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Conserved domains on  [gi|768009236|ref|XP_011525271|]
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acid phosphatase type 7 isoform X4 [Homo sapiens]

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; ...
 131-269 1.34e-56

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: 186.74  E-value: 1.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 131 HWSPRLAVFGDLGA---DNPKAVPRLRRDTqqGMYDAVLHVGDFAYNLDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 207
Cdd:cd00839    2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768009236 208 ERYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLVQRQFRWLESDLQ 269
Cdd:cd00839   80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLA 147
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 32-124 2.29e-12

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: 62.43  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236   32 PEQVHLSYPGEPGSMTVT-WTTWVPTRSEVQFGLQPSGpLPLRAQGTFVPFVDGGilRRKLYIHRVTLRKLLPGVQYVYR 110
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSwVTPSAVTSPVVQYGTSSSA-LTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 768009236  111 CGSA-QGWSRRFRFR 124
Cdd:pfam16656  78 VGDDnGGWSEVYSFT 92
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 131-269 1.34e-56

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: 186.74  E-value: 1.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 131 HWSPRLAVFGDLGA---DNPKAVPRLRRDTqqGMYDAVLHVGDFAYNLDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 207
Cdd:cd00839    2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768009236 208 ERYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLVQRQFRWLESDLQ 269
Cdd:cd00839   80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLA 147
PLN02533 PLN02533
probable purple acid phosphatase
 32-307 2.10e-19

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 88.97  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236  32 PEQVHLSYPGePGSMTVTWTTWVPTRSEVQFGlQPSGPLPLRAQGTFVPFvDGGILRRKLYIHRVTLRKLLPGVQYVYRC 111
Cdd:PLN02533  44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYG-TVSGKYEGSANGTSSSY-HYLLIYRSGQINDVVIGPLKPNTVYYYKC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 112 GSAQGwSRRFRFRALKngAHWSPRLAVFGDLGADnpKAVPRLRRDTQQGMYDAVLHVGDFAY-NLDQDnarVGDRFMRLI 190
Cdd:PLN02533 121 GGPSS-TQEFSFRTPP--SKFPIKFAVSGDLGTS--EWTKSTLEHVSKWDYDVFILPGDLSYaNFYQP---LWDTFGRLV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 191 EPVAASLPYMTCPGNHE-------ERYNFSNYKARFSMP----GDNEGLWYSWDLGPAHIISFSTEVYFflhygrHLVQR 259
Cdd:PLN02533 193 QPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGSYTDF------EPGSE 266

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 768009236 260 QFRWLESDLQPIrtgqpGRGSSLWGTGPCTAPTQIWTTAHDMKARSAK 307
Cdd:PLN02533 267 QYQWLENNLKKI-----DRKTTPWVVAVVHAPWYNSNEAHQGEKESVG 309
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
135-269 2.19e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 77.42  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 135 RLAVFGDL------GADNPKAVPRLRRDTQQGMYDAVLHVGDFAYNLDQDNARVGDRFMRLIEpvaasLPYMTCPGNHEE 208
Cdd:COG1409    2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768009236 209 RYNFS-NYKARFSMPgDNEGLWYSWDLGPAHIISFSTEVYffLHYGRHLVQRQFRWLESDLQ 269
Cdd:COG1409   77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP--GRSSGELGPEQLAWLEEELA 135
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 32-124 2.29e-12

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: 62.43  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236   32 PEQVHLSYPGEPGSMTVT-WTTWVPTRSEVQFGLQPSGpLPLRAQGTFVPFVDGGilRRKLYIHRVTLRKLLPGVQYVYR 110
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSwVTPSAVTSPVVQYGTSSSA-LTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 768009236  111 CGSA-QGWSRRFRFR 124
Cdd:pfam16656  78 VGDDnGGWSEVYSFT 92
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 135-241 1.51e-09

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: 55.30  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236  135 RLAVFGDLG-----ADNPKAVPRLRRDTQqgmYDAVLHVGDFAynldqDNARVGDRFMRLIEPVAASLPYMTCPGNHE-- 207
Cdd:pfam00149   2 RILVIGDLHlpgqlDDLLELLKKLLEEGK---PDLVLHAGDLV-----DRGPPSEEVLELLERLIKYVPVYLVRGNHDfd 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 768009236  208 --ERYNFSNYKARFSMPGDNEGLWYSWdLGPAHIIS 241
Cdd:pfam00149  74 ygECLRLYPYLGLLARPWKRFLEVFNF-LPLAGILS 108
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 131-269 1.34e-56

