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Conserved domains on  [gi|186503429|ref|NP_180287|]
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purple acid phosphatase 12 [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; ...
 157-455 7.67e-114

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: 336.96  E-value: 7.67e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 157 PDVPYTFGLIGDLGQ-TYDSNSTLSHYEMNPGKGQAVLFVGDLSYADRYPNhdNNRWDTWGRFVERSVAYQPWIWTAGNH 235
Cdd:cd00839    1 PDTPLKFAVFGDMGQnTNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 236 EIDFVPDIGEIepfKPFMNRYHTPHKASGSISPLWYSIKRASAYIIVMSCYSSYG---IYTPQYKWLEKELQGVNRTETP 312
Cdd:cd00839   79 EADYNGSTSKI---KFFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLkgdNISPQYDWLEADLAKVDRSRTP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 313 WLIVLVHSPFYSSYV--HHYMEGETLRVMYEQWFVKYKVDVVFAGHVHAYERSERVSNiaYNIVNGLCEPISDESAPIYI 390
Cdd:cd00839  156 WIIVMGHRPMYCSNDddADCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHI 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186503429 391 TIGDGGNSEGLLTDMMQPQPKYSAFREASFGHGLLEIKNRTHAYFSWNRNQDGnaVAADSVWLLN 455
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 ...
 60-149 7.81e-21

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: 86.69  E-value: 7.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429   60 PQQVHVTQGNHEgNGVIISWVTPVKPGSKTVQYWCENEKSRKQAEATVNTYRFFNYTSGYIHHCLIDDLEFDTKYYYEIG 139
Cdd:pfam16656   1 PEQVHLSLTGDS-TSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|..
gi 186503429  140 SGK--WSRRFWF 149
Cdd:pfam16656  80 DDNggWSEVYSF 91
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 157-455 7.67e-114

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: 336.96  E-value: 7.67e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 157 PDVPYTFGLIGDLGQ-TYDSNSTLSHYEMNPGKGQAVLFVGDLSYADRYPNhdNNRWDTWGRFVERSVAYQPWIWTAGNH 235
Cdd:cd00839    1 PDTPLKFAVFGDMGQnTNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 236 EIDFVPDIGEIepfKPFMNRYHTPHKASGSISPLWYSIKRASAYIIVMSCYSSYG---IYTPQYKWLEKELQGVNRTETP 312
Cdd:cd00839   79 EADYNGSTSKI---KFFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLkgdNISPQYDWLEADLAKVDRSRTP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 313 WLIVLVHSPFYSSYV--HHYMEGETLRVMYEQWFVKYKVDVVFAGHVHAYERSERVSNiaYNIVNGLCEPISDESAPIYI 390
Cdd:cd00839  156 WIIVMGHRPMYCSNDddADCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHI 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186503429 391 TIGDGGNSEGLLTDMMQPQPKYSAFREASFGHGLLEIKNRTHAYFSWNRNQDGnaVAADSVWLLN 455
Cdd:cd00839  234 VIGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDG--QVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 57-453 8.98e-92

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 285.04  E-value: 8.98e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429  57 PNSPQQVHVTQGNheGNGVIISWVTPVKPgSKTVQYWCENEKSRKQAEATVNTYRFF-NYTSGYIHHCLIDDLEFDTKYY 135
Cdd:PLN02533  41 PTHPDQVHISLVG--PDKMRISWITQDSI-PPSVVYGTVSGKYEGSANGTSSSYHYLlIYRSGQINDVVIGPLKPNTVYY 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 136 YEIGSGKWSRRFWFFIPPKSgpdVPYTFGLIGDLGQTYDSNSTLSHyeMNPGKGQAVLFVGDLSYADRYpnhdNNRWDTW 215
Cdd:PLN02533 118 YKCGGPSSTQEFSFRTPPSK---FPIKFAVSGDLGTSEWTKSTLEH--VSKWDYDVFILPGDLSYANFY----QPLWDTF 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 216 GRFVERSVAYQPWIWTAGNHEIDFVPdIGEIEPFKPFMNRYHTPHKASGSISPLWYSIKRASAYIIVMSCYSSYGIYTPQ 295
Cdd:PLN02533 189 GRLVQPLASQRPWMVTHGNHELEKIP-ILHPEKFTAYNARWRMPFEESGSTSNLYYSFNVYGVHIIMLGSYTDFEPGSEQ 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 296 YKWLEKELQGVNRTETPWLIVLVHSPFYSSYVHHYMEGET--LRVMYEQWFVKYKVDVVFAGHVHAYERSERVSNIAYni 373
Cdd:PLN02533 268 YQWLENNLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESvgMKESMETLLYKARVDLVFAGHVHAYERFDRVYQGKT-- 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 374 vnglcepisDESAPIYITIGDGGNSEGLLTDMMQPQPKYSAFREASFGHGLLEIKNRTHAYFSWNRNQDGNAVAADSVWL 453
Cdd:PLN02533 346 ---------DKCGPVYITIGDGGNREGLATKYIDPKPDISLFREASFGHGQLNVVDANTMEWTWHRNDDDQSVASDSVWL 416
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 60-149 7.81e-21

