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Conserved domains on  [gi|18401643|ref|NP_566587|]
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purple acid phosphatase 17 [Arabidopsis thaliana]

Protein Classification

purple acid phosphatase family protein( domain architecture ID 10164501)

purple acid phosphatase (PAP) family protein is a metallophosphatase containing an active site consisting of two metal ions (usually manganese, iron, or zinc); similar to human tartrate-resistant acid phosphatase type 5 (ACP5) which is involved in osteopontin/bone sialoprotein dephosphorylation in bone matrix

CATH:  3.60.21.10
EC:  3.1.3.2
Gene Ontology:  GO:0046872|GO:0016311|GO:0003993
PubMed:  25837850|8683579|8003970

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 46-321 3.12e-121

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: 350.47  E-value: 3.12e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  46 VSFIVIGDWGRR----GSFNQSLVAYQMGKIGEKIDLDFVVSTGDNFYDNGLFSEHDPNFEQSFSNIYTAPSLQKQWYSV 121
Cdd:cd07378   1 LRFLVLGDWGGKpnpyTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 122 LGNHDYRGDAEAQLSSVLREIDSRWICLRSFVVDAEL-------VEMFFVDTTPFVKEYYTEADGhsydWRAVPSRNSYV 194
Cdd:cd07378  81 LGNHDHRGNVSAQIAYTQRPNSKRWNFPNYYYDISFKfpssdvtVAFIMIDTVLLCGNTDDEASG----QPRGPPNKKLA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 195 KALLRDLEVSLKSSKARWKIVVGHHAMRSIGHHGDTKELNEELLPILKENGVDLYMNGHDHCLQHMSDeDSPIQFLTSGA 274
Cdd:cd07378 157 ETQLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVD-ESGTYYVISGA 235

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 18401643 275 GSKAWRGDINPVTINP----KLLKFYYDGQGFMSARFTHSDAEIVFYDVFG 321
Cdd:cd07378 236 GSKADPSDIHRDKVPQgyllFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 46-321 3.12e-121

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: 350.47  E-value: 3.12e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  46 VSFIVIGDWGRR----GSFNQSLVAYQMGKIGEKIDLDFVVSTGDNFYDNGLFSEHDPNFEQSFSNIYTAPSLQKQWYSV 121
Cdd:cd07378   1 LRFLVLGDWGGKpnpyTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 122 LGNHDYRGDAEAQLSSVLREIDSRWICLRSFVVDAEL-------VEMFFVDTTPFVKEYYTEADGhsydWRAVPSRNSYV 194
Cdd:cd07378  81 LGNHDHRGNVSAQIAYTQRPNSKRWNFPNYYYDISFKfpssdvtVAFIMIDTVLLCGNTDDEASG----QPRGPPNKKLA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 195 KALLRDLEVSLKSSKARWKIVVGHHAMRSIGHHGDTKELNEELLPILKENGVDLYMNGHDHCLQHMSDeDSPIQFLTSGA 274
Cdd:cd07378 157 ETQLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVD-ESGTYYVISGA 235

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 18401643 275 GSKAWRGDINPVTINP----KLLKFYYDGQGFMSARFTHSDAEIVFYDVFG 321
Cdd:cd07378 236 GSKADPSDIHRDKVPQgyllFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
46-297 4.29e-23

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 95.53  E-value: 4.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  46 VSFIVIGD---WGRRGSFNQSLVAYQMGKIgEKIDLDFVVSTGDNFYDnGLFSEHDpNFEQSFSniytapSLQKQWYSVL 122
Cdd:COG1409   1 FRFAHISDlhlGAPDGSDTAEVLAAALADI-NAPRPDFVVVTGDLTDD-GEPEEYA-AAREILA------RLGVPVYVVP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 123 GNHDYRGDAEAQLSSVLREIDSRwicLRSFVVDAELVEMFFVDTTPFvKEYYTEADGHSYDWravpsrnsyvkallrdLE 202
Cdd:COG1409  72 GNHDIRAAMAEAYREYFGDLPPG---GLYYSFDYGGVRFIGLDSNVP-GRSSGELGPEQLAW----------------LE 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 203 VSLKSSKARWKIVVGHHAMRSIGHHGDTKELN--EELLPILKENGVDLYMNGHDHclQHMSDEDSPIQFLTSGAGSKAWR 280
Cdd:COG1409 132 EELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVH--RYERTRRDGVPYIVAGSTGGQVR 209

