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Conserved domains on  [gi|66356586|ref|XP_625471|]
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hypothetical protein [Cryptosporidium parvum Iowa II]

Protein Classification

purple acid phosphatase family protein( domain architecture ID 10164501)

purple acid phosphatase (PAP) family protein is a metallophosphatase containing an active site consisting of two metal ions (usually manganese, iron, or zinc); similar to human tartrate-resistant acid phosphatase type 5 (ACP5) which is involved in osteopontin/bone sialoprotein dephosphorylation in bone matrix

CATH:  3.60.21.10
EC:  3.1.3.2
Gene Ontology:  GO:0046872|GO:0016311|GO:0003993
PubMed:  25837850|8683579|8003970

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 31-373 1.70e-96

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: 290.77  E-value: 1.70e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586  31 LTVFSIGDWGEK-----TECLVNVTTKMGSLESAMNPKFIISVGDNFYQRGVKSVEDAAWTEILEEPFGKLSKHLKVHSC 105
Cdd:cd07378   1 LRFLVLGDWGGKpnpytTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 106 LGDHDWRGSTTAQIDRTNYANNTRWYLPGYWWYEKVTFTSevslpslfeksglgeisannsfhfnssktenstsceidcl 185
Cdd:cd07378  81 LGNHDHRGNVSAQIAYTQRPNSKRWNFPNYYYDISFKFPS---------------------------------------- 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 186 deivdnlntmvnrnnswnedlsyktsiseyfsekqVNSTAVFIYIDSWTLTQDPFK--------KTSISYKYSQLEFIEQ 257
Cdd:cd07378 121 -----------------------------------SDVTVAFIMIDTVLLCGNTDDeasgqprgPPNKKLAETQLAWLEK 165

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 258 TLKAAVFenvDWIILVTHYSIYSSGLHGPHTRLASILLPLIKKYRVDFIISGHDHHSEILVPeDFNSYFQIVGASSKPRT 337
Cdd:cd07378 166 QLAASKA---DYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVD-ESGTYYVISGAGSKADP 241

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 66356586 338 SFGATDE--------NSIFKSNTCSFASFTFSKDIAVSRIFSIN 373
Cdd:cd07378 242 SDIHRDKvpqgyllfFSGFYSSGGGFAYLEITSSELVIRFVDSD 285
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 31-373 1.70e-96

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: 290.77  E-value: 1.70e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586  31 LTVFSIGDWGEK-----TECLVNVTTKMGSLESAMNPKFIISVGDNFYQRGVKSVEDAAWTEILEEPFGKLSKHLKVHSC 105
Cdd:cd07378   1 LRFLVLGDWGGKpnpytTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 106 LGDHDWRGSTTAQIDRTNYANNTRWYLPGYWWYEKVTFTSevslpslfeksglgeisannsfhfnssktenstsceidcl 185
Cdd:cd07378  81 LGNHDHRGNVSAQIAYTQRPNSKRWNFPNYYYDISFKFPS---------------------------------------- 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 186 deivdnlntmvnrnnswnedlsyktsiseyfsekqVNSTAVFIYIDSWTLTQDPFK--------KTSISYKYSQLEFIEQ 257
Cdd:cd07378 121 -----------------------------------SDVTVAFIMIDTVLLCGNTDDeasgqprgPPNKKLAETQLAWLEK 165

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 258 TLKAAVFenvDWIILVTHYSIYSSGLHGPHTRLASILLPLIKKYRVDFIISGHDHHSEILVPeDFNSYFQIVGASSKPRT 337
Cdd:cd07378 166 QLAASKA---DYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVD-ESGTYYVISGAGSKADP 241

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 66356586 338 SFGATDE--------NSIFKSNTCSFASFTFSKDIAVSRIFSIN 373
Cdd:cd07378 242 SDIHRDKvpqgyllfFSGFYSSGGGFAYLEITSSELVIRFVDSD 285
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 6-374 3.00e-21

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 94.89  E-value: 3.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586    6 MNIRSKYFGLATIFIVSILRYSL-CELTVFSIGDWG--EKTECLVNVTTKmgslESAMNPK--FIISVGDNFyQRGVKSV 80
Cdd:PTZ00422   1 IMSFCKLVLFSLFVLIFISSYSVkAQLRFASLGNWGtgSKQQKLVASYLK----QYAKNERvtFLVSPGSNF-PGGVDGL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586   81 EDAAWTEILEEPFGKLSKHLKV--HSCLGDHDWRGSTTAQIDRTN-------------YANNT----RWYLPGYWwyekv 141
Cdd:PTZ00422  76 NDPKWKHCFENVYSEESGDMQIpfFTVLGQADWDGNYNAELLKGQnvylnghgqtdieYDSNNdiypKWIMPNYW----- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586  142 tftsevslpslfeksglgeisannsFHFNSSKTENSTsceidcldeivdnlntmVNRNNSWNEDLSyktsiseyfsekqv 221
Cdd:PTZ00422 151 -------------------------YHYFTHFTDTSG-----------------PSLLKSGHKDMS-------------- 174

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586  222 nstAVFIYIDSWTL-TQDPFKKTSiSYKYSQLEfieQTLKAAVfENVDWIILVTHYSIYSSGLHGPHTRLASILLPLIKK 300
Cdd:PTZ00422 175 ---VAFIFIDTWILsSSFPYKKVS-ERAWQDLK---ATLEYAP-KIADYIIVVGDKPIYSSGSSKGDSYLSYYLLPLLKD 246

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66356586  301 YRVDFIISGHDHHSEILvpEDFNSYFQIVGASSKPRTSFGATDENSIFKSNTCSFASFTFSKDIAVSRIFSINS 374
Cdd:PTZ00422 247 AQVDLYISGYDRNMEVL--TDEGTAHINCGSGGNSGRKSIMKNSKSLFYSEDIGFCIHELNAEGMVTKFVSGNT 318
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
251-316 2.80e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.09  E-value: 2.80e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66356586 251 QLEFIEQTLKAAvfeNVDWIILVTHYSIYSSGLHGPHTRL--ASILLPLIKKYRVDFIISGHDHHSEI 316
Cdd:COG1409 126 QLAWLEEELAAA---PAKPVIVFLHHPPYSTGSGSDRIGLrnAEELLALLARYGVDLVLSGHVHRYER 190
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 31-373 1.70e-96

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: 290.77  E-value: 1.70e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586  31 LTVFSIGDWGEK-----TECLVNVTTKMGSLESAMNPKFIISVGDNFYQRGVKSVEDAAWTEILEEPFGKLSKHLKVHSC 105
Cdd:cd07378   1 LRFLVLGDWGGKpnpytTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 106 LGDHDWRGSTTAQIDRTNYANNTRWYLPGYWWYEKVTFTSevslpslfeksglgeisannsfhfnssktenstsceidcl 185
Cdd:cd07378  81 LGNHDHRGNVSAQIAYTQRPNSKRWNFPNYYYDISFKFPS---------------------------------------- 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 186 deivdnlntmvnrnnswnedlsyktsiseyfsekqVNSTAVFIYIDSWTLTQDPFK--------KTSISYKYSQLEFIEQ 257
Cdd:cd07378 121 -----------------------------------SDVTVAFIMIDTVLLCGNTDDeasgqprgPPNKKLAETQLAWLEK 165

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 258 TLKAAVFenvDWIILVTHYSIYSSGLHGPHTRLASILLPLIKKYRVDFIISGHDHHSEILVPeDFNSYFQIVGASSKPRT 337
Cdd:cd07378 166 QLAASKA---DYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVD-ESGTYYVISGAGSKADP 241

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 66356586 338 SFGATDE--------NSIFKSNTCSFASFTFSKDIAVSRIFSIN 373
Cdd:cd07378 242 SDIHRDKvpqgyllfFSGFYSSGGGFAYLEITSSELVIRFVDSD 285
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 6-374 3.00e-21

