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Conserved domains on  [gi|1827635|pdb|1KBP|A]
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Chain A, PURPLE ACID PHOSPHATASE

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; ...
 125-422 4.38e-117

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: 343.90  E-value: 4.38e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      125 DVPYTFGLIGDLGQS-FDSNTTLSHYELSPKKGQTVLFVGDLSYADRYPNhdNVRWDTWGRFTERSVAYQPWIWTAGNHE 203
Cdd:cd00839   2 DTPLKFAVFGDMGQNtNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      204 IEFAPEINEtepFKPFSYRYHVPYEASQSTSPFWYSIKRASAHIIVLSSYSAYGRG---TPQYTWLKKELRKVKRSETPW 280
Cdd:cd00839  80 ADYNGSTSK---IKFFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGdniSPQYDWLEADLAKVDRSRTPW 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      281 LIVLMHSPLYNSY--NHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYERSERVSNiaYKITDGLCTPVKDQSAPVYIT 358
Cdd:cd00839 157 IIVMGHRPMYCSNddDADCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHIV 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1KBP_A      359 IGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQDGVAVeaDSVWFFN 422
Cdd:cd00839 235 IGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDGQVA--DSFWIVK 296
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 27-118 5.29e-18

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


:

Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 78.61  E-value: 5.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A         27 PQQVHITQGDlVGRAMIISWVTMDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIHHTTIRKLKYNTKYYYEVG 106
Cdd:pfam16656   1 PEQVHLSLTG-DSTSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|....
1KBP_A        107 LRN--TTRRFSFIT 118
Cdd:pfam16656  80 DDNggWSEVYSFTT 93
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 125-422 4.38e-117

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: 343.90  E-value: 4.38e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      125 DVPYTFGLIGDLGQS-FDSNTTLSHYELSPKKGQTVLFVGDLSYADRYPNhdNVRWDTWGRFTERSVAYQPWIWTAGNHE 203
Cdd:cd00839   2 DTPLKFAVFGDMGQNtNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      204 IEFAPEINEtepFKPFSYRYHVPYEASQSTSPFWYSIKRASAHIIVLSSYSAYGRG---TPQYTWLKKELRKVKRSETPW 280
Cdd:cd00839  80 ADYNGSTSK---IKFFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGdniSPQYDWLEADLAKVDRSRTPW 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      281 LIVLMHSPLYNSY--NHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYERSERVSNiaYKITDGLCTPVKDQSAPVYIT 358
Cdd:cd00839 157 IIVMGHRPMYCSNddDADCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHIV 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1KBP_A      359 IGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQDGVAVeaDSVWFFN 422
Cdd:cd00839 235 IGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDGQVA--DSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 27-419 9.44e-103

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 312.00  E-value: 9.44e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A        27 PQQVHITqgdLVG-RAMIISWVTMDEPgSSAVRYWSEKNGRKRIAKGKMSTYRFF-NYSSGFIHHTTIRKLKYNTKYYYE 104
Cdd:PLN02533  44 PDQVHIS---LVGpDKMRISWITQDSI-PPSVVYGTVSGKYEGSANGTSSSYHYLlIYRSGQINDVVIGPLKPNTVYYYK 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A       105 VGLRNTTRRFSFITPPQtglDVPYTFGLIGDLGQSFDSNTTLSHyeLSPKKGQTVLFVGDLSYADRYpnhdNVRWDTWGR 184
Cdd:PLN02533 120 CGGPSSTQEFSFRTPPS---KFPIKFAVSGDLGTSEWTKSTLEH--VSKWDYDVFILPGDLSYANFY----QPLWDTFGR 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A       185 FTERSVAYQPWIWTAGNHEIEFAPeINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHIIVLSSYSAYGRGTPQYT 264
Cdd:PLN02533 191 LVQPLASQRPWMVTHGNHELEKIP-ILHPEKFTAYNARWRMPFEESGSTSNLYYSFNVYGVHIIMLGSYTDFEPGSEQYQ 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A       265 WLKKELRKVKRSETPWLIVLMHSPLYNSYNHHFMEGEA--MRTKFEAWFVKYKVDVVFAGHVHAYERSERVSNIAYkitd 342
Cdd:PLN02533 270 WLENNLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESvgMKESMETLLYKARVDLVFAGHVHAYERFDRVYQGKT---- 345

