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Conserved domains on  [gi|24641134|ref|NP_727465|]
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uncharacterized protein Dmel_CG1637, isoform B [Drosophila melanogaster]

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; ...
 148-450 3.44e-126

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: 368.16  E-value: 3.44e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 148 DWSPSLAIYGDMG---NENAQSLARLQQEtqRGMYDAIIHVGDFAYDMNTKNARVGDEFMRQIETVAAYLPYMVVPGNHE 224
Cdd:cd00839   2 DTPLKFAVFGDMGqntNNSTNTLDHLEKE--LGNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 225 EKFNFSNYRARFSMP---------GGTENMFYSFDLGPVHFVGISTEVYYFLNYGLKPlvfQFEWLREDLAKAnlpeNRN 295
Cdd:cd00839  80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGDNISP---QYDWLEADLAKV----DRS 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 296 KRPWIILYGHRPMYCSNENDNDCTHSETltrvgwpfvHMFGLEPLLYEFGVDVAIWAHEHSYERLWPIYDYKVRNGtlKD 375
Cdd:cd00839 153 RTPWIIVMGHRPMYCSNDDDADCIEGEK---------MREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANS--KD 221

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641134 376 SPYNDPSAPVHIVTGSAGCKEGREP-FKGKIPEWSAFHSQDYGYTRLKAHNRTHIHFEQVSDDkNGAIIDDFWLVK 450
Cdd:cd00839 222 NIYTNPKGPVHIVIGAAGNDEGLDDaFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQ-DGQVADSFWIVK 296
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 38-141 8.92e-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: 78.22  E-value: 8.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134    38 PEQVHLSFGErTDSEIVVTWSTRSLPPDqevgavSVVEYGQLVDGqvrLTQQARGKATKFVDGGHKqaTQFIHRVTLRDL 117
Cdd:pfam16656   1 PEQVHLSLTG-DSTSMTVSWVTPSAVTS------PVVQYGTSSSA---LTSTATATSSTYTTGDGG--TGYIHRATLTGL 68

                          90       100
                  ....*....|....*....|....*
gi 24641134   118 EPNATYSYHCGSD-FGWSAIFQFRT 141
Cdd:pfam16656  69 EPGTTYYYRVGDDnGGWSEVYSFTT 93
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 148-450 3.44e-126

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: 368.16  E-value: 3.44e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 148 DWSPSLAIYGDMG---NENAQSLARLQQEtqRGMYDAIIHVGDFAYDMNTKNARVGDEFMRQIETVAAYLPYMVVPGNHE 224
Cdd:cd00839   2 DTPLKFAVFGDMGqntNNSTNTLDHLEKE--LGNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 225 EKFNFSNYRARFSMP---------GGTENMFYSFDLGPVHFVGISTEVYYFLNYGLKPlvfQFEWLREDLAKAnlpeNRN 295
Cdd:cd00839  80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGDNISP---QYDWLEADLAKV----DRS 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 296 KRPWIILYGHRPMYCSNENDNDCTHSETltrvgwpfvHMFGLEPLLYEFGVDVAIWAHEHSYERLWPIYDYKVRNGtlKD 375
Cdd:cd00839 153 RTPWIIVMGHRPMYCSNDDDADCIEGEK---------MREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANS--KD 221

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641134 376 SPYNDPSAPVHIVTGSAGCKEGREP-FKGKIPEWSAFHSQDYGYTRLKAHNRTHIHFEQVSDDkNGAIIDDFWLVK 450
Cdd:cd00839 222 NIYTNPKGPVHIVIGAAGNDEGLDDaFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQ-DGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 20-448 1.63e-38

