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Conserved domains on  [gi|75262722|sp|Q9FMK9|]
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RecName: Full=Probable inactive purple acid phosphatase 29; Flags: Precursor

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; ...
 45-330 1.38e-73

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: 227.95  E-value: 1.38e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  45 GEFKILQVADMHFANGAKTQCQnvlpsqrAHCSDLNTTIFMSRVIAAEKPDLIVFTGDNIFGFDVKD--ALKSINAAFAP 122
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCWE-------GCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 123 AIASKIPWVAILGNHDqestftrqqvmnhivklpntlsqvnppeaahyidgfgnynlqihgaadsklqnksvlnlyflds 202
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 203 gdyssvpymeGYDWIKTSQQFWFDRTSKRLKREYNAKPnpqegiaPGLAYFHIPLPEFLSF-DSKNATKGVRQEGTSAAS 281
Cdd:cd07383  90 ----------GYDWIDPSQVEWFESTSAALKKKYGKNI-------PSLAFFHIPLPEYREVwNEKGKLGGINREKVCCQK 152

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 75262722 282 TNSGFFTTLIARGDVKSVFVGHDHVNDFCG-ELKGLNLCYGGGFGYHAYG 330
Cdd:cd07383 153 TNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTGYGGYG 202
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 45-330 1.38e-73

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: 227.95  E-value: 1.38e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  45 GEFKILQVADMHFANGAKTQCQnvlpsqrAHCSDLNTTIFMSRVIAAEKPDLIVFTGDNIFGFDVKD--ALKSINAAFAP 122
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCWE-------GCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 123 AIASKIPWVAILGNHDqestftrqqvmnhivklpntlsqvnppeaahyidgfgnynlqihgaadsklqnksvlnlyflds 202
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 203 gdyssvpymeGYDWIKTSQQFWFDRTSKRLKREYNAKPnpqegiaPGLAYFHIPLPEFLSF-DSKNATKGVRQEGTSAAS 281
Cdd:cd07383  90 ----------GYDWIDPSQVEWFESTSAALKKKYGKNI-------PSLAFFHIPLPEYREVwNEKGKLGGINREKVCCQK 152

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 75262722 282 TNSGFFTTLIARGDVKSVFVGHDHVNDFCG-ELKGLNLCYGGGFGYHAYG 330
Cdd:cd07383 153 TNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTGYGGYG 202
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
47-344 3.96e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 73.96  E-value: 3.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  47 FKILQVADMHFANGAKTQCQNVLPSQRAHcsdlnttifmsrvIAAEKPDLIVFTGDNIFgfdvkDALKSINAAFAPAIAS 126
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLAAALAD-------------INAPRPDFVVVTGDLTD-----DGEPEEYAAAREILAR 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 127 -KIPWVAILGNHDqestftrqqvmnhivklpntlsqVNPPEAAHYIDGFGNYNlqiHGAADSKLQNKSVLnLYFLDSGDY 205
Cdd:COG1409  63 lGVPVYVVPGNHD-----------------------IRAAMAEAYREYFGDLP---PGGLYYSFDYGGVR-FIGLDSNVP 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 206 SSVpymegYDWIKTSQQFWFDRTSKRLKREYNakpnpqegiapgLAYFHIPLPEFLSFDSKNATKGVRQegtsaastnsg 285
Cdd:COG1409 116 GRS-----SGELGPEQLAWLEEELAAAPAKPV------------IVFLHHPPYSTGSGSDRIGLRNAEE----------- 167

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75262722 286 fFTTLIARGDVKSVFVGHDHVNDFcGELKGLNLCYGGGFGYHAYGKAGWerraRVVVVD 344
Cdd:COG1409 168 -LLALLARYGVDLVLSGHVHRYER-TRRDGVPYIVAGSTGGQVRLPPGY----RVIEVD 220
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 47-138 1.31e-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: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722    47 FKILQVADMHFANGAktqcqnvlpsqrahcSDLNTTIfmSRVIAAEKPDLIVFTGDNIFGFDVKDALksinAAFAPAIAS 126
Cdd:pfam00149   1 MRILVIGDLHLPGQL---------------DDLLELL--KKLLEEGKPDLVLHAGDLVDRGPPSEEV----LELLERLIK 59

                          90
                  ....*....|..
gi 75262722   127 KIPWVAILGNHD 138
Cdd:pfam00149  60 YVPVYLVRGNHD 71
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 45-330 1.38e-73

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: 227.95  E-value: 1.38e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  45 GEFKILQVADMHFANGAKTQCQnvlpsqrAHCSDLNTTIFMSRVIAAEKPDLIVFTGDNIFGFDVKD--ALKSINAAFAP 122
Cdd:cd07383   1 GKFKILQFADLHFGEGEWTCWE-------GCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAVSP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 123 AIASKIPWVAILGNHDqestftrqqvmnhivklpntlsqvnppeaahyidgfgnynlqihgaadsklqnksvlnlyflds 202
Cdd:cd07383  74 LVERGIPWAATFGNHD---------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 203 gdyssvpymeGYDWIKTSQQFWFDRTSKRLKREYNAKPnpqegiaPGLAYFHIPLPEFLSF-DSKNATKGVRQEGTSAAS 281
Cdd:cd07383  90 ----------GYDWIDPSQVEWFESTSAALKKKYGKNI-------PSLAFFHIPLPEYREVwNEKGKLGGINREKVCCQK 152