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1KBP_A       343 glctpvkDQSAPVYITIGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQDGVAVEADSVW 419
Cdd:PLN02533 346 -------DKCGPVYITIGDGGNREGLATKYIDPKPDISLFREASFGHGQLNVVDANTMEWTWHRNDDDQSVASDSVW 415
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
159-363 2.33e-23

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 97.84  E-value: 2.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      159 VLFVGDLSYADRYPNHDNVRwdtwGRFTERSVayqPWIWTAGNHEIEFAPEINetepfkpfsYRYHVPYEASQstsPFWY 238
Cdd:COG1409  38 VVVTGDLTDDGEPEEYAAAR----EILARLGV---PVYVVPGNHDIRAAMAEA---------YREYFGDLPPG---GLYY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      239 SIKRASAHIIVLSS---YSAYGR-GTPQYTWLKKELRKVKRsetPWLIVLMHSPLYNSYNHHFMEGEAMRTKFEAWFVKY 314
Cdd:COG1409  99 SFDYGGVRFIGLDSnvpGRSSGElGPEQLAWLEEELAAAPA---KPVIVFLHHPPYSTGSGSDRIGLRNAEELLALLARY 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1KBP_A      315 KVDVVFAGHVHAYERSERVsNIAYKITDGLCTPVKDQSAPVYITIGDAG 363
Cdd:COG1409 176 GVDLVLSGHVHRYERTRRD-GVPYIVAGSTGGQVRLPPGYRVIEVDGDG 223
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 353-411 2.89e-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: 81.03  E-value: 2.89e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
1KBP_A        353 APVYITIGDAGNYgviDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQDGV 411
Cdd:pfam14008   1 APVHIVIGAAGNI---EGLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSDDGT 56
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 27-118 5.29e-18

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


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 78.61  E-value: 5.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A         27 PQQVHITQGDlVGRAMIISWVTMDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIHHTTIRKLKYNTKYYYEVG 106
Cdd:pfam16656   1 PEQVHLSLTG-DSTSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|....
1KBP_A        107 LRN--TTRRFSFIT 118
Cdd:pfam16656  80 DDNggWSEVYSFTT 93
P_estr_lig_assc TIGR04123
metallophosphoesterase, DNA ligase-associated; Members of this protein family are an ...
 157-208 2.41e-03

metallophosphoesterase, DNA ligase-associated; Members of this protein family are an uncharacterized putative metallophosphoesterase associated with a DNA ligase, a helicase, and a putative exonuclease. It may play a role in DNA repair. Its system is present in about 12 % of prokaryotic reference genomes.


Pssm-ID: 274996  Cd Length: 208  Bit Score: 39.07  E-value: 2.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
1KBP_A        157 QTVLFVGDLsYADRYpNHDNVRWDTWGRFTeRSVAYQPWIWTAGNHEIEFAP 208
Cdd:TIGR04123  66 RRLIVLGDL-FHDRI-GAERLTWEDFAAWR-RLHAGRDWVLIEGNHDRLAPD 114
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 125-422 4.38e-117

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: 343.90  E-value: 4.38e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      125 DVPYTFGLIGDLGQS-FDSNTTLSHYELSPKKGQTVLFVGDLSYADRYPNhdNVRWDTWGRFTERSVAYQPWIWTAGNHE 203
Cdd:cd00839   2 DTPLKFAVFGDMGQNtNNSTNTLDHLEKELGNYDAIIHVGDIAYADGYNN--GSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      204 IEFAPEINEtepFKPFSYRYHVPYEASQSTSPFWYSIKRASAHIIVLSSYSAYGRG---TPQYTWLKKELRKVKRSETPW 280
Cdd:cd00839  80 ADYNGSTSK---IKFFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGdniSPQYDWLEADLAKVDRSRTPW 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      281 LIVLMHSPLYNSY--NHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYERSERVSNiaYKITDGLCTPVKDQSAPVYIT 358
Cdd:cd00839 157 IIVMGHRPMYCSNddDADCIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYN--NTVANSKDNIYTNPKGPVHIV 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1KBP_A      359 IGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQDGVAVeaDSVWFFN 422
Cdd:cd00839 235 IGAAGNDEGLDDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQDGQVA--DSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 27-419 9.44e-103

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 312.00  E-value: 9.44e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A        27 PQQVHITqgdLVG-RAMIISWVTMDEPgSSAVRYWSEKNGRKRIAKGKMSTYRFF-NYSSGFIHHTTIRKLKYNTKYYYE 104
Cdd:PLN02533  44 PDQVHIS---LVGpDKMRISWITQDSI-PPSVVYGTVSGKYEGSANGTSSSYHYLlIYRSGQINDVVIGPLKPNTVYYYK 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A       105 VGLRNTTRRFSFITPPQtglDVPYTFGLIGDLGQSFDSNTTLSHyeLSPKKGQTVLFVGDLSYADRYpnhdNVRWDTWGR 184
Cdd:PLN02533 120 CGGPSSTQEFSFRTPPS---KFPIKFAVSGDLGTSEWTKSTLEH--VSKWDYDVFILPGDLSYANFY----QPLWDTFGR 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A       185 FTERSVAYQPWIWTAGNHEIEFAPeINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHIIVLSSYSAYGRGTPQYT 264
Cdd:PLN02533 191 LVQPLASQRPWMVTHGNHELEKIP-ILHPEKFTAYNARWRMPFEESGSTSNLYYSFNVYGVHIIMLGSYTDFEPGSEQYQ 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A       265 WLKKELRKVKRSETPWLIVLMHSPLYNSYNHHFMEGEA--MRTKFEAWFVKYKVDVVFAGHVHAYERSERVSNIAYkitd 342
Cdd:PLN02533 270 WLENNLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESvgMKESMETLLYKARVDLVFAGHVHAYERFDRVYQGKT---- 345

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1KBP_A       343 glctpvkDQSAPVYITIGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQDGVAVEADSVW 419
Cdd:PLN02533 346 -------DKCGPVYITIGDGGNREGLATKYIDPKPDISLFREASFGHGQLNVVDANTMEWTWHRNDDDQSVASDSVW 415
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
159-363 2.33e-23

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 97.84  E-value: 2.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      159 VLFVGDLSYADRYPNHDNVRwdtwGRFTERSVayqPWIWTAGNHEIEFAPEINetepfkpfsYRYHVPYEASQstsPFWY 238
Cdd:COG1409  38 VVVTGDLTDDGEPEEYAAAR----EILARLGV---PVYVVPGNHDIRAAMAEA---------YREYFGDLPPG---GLYY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      239 SIKRASAHIIVLSS---YSAYGR-GTPQYTWLKKELRKVKRsetPWLIVLMHSPLYNSYNHHFMEGEAMRTKFEAWFVKY 314
Cdd:COG1409  99 SFDYGGVRFIGLDSnvpGRSSGElGPEQLAWLEEELAAAPA---KPVIVFLHHPPYSTGSGSDRIGLRNAEELLALLARY 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1KBP_A      315 KVDVVFAGHVHAYERSERVsNIAYKITDGLCTPVKDQSAPVYITIGDAG 363
Cdd:COG1409 176 GVDLVLSGHVHRYERTRRD-GVPYIVAGSTGGQVRLPPGYRVIEVDGDG 223
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 353-411 2.89e-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: 81.03  E-value: 2.89e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
1KBP_A        353 APVYITIGDAGNYgviDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQDGV 411
Cdd:pfam14008   1 APVHIVIGAAGNI---EGLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSDDGT 56
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 27-118 5.29e-18

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


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 78.61  E-value: 5.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A         27 PQQVHITQGDlVGRAMIISWVTMDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIHHTTIRKLKYNTKYYYEVG 106
Cdd:pfam16656   1 PEQVHLSLTG-DSTSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTGYIHRATLTGLEPGTTYYYRVG 79

                          90
                  ....*....|....
1KBP_A        107 LRN--TTRRFSFIT 118
Cdd:pfam16656  80 DDNggWSEVYSFTT 93
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 128-247 2.10e-10

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 57.99  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A        128 YTFGLIGDLG--QSFDSNTTLSHYELSPKKGQTVLFVGDLSyadrypnHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIE 205
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLV-------DRGPPSEEVLELLERLIKYVPVYLVRGNHDFD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
1KBP_A        206 FapeiNETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHI 247
Cdd:pfam00149  74 Y----GECLRLYPYLGLLARPWKRFLEVFNFLPLAGILSGHT 111
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 255-343 1.66e-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: 49.96  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      255 AYGRGTPQYTWLKKELRKVKRSETPWL-----IVLMHSPLYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYER 329
Cdd:cd00838  37 VDYGPDPEEVELKALRLLLAGIPVYVVpgnhdILVTHGPPYDPLDEGSPGEDPGSEALLELLDKYGPDLVLSGHTHVPGR 116

                        90
                ....*....|....
1KBP_A      330 SERVSNIAYKITDG 343
Cdd:cd00838 117 REVDKGGTLVVNPG 130
P_estr_lig_assc TIGR04123
metallophosphoesterase, DNA ligase-associated; Members of this protein family are an ...
 157-208 2.41e-03

metallophosphoesterase, DNA ligase-associated; Members of this protein family are an uncharacterized putative metallophosphoesterase associated with a DNA ligase, a helicase, and a putative exonuclease. It may play a role in DNA repair. Its system is present in about 12 % of prokaryotic reference genomes.


Pssm-ID: 274996  Cd Length: 208  Bit Score: 39.07  E-value: 2.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
1KBP_A        157 QTVLFVGDLsYADRYpNHDNVRWDTWGRFTeRSVAYQPWIWTAGNHEIEFAP 208
Cdd:TIGR04123  66 RRLIVLGDL-FHDRI-GAERLTWEDFAAWR-RLHAGRDWVLIEGNHDRLAPD 114
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 194-338 3.37e-03

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: 39.23  E-value: 3.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      194 PWIWTAGNHEI--EFAPEINETEpfKPFSYRYHVPYeasqstspFWYSIK------RASAHIIVLSS----------YSA 255
Cdd:cd07378  76 PWYLVLGNHDHrgNVSAQIAYTQ--RPNSKRWNFPN--------YYYDISfkfpssDVTVAFIMIDTvllcgntddeASG 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      256 YGRGTP-------QYTWLKKELRKVKRSetpWLIVLMHSPLYNSYNHHfmegeamRTKFEAWFV-----KYKVDVVFAGH 323
Cdd:cd07378 146 QPRGPPnkklaetQLAWLEKQLAASKAD---YKIVVGHYPIYSSGEHG-------PTKCLVDILlpllkKYKVDAYLSGH 215

                       170
                ....*....|....*
1KBP_A      324 VHAYERSERVSNIAY 338
Cdd:cd07378 216 DHNLQHIVDESGTYY 230
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 159-365 7.18e-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: 38.03  E-value: 7.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      159 VLFVGDLSyadrypnhDNVRWDTWGRFTERSVAYQ-PWIWTAGNHE--IEFAPEINETEPFKPFSYRYHVPYEASQstsp 235
Cdd:cd07402  43 VVVTGDLS--------DDGSPESYERLRELLAPLPaPVYWIPGNHDdrAAMREALPEPPYDDNGPVQYVVDFGGWR---- 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      236 fwysikrasahIIVLSSY---SAYGRGTP-QYTWLKKELRKvkRSETPWLIVLMHSPLynSYNHHFMEGEAMRT--KFEA 309
Cdd:cd07402 111 -----------LILLDTSvpgVHHGELSDeQLDWLEAALAE--APDRPTLIFLHHPPF--PLGIPWMDAIRLRNsqALFA 175

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      310 WFVKY-KVDVVFAGHVHaYERSERVSNIAYKITDGLCTPVK---DQSAPVYITIGDAGNY 365
Cdd:cd07402 176 VLARHpQVKAILCGHIH-RPISGSFRGIPFSTAPSTCHQFAldlDDFALDAEAPGPRNLL 234
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 194-338 7.34e-03

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: 38.08  E-value: 7.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KBP_A      194 PWIWTAGNHEiefapeinetepFKPFSYRYHVPYEASQSTSPFWYSIKRASAHIIVLSSYSAY--GRGTPQYTWLKKELR 271
Cdd:cd07396  83 PVHHVLGNHE------------FYNFPREYLNHLKTLNGEDAYYYSFSPGPGFRFLVLDFVKFngGIGEEQLAWLRNELT 150

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1KBP_A      272 KVKRSETPwLIVLMHSPLY--NSYNHHFM--EGEAMRTKFeawfvKYK-VDVVFAGHVHAYERSERVSNIAY 338
Cdd:cd07396 151 SADANGEK-VIVLSHLPIYpeAADPQCLLwnYEEVLAILE-----SYPcVKACFSGHNHEGGYEQDSHGVHH 216
 
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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