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Conserved domains on  [gi|1190372198|ref|XP_020833939|]
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acid phosphatase type 7 [Phascolarctos cinereus]

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; ...
 244-543 3.24e-138

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: 402.06  E-value: 3.24e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 244 PNWSPRLAVFGDMGA---DNPQALPRLRRETqqGMYDVVLHVGDFAYNMDQDNARVGDTFMRLIEPVAASVPYMTCPGNH 320
Cdd:cd00839     1 PDTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 321 EERYNFSNYRARFSMP---------GDTEGLWYSWDLGPAHIISFSTEVYFYLHYgrhLIQKQFRWLERDLQKANNNRal 391
Cdd:cd00839    79 EADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 392 RPWIITMGHRPMYCSNADLDDCTQHESKirkglsgsRYGLEDLFYKYGVDLQLWAHEHSYERLWPIYDYQVYNGSrESPY 471
Cdd:cd00839   154 TPWIIVMGHRPMYCSNDDDADCIEGEKM--------REALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIY 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190372198 472 TNPRGPIHIITGSAGCEELL-TPFAPFPRPWSAIRVKEYGFTRLHILNSTHLHVQQVSdDQDGKIVDDVWLVR 543
Cdd:cd00839   225 TNPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 146-238 1.55e-17

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: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 146 PEQIHLSYPGEAGCMTVTWTTW-VPAASEVQFGLQlGGVLPLRAQGTSSPFVDGGflRRKLYMHRVTLRGLLPGVHYVYR 224
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 1190372198 225 CGSA-QGWSRRFRFR 238
Cdd:pfam16656  78 VGDDnGGWSEVYSFT 92
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 244-543 3.24e-138

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: 402.06  E-value: 3.24e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 244 PNWSPRLAVFGDMGA---DNPQALPRLRRETqqGMYDVVLHVGDFAYNMDQDNARVGDTFMRLIEPVAASVPYMTCPGNH 320
Cdd:cd00839     1 PDTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 321 EERYNFSNYRARFSMP---------GDTEGLWYSWDLGPAHIISFSTEVYFYLHYgrhLIQKQFRWLERDLQKANNNRal 391
Cdd:cd00839    79 EADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 392 RPWIITMGHRPMYCSNADLDDCTQHESKirkglsgsRYGLEDLFYKYGVDLQLWAHEHSYERLWPIYDYQVYNGSrESPY 471
Cdd:cd00839   154 TPWIIVMGHRPMYCSNDDDADCIEGEKM--------REALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIY 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190372198 472 TNPRGPIHIITGSAGCEELL-TPFAPFPRPWSAIRVKEYGFTRLHILNSTHLHVQQVSdDQDGKIVDDVWLVR 543
Cdd:cd00839   225 TNPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 146-541 2.12e-45

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 165.63  E-value: 2.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 146 PEQIHLSYPGeAGCMTVTWTTWVPAASEVQFGlQLGGVLPLRAQGTSSPFvDGGFLRRKLYMHRVTLRGLLPGVHYVYRC 225
Cdd:PLN02533   44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYG-TVSGKYEGSANGTSSSY-HYLLIYRSGQINDVVIGPLKPNTVYYYKC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 226 GSAQGwSRRFRFRalqSGPNWSP-RLAVFGDMGAD--NPQALPRLRRETqqgmYDVVLHVGDFAY-NMDQDnarVGDTFM 301
Cdd:PLN02533  121 GGPSS-TQEFSFR---TPPSKFPiKFAVSGDLGTSewTKSTLEHVSKWD----YDVFILPGDLSYaNFYQP---LWDTFG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 302 RLIEPVAASVPYMTCPGNHE-------ERYNFSNYRARFSMP----GDTEGLWYSWDLGPAHIISFSTevyfYLHYGRHl 370
Cdd:PLN02533  190 RLVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGS----YTDFEPG- 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 371 iQKQFRWLERDLQKAnnNRALRPWIITMGHRPMYCSNadlddcTQHESKirKGLSGSRYGLEDLFYKYGVDLQLWAHEHS 450
Cdd:PLN02533  265 -SEQYQWLENNLKKI--DRKTTPWVVAVVHAPWYNSN------EAHQGE--KESVGMKESMETLLYKARVDLVFAGHVHA 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 451 YERLwpiydYQVYNGSrespyTNPRGPIHIITGSAGCEELLTPFAPFPRP-WSAIRVKEYGFTRLHILNSTHLHVQ-QVS 528
Cdd:PLN02533  334 YERF-----DRVYQGK-----TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTwHRN 403