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 144.82  E-value: 1.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134   20 PGIRSTPI---DQDVDIVHyqPEQVHLSFgeRTDSEIVVTWSTR-SLPPDQEVGAVSvveyGQLvDGQVRLTQQARGKAT 95
Cdd:PLN02533  25 PGTRKNLVihpDNEDDPTH--PDQVHISL--VGPDKMRISWITQdSIPPSVVYGTVS----GKY-EGSANGTSSSYHYLL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134   96 KFVDGGhkqatqfIHRVTLRDLEPNATYSYHCGsdfGWSAI--FQFRTVPSasvDWSPSLAIYGDMG-NENAQSLArlqQ 172
Cdd:PLN02533  96 IYRSGQ-------INDVVIGPLKPNTVYYYKCG---GPSSTqeFSFRTPPS---KFPIKFAVSGDLGtSEWTKSTL---E 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134  173 ETQRGMYDAIIHVGDFAY-DMNTKnarVGDEFMRQIETVAAYLPYMVVPGNHE-EKF------NFSNYRARFSMP----G 240
Cdd:PLN02533 160 HVSKWDYDVFILPGDLSYaNFYQP---LWDTFGRLVQPLASQRPWMVTHGNHElEKIpilhpeKFTAYNARWRMPfeesG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134  241 GTENMFYSFDLGPVHFVGISTevyyFLNYGlkPLVFQFEWLREDLAKANlpenRNKRPWIILYGHRPMYCSNENDNDCTH 320
Cdd:PLN02533 237 STSNLYYSFNVYGVHIIMLGS----YTDFE--PGSEQYQWLENNLKKID----RKTTPWVVAVVHAPWYNSNEAHQGEKE 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134  321 SETLTRvgwpfvhmfGLEPLLYEFGVDVAIWAHEHSYERLWPIYDYKVrngtlkdspynDPSAPVHIVTGSAGCKEG-RE 399
Cdd:PLN02533 307 SVGMKE---------SMETLLYKARVDLVFAGHVHAYERFDRVYQGKT-----------DKCGPVYITIGDGGNREGlAT 366

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 24641134  400 PFKGKIPEWSAFHSQDYGYTRLKAHNRTHIHFE-QVSDDKNGAIIDDFWL 448
Cdd:PLN02533 367 KYIDPKPDISLFREASFGHGQLNVVDANTMEWTwHRNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
155-362 2.24e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.92  E-value: 2.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 155 IYGDMGNENAQSLARLQQETQRGMYDAIIHVGDFAYDMNTKNARVGDEFMRQIEtvaayLPYMVVPGNHEEKFNFS-NYR 233
Cdd:COG1409  11 LGAPDGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDIRAAMAeAYR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 234 ARFSMPGGtENMFYSFDLGPVHFVGISTEVYYFLNYGLKPlvFQFEWLREDLAKAnlpenrnKRPWIILYGHRPMYCSNE 313
Cdd:COG1409  86 EYFGDLPP-GGLYYSFDYGGVRFIGLDSNVPGRSSGELGP--EQLAWLEEELAAA-------PAKPVIVFLHHPPYSTGS 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 24641134 314 NDNDcthsetltrvgWPFVHMFGLEPLLYEFGVDVAIWAHEHSYERLWP 362
Cdd:COG1409 156 GSDR-----------IGLRNAEELLALLARYGVDLVLSGHVHRYERTRR 193
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 383-444 4.21e-22

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: 89.12  E-value: 4.21e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641134   383 APVHIVTGSAGCKEGrePFKGKIPEWSAFHSQDYGYTRLKAHNRTHIHFEQVSDDkNGAIID 444
Cdd:pfam14008   1 APVHIVIGAAGNIEG--LFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 38-141 8.92e-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: 78.22  E-value: 8.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134    38 PEQVHLSFGErTDSEIVVTWSTRSLPPDqevgavSVVEYGQLVDGqvrLTQQARGKATKFVDGGHKqaTQFIHRVTLRDL 117
Cdd:pfam16656   1 PEQVHLSLTG-DSTSMTVSWVTPSAVTS------PVVQYGTSSSA---LTSTATATSSTYTTGDGG--TGYIHRATLTGL 68

                          90       100
                  ....*....|....*....|....*
gi 24641134   118 EPNATYSYHCGSD-FGWSAIFQFRT 141
Cdd:pfam16656  69 EPGTTYYYRVGDDnGGWSEVYSFTT 93
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 148-450 3.44e-126

