQARPDinLILSGHTHAGQIFPWNVGAYLLN---- 402
Cdd:COG1408  153 GVDD------PHAGRFPDLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVD--LQLSGHTHGGQIRLPGIGALLTPvrlg 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 317008614 403 -PFFAGLYQVGKaTFVYVSPGTAYYGIPMRLGSRAEITELIL 443
Cdd:COG1408  225 rKYVAGLYREGG-TQLYVSRGLGTSGPPVRFGCPPEITLITL 265
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 168-443 1.62e-11

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 64.49  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 168 LAVAVTAVLSTIGLLNAAQPPVVKTVEVPIHQLPASMDNLKIVLLSDIHLGPTVGRTKMEMFVRMVNRLEPDITVIVGDL 247
Cdd:PRK11340  11 AAAATIATSSGFGYMHYWEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 248 SD----SEASVLRTAVAPLGQLHSrlgTYFVTGNHEYYTSDVSNWFT--LLESLHVRPLHNENVKISAPgdpdsagrDRE 321
Cdd:PRK11340  91 VLfdmpLNFSAFSDVLSPLAECAP---TFACFGNHDRPVGTEKNHLIgeTLKSAGITVLFNQATVIATP--------NRQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 322 WVcLAGVDDIEADILHYsghgmdlDKALEGCSPddaTILLAHQPlaAKRALQARPDINLILSGHTHAGQIFPWNVGAYLL 401
Cdd:PRK11340 160 FE-LVGTGDLWAGQCKP-------PPASEANLP---RLVLAHNP--DSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFA 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 317008614 402 ----NPFFAGLYQVGKATfVYVSPGTAYYGiPMRLGSRAEITELIL 443
Cdd:PRK11340 227 pvedKRYVAGLNAFGERQ-IYTTRGVGSLY-GLRLNCRPEVTMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 207-305 6.06e-06

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: 45.28  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614  207 LKIVLLSDIHLGPTVGRTkMEMFVRMVNRLEPDITVIVGDLSDsEASVLRTAVAPLGQLHSRLGTYFVTGNHEYYTSDVS 286
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDL-LELLKKLLEEGKPDLVLHAGDLVD-RGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGECL 78

                          90
                  ....*....|....*....
gi 317008614  287 NWFTLLESLHVRPLHNENV 305
Cdd:pfam00149  79 RLYPYLGLLARPWKRFLEV 97
 
Name Accession Description Interval E-value
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 206-443 2.28e-97

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: 291.49  E-value: 2.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 206 NLKIVLLSDIHLGPTVGRTKMEMFVRMVNRLEPDITVIVGDLSDSEASVLRTAVAPLGQLHSRLGTYFVTGNHEYYTSDV 285
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 286 SNWFTLLESLHVRPLHNENVKISapgdpdsagRDREWVCLAGVDDieadiLHYSGHGMDLDKALEGCSPDDATILLAHQP 365
Cdd:cd07385   81 EVWIAALEKAGITVLRNESVELS---------RDGATIGLAGSGV-----DDIGGHGEDLEKALKGLDENDPVILLAHNP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 366 LAAKRAlqARPDINLILSGHTHAGQIFPWNVGA--YLLNPFFAGLYQVGKATFVYVSPGTAYYGIPMRLGSRAEITELIL 443
Cdd:cd07385  147 DAAEEA--QRPGVDLVLSGHTHGGQIFPPNYGVlsKLGFPYDSGLYQIGGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
167-443 2.79e-88

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 269.74  E-value: 2.79e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 167 ALAVAVTAVLSTIGLLNAAQPPVVKTVEVPIHQLPASMDNLKIVLLSDIHLGPTVGRTKMEMFVRMVNRLEPDITVIVGD 246
Cdd:COG1408    3 LALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 247 LSDSEASVLRTAVAPLGQLHSRLGTYFVTGNHEYYtSDVSNWFTLLESLHVRPLHNENVKISAPGDPdsagrdrewVCLA 326
Cdd:COG1408   83 LVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYY-AGLEELRAALEEAGVRVLRNEAVTLERGGDR---------LNLA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 327 GVDDieadilHYSGHGMDLDKALEGCSPDDATILLAHQPLAAKRALQARPDinLILSGHTHAGQIFPWNVGAYLLN---- 402
Cdd:COG1408  153 GVDD------PHAGRFPDLEKALAGVPPDAPRILLAHNPDVFDEAAAAGVD--LQLSGHTHGGQIRLPGIGALLTPvrlg 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 317008614 403 -PFFAGLYQVGKaTFVYVSPGTAYYGIPMRLGSRAEITELIL 443
Cdd:COG1408  225 rKYVAGLYREGG-TQLYVSRGLGTSGPPVRFGCPPEITLITL 265
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
207-395 2.99e-14