                         410
                  ....*....|...
gi 1190372198 529 DDQDGKIVDDVWL 541
Cdd:PLN02533  404 DDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
249-486 7.70e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 108.63  E-value: 7.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 249 RLAVFGDM------GADNPQALPRLRRETQQGMYDVVLHVGDFAYNMDQDNARVGDTFMRLIEpvaasVPYMTCPGNHEE 322
Cdd:COG1409     2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 323 RYNFS-NYRARFSMPgDTEGLWYSWDLGPAHIISFSTEVYfYLHYGrHLIQKQFRWLERDLQKANNNralrpWIITMGHR 401
Cdd:COG1409    77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP-GRSSG-ELGPEQLAWLEEELAAAPAK-----PVIVFLHH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 402 PMYCSNADLDdctqheskiRKGLSGSRYgLEDLFYKYGVDLQLWAHEHSYERlwpiydyqvyngsrespyTNPRGPIHII 481
Cdd:COG1409   149 PPYSTGSGSD---------RIGLRNAEE-LLALLARYGVDLVLSGHVHRYER------------------TRRDGVPYIV 200


                  ....*
gi 1190372198 482 TGSAG 486
Cdd:COG1409   201 AGSTG 205
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 476-537 1.03e-18

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: 79.88  E-value: 1.03e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1190372198 476 GPIHIITGSAGCEEllTPFAPFPRPWSAIRVKEYGFTRLHILNSTHLHVQQVSDDqDGKIVD 537
Cdd:pfam14008   1 APVHIVIGAAGNIE--GLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 146-238 1.55e-17

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: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 146 PEQIHLSYPGEAGCMTVTWTTW-VPAASEVQFGLQlGGVLPLRAQGTSSPFVDGGflRRKLYMHRVTLRGLLPGVHYVYR 224
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 1190372198 225 CGSA-QGWSRRFRFR 238
Cdd:pfam16656  78 VGDDnGGWSEVYSFT 92
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 244-543 3.24e-138

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: 402.06  E-value: 3.24e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 244 PNWSPRLAVFGDMGA---DNPQALPRLRRETqqGMYDVVLHVGDFAYNMDQDNARVGDTFMRLIEPVAASVPYMTCPGNH 320
Cdd:cd00839     1 PDTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 321 EERYNFSNYRARFSMP---------GDTEGLWYSWDLGPAHIISFSTEVYFYLHYgrhLIQKQFRWLERDLQKANNNRal 391
Cdd:cd00839    79 EADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 392 RPWIITMGHRPMYCSNADLDDCTQHESKirkglsgsRYGLEDLFYKYGVDLQLWAHEHSYERLWPIYDYQVYNGSrESPY 471
Cdd:cd00839   154 TPWIIVMGHRPMYCSNDDDADCIEGEKM--------REALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIY 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190372198 472 TNPRGPIHIITGSAGCEELL-TPFAPFPRPWSAIRVKEYGFTRLHILNSTHLHVQQVSdDQDGKIVDDVWLVR 543
Cdd:cd00839   225 TNPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 146-541 2.12e-45