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 94.89  E-value: 3.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586    6 MNIRSKYFGLATIFIVSILRYSL-CELTVFSIGDWG--EKTECLVNVTTKmgslESAMNPK--FIISVGDNFyQRGVKSV 80
Cdd:PTZ00422   1 IMSFCKLVLFSLFVLIFISSYSVkAQLRFASLGNWGtgSKQQKLVASYLK----QYAKNERvtFLVSPGSNF-PGGVDGL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586   81 EDAAWTEILEEPFGKLSKHLKV--HSCLGDHDWRGSTTAQIDRTN-------------YANNT----RWYLPGYWwyekv 141
Cdd:PTZ00422  76 NDPKWKHCFENVYSEESGDMQIpfFTVLGQADWDGNYNAELLKGQnvylnghgqtdieYDSNNdiypKWIMPNYW----- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586  142 tftsevslpslfeksglgeisannsFHFNSSKTENSTsceidcldeivdnlntmVNRNNSWNEDLSyktsiseyfsekqv 221
Cdd:PTZ00422 151 -------------------------YHYFTHFTDTSG-----------------PSLLKSGHKDMS-------------- 174

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586  222 nstAVFIYIDSWTL-TQDPFKKTSiSYKYSQLEfieQTLKAAVfENVDWIILVTHYSIYSSGLHGPHTRLASILLPLIKK 300
Cdd:PTZ00422 175 ---VAFIFIDTWILsSSFPYKKVS-ERAWQDLK---ATLEYAP-KIADYIIVVGDKPIYSSGSSKGDSYLSYYLLPLLKD 246

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66356586  301 YRVDFIISGHDHHSEILvpEDFNSYFQIVGASSKPRTSFGATDENSIFKSNTCSFASFTFSKDIAVSRIFSINS 374
Cdd:PTZ00422 247 AQVDLYISGYDRNMEVL--TDEGTAHINCGSGGNSGRKSIMKNSKSLFYSEDIGFCIHELNAEGMVTKFVSGNT 318
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
251-316 2.80e-10

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 60.09  E-value: 2.80e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66356586 251 QLEFIEQTLKAAvfeNVDWIILVTHYSIYSSGLHGPHTRL--ASILLPLIKKYRVDFIISGHDHHSEI 316
Cdd:COG1409 126 QLAWLEEELAAA---PAKPVIVFLHHPPYSTGSGSDRIGLrnAEELLALLARYGVDLVLSGHVHRYER 190
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 227-312 1.79e-09

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: 58.46  E-value: 1.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 227 FIYIDSWTltqDPFKKTSISykySQLEFIEQTLKAAVFENVDWIILVTHYSIYSSGLHGPHTRLA----SILLPLIKKYR 302
Cdd:cd00839 120 FISLSTET---DFLKGDNIS---PQYDWLEADLAKVDRSRTPWIIVMGHRPMYCSNDDDADCIEGekmrEALEDLFYKYG 193

                        90
                ....*....|
gi 66356586 303 VDFIISGHDH 312
Cdd:cd00839 194 VDLVLSGHVH 203
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 245-330 1.13e-08

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: 53.42  E-value: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66356586 245 ISYKYSQLEFIEQTLKAAVFENVDWI-------ILVTHYSIYSSGLHGPHTRLA--SILLPLIKKYRVDFIISGHDHHSE 315
Cdd:cd00838  36 LVDYGPDPEEVELKALRLLLAGIPVYvvpgnhdILVTHGPPYDPLDEGSPGEDPgsEALLELLDKYGPDLVLSGHTHVPG 115

                        90
                ....*....|....*
gi 66356586 316 ILVPEDFNSYFQIVG 330
Cdd:cd00838 116 RREVDKGGTLVVNPG 130
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
247-314 2.15e-04

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 42.31  E-value: 2.15e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66356586 247 YKYSQLEfIEQTLKAAVFENVDwiILVTHYSIYSSGLHGPHTRL---ASILLPLIKKYRVDFIISGHDHHS 314
Cdd:COG2129 110 YEYTEEE-IEERLAKLREKDVD--ILLTHAPPYGTTLDRVEDGPhvgSKALRELIEEFQPKLVLHGHIHES 177
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 270-333 5.02e-04

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 39.97  E-value: 5.02e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66356586 270 IILVTHYSIYSSGLHG---PHTRLASILLPLIKKYRVDFIISGHDHHSEILVPEDFNSYFqIVGASS 333
Cdd:cd07400  73 AIVALHHPLLPPPDTGrerNVLLDAGDALKLLKELGVDLVLHGHKHVPAVWNLGLLNGIV-VVNAGT 138
 
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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