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: 186.74  E-value: 1.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 131 HWSPRLAVFGDLGA---DNPKAVPRLRRDTqqGMYDAVLHVGDFAYNLDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 207
Cdd:cd00839    2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768009236 208 ERYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLVQRQFRWLESDLQ 269
Cdd:cd00839   80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLA 147
PLN02533 PLN02533
probable purple acid phosphatase
 32-307 2.10e-19

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 88.97  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236  32 PEQVHLSYPGePGSMTVTWTTWVPTRSEVQFGlQPSGPLPLRAQGTFVPFvDGGILRRKLYIHRVTLRKLLPGVQYVYRC 111
Cdd:PLN02533  44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYG-TVSGKYEGSANGTSSSY-HYLLIYRSGQINDVVIGPLKPNTVYYYKC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 112 GSAQGwSRRFRFRALKngAHWSPRLAVFGDLGADnpKAVPRLRRDTQQGMYDAVLHVGDFAY-NLDQDnarVGDRFMRLI 190
Cdd:PLN02533 121 GGPSS-TQEFSFRTPP--SKFPIKFAVSGDLGTS--EWTKSTLEHVSKWDYDVFILPGDLSYaNFYQP---LWDTFGRLV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 191 EPVAASLPYMTCPGNHE-------ERYNFSNYKARFSMP----GDNEGLWYSWDLGPAHIISFSTEVYFflhygrHLVQR 259
Cdd:PLN02533 193 QPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGSYTDF------EPGSE 266

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 768009236 260 QFRWLESDLQPIrtgqpGRGSSLWGTGPCTAPTQIWTTAHDMKARSAK 307
Cdd:PLN02533 267 QYQWLENNLKKI-----DRKTTPWVVAVVHAPWYNSNEAHQGEKESVG 309
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
135-269 2.19e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 77.42  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 135 RLAVFGDL------GADNPKAVPRLRRDTQQGMYDAVLHVGDFAYNLDQDNARVGDRFMRLIEpvaasLPYMTCPGNHEE 208
Cdd:COG1409    2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768009236 209 RYNFS-NYKARFSMPgDNEGLWYSWDLGPAHIISFSTEVYffLHYGRHLVQRQFRWLESDLQ 269
Cdd:COG1409   77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP--GRSSGELGPEQLAWLEEELA 135
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 32-124 2.29e-12

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: 62.43  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236   32 PEQVHLSYPGEPGSMTVT-WTTWVPTRSEVQFGLQPSGpLPLRAQGTFVPFVDGGilRRKLYIHRVTLRKLLPGVQYVYR 110
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSwVTPSAVTSPVVQYGTSSSA-LTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 768009236  111 CGSA-QGWSRRFRFR 124
Cdd:pfam16656  78 VGDDnGGWSEVYSFT 92
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 135-241 1.51e-09

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: 55.30  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236  135 RLAVFGDLG-----ADNPKAVPRLRRDTQqgmYDAVLHVGDFAynldqDNARVGDRFMRLIEPVAASLPYMTCPGNHE-- 207
Cdd:pfam00149   2 RILVIGDLHlpgqlDDLLELLKKLLEEGK---PDLVLHAGDLV-----DRGPPSEEVLELLERLIKYVPVYLVRGNHDfd 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 768009236  208 --ERYNFSNYKARFSMPGDNEGLWYSWdLGPAHIIS 241
Cdd:pfam00149  74 ygECLRLYPYLGLLARPWKRFLEVFNF-LPLAGILS 108
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 163-268 1.69e-05

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: 45.73  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009236 163 DAVLHVGDFAynldqDNARVG--DRFMRLIEPVAAslPYMTCPGNHEERYNFsnYKARFSMP-GDNEGLWYSWDLGPAHI 239
Cdd:cd07402   41 DLVVVTGDLS-----DDGSPEsyERLRELLAPLPA--PVYWIPGNHDDRAAM--REALPEPPyDDNGPVQYVVDFGGWRL 111

                         90       100
                 ....*....|....*....|....*....
gi 768009236 240 ISFSTEVYFFLHYgrHLVQRQFRWLESDL 268
Cdd:cd07402  112 ILLDTSVPGVHHG--ELSDEQLDWLEAAL 138
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 137-207 1.24e-03

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: 38.79  E-value: 1.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768009236 137 AVFGDL--GADNPKAVPRLRRDTQQGmYDAVLHVGDFAYNlDQDNARVGDRFMRLIepvAASLPYMTCPGNHE 207
Cdd:cd00838    1 LVISDIhgNLEALEAVLEAALAKAEK-PDLVICLGDLVDY-GPDPEEVELKALRLL---LAGIPVYVVPGNHD 68
 
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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