                       250
                ....*....|....*....
gi 18401643 281 GD--INPVTINPKLLKFYY 297
Cdd:COG1409 210 LPpgYRVIEVDGDGLTVEV 228
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 14-334 5.18e-19

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 86.80  E-value: 5.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643   14 SLSLLLCIFTTFvvvsngelqrFIEPAKSDGSVSFIVIGDWGRrGSFNQSLVAYQMGKIGEKIDLDFVVSTGDNFyDNGL 93
Cdd:PTZ00422   5 CKLVLFSLFVLI----------FISSYSVKAQLRFASLGNWGT-GSKQQKLVASYLKQYAKNERVTFLVSPGSNF-PGGV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643   94 FSEHDPNFEQSFSNIYT--APSLQKQWYSVLGNHDYRGDAEAQLssvLREidsrwiclrsfvvdaelVEMFFVDTTPFVK 171
Cdd:PTZ00422  73 DGLNDPKWKHCFENVYSeeSGDMQIPFFTVLGQADWDGNYNAEL---LKG-----------------QNVYLNGHGQTDI 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  172 EYYTEADG-----------HSYDWRAVPSRNSYVKALLRDLEVSL---------------KSSKARWK------------ 213
Cdd:PTZ00422 133 EYDSNNDIypkwimpnywyHYFTHFTDTSGPSLLKSGHKDMSVAFifidtwilsssfpykKVSERAWQdlkatleyapki 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  214 ----IVVGHHAMRSIGH-HGDTKeLNEELLPILKENGVDLYMNGHDHCLQHMSDEDspIQFLTSGAGSKAWRgdiNPVTI 288
Cdd:PTZ00422 213 adyiIVVGDKPIYSSGSsKGDSY-LSYYLLPLLKDAQVDLYISGYDRNMEVLTDEG--TAHINCGSGGNSGR---KSIMK 286

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 18401643  289 NPKLLkFYYDGQGFMSarFTHSDAEIVFYDVFGEILHKWVTSKQLL 334
Cdd:PTZ00422 287 NSKSL-FYSEDIGFCI--HELNAEGMVTKFVSGNTGEVLYTHKQPL 329
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 48-163 1.75e-07

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: 49.13  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643    48 FIVIGDWGRRGSFNQSLVAYQmgKIGEKIDLDFVVSTGDnFYDNGLFSEhdpnfeqSFSNIYTAPSLQKQWYSVLGNHDY 127
Cdd:pfam00149   3 ILVIGDLHLPGQLDDLLELLK--KLLEEGKPDLVLHAGD-LVDRGPPSE-------EVLELLERLIKYVPVYLVRGNHDF 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18401643   128 RGDAEAQLSSVLREIDSRWICLRSFVVDAELVEMFF 163
Cdd:pfam00149  73 DYGECLRLYPYLGLLARPWKRFLEVFNFLPLAGILS 108
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 46-321 3.12e-121

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: 350.47  E-value: 3.12e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  46 VSFIVIGDWGRR----GSFNQSLVAYQMGKIGEKIDLDFVVSTGDNFYDNGLFSEHDPNFEQSFSNIYTAPSLQKQWYSV 121
Cdd:cd07378   1 LRFLVLGDWGGKpnpyTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 122 LGNHDYRGDAEAQLSSVLREIDSRWICLRSFVVDAEL-------VEMFFVDTTPFVKEYYTEADGhsydWRAVPSRNSYV 194
Cdd:cd07378  81 LGNHDHRGNVSAQIAYTQRPNSKRWNFPNYYYDISFKfpssdvtVAFIMIDTVLLCGNTDDEASG----QPRGPPNKKLA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 195 KALLRDLEVSLKSSKARWKIVVGHHAMRSIGHHGDTKELNEELLPILKENGVDLYMNGHDHCLQHMSDeDSPIQFLTSGA 274
Cdd:cd07378 157 ETQLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVD-ESGTYYVISGA 235