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 165.63  E-value: 2.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 146 PEQIHLSYPGeAGCMTVTWTTWVPAASEVQFGlQLGGVLPLRAQGTSSPFvDGGFLRRKLYMHRVTLRGLLPGVHYVYRC 225
Cdd:PLN02533   44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYG-TVSGKYEGSANGTSSSY-HYLLIYRSGQINDVVIGPLKPNTVYYYKC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 226 GSAQGwSRRFRFRalqSGPNWSP-RLAVFGDMGAD--NPQALPRLRRETqqgmYDVVLHVGDFAY-NMDQDnarVGDTFM 301
Cdd:PLN02533  121 GGPSS-TQEFSFR---TPPSKFPiKFAVSGDLGTSewTKSTLEHVSKWD----YDVFILPGDLSYaNFYQP---LWDTFG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 302 RLIEPVAASVPYMTCPGNHE-------ERYNFSNYRARFSMP----GDTEGLWYSWDLGPAHIISFSTevyfYLHYGRHl 370
Cdd:PLN02533  190 RLVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGS----YTDFEPG- 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 371 iQKQFRWLERDLQKAnnNRALRPWIITMGHRPMYCSNadlddcTQHESKirKGLSGSRYGLEDLFYKYGVDLQLWAHEHS 450
Cdd:PLN02533  265 -SEQYQWLENNLKKI--DRKTTPWVVAVVHAPWYNSN------EAHQGE--KESVGMKESMETLLYKARVDLVFAGHVHA 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 451 YERLwpiydYQVYNGSrespyTNPRGPIHIITGSAGCEELLTPFAPFPRP-WSAIRVKEYGFTRLHILNSTHLHVQ-QVS 528
Cdd:PLN02533  334 YERF-----DRVYQGK-----TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTwHRN 403

                         410
                  ....*....|...
gi 1190372198 529 DDQDGKIVDDVWL 541
Cdd:PLN02533  404 DDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
249-486 7.70e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 108.63  E-value: 7.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 249 RLAVFGDM------GADNPQALPRLRRETQQGMYDVVLHVGDFAYNMDQDNARVGDTFMRLIEpvaasVPYMTCPGNHEE 322
Cdd:COG1409     2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 323 RYNFS-NYRARFSMPgDTEGLWYSWDLGPAHIISFSTEVYfYLHYGrHLIQKQFRWLERDLQKANNNralrpWIITMGHR 401
Cdd:COG1409    77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP-GRSSG-ELGPEQLAWLEEELAAAPAK-----PVIVFLHH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 402 PMYCSNADLDdctqheskiRKGLSGSRYgLEDLFYKYGVDLQLWAHEHSYERlwpiydyqvyngsrespyTNPRGPIHII 481
Cdd:COG1409   149 PPYSTGSGSD---------RIGLRNAEE-LLALLARYGVDLVLSGHVHRYER------------------TRRDGVPYIV 200


                  ....*
gi 1190372198 482 TGSAG 486
Cdd:COG1409   201 AGSTG 205
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 476-537 1.03e-18

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: 79.88  E-value: 1.03e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1190372198 476 GPIHIITGSAGCEEllTPFAPFPRPWSAIRVKEYGFTRLHILNSTHLHVQQVSDDqDGKIVD 537
Cdd:pfam14008   1 APVHIVIGAAGNIE--GLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 146-238 1.55e-17

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: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 146 PEQIHLSYPGEAGCMTVTWTTW-VPAASEVQFGLQlGGVLPLRAQGTSSPFVDGGflRRKLYMHRVTLRGLLPGVHYVYR 224
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 1190372198 225 CGSA-QGWSRRFRFR 238
Cdd:pfam16656  78 VGDDnGGWSEVYSFT 92
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 249-355 1.19e-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: 56.07  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 249 RLAVFGDMG-----ADNPQALPRLRRETQqgmYDVVLHVGDFAYNMDQDnarvgDTFMRLIEPVAASVPYMTCPGNHE-- 321
Cdd:pfam00149   2 RILVIGDLHlpgqlDDLLELLKKLLEEGK---PDLVLHAGDLVDRGPPS-----EEVLELLERLIKYVPVYLVRGNHDfd 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1190372198 322 --ERYNFSNYRARFSMPGDTEGLWYSWdLGPAHIIS 355
Cdd:pfam00149  74 ygECLRLYPYLGLLARPWKRFLEVFNF-LPLAGILS 108
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 262-411 5.54e-07

