NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6323393|ref|NP_013465|]
View 

phosphoprotein phosphatase [Saccharomyces cerevisiae S288C]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10164588)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc); similar to Kluyveromyces lactis protein SIA1 that may be involved in the activation of the plasma membrane proton-ATPase by glucose; may be inactive

CATH:  3.60.21.10
Gene Ontology:  GO:0046872
PubMed:  25837850|8003970
SCOP:  3001067

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_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 246-518 9.99e-65

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: 210.23  E-value: 9.99e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  246 GKFKIVQLADLHLGVGESECIdeypkhEACKADPKTETFVQQVLDIEKPQLVVFTGDQIMGDRSI-QDSETVLLKAVAPV 324
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCW------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTAdDNATSYLDKAVSPL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  325 IARKIPWAMVWGNHDdegsltrwqlseiasvlpyslfkfsphdthdntfgvgnyiyqifsnndtevpvgtlyfldshkys 404
Cdd:cd07383  75 VERGIPWAATFGNHD----------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  405 tvgkiypGYDWIKESQWKYIEDYHDVNLKF--KTGLSMAFFHIPLPEYLNIESkthpgEKNPLIGMYKEGVTAPKYNSEG 482
Cdd:cd07383  90 -------GYDWIDPSQVEWFESTSAALKKKygKNIPSLAFFHIPLPEYREVWN-----EKGKLGGINREKVCCQKTNSGF 157

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6323393  483 ITTL-DRLSVDVVSCGHDHCNDYCLRDdstPNKIWLC 518
Cdd:cd07383 158 FKALvKRGDVKAVFCGHDHGNDFCGRW---KNGIWLC 191
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 246-518 9.99e-65

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: 210.23  E-value: 9.99e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  246 GKFKIVQLADLHLGVGESECIdeypkhEACKADPKTETFVQQVLDIEKPQLVVFTGDQIMGDRSI-QDSETVLLKAVAPV 324
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCW------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTAdDNATSYLDKAVSPL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  325 IARKIPWAMVWGNHDdegsltrwqlseiasvlpyslfkfsphdthdntfgvgnyiyqifsnndtevpvgtlyfldshkys 404
Cdd:cd07383  75 VERGIPWAATFGNHD----------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  405 tvgkiypGYDWIKESQWKYIEDYHDVNLKF--KTGLSMAFFHIPLPEYLNIESkthpgEKNPLIGMYKEGVTAPKYNSEG 482
Cdd:cd07383  90 -------GYDWIDPSQVEWFESTSAALKKKygKNIPSLAFFHIPLPEYREVWN-----EKGKLGGINREKVCCQKTNSGF 157

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6323393  483 ITTL-DRLSVDVVSCGHDHCNDYCLRDdstPNKIWLC 518
Cdd:cd07383 158 FKALvKRGDVKAVFCGHDHGNDFCGRW---KNGIWLC 191
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
248-508 4.42e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.09  E-value: 4.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  248 FKIVQLADLHLGVGESEcideypkheacKADPKTETFVQQVLDiEKPQLVVFTGDqimgdrSIQDSETVLLKAVAPVIAR 327
Cdd:COG1409   1 FRFAHISDLHLGAPDGS-----------DTAEVLAAALADINA-PRPDFVVVTGD------LTDDGEPEEYAAAREILAR 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  328 -KIPWAMVWGNHDDEGSLTRWQlseiasvlpYSLFKFSPHDTHDNTFGVGNYiyqifsnndtevpvgTLYFLDSHKYSTV 406
Cdd:COG1409  63 lGVPVYVVPGNHDIRAAMAEAY---------REYFGDLPPGGLYYSFDYGGV---------------RFIGLDSNVPGRS 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  407 gkiypgYDWIKESQWKYIEDyhdvNL-KFKTGLSMAFFHIPLPeylnieSKTHPGEKNPLIGmykegvtapkyNSEGITT 485
Cdd:COG1409 119 ------SGELGPEQLAWLEE----ELaAAPAKPVIVFLHHPPY------STGSGSDRIGLRN-----------AEELLAL 171

                       250       260
                ....*....|....*....|...
gi 6323393  486 LDRLSVDVVSCGHDHCNDYCLRD 508
Cdd:COG1409 172 LARYGVDLVLSGHVHRYERTRRD 194
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 248-340 1.72e-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: 44.13  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393    248 FKIVQLADLHLGVGesecideypkheackaDPKTETFVQQVLDIEKPQLVVFTGDQImgDRSIQDSETVLLkaVAPVIAR 327
Cdd:pfam00149   1 MRILVIGDLHLPGQ----------------LDDLLELLKKLLEEGKPDLVLHAGDLV--DRGPPSEEVLEL--LERLIKY 60

                          90
                  ....*....|...
gi 6323393    328 kIPWAMVWGNHDD 340
Cdd:pfam00149  61 -VPVYLVRGNHDF 72
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 246-518 9.99e-65

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: 210.23  E-value: 9.99e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  246 GKFKIVQLADLHLGVGESECIdeypkhEACKADPKTETFVQQVLDIEKPQLVVFTGDQIMGDRSI-QDSETVLLKAVAPV 324
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCW------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTAdDNATSYLDKAVSPL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  325 IARKIPWAMVWGNHDdegsltrwqlseiasvlpyslfkfsphdthdntfgvgnyiyqifsnndtevpvgtlyfldshkys 404
Cdd:cd07383  75 VERGIPWAATFGNHD----------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  405 tvgkiypGYDWIKESQWKYIEDYHDVNLKF--KTGLSMAFFHIPLPEYLNIESkthpgEKNPLIGMYKEGVTAPKYNSEG 482
Cdd:cd07383  90 -------GYDWIDPSQVEWFESTSAALKKKygKNIPSLAFFHIPLPEYREVWN-----EKGKLGGINREKVCCQKTNSGF 157