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 72.03  E-value: 2.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 207 LKIVLLSDIHLGPTVG---RTKMEMFVRMVNRLEPDITVIVGDLS-DSEASVLRTAVAPLGQLHSRLgtYFVTGNHEYYT 282
Cdd:COG1409    1 FRFAHISDLHLGAPDGsdtAEVLAAALADINAPRPDFVVVTGDLTdDGEPEEYAAAREILARLGVPV--YVVPGNHDIRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 283 SDVSNWFTLLeslhvrplhnenvkisapGDPDSAGRDREW----VCLAGVDDieADILHYSGHGMD-----LDKALEGcS 353
Cdd:COG1409   79 AMAEAYREYF------------------GDLPPGGLYYSFdyggVRFIGLDS--NVPGRSSGELGPeqlawLEEELAA-A 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 317008614 354 PDDATILLAHQPLA-------------AKRALQ--ARPDINLILSGHTHAGQIFPWN 395
Cdd:COG1409  138 PAKPVIVFLHHPPYstgsgsdriglrnAEELLAllARYGVDLVLSGHVHRYERTRRD 194
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
208-389 5.39e-13

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 67.73  E-value: 5.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 208 KIVLLSDIHLGptvgRTKMEMFVRMVNRLEPDITVIVGDLSD-SEASVLRTAVAPLGQLHSRlgTYFVTGNHEYYtsdvs 286
Cdd:COG2129    1 KILAVSDLHGN----FDLLEKLLELARAEDADLVILAGDLTDfGTAEEAREVLEELAALGVP--VLAVPGNHDDP----- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 287 NWFTLLESLHVRPLHNENVKI----------SAPGDPDSAGRDREWvclagvddieadilhysghgmDLDKALEGCSPDD 356
Cdd:COG2129   70 EVLDALEESGVHNLHGRVVEIgglriaglggSRPTPFGTPYEYTEE---------------------EIEERLAKLREKD 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 317008614 357 ATILLAHQP------------------LAAKRALQARPDinLILSGHTHAG 389
Cdd:COG2129  129 VDILLTHAPpygttldrvedgphvgskALRELIEEFQPK--LVLHGHIHES 177
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 168-443 1.62e-11

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 64.49  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 168 LAVAVTAVLSTIGLLNAAQPPVVKTVEVPIHQLPASMDNLKIVLLSDIHLGPTVGRTKMEMFVRMVNRLEPDITVIVGDL 247
Cdd:PRK11340  11 AAAATIATSSGFGYMHYWEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 248 SD----SEASVLRTAVAPLGQLHSrlgTYFVTGNHEYYTSDVSNWFT--LLESLHVRPLHNENVKISAPgdpdsagrDRE 321
Cdd:PRK11340  91 VLfdmpLNFSAFSDVLSPLAECAP---TFACFGNHDRPVGTEKNHLIgeTLKSAGITVLFNQATVIATP--------NRQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 322 WVcLAGVDDIEADILHYsghgmdlDKALEGCSPddaTILLAHQPlaAKRALQARPDINLILSGHTHAGQIFPWNVGAYLL 401
Cdd:PRK11340 160 FE-LVGTGDLWAGQCKP-------PPASEANLP---RLVLAHNP--DSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFA 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 317008614 402 ----NPFFAGLYQVGKATfVYVSPGTAYYGiPMRLGSRAEITELIL 443
Cdd:PRK11340 227 pvedKRYVAGLNAFGERQ-IYTTRGVGSLY-GLRLNCRPEVTMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 207-305 6.06e-06

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: 45.28  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614  207 LKIVLLSDIHLGPTVGRTkMEMFVRMVNRLEPDITVIVGDLSDsEASVLRTAVAPLGQLHSRLGTYFVTGNHEYYTSDVS 286
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDL-LELLKKLLEEGKPDLVLHAGDLVD-RGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGECL 78

                          90
                  ....*....|....*....
gi 317008614  287 NWFTLLESLHVRPLHNENV 305
Cdd:pfam00149  79 RLYPYLGLLARPWKRFLEV 97
MPP_UshA_N_like cd00845
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes ...
 207-418 4.67e-05

Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277323 [Multi-domain]  Cd Length: 255  Bit Score: 44.60  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 207 LKIVLLSDIH--LGPTVGRT-----KMEMFVRMVNRLEPD-ITVIVGDLSDSEASVLRTAVAPLGQLHSRLGTYFVT-GN 277
Cdd:cd00845    1 LTILHTNDLHghLDPHSNGGiggaaRLAGLVKQIRAENPNtLLLDAGDNFQGSPLSTLTDGEAVIDLMNALGYDAATvGN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 278 HE-YYTSDVsnwFTLLESLHVRPLHNENVKISAPGDPDSAGR---------------------DREWVCLAGVDDIEADI 335
Cdd:cd00845   81 HEfDYGLDQ---LEELLKQAKFPWLSANVYEDGTGTGEPGAKpytiitvdgvkvgviglttpdTPTVTPPEGNRGVEFPD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 336 LHYSGHGMDLDKALEGCspdDATILLAHQPLAAKRAL-QARPDINLILSGHTHAGQIFPWNV-GAYLLNPFFAGLYqVGK 413
Cdd:cd00845  158 PAEAIAEAAEELKAEGV---DVIIALSHLGIDTDERLaAAVKGIDVILGGHSHTLLEEPEVVnGTLIVQAGAYGKY-VGR 233


                 ....*
gi 317008614 414 ATFVY 418
Cdd:cd00845  234 VDLEF 238
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 209-387 5.52e-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: 44.58  E-value: 5.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 209 IVLLSDIHLGPTVGRT-----KMEMFVRMVNRL-----EPDITVIVGDLSD--SEAS--VLRTAVAPLgqlhsRLGTYFV 274
Cdd:cd07402    1 IAQISDTHLFAPGEGAllgvdTAARLAAAVAQVnalhpRPDLVVVTGDLSDdgSPESyeRLRELLAPL-----PAPVYWI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 275 TGNHEYytsdvsnwftlleslhvRPLHNEnvkiSAPGDPDSAGRDREWVC------LAGVDDIEADILH--YSGHGMD-L 345
Cdd:cd07402   76 PGNHDD-----------------RAAMRE----ALPEPPYDDNGPVQYVVdfggwrLILLDTSVPGVHHgeLSDEQLDwL 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 317008614 346 DKALEGcSPDDATILLAHQPL-----------------AAKRALQARPDINLILSGHTH 387
Cdd:cd07402  135 EAALAE-APDRPTLIFLHHPPfplgipwmdairlrnsqALFAVLARHPQVKAILCGHIH 192
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 207-290 1.09e-04

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 43.05  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 207 LKIVLLSDIHLGPTVGrTKMEMF------VRMVNRL----EPDITVIVGDLSDSEA-------SVLRTAVAPLGQlhsrL 269
Cdd:cd07383    3 FKILQFADLHFGEGEW-TCWEGCeadlktVEFIESVldeeKPDLVVLTGDLITGENtaddnatSYLDKAVSPLVE----R 77

                         90       100
                 ....*....|....*....|....*.
gi 317008614 270 GTYFVT--GNHEYY---TSDVSNWFT 290
Cdd:cd07383   78 GIPWAAtfGNHDGYdwiDPSQVEWFE 103
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
208-364 2.29e-04

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 42.59  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 208 KIVLLSDIHLGPTVGRTKMEM--------FVRMVNRLEPDITVIVGDLSDSE---ASVLRTAVAPLGQLHSR-LGTYFVT 275
Cdd:COG0420    2 RFLHTADWHLGKPLHGASRREdqlaaldrLVDLAIEEKVDAVLIAGDLFDSAnpsPEAVRLLAEALRRLSEAgIPVVLIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 276 GNHEYYtSDVSNWFTLLESLHVRPLHNENVK-ISAPGDPDsagrdrewVCLAGVDDIEADIlhYSGHGMDLDKALEGCSP 354
Cdd:COG0420   82 GNHDSP-SRLSAGSPLLENLGVHVFGSVEPEpVELEDGLG--------VAVYGLPYLRPSD--EEALRDLLERLPRALDP 150

                        170
                 ....*....|
gi 317008614 355 DDATILLAHQ 364
Cdd:COG0420  151 GGPNILLLHG 160
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 209-249 2.38e-03

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: 38.04  E-value: 2.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 317008614 209 IVLLSDIHLGPTVGRTKME-MFVRMVNRLEPDITVIVGDLSD 249
Cdd:cd07400    1 IAHISDLHFGEERKPEVLElNLLDEINALKPDLVVVTGDLTQ 42
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 210-279 8.64e-03

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: 36.48  E-value: 8.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317008614 210 VLLSDIHLGPTVGRTKMEMFVrmVNRLEPDITVIVGDLSDSEASVLRTAVAPLGQLHSRLGTYFVTGNHE 279
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAAL--AKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHD 68
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH