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Conserved domains on  [gi|392921259|ref|NP_001256452|]
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Purple acid phosphatase [Caenorhabditis elegans]

Protein Classification

purple acid phosphatase family protein( domain architecture ID 11244682)

purple acid phosphatase (PAP) family protein contains an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to PAP, a binuclear metallohydrolase that catalyzes the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters, and anhydrides

CATH:  3.60.21.10
EC:  3.1.3.-
Gene Ontology:  GO:0042578|GO:0046872|GO:0016311
PubMed:  25837850|8683579

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 112-413 1.11e-109

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: 325.79  E-value: 1.11e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 112 DPQSYKVCVFGDLGYWHGNSTESIIKHGL-AGDFDFIVHLGDIAYDLHTNNGQVGDSYLNVFEPLISKVPYMVIAGNHED 190
Cdd:cd00839    1 PDTPLKFAVFGDMGQNTNNSTNTLDHLEKeLGNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 191 DYQNFTNYQKRFSVP------DNGHNDNQFYSFDLGPVHWVGVSTETYGYYYEYGMDpvmtQYDWLKRDLTTANSNRaaH 264
Cdd:cd00839   81 DYNGSTSKIKFFMPGrgmppsPSGSTENLWYSFDVGPVHFISLSTETDFLKGDNISP----QYDWLEADLAKVDRSR--T 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 265 PWIFTFQHRPFYCSNVNSAECQSFENrlvrtgwlDMPGLEPLFLQTSVDFGFWGHEHSYERFYPVADRAYWN-DPNAYIN 343
Cdd:cd00839  155 PWIIVMGHRPMYCSNDDDADCIEGEK--------MREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANsKDNIYTN 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921259 344 PKAPVYLISGSAGCHT-PDALFTDKPWPWSAARNNDYGWSIVTVANRTHIRVEQISIDKNeQTVDDFWVIK 413
Cdd:cd00839  227 PKGPVHIVIGAAGNDEgLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDG-QVADSFWIVK 296
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 24-108 9.82e-18

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


:

Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 77.84  E-value: 9.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259   24 PDQVHISFTGDMTEMAVVWNTFSEV-SQDVTYGKTGSGATSTAKGSSEAWVFG-GITRYRHKAIMTGLEYSTEYDYTIA- 100
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVtSPVVQYGTSSSALTSTATATSSTYTTGdGGTGYIHRATLTGLEPGTTYYYRVGd 80

                          90
                  ....*....|...
gi 392921259  101 -----SRKFSFKT 108
Cdd:pfam16656  81 dnggwSEVYSFTT 93
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 112-413 1.11e-109

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: 325.79  E-value: 1.11e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 112 DPQSYKVCVFGDLGYWHGNSTESIIKHGL-AGDFDFIVHLGDIAYDLHTNNGQVGDSYLNVFEPLISKVPYMVIAGNHED 190
Cdd:cd00839    1 PDTPLKFAVFGDMGQNTNNSTNTLDHLEKeLGNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 191 DYQNFTNYQKRFSVP------DNGHNDNQFYSFDLGPVHWVGVSTETYGYYYEYGMDpvmtQYDWLKRDLTTANSNRaaH 264
Cdd:cd00839   81 DYNGSTSKIKFFMPGrgmppsPSGSTENLWYSFDVGPVHFISLSTETDFLKGDNISP----QYDWLEADLAKVDRSR--T 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 265 PWIFTFQHRPFYCSNVNSAECQSFENrlvrtgwlDMPGLEPLFLQTSVDFGFWGHEHSYERFYPVADRAYWN-DPNAYIN 343
Cdd:cd00839  155 PWIIVMGHRPMYCSNDDDADCIEGEK--------MREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANsKDNIYTN 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921259 344 PKAPVYLISGSAGCHT-PDALFTDKPWPWSAARNNDYGWSIVTVANRTHIRVEQISIDKNeQTVDDFWVIK 413
Cdd:cd00839  227 PKGPVHIVIGAAGNDEgLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDG-QVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 22-411 2.06e-39

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 147.14  E-value: 2.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259  22 TTPDQVHISFTGDmTEMAVVWNTFSEVSQDVTYGKTGSGATSTAKGSSEAWVFGGITRYR--HKAIMTGLEYSTEYDYTI 99
Cdd:PLN02533  42 THPDQVHISLVGP-DKMRISWITQDSIPPSVVYGTVSGKYEGSANGTSSSYHYLLIYRSGqiNDVVIGPLKPNTVYYYKC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 100 ----ASRKFSFKTlsnDPQSY--KVCVFGDLGY--WhgnsTESIIKHGLAGDFDFIVHLGDIAYdlhTNNGQ-VGDSYLN 170
Cdd:PLN02533 121 ggpsSTQEFSFRT---PPSKFpiKFAVSGDLGTseW----TKSTLEHVSKWDYDVFILPGDLSY---ANFYQpLWDTFGR 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 171 VFEPLISKVPYMVIAGNHEDD------YQNFTNYQKRFSVP--DNGHNDNQFYSFDLGPVHWVGVSTETYgyyyeygMDP 242
Cdd:PLN02533 191 LVQPLASQRPWMVTHGNHELEkipilhPEKFTAYNARWRMPfeESGSTSNLYYSFNVYGVHIIMLGSYTD-------FEP 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 243 VMTQYDWLKRDLTTANsnRAAHPWIFTFQHRPFYCSN-VNSAECQSFENRlvrtgwldmPGLEPLFLQTSVDFGFWGHEH 321
Cdd:PLN02533 264 GSEQYQWLENNLKKID--RKTTPWVVAVVHAPWYNSNeAHQGEKESVGMK---------ESMETLLYKARVDLVFAGHVH 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 322 SYERFypvaDRAYWNDpnayINPKAPVYLISGSAGCHTPDALFTDKPWP-WSAARNNDYGWSIVTVANRTHIRVEQISID 400
Cdd:PLN02533 333 AYERF----DRVYQGK----TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTWHRND 404

                        410
                 ....*....|...
gi 392921259 401 kNEQTV--DDFWV 411
Cdd:PLN02533 405 -DDQSVasDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
116-328 6.66e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 85.51  E-value: 6.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 116 YKVCVFGDLGYWHGN------STESIIKHGLAGDFDFIVHLGDIaydlhTNNGQVG--DSYLNVFEPLisKVPYMVIAGN 187
Cdd:COG1409    1 FRFAHISDLHLGAPDgsdtaeVLAAALADINAPRPDFVVVTGDL-----TDDGEPEeyAAAREILARL--GVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 188 HEDDYQNFTNYQKRFSVPDnghNDNQFYSFDLGPVHWVGVSTETYGYYYEYGMDpvmTQYDWLKRDLTtansnRAAHPWI 267
Cdd:COG1409   74 HDIRAAMAEAYREYFGDLP---PGGLYYSFDYGGVRFIGLDSNVPGRSSGELGP---EQLAWLEEELA-----AAPAKPV 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921259 268 FTFQHRPFYCSNVnsaecqsfenRLVRTGWLDMPGLEPLFLQTSVDFGFWGHEHSYERFYP 328
Cdd:COG1409  143 IVFLHHPPYSTGS----------GSDRIGLRNAEELLALLARYGVDLVLSGHVHRYERTRR 193
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 24-108 9.82e-18

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 77.84  E-value: 9.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259   24 PDQVHISFTGDMTEMAVVWNTFSEV-SQDVTYGKTGSGATSTAKGSSEAWVFG-GITRYRHKAIMTGLEYSTEYDYTIA- 100
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVtSPVVQYGTSSSALTSTATATSSTYTTGdGGTGYIHRATLTGLEPGTTYYYRVGd 80

                          90
                  ....*....|...
gi 392921259  101 -----SRKFSFKT 108
Cdd:pfam16656  81 dnggwSEVYSFTT 93
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 346-408 2.72e-14

Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of Purple acid phosphatase proteins.


Pssm-ID: 464064 [Multi-domain]  Cd Length: 60  Bit Score: 67.16  E-value: 2.72e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392921259  346 APVYLISGSAGCHtpDALFTDKPWPWSAARNNDYGWSIVTVANRTHIRVEQISIDKNeqTVDD 408
Cdd:pfam14008   1 APVHIVIGAAGNI--EGLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSDDG--TVLD 59
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 112-413 1.11e-109

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: 325.79  E-value: 1.11e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 112 DPQSYKVCVFGDLGYWHGNSTESIIKHGL-AGDFDFIVHLGDIAYDLHTNNGQVGDSYLNVFEPLISKVPYMVIAGNHED 190
Cdd:cd00839    1 PDTPLKFAVFGDMGQNTNNSTNTLDHLEKeLGNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 191 DYQNFTNYQKRFSVP------DNGHNDNQFYSFDLGPVHWVGVSTETYGYYYEYGMDpvmtQYDWLKRDLTTANSNRaaH 264
Cdd:cd00839   81 DYNGSTSKIKFFMPGrgmppsPSGSTENLWYSFDVGPVHFISLSTETDFLKGDNISP----QYDWLEADLAKVDRSR--T 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 265 PWIFTFQHRPFYCSNVNSAECQSFENrlvrtgwlDMPGLEPLFLQTSVDFGFWGHEHSYERFYPVADRAYWN-DPNAYIN 343
Cdd:cd00839  155 PWIIVMGHRPMYCSNDDDADCIEGEK--------MREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANsKDNIYTN 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921259 344 PKAPVYLISGSAGCHT-PDALFTDKPWPWSAARNNDYGWSIVTVANRTHIRVEQISIDKNeQTVDDFWVIK 413
Cdd:cd00839  227 PKGPVHIVIGAAGNDEgLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDG-QVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 22-411 2.06e-39

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 147.14  E-value: 2.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259  22 TTPDQVHISFTGDmTEMAVVWNTFSEVSQDVTYGKTGSGATSTAKGSSEAWVFGGITRYR--HKAIMTGLEYSTEYDYTI 99
Cdd:PLN02533  42 THPDQVHISLVGP-DKMRISWITQDSIPPSVVYGTVSGKYEGSANGTSSSYHYLLIYRSGqiNDVVIGPLKPNTVYYYKC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 100 ----ASRKFSFKTlsnDPQSY--KVCVFGDLGY--WhgnsTESIIKHGLAGDFDFIVHLGDIAYdlhTNNGQ-VGDSYLN 170
Cdd:PLN02533 121 ggpsSTQEFSFRT---PPSKFpiKFAVSGDLGTseW----TKSTLEHVSKWDYDVFILPGDLSY---ANFYQpLWDTFGR 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 171 VFEPLISKVPYMVIAGNHEDD------YQNFTNYQKRFSVP--DNGHNDNQFYSFDLGPVHWVGVSTETYgyyyeygMDP 242
Cdd:PLN02533 191 LVQPLASQRPWMVTHGNHELEkipilhPEKFTAYNARWRMPfeESGSTSNLYYSFNVYGVHIIMLGSYTD-------FEP 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 243 VMTQYDWLKRDLTTANsnRAAHPWIFTFQHRPFYCSN-VNSAECQSFENRlvrtgwldmPGLEPLFLQTSVDFGFWGHEH 321
Cdd:PLN02533 264 GSEQYQWLENNLKKID--RKTTPWVVAVVHAPWYNSNeAHQGEKESVGMK---------ESMETLLYKARVDLVFAGHVH 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 322 SYERFypvaDRAYWNDpnayINPKAPVYLISGSAGCHTPDALFTDKPWP-WSAARNNDYGWSIVTVANRTHIRVEQISID 400
Cdd:PLN02533 333 AYERF----DRVYQGK----TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTWHRND 404

                        410
                 ....*....|...
gi 392921259 401 kNEQTV--DDFWV 411
Cdd:PLN02533 405 -DDQSVasDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
116-328 6.66e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 85.51  E-value: 6.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 116 YKVCVFGDLGYWHGN------STESIIKHGLAGDFDFIVHLGDIaydlhTNNGQVG--DSYLNVFEPLisKVPYMVIAGN 187
Cdd:COG1409    1 FRFAHISDLHLGAPDgsdtaeVLAAALADINAPRPDFVVVTGDL-----TDDGEPEeyAAAREILARL--GVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 188 HEDDYQNFTNYQKRFSVPDnghNDNQFYSFDLGPVHWVGVSTETYGYYYEYGMDpvmTQYDWLKRDLTtansnRAAHPWI 267
Cdd:COG1409   74 HDIRAAMAEAYREYFGDLP---PGGLYYSFDYGGVRFIGLDSNVPGRSSGELGP---EQLAWLEEELA-----AAPAKPV 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921259 268 FTFQHRPFYCSNVnsaecqsfenRLVRTGWLDMPGLEPLFLQTSVDFGFWGHEHSYERFYP 328
Cdd:COG1409  143 IVFLHHPPYSTGS----------GSDRIGLRNAEELLALLARYGVDLVLSGHVHRYERTRR 193
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 24-108 9.82e-18

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 77.84  E-value: 9.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259   24 PDQVHISFTGDMTEMAVVWNTFSEV-SQDVTYGKTGSGATSTAKGSSEAWVFG-GITRYRHKAIMTGLEYSTEYDYTIA- 100
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVtSPVVQYGTSSSALTSTATATSSTYTTGdGGTGYIHRATLTGLEPGTTYYYRVGd 80

                          90
                  ....*....|...
gi 392921259  101 -----SRKFSFKT 108
Cdd:pfam16656  81 dnggwSEVYSFTT 93
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 346-408 2.72e-14

Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of Purple acid phosphatase proteins.


Pssm-ID: 464064 [Multi-domain]  Cd Length: 60  Bit Score: 67.16  E-value: 2.72e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392921259  346 APVYLISGSAGCHtpDALFTDKPWPWSAARNNDYGWSIVTVANRTHIRVEQISIDKNeqTVDD 408
Cdd:pfam14008   1 APVHIVIGAAGNI--EGLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSDDG--TVLD 59
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 116-226 4.52e-10

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: 56.84  E-value: 4.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259  116 YKVCVFGDLGYWHG-NSTESIIKHGLA-GDFDFIVHLGDIaydlhTNNGQVGDSYLNVFEPLISKVPYMVIAGNHEDDYQ 193
Cdd:pfam00149   1 MRILVIGDLHLPGQlDDLLELLKKLLEeGKPDLVLHAGDL-----VDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYG 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 392921259  194 NFTNYQKRFSVPDNGHNDNQFYSFDLGPVHWVG 226
Cdd:pfam00149  76 ECLRLYPYLGLLARPWKRFLEVFNFLPLAGILS 108
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
117-192 8.63e-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: 8.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392921259 117 KVCVFGDLgywHGNST--ESIIKHGLAGDFDFIVHLGDIaydlhTNNGQVgDSYLNVFEPLIS-KVPYMVIAGNHEDDY 192
Cdd:COG2129    1 KILAVSDL---HGNFDllEKLLELARAEDADLVILAGDL-----TDFGTA-EEAREVLEELAAlGVPVLAVPGNHDDPE 70
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 145-382 4.03e-05

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: 45.39  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 145 DFIVHLGDIAYD---LHTNNGQVGDSYLNVFEPLISKVPYMVIAGNH--------EDDYQNFTNYqKRFSVPDNGHNDN- 212
Cdd:cd07378   38 DFILSLGDNFYDdgvKDVDDPRFQETFEDVYSAPSLQVPWYLVLGNHdhrgnvsaQIAYTQRPNS-KRWNFPNYYYDISf 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 213 QFYSFD-------LGPVHWVGVSTETYGYYYEYGMDPVM--TQYDWLKRDLTTANSNraahpWIFTFQHRPFYcsnvnsa 283
Cdd:cd07378  117 KFPSSDvtvafimIDTVLLCGNTDDEASGQPRGPPNKKLaeTQLAWLEKQLAASKAD-----YKIVVGHYPIY------- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 284 ecQSFENRlvRTGWLDMPgLEPLFLQTSVDFGFWGHEHSYErfypvadraywndpnaYINPKAPV-YLISGSAGCHTPDA 362
Cdd:cd07378  185 --SSGEHG--PTKCLVDI-LLPLLKKYKVDAYLSGHDHNLQ----------------HIVDESGTyYVISGAGSKADPSD 243

                        250       260
                 ....*....|....*....|
gi 392921259 363 LFTDKPWPWSAARNNDYGWS 382
Cdd:cd07378  244 IHRDKVPQGYLLFFSGFYSS 263
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 120-189 5.18e-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: 43.02  E-value: 5.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392921259 120 VFGDLgywHGNSTESII----KHGLAGDFDFIVHLGDIAYDLHTNNgqvgDSYLNVFEPLISKVPYMVIAGNHE 189
Cdd:cd00838    2 VISDI---HGNLEALEAvleaALAKAEKPDLVICLGDLVDYGPDPE----EVELKALRLLLAGIPVYVVPGNHD 68
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 140-322 1.38e-03

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 40.34  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 140 LAGDFDFIVHLGDIaydlhTNNGQVgDSYLN---VFEPLisKVPYMVIAGNHeDDYQNFtnyQKRFsvPDNGHNDNQF-- 214
Cdd:cd07402   36 LHPRPDLVVVTGDL-----SDDGSP-ESYERlreLLAPL--PAPVYWIPGNH-DDRAAM---REAL--PEPPYDDNGPvq 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 215 YSFDLGPVHWVGVSTETYGYYYEYGMDpvmTQYDWLKRDLttanSNRAAHPWIFTFQHRPFycsNVNSAECQSFenRLVR 294
Cdd:cd07402  102 YVVDFGGWRLILLDTSVPGVHHGELSD---EQLDWLEAAL----AEAPDRPTLIFLHHPPF---PLGIPWMDAI--RLRN 169

                        170       180
                 ....*....|....*....|....*...
gi 392921259 295 TGWLdmpgLEPLFLQTSVDFGFWGHEHS 322
Cdd:cd07402  170 SQAL----FAVLARHPQVKAILCGHIHR 193
MPP_YvnB cd07399
Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an ...
 130-189 1.95e-03

Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an uncharacterized Bacillus subtilis protein with a metallophosphatase domain. This family includes bacterial and eukaryotic proteins similar to YvnB. YvnB 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: 277344 [Multi-domain]  Cd Length: 207  Bit Score: 39.40  E-value: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259 130 NSTESIIKHGLAGDFDFIVHLGDIAYDLHTNNGQVGDSYLNVFEPliSKVPYMVIAGNHE 189
Cdd:cd07399   22 AQTEWIVDERENKNIDFVFHTGDVTDHGVDKEWEVAAAAFNVLDD--SGVPYSVLAGNHD 79
PhoD COG3540
Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];
83-155 2.83e-03

Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];


Pssm-ID: 442761 [Multi-domain]  Cd Length: 482  Bit Score: 39.90  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921259  83 KAIMTGLEYSTEYDYTI-----ASRKFSFKTL--SNDPQSYKVCVFGDLGYWHGNSTesIIKHGLAGDFDFIVHLGDIAY 155
Cdd:COG3540   95 KVDVTGLEPGTRYFYRFraggeTSPVGRFRTApaPGAPDRLRFAFASCQNYEGGYFT--AYRAMAEEDPDFVLHLGDYIY 172
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
117-191 7.64e-03

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 37.59  E-value: 7.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392921259 117 KVCVFGDLgywHGN--STESIIKHGLAGDFDFIVHLGDIAYDLHTNNGqvgdsylnVFEpLISKVPYMVIAGNHEDD 191
Cdd:COG0622    1 KIAVISDT---HGNlpALEAVLEDLEREGVDLIVHLGDLVGYGPDPPE--------VLD-LLRELPIVAVRGNHDGA 65
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 133-192 8.46e-03

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: 37.66  E-value: 8.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921259 133 ESIIKHGlagDFDFIVHLGDIAYDLHTNNGQVGDSYLNVFEPLIS-KVPYMVIAGNHeDDY 192
Cdd:cd07383   35 ESVLDEE---KPDLVVLTGDLITGENTADDNATSYLDKAVSPLVErGIPWAATFGNH-DGY 91
 
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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