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Conserved domains on  [gi|15227205|ref|NP_179235|]
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purple acid phosphatase 10 [Arabidopsis thaliana]

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; ...
 156-454 6.24e-111

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: 329.64  E-value: 6.24e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 156 PDVPYTFGLIGDLGQS-YDSNITLTHYENNPTKGQAVLFVGDISYADTYPDhdNRRWDSWGRFAERSTAYQPWIWTTGNH 234
Cdd:cd00839   1 PDTPLKFAVFGDMGQNtNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 235 ELDFAPEIGENRPFKPFthrYRTPYRSSGSTEPFWYSIKRGPAYIIVLASYSAYGKY---TPQYQWLEEEFPKVNRTETP 311
Cdd:cd00839  79 EADYNGSTSKIKFFMPG---RGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGdniSPQYDWLEADLAKVDRSRTP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 312 WLIVLMHSPWYNSYDY--HYMEGETMRVMYEAWFVKYKVDVVFAGHVHAYERSERVSNiaYNVVNGICTPVKDQSAPVYI 389
Cdd:cd00839 156 WIIVMGHRPMYCSNDDdaDCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHI 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227205 390 TIGDGGNIEGLATKMTEPQPKYSAFREASFGHAIFSIKNRTHAHYGWHRNHDGyaVEGDRMWFYN 454
Cdd:cd00839 234 VIGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDG--QVADSFWIVK 296
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 59-150 1.23e-15

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: 72.06  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205    59 PQQVHITQGDVEGkAVIVSWVTQEAKGSNKVIYWKENSTKKHKAHGKTNTYKFYNYTSGFIHHCPIRNLEYDTKYYYVLG 138
Cdd:pfam16656   1 PEQVHLSLTGDST-SMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|...
gi 15227205   139 VGQTERKFWF-FT 150
Cdd:pfam16656  80 DDNGGWSEVYsFT 92
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 156-454 6.24e-111

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: 329.64  E-value: 6.24e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 156 PDVPYTFGLIGDLGQS-YDSNITLTHYENNPTKGQAVLFVGDISYADTYPDhdNRRWDSWGRFAERSTAYQPWIWTTGNH 234
Cdd:cd00839   1 PDTPLKFAVFGDMGQNtNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 235 ELDFAPEIGENRPFKPFthrYRTPYRSSGSTEPFWYSIKRGPAYIIVLASYSAYGKY---TPQYQWLEEEFPKVNRTETP 311
Cdd:cd00839  79 EADYNGSTSKIKFFMPG---RGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGdniSPQYDWLEADLAKVDRSRTP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 312 WLIVLMHSPWYNSYDY--HYMEGETMRVMYEAWFVKYKVDVVFAGHVHAYERSERVSNiaYNVVNGICTPVKDQSAPVYI 389
Cdd:cd00839 156 WIIVMGHRPMYCSNDDdaDCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHI 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227205 390 TIGDGGNIEGLATKMTEPQPKYSAFREASFGHAIFSIKNRTHAHYGWHRNHDGyaVEGDRMWFYN 454
Cdd:cd00839 234 VIGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDG--QVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 59-451 5.12e-96

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 296.21  E-value: 5.12e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205   59 PQQVHITQgdVEGKAVIVSWVTQEAKgSNKVIYWKENSTKKHKAHGKTNTYKFY-NYTSGFIHHCPIRNLEYDTKYYYVL 137
Cdd:PLN02533  44 PDQVHISL--VGPDKMRISWITQDSI-PPSVVYGTVSGKYEGSANGTSSSYHYLlIYRSGQINDVVIGPLKPNTVYYYKC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205  138 GVGQTERKFWFFTPPEigpDVPYTFGLIGDLGQSYDSNITLTHYennpTKGQAVLFV--GDISYADTYpdhdNRRWDSWG 215
Cdd:PLN02533 121 GGPSSTQEFSFRTPPS---KFPIKFAVSGDLGTSEWTKSTLEHV----SKWDYDVFIlpGDLSYANFY----QPLWDTFG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205  216 RFAERSTAYQPWIWTTGNHELDFAPEIGENrPFKPFTHRYRTPYRSSGSTEPFWYSIKRGPAYIIVLASYSAYGKYTPQY 295
Cdd:PLN02533 190 RLVQPLASQRPWMVTHGNHELEKIPILHPE-KFTAYNARWRMPFEESGSTSNLYYSFNVYGVHIIMLGSYTDFEPGSEQY 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205  296 QWLEEEFPKVNRTETPWLIVLMHSPWYNSYDYHYMEGET--MRVMYEAWFVKYKVDVVFAGHVHAYERSERVSNIAYnvv 373
Cdd:PLN02533 269 QWLENNLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESvgMKESMETLLYKARVDLVFAGHVHAYERFDRVYQGKT--- 345

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227205  374 ngictpvkDQSAPVYITIGDGGNIEGLATKMTEPQPKYSAFREASFGHAIFSIKNRTHAHYGWHRNHDGYAVEGDRMW 451
Cdd:PLN02533 346 --------DKCGPVYITIGDGGNREGLATKYIDPKPDISLFREASFGHGQLNVVDANTMEWTWHRNDDDQSVASDSVW 415
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
190-395 1.23e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 87.82  E-value: 1.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 190 AVLFVGDISYADTYpdhdnrrwDSWGRFAER-STAYQPWIWTTGNHELDFApeigenrpfkpFTHRYRTPYRSsGSTEPF 268
Cdd:COG1409  37 FVVVTGDLTDDGEP--------EEYAAAREIlARLGVPVYVVPGNHDIRAA-----------MAEAYREYFGD-LPPGGL 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 269 WYSIKRGPAYIIVLAS---YSAYGKYTP-QYQWLEEEFpkvNRTETPWLIVLMHSPWYNSYDYHYMEGETMRVMYEAWFV 344
Cdd:COG1409  97 YYSFDYGGVRFIGLDSnvpGRSSGELGPeQLAWLEEEL---AAAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEELLALLA 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15227205 345 KYKVDVVFAGHVHAYERSERVsNIAYNVVNGICTPVKDQSAPVYITIGDGG 395
Cdd:COG1409 174 RYGVDLVLSGHVHRYERTRRD-GVPYIVAGSTGGQVRLPPGYRVIEVDGDG 223
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 385-442 2.35e-19

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: 81.42  E-value: 2.35e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15227205   385 APVYITIGDGGNIEGLatkMTEPQPKYSAFREASFGHAIFSIKNRTHAHYGWHRNHDG 442
Cdd:pfam14008   1 APVHIVIGAAGNIEGL---FVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSDDG 55
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 59-150 1.23e-15

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: 72.06  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205    59 PQQVHITQGDVEGkAVIVSWVTQEAKGSNKVIYWKENSTKKHKAHGKTNTYKFYNYTSGFIHHCPIRNLEYDTKYYYVLG 138
Cdd:pfam16656   1 PEQVHLSLTGDST-SMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|...
gi 15227205   139 VGQTERKFWF-FT 150
Cdd:pfam16656  80 DDNGGWSEVYsFT 92
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 156-454 6.24e-111

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: 329.64  E-value: 6.24e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 156 PDVPYTFGLIGDLGQS-YDSNITLTHYENNPTKGQAVLFVGDISYADTYPDhdNRRWDSWGRFAERSTAYQPWIWTTGNH 234
Cdd:cd00839   1 PDTPLKFAVFGDMGQNtNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 235 ELDFAPEIGENRPFKPFthrYRTPYRSSGSTEPFWYSIKRGPAYIIVLASYSAYGKY---TPQYQWLEEEFPKVNRTETP 311
Cdd:cd00839  79 EADYNGSTSKIKFFMPG---RGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGdniSPQYDWLEADLAKVDRSRTP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 312 WLIVLMHSPWYNSYDY--HYMEGETMRVMYEAWFVKYKVDVVFAGHVHAYERSERVSNiaYNVVNGICTPVKDQSAPVYI 389
Cdd:cd00839 156 WIIVMGHRPMYCSNDDdaDCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHI 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227205 390 TIGDGGNIEGLATKMTEPQPKYSAFREASFGHAIFSIKNRTHAHYGWHRNHDGyaVEGDRMWFYN 454
Cdd:cd00839 234 VIGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDG--QVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 59-451 5.12e-96

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 296.21  E-value: 5.12e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205   59 PQQVHITQgdVEGKAVIVSWVTQEAKgSNKVIYWKENSTKKHKAHGKTNTYKFY-NYTSGFIHHCPIRNLEYDTKYYYVL 137
Cdd:PLN02533  44 PDQVHISL--VGPDKMRISWITQDSI-PPSVVYGTVSGKYEGSANGTSSSYHYLlIYRSGQINDVVIGPLKPNTVYYYKC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205  138 GVGQTERKFWFFTPPEigpDVPYTFGLIGDLGQSYDSNITLTHYennpTKGQAVLFV--GDISYADTYpdhdNRRWDSWG 215
Cdd:PLN02533 121 GGPSSTQEFSFRTPPS---KFPIKFAVSGDLGTSEWTKSTLEHV----SKWDYDVFIlpGDLSYANFY----QPLWDTFG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205  216 RFAERSTAYQPWIWTTGNHELDFAPEIGENrPFKPFTHRYRTPYRSSGSTEPFWYSIKRGPAYIIVLASYSAYGKYTPQY 295
Cdd:PLN02533 190 RLVQPLASQRPWMVTHGNHELEKIPILHPE-KFTAYNARWRMPFEESGSTSNLYYSFNVYGVHIIMLGSYTDFEPGSEQY 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205  296 QWLEEEFPKVNRTETPWLIVLMHSPWYNSYDYHYMEGET--MRVMYEAWFVKYKVDVVFAGHVHAYERSERVSNIAYnvv 373
Cdd:PLN02533 269 QWLENNLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESvgMKESMETLLYKARVDLVFAGHVHAYERFDRVYQGKT--- 345

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227205  374 ngictpvkDQSAPVYITIGDGGNIEGLATKMTEPQPKYSAFREASFGHAIFSIKNRTHAHYGWHRNHDGYAVEGDRMW 451
Cdd:PLN02533 346 --------DKCGPVYITIGDGGNREGLATKYIDPKPDISLFREASFGHGQLNVVDANTMEWTWHRNDDDQSVASDSVW 415
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
190-395 1.23e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 87.82  E-value: 1.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 190 AVLFVGDISYADTYpdhdnrrwDSWGRFAER-STAYQPWIWTTGNHELDFApeigenrpfkpFTHRYRTPYRSsGSTEPF 268
Cdd:COG1409  37 FVVVTGDLTDDGEP--------EEYAAAREIlARLGVPVYVVPGNHDIRAA-----------MAEAYREYFGD-LPPGGL 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 269 WYSIKRGPAYIIVLAS---YSAYGKYTP-QYQWLEEEFpkvNRTETPWLIVLMHSPWYNSYDYHYMEGETMRVMYEAWFV 344
Cdd:COG1409  97 YYSFDYGGVRFIGLDSnvpGRSSGELGPeQLAWLEEEL---AAAPAKPVIVFLHHPPYSTGSGSDRIGLRNAEELLALLA 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15227205 345 KYKVDVVFAGHVHAYERSERVsNIAYNVVNGICTPVKDQSAPVYITIGDGG 395
Cdd:COG1409 174 RYGVDLVLSGHVHRYERTRRD-GVPYIVAGSTGGQVRLPPGYRVIEVDGDG 223
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 385-442 2.35e-19

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: 81.42  E-value: 2.35e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15227205   385 APVYITIGDGGNIEGLatkMTEPQPKYSAFREASFGHAIFSIKNRTHAHYGWHRNHDG 442
Cdd:pfam14008   1 APVHIVIGAAGNIEGL---FVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSDDG 55
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 59-150 1.23e-15

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: 72.06  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205    59 PQQVHITQGDVEGkAVIVSWVTQEAKGSNKVIYWKENSTKKHKAHGKTNTYKFYNYTSGFIHHCPIRNLEYDTKYYYVLG 138
Cdd:pfam16656   1 PEQVHLSLTGDST-SMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|...
gi 15227205   139 VGQTERKFWF-FT 150
Cdd:pfam16656  80 DDNGGWSEVYsFT 92
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 160-272 1.27e-07

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 49.90  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205   160 YTFGLIGDLG--QSYDSNITLTHYENNPTKGQAVLFVGDISyadtypdHDNRRWDSWGRFAERSTAYQPWIWTTGNHELD 237
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLV-------DRGPPSEEVLELLERLIKYVPVYLVRGNHDFD 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15227205   238 FapeiGENRPFKPFTHRYRTPYRSSGSTEPFWYSI 272
Cdd:pfam00149  74 Y----GECLRLYPYLGLLARPWKRFLEVFNFLPLA 104
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 273-375 3.34e-06

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: 46.49  E-value: 3.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 273 KRGPAYIIVLASYSAYGkytPQYQWLEEEFPKVNRTETPWL-------IVLMHSPWYNSYDYHYMEGETMRVMYEAWFVK 345
Cdd:cd00838  24 AEKPDLVICLGDLVDYG---PDPEEVELKALRLLLAGIPVYvvpgnhdILVTHGPPYDPLDEGSPGEDPGSEALLELLDK 100

                        90       100       110
                ....*....|....*....|....*....|
gi 15227205 346 YKVDVVFAGHVHAYERSERVSNIAYNVVNG 375
Cdd:cd00838 101 YGPDLVLSGHTHVPGRREVDKGGTLVVNPG 130
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 190-395 2.12e-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: 39.57  E-value: 2.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 190 AVLFVGDISyadtypdHDNRRwDSWGRFAERSTAYQ-PWIWTTGNHelDFAPEIgenRPFKPfthryRTPYRSSGSTEpf 268
Cdd:cd07402  42 LVVVTGDLS-------DDGSP-ESYERLRELLAPLPaPVYWIPGNH--DDRAAM---REALP-----EPPYDDNGPVQ-- 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227205 269 wYSIKRGPAYIIVLASY---SAYGKYTP-QYQWLEEEFPkvNRTETPWLIVLMHSPWYNSYDYHYMEG-----ETMRVMY 339
Cdd:cd07402 102 -YVVDFGGWRLILLDTSvpgVHHGELSDeQLDWLEAALA--EAPDRPTLIFLHHPPFPLGIPWMDAIRlrnsqALFAVLA 178

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15227205 340 EAWFVKYkvdvVFAGHVHaYERSERVSNIAYNVVNGICTPVK---DQSAPVYITIGDGG 395
Cdd:cd07402 179 RHPQVKA----ILCGHIH-RPISGSFRGIPFSTAPSTCHQFAldlDDFALDAEAPGPRN 232
 
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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