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 18401643 275 GSKAWRGDINPVTINP----KLLKFYYDGQGFMSARFTHSDAEIVFYDVFG 321
Cdd:cd07378 236 GSKADPSDIHRDKVPQgyllFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
46-297 4.29e-23

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 95.53  E-value: 4.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  46 VSFIVIGD---WGRRGSFNQSLVAYQMGKIgEKIDLDFVVSTGDNFYDnGLFSEHDpNFEQSFSniytapSLQKQWYSVL 122
Cdd:COG1409   1 FRFAHISDlhlGAPDGSDTAEVLAAALADI-NAPRPDFVVVTGDLTDD-GEPEEYA-AAREILA------RLGVPVYVVP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 123 GNHDYRGDAEAQLSSVLREIDSRwicLRSFVVDAELVEMFFVDTTPFvKEYYTEADGHSYDWravpsrnsyvkallrdLE 202
Cdd:COG1409  72 GNHDIRAAMAEAYREYFGDLPPG---GLYYSFDYGGVRFIGLDSNVP-GRSSGELGPEQLAW----------------LE 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 203 VSLKSSKARWKIVVGHHAMRSIGHHGDTKELN--EELLPILKENGVDLYMNGHDHclQHMSDEDSPIQFLTSGAGSKAWR 280
Cdd:COG1409 132 EELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVH--RYERTRRDGVPYIVAGSTGGQVR 209

                       250
                ....*....|....*....
gi 18401643 281 GD--INPVTINPKLLKFYY 297
Cdd:COG1409 210 LPpgYRVIEVDGDGLTVEV 228
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 14-334 5.18e-19

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 86.80  E-value: 5.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643   14 SLSLLLCIFTTFvvvsngelqrFIEPAKSDGSVSFIVIGDWGRrGSFNQSLVAYQMGKIGEKIDLDFVVSTGDNFyDNGL 93
Cdd:PTZ00422   5 CKLVLFSLFVLI----------FISSYSVKAQLRFASLGNWGT-GSKQQKLVASYLKQYAKNERVTFLVSPGSNF-PGGV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643   94 FSEHDPNFEQSFSNIYT--APSLQKQWYSVLGNHDYRGDAEAQLssvLREidsrwiclrsfvvdaelVEMFFVDTTPFVK 171
Cdd:PTZ00422  73 DGLNDPKWKHCFENVYSeeSGDMQIPFFTVLGQADWDGNYNAEL---LKG-----------------QNVYLNGHGQTDI 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  172 EYYTEADG-----------HSYDWRAVPSRNSYVKALLRDLEVSL---------------KSSKARWK------------ 213
Cdd:PTZ00422 133 EYDSNNDIypkwimpnywyHYFTHFTDTSGPSLLKSGHKDMSVAFifidtwilsssfpykKVSERAWQdlkatleyapki 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  214 ----IVVGHHAMRSIGH-HGDTKeLNEELLPILKENGVDLYMNGHDHCLQHMSDEDspIQFLTSGAGSKAWRgdiNPVTI 288
Cdd:PTZ00422 213 adyiIVVGDKPIYSSGSsKGDSY-LSYYLLPLLKDAQVDLYISGYDRNMEVLTDEG--TAHINCGSGGNSGR---KSIMK 286

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 18401643  289 NPKLLkFYYDGQGFMSarFTHSDAEIVFYDVFGEILHKWVTSKQLL 334
Cdd:PTZ00422 287 NSKSL-FYSEDIGFCI--HELNAEGMVTKFVSGNTGEVLYTHKQPL 329
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 48-163 1.75e-07