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 75262722 282 TNSGFFTTLIARGDVKSVFVGHDHVNDFCG-ELKGLNLCYGGGFGYHAYG 330
Cdd:cd07383 153 TNSGFFKALVKRGDVKAVFCGHDHGNDFCGrWKNGIWLCYGRHTGYGGYG 202
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
47-344 3.96e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 73.96  E-value: 3.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  47 FKILQVADMHFANGAKTQCQNVLPSQRAHcsdlnttifmsrvIAAEKPDLIVFTGDNIFgfdvkDALKSINAAFAPAIAS 126
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLAAALAD-------------INAPRPDFVVVTGDLTD-----DGEPEEYAAAREILAR 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 127 -KIPWVAILGNHDqestftrqqvmnhivklpntlsqVNPPEAAHYIDGFGNYNlqiHGAADSKLQNKSVLnLYFLDSGDY 205
Cdd:COG1409  63 lGVPVYVVPGNHD-----------------------IRAAMAEAYREYFGDLP---PGGLYYSFDYGGVR-FIGLDSNVP 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722 206 SSVpymegYDWIKTSQQFWFDRTSKRLKREYNakpnpqegiapgLAYFHIPLPEFLSFDSKNATKGVRQegtsaastnsg 285
Cdd:COG1409 116 GRS-----SGELGPEQLAWLEEELAAAPAKPV------------IVFLHHPPYSTGSGSDRIGLRNAEE----------- 167

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75262722 286 fFTTLIARGDVKSVFVGHDHVNDFcGELKGLNLCYGGGFGYHAYGKAGWerraRVVVVD 344
Cdd:COG1409 168 -LLALLARYGVDLVLSGHVHRYER-TRRDGVPYIVAGSTGGQVRLPPGY----RVIEVD 220
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 46-141 2.60e-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: 53.82  E-value: 2.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  46 EFKILQVADMHF-ANGAKTQCQNVLpsqrahcsdlnttifmsRVIAAEKPDLIVFTGDNIFGfDVKDaLKSINAAFAPaI 124
Cdd:cd07385   1 GLRIVQLSDIHLgPFVGRTRLQKVV-----------------RKVNELNPDLIVITGDLVDG-DVSV-LRLLASPLSK-L 60

                        90
                ....*....|....*..
gi 75262722 125 ASKIPWVAILGNHDQES 141
Cdd:cd07385  61 KAPLGVYFVLGNHDYYS 77
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
47-138 4.90e-08

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 53.65  E-value: 4.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  47 FKILQVADMHFangaktqcqnvlpsqrahcSDLNTTIFMSRV---IAAEKPDLIVFTGDNIFGF-----DVKDALKSINA 118
Cdd:COG1408  43 LRIVQLSDLHL-------------------GPFIGGERLERLvekINALKPDLVVLTGDLVDGSvaeleALLELLKKLKA 103

                        90       100
                ....*....|....*....|
gi 75262722 119 afapaiasKIPWVAILGNHD 138
Cdd:COG1408 104 --------PLGVYAVLGNHD 115
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 74-138 3.63e-07

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: 48.80  E-value: 3.63e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75262722  74 AHCSDL------NTTIFMSRVIAAEKPDLIVFTGDNIFGFDVKDALksiNAAFAPAIASKIPWVAILGNHD 138
Cdd:cd00838   1 LVISDIhgnleaLEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEV---ELKALRLLLAGIPVYVVPGNHD 68
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
47-142 1.04e-06

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 49.53  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  47 FKILQVADMHFanGAKTQCQNVLPSQRAhcsdlnttiFMSRVIA---AEKPDLIVFTGDnIFgfDV----KDALKSINAA 119
Cdd:COG0420   1 MRFLHTADWHL--GKPLHGASRREDQLA---------ALDRLVDlaiEEKVDAVLIAGD-LF--DSanpsPEAVRLLAEA 66

                        90       100
                ....*....|....*....|...
gi 75262722 120 FAPAIASKIPWVAILGNHDQEST 142
Cdd:COG0420  67 LRRLSEAGIPVVLIAGNHDSPSR 89
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 47-138 1.31e-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: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722    47 FKILQVADMHFANGAktqcqnvlpsqrahcSDLNTTIfmSRVIAAEKPDLIVFTGDNIFGFDVKDALksinAAFAPAIAS 126
Cdd:pfam00149   1 MRILVIGDLHLPGQL---------------DDLLELL--KKLLEEGKPDLVLHAGDLVDRGPPSEEV----LELLERLIK 59

                          90
                  ....*....|..
gi 75262722   127 KIPWVAILGNHD 138
Cdd:pfam00149  60 YVPVYLVRGNHD 71
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 85-138 5.75e-04

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: 41.54  E-value: 5.75e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75262722  85 MSRVIAAEKPDLIVFTGDNIFGFDVKD----ALKSINAAFAPAIASKIPWVAILGNHD 138
Cdd:cd07378  28 MAKVASKLGIDFILSLGDNFYDDGVKDvddpRFQETFEDVYSAPSLQVPWYLVLGNHD 85
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 80-144 8.39e-03

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 37.66  E-value: 8.39e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75262722  80 NTTIFMSRVIA-AEKPDLIVFTGDniFGFDVKDALKSI----NAAFAPaIASKIPWVAILGNHDQESTFT 144
Cdd:cd00839  19 NSTNTLDHLEKeLGNYDAIIHVGD--IAYADGYNNGSRwdtfMRQIEP-LASYVPYMVAPGNHEADYNGS 85
 
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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