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: 86.69  E-value: 7.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429   60 PQQVHVTQGNHEgNGVIISWVTPVKPGSKTVQYWCENEKSRKQAEATVNTYRFFNYTSGYIHHCLIDDLEFDTKYYYEIG 139
Cdd:pfam16656   1 PEQVHLSLTGDS-TSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|..
gi 186503429  140 SGK--WSRRFWF 149
Cdd:pfam16656  80 DDNggWSEVYSF 91
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 386-443 5.96e-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: 80.26  E-value: 5.96e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 186503429  386 APIYITIGDGGNSEGLLTdmmQPQPKYSAFREASFGHGLLEIKNRTHAYFSWNRNQDG 443
Cdd:pfam14008   1 APVHIVIGAAGNIEGLFV---PPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSDDG 55
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
161-396 4.36e-17

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 80.12  E-value: 4.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 161 YTFGLIGDL----GQTYDSNSTLSHY--EMNPGKGQAVLFVGDLSYADRYPNhdnnrWDTWGRFVERsvAYQPWIWTAGN 234
Cdd:COG1409    1 FRFAHISDLhlgaPDGSDTAEVLAAAlaDINAPRPDFVVVTGDLTDDGEPEE-----YAAAREILAR--LGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 235 HEIDfvpdigeiepfkPFMNRYHTPHKASGSISPLWYSIKRASAYIIVMSC---YSSYGIYTP-QYKWLEKELQgvnRTE 310
Cdd:COG1409   74 HDIR------------AAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSnvpGRSSGELGPeQLAWLEEELA---AAP 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 311 TPWLIVLVHSPFYSSYVHHYMEGETLRVMYEQWFVKYKVDVVFAGHVHAYERSERVsNIAYNIVNGLCEPISDESAPIYI 390
Cdd:COG1409  139 AKPVIVFLHHPPYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYERTRRD-GVPYIVAGSTGGQVRLPPGYRVI 217


                 ....*.
gi 186503429 391 TIGDGG 396
Cdd:COG1409  218 EVDGDG 223
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 57-144 9.77e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 35.55  E-value: 9.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429  57 PNSPQQVHVTQGNHegNGVIISWVTPVKPGSKTVQYWCENEKSRKQAEATVNTyrffnyTSGYIHHCLIDDLEFDTKY-- 134
Cdd:cd00063    1 PSPPTNLRVTDVTS--TSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEV------TPGSETSYTLTGLKPGTEYef 72

                         90
                 ....*....|....
gi 186503429 135 ----YYEIGSGKWS 144
Cdd:cd00063   73 rvraVNGGGESPPS 86
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 157-455 7.67e-114

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: 336.96  E-value: 7.67e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 157 PDVPYTFGLIGDLGQ-TYDSNSTLSHYEMNPGKGQAVLFVGDLSYADRYPNhdNNRWDTWGRFVERSVAYQPWIWTAGNH 235
Cdd:cd00839    1 PDTPLKFAVFGDMGQnTNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 236 EIDFVPDIGEIepfKPFMNRYHTPHKASGSISPLWYSIKRASAYIIVMSCYSSYG---IYTPQYKWLEKELQGVNRTETP 312
Cdd:cd00839   79 EADYNGSTSKI---KFFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLkgdNISPQYDWLEADLAKVDRSRTP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 313 WLIVLVHSPFYSSYV--HHYMEGETLRVMYEQWFVKYKVDVVFAGHVHAYERSERVSNiaYNIVNGLCEPISDESAPIYI 390
Cdd:cd00839  156 WIIVMGHRPMYCSNDddADCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHI 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186503429 391 TIGDGGNSEGLLTDMMQPQPKYSAFREASFGHGLLEIKNRTHAYFSWNRNQDGnaVAADSVWLLN 455
Cdd:cd00839  234 VIGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDG--QVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 57-453 8.98e-92

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 285.04  E-value: 8.98e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429  57 PNSPQQVHVTQGNheGNGVIISWVTPVKPgSKTVQYWCENEKSRKQAEATVNTYRFF-NYTSGYIHHCLIDDLEFDTKYY 135
Cdd:PLN02533  41 PTHPDQVHISLVG--PDKMRISWITQDSI-PPSVVYGTVSGKYEGSANGTSSSYHYLlIYRSGQINDVVIGPLKPNTVYY 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 136 YEIGSGKWSRRFWFFIPPKSgpdVPYTFGLIGDLGQTYDSNSTLSHyeMNPGKGQAVLFVGDLSYADRYpnhdNNRWDTW 215
Cdd:PLN02533 118 YKCGGPSSTQEFSFRTPPSK---FPIKFAVSGDLGTSEWTKSTLEH--VSKWDYDVFILPGDLSYANFY----QPLWDTF 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 216 GRFVERSVAYQPWIWTAGNHEIDFVPdIGEIEPFKPFMNRYHTPHKASGSISPLWYSIKRASAYIIVMSCYSSYGIYTPQ 295
Cdd:PLN02533 189 GRLVQPLASQRPWMVTHGNHELEKIP-ILHPEKFTAYNARWRMPFEESGSTSNLYYSFNVYGVHIIMLGSYTDFEPGSEQ 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 296 YKWLEKELQGVNRTETPWLIVLVHSPFYSSYVHHYMEGET--LRVMYEQWFVKYKVDVVFAGHVHAYERSERVSNIAYni 373
Cdd:PLN02533 268 YQWLENNLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESvgMKESMETLLYKARVDLVFAGHVHAYERFDRVYQGKT-- 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 374 vnglcepisDESAPIYITIGDGGNSEGLLTDMMQPQPKYSAFREASFGHGLLEIKNRTHAYFSWNRNQDGNAVAADSVWL 453
Cdd:PLN02533 346 ---------DKCGPVYITIGDGGNREGLATKYIDPKPDISLFREASFGHGQLNVVDANTMEWTWHRNDDDQSVASDSVWL 416
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 60-149 7.81e-21

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: 86.69  E-value: 7.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429   60 PQQVHVTQGNHEgNGVIISWVTPVKPGSKTVQYWCENEKSRKQAEATVNTYRFFNYTSGYIHHCLIDDLEFDTKYYYEIG 139
Cdd:pfam16656   1 PEQVHLSLTGDS-TSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|..
gi 186503429  140 SGK--WSRRFWF 149
Cdd:pfam16656  80 DDNggWSEVYSF 91
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 386-443 5.96e-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: 80.26  E-value: 5.96e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 186503429  386 APIYITIGDGGNSEGLLTdmmQPQPKYSAFREASFGHGLLEIKNRTHAYFSWNRNQDG 443
Cdd:pfam14008   1 APVHIVIGAAGNIEGLFV---PPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSDDG 55
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
161-396 4.36e-17

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 80.12  E-value: 4.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 161 YTFGLIGDL----GQTYDSNSTLSHY--EMNPGKGQAVLFVGDLSYADRYPNhdnnrWDTWGRFVERsvAYQPWIWTAGN 234
Cdd:COG1409    1 FRFAHISDLhlgaPDGSDTAEVLAAAlaDINAPRPDFVVVTGDLTDDGEPEE-----YAAAREILAR--LGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 235 HEIDfvpdigeiepfkPFMNRYHTPHKASGSISPLWYSIKRASAYIIVMSC---YSSYGIYTP-QYKWLEKELQgvnRTE 310
Cdd:COG1409   74 HDIR------------AAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLDSnvpGRSSGELGPeQLAWLEEELA---AAP 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 311 TPWLIVLVHSPFYSSYVHHYMEGETLRVMYEQWFVKYKVDVVFAGHVHAYERSERVsNIAYNIVNGLCEPISDESAPIYI 390
Cdd:COG1409  139 AKPVIVFLHHPPYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYERTRRD-GVPYIVAGSTGGQVRLPPGYRVI 217


                 ....*.
gi 186503429 391 TIGDGG 396
Cdd:COG1409  218 EVDGDG 223
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 161-273 7.91e-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: 53.37  E-value: 7.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429  161 YTFGLIGDL---GQTYDSNSTLSHYEmNPGKGQAVLFVGDLSyadrypnHDNNRWDTWGRFVERSVAYQPWIWTAGNHEI 237
Cdd:pfam00149   1 MRILVIGDLhlpGQLDDLLELLKKLL-EEGKPDLVLHAGDLV-------DRGPPSEEVLELLERLIKYVPVYLVRGNHDF 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 186503429  238 DFvpdiGEIEPFKPFMNRYHTPHKASGSISPLWYSI 273
Cdd:pfam00149  73 DY----GECLRLYPYLGLLARPWKRFLEVFNFLPLA 104
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 315-376 7.16e-07

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: 48.42  E-value: 7.16e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186503429 315 IVLVHSPFYSSYVHHYMEGETLRVMYEQWFVKYKVDVVFAGHVHAYERSERVSNIAYNIVNG 376
Cdd:cd00838   69 ILVTHGPPYDPLDEGSPGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVVNPG 130
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 191-398 3.34e-06

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: 48.04  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 191 AVLFVGDLSyadrypnhDNNRWDTWGRFVERSVAYQ-PWIWTAGNHeiDFVPdigeiePFKPFMnryhtPHKASGSISPL 269
Cdd:cd07402   42 LVVVTGDLS--------DDGSPESYERLRELLAPLPaPVYWIPGNH--DDRA------AMREAL-----PEPPYDDNGPV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 270 WYSIKRASAYIIVM-SCYS--SYGIYTP-QYKWLEKELQgvNRTETPWLIVLVHSPFYSSyvHHYMEGETLRvmYEQWF- 344
Cdd:cd07402  101 QYVVDFGGWRLILLdTSVPgvHHGELSDeQLDWLEAALA--EAPDRPTLIFLHHPPFPLG--IPWMDAIRLR--NSQALf 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186503429 345 ---VKY-KVDVVFAGHVHaYERSERVSNIAYNIVNGLCEPI---SDESAPIYITIGDGGNS 398
Cdd:cd07402  175 avlARHpQVKAILCGHIH-RPISGSFRGIPFSTAPSTCHQFaldLDDFALDAEAPGPRNLL 234
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 161-380 5.70e-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: 45.01  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 161 YTFGLIGDLGQTYDSNST-----LSHY------EMNPgkgQAVLFVGDLSYADRYPNHDNNRWD-TWGRFVERSVAYQPW 228
Cdd:cd07378    1 LRFLVLGDWGGKPNPYTTaaqslVAKQmakvasKLGI---DFILSLGDNFYDDGVKDVDDPRFQeTFEDVYSAPSLQVPW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 229 IWTAGNHeiDFVPDI-GEIEPFK-PFMNRYHTPHkasgsispLWYSIK------RASAYIIV-----------------M 283
Cdd:cd07378   78 YLVLGNH--DHRGNVsAQIAYTQrPNSKRWNFPN--------YYYDISfkfpssDVTVAFIMidtvllcgntddeasgqP 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429 284 SCYSSYGIYTPQYKWLEKELQGVNRTetpWLIVLVHSPFYSSYVHH--YMEGETLRVMYEqwfvKYKVDVVFAGHVHAYE 361
Cdd:cd07378  148 RGPPNKKLAETQLAWLEKQLAASKAD---YKIVVGHYPIYSSGEHGptKCLVDILLPLLK----KYKVDAYLSGHDHNLQ 220

                        250
                 ....*....|....*....
gi 186503429 362 RSERVSNIAYNIVNGLCEP 380
Cdd:cd07378  221 HIVDESGTYYVISGAGSKA 239
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 57-144 9.77e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 35.55  E-value: 9.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503429  57 PNSPQQVHVTQGNHegNGVIISWVTPVKPGSKTVQYWCENEKSRKQAEATVNTyrffnyTSGYIHHCLIDDLEFDTKY-- 134
Cdd:cd00063    1 PSPPTNLRVTDVTS--TSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEV------TPGSETSYTLTGLKPGTEYef 72

                         90
                 ....*....|....
gi 186503429 135 ----YYEIGSGKWS 144
Cdd:cd00063   73 rvraVNGGGESPPS 86
 
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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