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Conserved domains on  [gi|15242042|ref|NP_200524|]
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purple acid phosphatase 28 [Arabidopsis thaliana]

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

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List of domain hits

 Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 56-341 3.38e-76

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: 234.88  E-value: 3.38e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  56 GTFKILQVADMHFGMGMITRCrdvldseFEYCSDLNTTRFLRRMIESERPDLIAFTGDNIFGSSTTD--AAESLLEAIGP 133
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCW-------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 134 AIEYGIPWAAVLGNHDhestlnrlelmtflslmdfsvsqinplvedetkgdtmrlidgfgnyrvrvygapgsvlanstvf 213
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 214 dlfffdsgdreivqgkrTYGWIKESQLRWLQDTSIQGHSQrIHVNPPALAFFHIPILEVRELWYTPF--IGQFQEGVACS 291
Cdd:cd07383  90 -----------------GYDWIDPSQVEWFESTSAALKKK-YGKNIPSLAFFHIPLPEYREVWNEKGklGGINREKVCCQ 151

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242042 292 IVQSGVLQTFVSMGNVKAAFMGHDHVNDFCG-TLKGVWFCYGGGFGYHAYG 341
Cdd:cd07383 152 KTNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTGYGGYG 202
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 56-341 3.38e-76

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: 234.88  E-value: 3.38e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  56 GTFKILQVADMHFGMGMITRCrdvldseFEYCSDLNTTRFLRRMIESERPDLIAFTGDNIFGSSTTD--AAESLLEAIGP 133
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCW-------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 134 AIEYGIPWAAVLGNHDhestlnrlelmtflslmdfsvsqinplvedetkgdtmrlidgfgnyrvrvygapgsvlanstvf 213
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 214 dlfffdsgdreivqgkrTYGWIKESQLRWLQDTSIQGHSQrIHVNPPALAFFHIPILEVRELWYTPF--IGQFQEGVACS 291
Cdd:cd07383  90 -----------------GYDWIDPSQVEWFESTSAALKKK-YGKNIPSLAFFHIPLPEYREVWNEKGklGGINREKVCCQ 151

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242042 292 IVQSGVLQTFVSMGNVKAAFMGHDHVNDFCG-TLKGVWFCYGGGFGYHAYG 341
Cdd:cd07383 152 KTNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTGYGGYG 202
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
58-353 4.02e-18

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 82.82  E-value: 4.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  58 FKILQVADMHFGMGMITRCRDVLDSefeycsdlnttrfLRRMIESERPDLIAFTGDNifgssTTDAAESLLEAIGPAI-E 136
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLAA-------------ALADINAPRPDFVVVTGDL-----TDDGEPEEYAAAREILaR 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 137 YGIPWAAVLGNHDHESTLNRLELmtflslmdfsvsqinplvedetkgDTMRLIDGFGNYRVRVYGApgsvlanstvFDLF 216
Cdd:COG1409  63 LGVPVYVVPGNHDIRAAMAEAYR------------------------EYFGDLPPGGLYYSFDYGG----------VRFI 108

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 217 FFDSGDReivqgKRTYGWIKESQLRWLQDTsIQGHSQRihvnpPALAFFHIPILEVRELWYTPFIGQFQEgvacsivqsg 296
Cdd:COG1409 109 GLDSNVP-----GRSSGELGPEQLAWLEEE-LAAAPAK-----PVIVFLHHPPYSTGSGSDRIGLRNAEE---------- 167

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242042 297 vLQTFVSMGNVKAAFMGHDHVNDFcGTLKGVWFCYGGGFGYHAYGRPNWhrraRVIE 353
Cdd:COG1409 168 -LLALLARYGVDLVLSGHVHRYER-TRRDGVPYIVAGSTGGQVRLPPGY----RVIE 218
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 58-149 6.63e-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: 41.82  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042    58 FKILQVADMHfgmgmitrcrdvLDSEFEYcsdlnTTRFLRRMIESERPDLIAFTGDNIFGSSTTDAAESLLEAIGPaiey 137
Cdd:pfam00149   1 MRILVIGDLH------------LPGQLDD-----LLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIK---- 59