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: 50.74  E-value: 5.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 262 QALPRLRREtqQGMYDVVLHVGDFAynmdqDNARVG--DTFMRLIEPVAAsvPYMTCPGNHEERYNFSNYRARfSMPGDT 339
Cdd:cd07402    28 AAVAQVNAL--HPRPDLVVVTGDLS-----DDGSPEsyERLRELLAPLPA--PVYWIPGNHDDRAAMREALPE-PPYDDN 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1190372198 340 EGLWYSWDLGPAHIISFSTEVYFYLHYgrHLIQKQFRWLERDLQKANNnralRPWIITMGHRPMYCSNADLD 411
Cdd:cd07402    98 GPVQYVVDFGGWRLILLDTSVPGVHHG--ELSDEQLDWLEAALAEAPD----RPTLIFLHHPPFPLGIPWMD 163
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 311-519 4.96e-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: 42.31  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 311 VPYMTCPGNHEERYNFS-----NYRARFS---MPGdtegLWY--SWDLGP----AHIISFSTEV----YFYLHYGRH--- 369
Cdd:cd07378    75 VPWYLVLGNHDHRGNVSaqiayTQRPNSKrwnFPN----YYYdiSFKFPSsdvtVAFIMIDTVLlcgnTDDEASGQPrgp 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 370 ----LIQKQFRWLERDLQKANNNralrpWIITMGHRPMY--CSNADlDDCTQHEskirkglsgsrygLEDLFYKYGVDLQ 443
Cdd:cd07378   151 pnkkLAETQLAWLEKQLAASKAD-----YKIVVGHYPIYssGEHGP-TKCLVDI-------------LLPLLKKYKVDAY 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 444 LWAHEHSYERLwpiydyqvyngsRESPYTNprgpiHIITGSAGCEELLTPFAP-----FPRPWSAIRVKEYGFTRLHILN 518
Cdd:cd07378   212 LSGHDHNLQHI------------VDESGTY-----YVISGAGSKADPSDIHRDkvpqgYLLFFSGFYSSGGGFAYLEITS 274


                  .
gi 1190372198 519 S 519
Cdd:cd07378   275 S 275
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 262-409 8.44e-04

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 41.16  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 262 QALPRLRRE----TQQGMYDVVLHVGDFaynMDQDNARvgDTFMRLIEPV-----AASVPYMTCPGNHEeRYNFS-NYRA 331
Cdd:cd07396    29 NSLGVLERAveewNRESNLAFVVQLGDI---IDGYNAK--DRSKEALDAVlsildRLKGPVHHVLGNHE-FYNFPrEYLN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190372198 332 RFSMPGDTEGLWYSWDLGPahiiSFSTEVYFYLHYGRHLIQKQFRWLERDLQ--KANNNRalrpwIITMGHRPMYCSNAD 409
Cdd:cd07396   103 HLKTLNGEDAYYYSFSPGP----GFRFLVLDFVKFNGGIGEEQLAWLRNELTsaDANGEK-----VIVLSHLPIYPEAAD 173
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 251-321 4.27e-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: 37.63  E-value: 4.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190372198 251 AVFGD--MGADNPQALPRLRRETQQGmYDVVLHVGDFAYNMDQDNarvgDTFMRLIEPVAASVPYMTCPGNHE 321
Cdd:cd00838     1 LVISDihGNLEALEAVLEAALAKAEK-PDLVICLGDLVDYGPDPE----EVELKALRLLLAGIPVYVVPGNHD 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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