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: 368.16  E-value: 3.44e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 148 DWSPSLAIYGDMG---NENAQSLARLQQEtqRGMYDAIIHVGDFAYDMNTKNARVGDEFMRQIETVAAYLPYMVVPGNHE 224
Cdd:cd00839   2 DTPLKFAVFGDMGqntNNSTNTLDHLEKE--LGNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 225 EKFNFSNYRARFSMP---------GGTENMFYSFDLGPVHFVGISTEVYYFLNYGLKPlvfQFEWLREDLAKAnlpeNRN 295
Cdd:cd00839  80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGDNISP---QYDWLEADLAKV----DRS 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 296 KRPWIILYGHRPMYCSNENDNDCTHSETltrvgwpfvHMFGLEPLLYEFGVDVAIWAHEHSYERLWPIYDYKVRNGtlKD 375
Cdd:cd00839 153 RTPWIIVMGHRPMYCSNDDDADCIEGEK---------MREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANS--KD 221

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641134 376 SPYNDPSAPVHIVTGSAGCKEGREP-FKGKIPEWSAFHSQDYGYTRLKAHNRTHIHFEQVSDDkNGAIIDDFWLVK 450
Cdd:cd00839 222 NIYTNPKGPVHIVIGAAGNDEGLDDaFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQ-DGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 20-448 1.63e-38

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 144.82  E-value: 1.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134   20 PGIRSTPI---DQDVDIVHyqPEQVHLSFgeRTDSEIVVTWSTR-SLPPDQEVGAVSvveyGQLvDGQVRLTQQARGKAT 95
Cdd:PLN02533  25 PGTRKNLVihpDNEDDPTH--PDQVHISL--VGPDKMRISWITQdSIPPSVVYGTVS----GKY-EGSANGTSSSYHYLL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134   96 KFVDGGhkqatqfIHRVTLRDLEPNATYSYHCGsdfGWSAI--FQFRTVPSasvDWSPSLAIYGDMG-NENAQSLArlqQ 172
Cdd:PLN02533  96 IYRSGQ-------INDVVIGPLKPNTVYYYKCG---GPSSTqeFSFRTPPS---KFPIKFAVSGDLGtSEWTKSTL---E 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134  173 ETQRGMYDAIIHVGDFAY-DMNTKnarVGDEFMRQIETVAAYLPYMVVPGNHE-EKF------NFSNYRARFSMP----G 240
Cdd:PLN02533 160 HVSKWDYDVFILPGDLSYaNFYQP---LWDTFGRLVQPLASQRPWMVTHGNHElEKIpilhpeKFTAYNARWRMPfeesG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134  241 GTENMFYSFDLGPVHFVGISTevyyFLNYGlkPLVFQFEWLREDLAKANlpenRNKRPWIILYGHRPMYCSNENDNDCTH 320
Cdd:PLN02533 237 STSNLYYSFNVYGVHIIMLGS----YTDFE--PGSEQYQWLENNLKKID----RKTTPWVVAVVHAPWYNSNEAHQGEKE 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134  321 SETLTRvgwpfvhmfGLEPLLYEFGVDVAIWAHEHSYERLWPIYDYKVrngtlkdspynDPSAPVHIVTGSAGCKEG-RE 399
Cdd:PLN02533 307 SVGMKE---------SMETLLYKARVDLVFAGHVHAYERFDRVYQGKT-----------DKCGPVYITIGDGGNREGlAT 366

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 24641134  400 PFKGKIPEWSAFHSQDYGYTRLKAHNRTHIHFE-QVSDDKNGAIIDDFWL 448
Cdd:PLN02533 367 KYIDPKPDISLFREASFGHGQLNVVDANTMEWTwHRNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
155-362 2.24e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.92  E-value: 2.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 155 IYGDMGNENAQSLARLQQETQRGMYDAIIHVGDFAYDMNTKNARVGDEFMRQIEtvaayLPYMVVPGNHEEKFNFS-NYR 233
Cdd:COG1409  11 LGAPDGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDIRAAMAeAYR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 234 ARFSMPGGtENMFYSFDLGPVHFVGISTEVYYFLNYGLKPlvFQFEWLREDLAKAnlpenrnKRPWIILYGHRPMYCSNE 313
Cdd:COG1409  86 EYFGDLPP-GGLYYSFDYGGVRFIGLDSNVPGRSSGELGP--EQLAWLEEELAAA-------PAKPVIVFLHHPPYSTGS 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 24641134 314 NDNDcthsetltrvgWPFVHMFGLEPLLYEFGVDVAIWAHEHSYERLWP 362
Cdd:COG1409 156 GSDR-----------IGLRNAEELLALLARYGVDLVLSGHVHRYERTRR 193
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 383-444 4.21e-22

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: 89.12  E-value: 4.21e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641134   383 APVHIVTGSAGCKEGrePFKGKIPEWSAFHSQDYGYTRLKAHNRTHIHFEQVSDDkNGAIID 444
Cdd:pfam14008   1 APVHIVIGAAGNIEG--LFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 38-141 8.92e-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: 78.22  E-value: 8.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134    38 PEQVHLSFGErTDSEIVVTWSTRSLPPDqevgavSVVEYGQLVDGqvrLTQQARGKATKFVDGGHKqaTQFIHRVTLRDL 117
Cdd:pfam16656   1 PEQVHLSLTG-DSTSMTVSWVTPSAVTS------PVVQYGTSSSA---LTSTATATSSTYTTGDGG--TGYIHRATLTGL 68

                          90       100
                  ....*....|....*....|....*
gi 24641134   118 EPNATYSYHCGSD-FGWSAIFQFRT 141
Cdd:pfam16656  69 EPGTTYYYRVGDDnGGWSEVYSFTT 93
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 148-417 6.01e-07

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: 50.79  E-value: 6.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 148 DWSPSLAIYGDMG-NENAQSLARLQQETQrgmYDAIIHVGDFAYDMNtknarVGDEFMRQIETV--------AAYLPYMV 218
Cdd:cd07378   8 DWGGKPNPYTTAAqSLVAKQMAKVASKLG---IDFILSLGDNFYDDG-----VKDVDDPRFQETfedvysapSLQVPWYL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 219 VPGNHEEKFNFS-----NYRARFS---MPGGTENMFYSF--DLGPVHFVGISTEV-----YYFLNYGLKPLVF------Q 277
Cdd:cd07378  80 VLGNHDHRGNVSaqiayTQRPNSKrwnFPNYYYDISFKFpsSDVTVAFIMIDTVLlcgntDDEASGQPRGPPNkklaetQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 278 FEWLREDLAKAnlpenrnKRPWIILYGHRPMYCSNENDND-CTHSEtltrvgwpfvhmfgLEPLLYEFGVDVAIWAHEHS 356
Cdd:cd07378 160 LAWLEKQLAAS-------KADYKIVVGHYPIYSSGEHGPTkCLVDI--------------LLPLLKKYKVDAYLSGHDHN 218

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641134 357 YERLwpiydykvrngtlkdspyNDPSAPVHIVTGSAGCKEGREPFKGKIP-EWSAFHSQDYG 417
Cdd:cd07378 219 LQHI------------------VDESGTYYVISGAGSKADPSDIHRDKVPqGYLLFFSGFYS 262
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 153-249 1.54e-06

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: 46.82  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134   153 LAIYGDM-GNENAQSLARLQQETQR-GMYDAIIHVGDFAYDMNtknarVGDEFMRQIETVAAYLPYMVVPGNHE----EK 226
Cdd:pfam00149   3 ILVIGDLhLPGQLDDLLELLKKLLEeGKPDLVLHAGDLVDRGP-----PSEEVLELLERLIKYVPVYLVRGNHDfdygEC 77

                          90       100
                  ....*....|....*....|...
gi 24641134   227 FNFSNYRARFSMPGGTENMFYSF 249
Cdd:pfam00149  78 LRLYPYLGLLARPWKRFLEVFNF 100
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
162-373 7.18e-04

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 40.77  E-value: 7.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 162 ENAQSLARLQQETQRGMYDAIIHVGDFAYDMNTKNARVGDEFMRQIETvaaylPYMVVPGNHEEKFNFSNYRarfsmPGG 241
Cdd:COG2129  10 GNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAALGV-----PVLAVPGNHDDPEVLDALE-----ESG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 242 TENM-FYSFDLGPVHFVGISTEVYYFLNyglKPLVFQFEWLREDLAKAnlpenRNKRPWIILYGHRPMYCSNENDNDCTH 320
Cdd:COG2129  80 VHNLhGRVVEIGGLRIAGLGGSRPTPFG---TPYEYTEEEIEERLAKL-----REKDVDILLTHAPPYGTTLDRVEDGPH 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 24641134 321 setltrVGWPfvhmfGLEPLLYEFGVDVAIwaHEHSYERlwpiYDYKVRNGTL 373
Cdd:COG2129 152 ------VGSK-----ALRELIEEFQPKLVL--HGHIHES----RGVDKIGGTR 187
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 150-308 4.21e-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: 38.80  E-value: 4.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 150 SPSLAIYG-DMGNENAQSLARLQQETQRgmYDAIIHVGDFAyDMNTKNARvgDEFMRQIETVAAylPYMVVPGNHEEKFN 228
Cdd:cd07402  12 PGEGALLGvDTAARLAAAVAQVNALHPR--PDLVVVTGDLS-DDGSPESY--ERLRELLAPLPA--PVYWIPGNHDDRAA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 229 FSNYRARfSMPGGTENMFYSFDLGPVHFVGISTEVYYFLNYGLKPlvFQFEWLREDLAKAnlPEnrnkRPWIILYGHRPM 308
Cdd:cd07402  85 MREALPE-PPYDDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSD--EQLDWLEAALAEA--PD----RPTLIFLHHPPF 155
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 165-309 5.64e-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: 38.47  E-value: 5.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134 165 QSLARLQ----QETQRGMYDAIIHVGDFaydMNTKNARvgDEFMRQIETVAAYL-----PYMVVPGNHEeKFNFS-NYRA 234
Cdd:cd07396  29 NSLGVLEraveEWNRESNLAFVVQLGDI---IDGYNAK--DRSKEALDAVLSILdrlkgPVHHVLGNHE-FYNFPrEYLN 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641134 235 RFSMPGGTENMFYSFDLGP-VHFVGIsteVYYFLNYGLKPLvfQFEWLREDLAKAnlpENRNKRpwIILYGHRPMY 309
Cdd:cd07396 103 HLKTLNGEDAYYYSFSPGPgFRFLVL---DFVKFNGGIGEE--QLAWLRNELTSA---DANGEK--VIVLSHLPIY 168
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 179-224 6.35e-03

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 36.86  E-value: 6.35e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24641134 179 YDAIIHVGDFAYDMNTKNARVGdefmRQIETVAAYLPYMVVPGNHE 224
Cdd:cd00838  27 PDLVICLGDLVDYGPDPEEVEL----KALRLLLAGIPVYVVPGNHD 68
fn3 pfam00041
Fibronectin type III domain;
37-124 8.90e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 35.47  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641134    37 QPEQVHLSfgERTDSEIVVTWStrslPPDQEVGAVS--VVEYGQLVDGQVRLTQQargkatkfVDGGHkqatqfiHRVTL 114
Cdd:pfam00041   2 APSNLTVT--DVTSTSLTVSWT----PPPDGNGPITgyEVEYRPKNSGEPWNEIT--------VPGTT-------TSVTL 60

                          90
                  ....*....|
gi 24641134   115 RDLEPNATYS 124
Cdd:pfam00041  61 TGLKPGTEYE 70
 
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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