                          90
                  ....*....|..
gi 15242042   138 GIPWAAVLGNHD 149
Cdd:pfam00149  60 YVPVYLVRGNHD 71
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 56-341 3.38e-76

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: 234.88  E-value: 3.38e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  56 GTFKILQVADMHFGMGMITRCrdvldseFEYCSDLNTTRFLRRMIESERPDLIAFTGDNIFGSSTTD--AAESLLEAIGP 133
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCW-------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 134 AIEYGIPWAAVLGNHDhestlnrlelmtflslmdfsvsqinplvedetkgdtmrlidgfgnyrvrvygapgsvlanstvf 213
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 214 dlfffdsgdreivqgkrTYGWIKESQLRWLQDTSIQGHSQrIHVNPPALAFFHIPILEVRELWYTPF--IGQFQEGVACS 291
Cdd:cd07383  90 -----------------GYDWIDPSQVEWFESTSAALKKK-YGKNIPSLAFFHIPLPEYREVWNEKGklGGINREKVCCQ 151

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242042 292 IVQSGVLQTFVSMGNVKAAFMGHDHVNDFCG-TLKGVWFCYGGGFGYHAYG 341
Cdd:cd07383 152 KTNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTGYGGYG 202
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
58-353 4.02e-18

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 82.82  E-value: 4.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  58 FKILQVADMHFGMGMITRCRDVLDSefeycsdlnttrfLRRMIESERPDLIAFTGDNifgssTTDAAESLLEAIGPAI-E 136
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLAA-------------ALADINAPRPDFVVVTGDL-----TDDGEPEEYAAAREILaR 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 137 YGIPWAAVLGNHDHESTLNRLELmtflslmdfsvsqinplvedetkgDTMRLIDGFGNYRVRVYGApgsvlanstvFDLF 216
Cdd:COG1409  63 LGVPVYVVPGNHDIRAAMAEAYR------------------------EYFGDLPPGGLYYSFDYGG----------VRFI 108

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042 217 FFDSGDReivqgKRTYGWIKESQLRWLQDTsIQGHSQRihvnpPALAFFHIPILEVRELWYTPFIGQFQEgvacsivqsg 296
Cdd:COG1409 109 GLDSNVP-----GRSSGELGPEQLAWLEEE-LAAAPAK-----PVIVFLHHPPYSTGSGSDRIGLRNAEE---------- 167

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242042 297 vLQTFVSMGNVKAAFMGHDHVNDFcGTLKGVWFCYGGGFGYHAYGRPNWhrraRVIE 353
Cdd:COG1409 168 -LLALLARYGVDLVLSGHVHRYER-TRRDGVPYIVAGSTGGQVRLPPGY----RVIE 218
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
27-158 4.63e-13

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 68.67  E-value: 4.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  27 SLISHKLHINYNKIRLKR----SPNLPLRFRDdgtFKILQVADMHFGMGMITRcrdvldsefeycsdlnttrFLRRMIE- 101
Cdd:COG1408  11 ALLAYGLYIEPRRLRVRRytvpIPKLPPAFDG---LRIVQLSDLHLGPFIGGE-------------------RLERLVEk 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242042 102 --SERPDLIAFTGDNIfgSSTTDAAESLLEAIGP--AIeYGIpwAAVLGNHDHESTLNRLE 158
Cdd:COG1408  69 inALKPDLVVLTGDLV--DGSVAELEALLELLKKlkAP-LGV--YAVLGNHDYYAGLEELR 124
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
58-203 3.29e-08