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: 49.13  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643    48 FIVIGDWGRRGSFNQSLVAYQmgKIGEKIDLDFVVSTGDnFYDNGLFSEhdpnfeqSFSNIYTAPSLQKQWYSVLGNHDY 127
Cdd:pfam00149   3 ILVIGDLHLPGQLDDLLELLK--KLLEEGKPDLVLHAGD-LVDRGPPSE-------EVLELLERLIKYVPVYLVRGNHDF 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18401643   128 RGDAEAQLSSVLREIDSRWICLRSFVVDAELVEMFF 163
Cdd:pfam00149  73 DYGECLRLYPYLGLLARPWKRFLEVFNFLPLAGILS 108
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 214-273 1.13e-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: 41.48  E-value: 1.13e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401643 214 IVVGHHAMRSIGHHGDTKEL--NEELLPILKENGVDLYMNGHDHCLQHMSDEDSPIQFLTSG 273
Cdd:cd00838  69 ILVTHGPPYDPLDEGSPGEDpgSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVVNPG 130
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 42-255 1.22e-04

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: 43.06  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  42 SDGSVSFIVIGDWGRRGSFNQSLVayqMGKIGEKIDLDFVVSTGDNFYDNGlfSEHDP---NFEQSFSNIYTapslQKQW 118
Cdd:cd00839   1 PDTPLKFAVFGDMGQNTNNSTNTL---DHLEKELGNYDAIIHVGDIAYADG--YNNGSrwdTFMRQIEPLAS----YVPY 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 119 YSVLGNHDYrgdaEAQLSSVlrEIDSRWICLRSFVVDAELVEMF----------FVDTTPFVKEYYTEADGHSYDWravp 188
Cdd:cd00839  72 MVAPGNHEA----DYNGSTS--KIKFFMPGRGMPPSPSGSTENLwysfdvgpvhFISLSTETDFLKGDNISPQYDW---- 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401643 189 srnsyvkaLLRDLEvSLKSSKARWKIVVGHHAM----RSIGHHGDTKELNEELLPILKENGVDLYMNGHDH 255
Cdd:cd00839 142 --------LEADLA-KVDRSRTPWIIVMGHRPMycsnDDDADCIEGEKMREALEDLFYKYGVDLVLSGHVH 203
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 214-255 1.31e-04

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: 41.51  E-value: 1.31e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18401643 214 IVVGHHAMRSI---GHHGDTKELNEELLPILKENGVDLYMNGHDH 255
Cdd:cd07400  74 IVALHHPLLPPpdtGRERNVLLDAGDALKLLKELGVDLVLHGHKH 118
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
79-150 1.26e-03

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 39.78  E-value: 1.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401643  79 DFVVSTGDNFYDNglfSEHDPNFEQSFSNIyTAPsLQKqwYSVLGNHDYRGDAEAqLSSVLREIDsrWICLR 150
Cdd:COG1408  75 DLVVLTGDLVDGS---VAELEALLELLKKL-KAP-LGV--YAVLGNHDYYAGLEE-LRAALEEAG--VRVLR 136
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 71-272 1.91e-03

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 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: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 39.27  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643  71 KIGEKIDLDFVVSTGD---NFYDNGLFS---EHDPnfEQSFSNIYTAPSL--QKQWYSVLGNHDYRGDAE-------AQL 135
Cdd:cd07401  27 NFIDVIKPTLVLITGDltdNKTGNKLPSyqyQEEW--QWKYYNILKESSVinKEYLFDIRGNHDLFGIVSfdsqnnyYRK 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401643 136 SSVLREIDSRwiclrsfvvdaELVEMFFVDTTPFVKEYYTEADG----HSYdwraVPSRNsyvKALLRDLEVSLKSSK-A 210
Cdd:cd07401 105 YSNTGRDHSH-----------SFSSTTRFGNYSFIGFDPTIFPGpkrpFNF----FGSLD---KKLLDRLEKELEKSKnS 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401643 211 RWKIVVGHHAMRSIGHHGdTKELNEELLPILKENGVDLYMNGHDHCLQ---HMSDeDSPIQFLTS 272
Cdd:cd07401 167 KYTIWFGHYPHSLIISPS-AKSSSKTFKDLLKKYNVTAYLCGHLHPLGgepVHYA-GHPIAIITN 229
 
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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