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6323393  483 ITTL-DRLSVDVVSCGHDHCNDYCLRDdstPNKIWLC 518
Cdd:cd07383 158 FKALvKRGDVKAVFCGHDHGNDFCGRW---KNGIWLC 191
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
248-508 4.42e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.09  E-value: 4.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  248 FKIVQLADLHLGVGESEcideypkheacKADPKTETFVQQVLDiEKPQLVVFTGDqimgdrSIQDSETVLLKAVAPVIAR 327
Cdd:COG1409   1 FRFAHISDLHLGAPDGS-----------DTAEVLAAALADINA-PRPDFVVVTGD------LTDDGEPEEYAAAREILAR 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  328 -KIPWAMVWGNHDDEGSLTRWQlseiasvlpYSLFKFSPHDTHDNTFGVGNYiyqifsnndtevpvgTLYFLDSHKYSTV 406
Cdd:COG1409  63 lGVPVYVVPGNHDIRAAMAEAY---------REYFGDLPPGGLYYSFDYGGV---------------RFIGLDSNVPGRS 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  407 gkiypgYDWIKESQWKYIEDyhdvNL-KFKTGLSMAFFHIPLPeylnieSKTHPGEKNPLIGmykegvtapkyNSEGITT 485
Cdd:COG1409 119 ------SGELGPEQLAWLEE----ELaAAPAKPVIVFLHHPPY------STGSGSDRIGLRN-----------AEELLAL 171

                       250       260
                ....*....|....*....|...
gi 6323393  486 LDRLSVDVVSCGHDHCNDYCLRD 508
Cdd:COG1409 172 LARYGVDLVLSGHVHRYERTRRD 194
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
248-347 4.88e-08

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 54.42  E-value: 4.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  248 FKIVQLADLHLGVGESEcideypkheackadPKTETFVQQVLDiEKPQLVVFTGDQImgDRSIQDSETVL-----LKAVA 322
Cdd:COG1408  43 LRIVQLSDLHLGPFIGG--------------ERLERLVEKINA-LKPDLVVLTGDLV--DGSVAELEALLellkkLKAPL 105

                        90       100
                ....*....|....*....|....*
gi 6323393  323 PVIArkipwamVWGNHDDEGSLTRW 347
Cdd:COG1408 106 GVYA-------VLGNHDYYAGLEEL 123
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 248-354 7.03e-08

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: 53.44  E-value: 7.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  248 FKIVQLADLHLGvgesecidEYPKheackadpktETFVQQVLDI---EKPQLVVFTGDQIMGDRS-IQDSETVL--LKAV 321
Cdd:cd07385   2 LRIVQLSDIHLG--------PFVG----------RTRLQKVVRKvneLNPDLIVITGDLVDGDVSvLRLLASPLskLKAP 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 6323393  322 APVIArkipwamVWGNHDDEGSLTRWQLSEIAS 354
Cdd:cd07385  64 LGVYF-------VLGNHDYYSGDVEVWIAALEK 89
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
248-348 4.34e-06

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 48.37  E-value: 4.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  248 FKIVQLADLHLGvgesecideYPKH-----EAckadpkTETFVQQVLDI---EKPQLVVFTGDqIMgDRSIQDSETVLL- 318
Cdd:COG0420   1 MRFLHTADWHLG---------KPLHgasrrED------QLAALDRLVDLaieEKVDAVLIAGD-LF-DSANPSPEAVRLl 63

                        90       100       110
                ....*....|....*....|....*....|.
gi 6323393  319 -KAVAPVIARKIPWAMVWGNHDDEGSLTRWQ 348
Cdd:COG0420  64 aEALRRLSEAGIPVVLIAGNHDSPSRLSAGS 94
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 248-340 1.72e-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: 44.13  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393    248 FKIVQLADLHLGVGesecideypkheackaDPKTETFVQQVLDIEKPQLVVFTGDQImgDRSIQDSETVLLkaVAPVIAR 327
Cdd:pfam00149   1 MRILVIGDLHLPGQ----------------LDDLLELLKKLLEEGKPDLVLHAGDLV--DRGPPSEEVLEL--LERLIKY 60

                          90
                  ....*....|...
gi 6323393    328 kIPWAMVWGNHDD 340
Cdd:pfam00149  61 -VPVYLVRGNHDF 72
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 251-339 9.20e-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: 42.64  E-value: 9.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  251 VQLADLHLGVGESECIDEypkheackadpktetfvQQVLDIEKPQLVVFTGDQIMGDRSIQDSEtvllKAVAPVIARKIP 330
Cdd:cd00838   1 LVISDIHGNLEALEAVLE-----------------AALAKAEKPDLVICLGDLVDYGPDPEEVE----LKALRLLLAGIP 59


                ....*....
gi 6323393  331 WAMVWGNHD 339
Cdd:cd00838  60 VYVVPGNHD 68
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 249-340 7.19e-04

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: 40.72  E-value: 7.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323393  249 KIVQLADLHLGVGESEcIDEYpkHEACKAdpktetFVQQVLDI---EKPQLVVFTGDqIMgDRSIQDSETV--LLKAVAP 323
Cdd:cd00840   1 RFLHTADWHLGYPLYG-LSRR--EEDFFK------AFEEIVDLaieEKVDFVLIAGD-LF-DSNNPSPEALklAIEGLRR 69

                        90
                ....*....|....*..
gi 6323393  324 VIARKIPWAMVWGNHDD 340
Cdd:cd00840  70 LCEAGIPVFVIAGNHDS 86
 
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