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 54.15  E-value: 3.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  58 FKILQVADMHFGMgmiTRCRDVLDSEFEycsdlnttRFLRRMIE---SERPDLIAFTGDnIFGSST--TDAAESLLEAIG 132
Cdd:COG0420   1 MRFLHTADWHLGK---PLHGASRREDQL--------AALDRLVDlaiEEKVDAVLIAGD-LFDSANpsPEAVRLLAEALR 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242042 133 PAIEYGIPWAAVLGNHDHESTLNRlelmtFLSLMDfsvsqiNPLVE--DETKGDTMRLIDGFGnyrVRVYGAP 203
Cdd:COG0420  69 RLSEAGIPVVLIAGNHDSPSRLSA-----GSPLLE------NLGVHvfGSVEPEPVELEDGLG---VAVYGLP 127
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 58-156 7.20e-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: 52.67  E-value: 7.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  58 FKILQVADMHFGMgmitrcrdVLDSEFeycsdlntTRFLRRMIESERPDLIAFTGDNIFGSstTDAAESLLEAIGPAI-E 136
Cdd:cd07385   2 LRIVQLSDIHLGP--------FVGRTR--------LQKVVRKVNELNPDLIVITGDLVDGD--VSVLRLLASPLSKLKaP 63

                        90       100
                ....*....|....*....|
gi 15242042 137 YGIpwAAVLGNHDHESTLNR 156
Cdd:cd07385  64 LGV--YFVLGNHDYYSGDVE 81
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
59-158 7.14e-06

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 46.55  E-value: 7.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  59 KILQVADMHFGMGMITRcrdvldsefeycsdlnttrfLRRMIESERPDLIAFTGDnIFGSSTTDAAESLLEAIGpaiEYG 138
Cdd:COG2129   1 KILAVSDLHGNFDLLEK--------------------LLELARAEDADLVILAGD-LTDFGTAEEAREVLEELA---ALG 56

                        90       100
                ....*....|....*....|
gi 15242042 139 IPWAAVLGNHDHESTLNRLE 158
Cdd:COG2129  57 VPVLAVPGNHDDPEVLDALE 76
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 58-149 6.63e-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: 41.82  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042    58 FKILQVADMHfgmgmitrcrdvLDSEFEYcsdlnTTRFLRRMIESERPDLIAFTGDNIFGSSTTDAAESLLEAIGPaiey 137
Cdd:pfam00149   1 MRILVIGDLH------------LPGQLDD-----LLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIK---- 59

                          90
                  ....*....|..
gi 15242042   138 GIPWAAVLGNHD 149
Cdd:pfam00149  60 YVPVYLVRGNHD 71
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 100-149 2.22e-04

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 40.71  E-value: 2.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15242042 100 IESERPDLIAFTGDNIFGSSTTDAAESLLEAigpAIEYGIPWAAVLGNHD 149
Cdd:cd00838  22 AKAEKPDLVICLGDLVDYGPDPEEVELKALR---LLLAGIPVYVVPGNHD 68
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 91-150 2.68e-03

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 39.23  E-value: 2.68e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242042  91 NTTRFLRRMIESERPDLIAFTGDNIFGS---STTDAA-ESLLEAIGPAIEYGIPWAAVLGNHDH 150
Cdd:cd07378  23 LVAKQMAKVASKLGIDFILSLGDNFYDDgvkDVDDPRfQETFEDVYSAPSLQVPWYLVLGNHDH 86
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 59-150 6.38e-03

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 37.63  E-value: 6.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242042  59 KILQVADMHFGMGMITRCRdVLDSEFEycsdlnttrFLRRMIE---SERPDLIAFTGDnIFGSS--TTDAAESLLEAIGP 133
Cdd:cd00840   1 RFLHTADWHLGYPLYGLSR-REEDFFK---------AFEEIVDlaiEEKVDFVLIAGD-LFDSNnpSPEALKLAIEGLRR 69

                        90
                ....*....|....*..
gi 15242042 134 AIEYGIPWAAVLGNHDH 150
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.
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