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Conserved domains on  [gi|50539964|ref|NP_001002452|]
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tartrate-resistant acid phosphatase type 5b precursor [Danio rerio]

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

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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 ...
 29-312 5.77e-143

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: 405.17  E-value: 5.77e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  29 LRFVGIGDWGGRPSyPFYTPHEADTAKELARVAQSSGLDFVLSLGDNFYYDGVKDVDDTRFKFSYEQVFSHPALMtIPWY 108
Cdd:cd07378   1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQ-VPWY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 109 LIAGNHDHRGNVSAQIAYSSR--SERWIYPDLYYELNFKVPHSNTSLTILMTDTVVVCGNTYDGLD--PVGPEDLAAANK 184
Cdd:cd07378  79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASgqPRGPPNKKLAET 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 185 QLAWIEQRLQSTKADFVIVVGHYPIWSIGHHGPTKCLISKLRPLLKKYNVSLYLSGHDHSLQFIREDDGSSFVVSGAGVE 264
Cdd:cd07378 159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 50539964 265 EDSSTDHRKSFPSAWQLFSSPVNQTSGSFVYFEVNKSEMLINYLQPDG 312
Cdd:cd07378 239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 29-312 5.77e-143

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: 405.17  E-value: 5.77e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  29 LRFVGIGDWGGRPSyPFYTPHEADTAKELARVAQSSGLDFVLSLGDNFYYDGVKDVDDTRFKFSYEQVFSHPALMtIPWY 108
Cdd:cd07378   1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQ-VPWY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 109 LIAGNHDHRGNVSAQIAYSSR--SERWIYPDLYYELNFKVPHSNTSLTILMTDTVVVCGNTYDGLD--PVGPEDLAAANK 184
Cdd:cd07378  79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASgqPRGPPNKKLAET 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 185 QLAWIEQRLQSTKADFVIVVGHYPIWSIGHHGPTKCLISKLRPLLKKYNVSLYLSGHDHSLQFIREDDGSSFVVSGAGVE 264
Cdd:cd07378 159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 50539964 265 EDSSTDHRKSFPSAWQLFSSPVNQTSGSFVYFEVNKSEMLINYLQPDG 312
Cdd:cd07378 239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
45-261 1.73e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 107.47  E-value: 1.73e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  45 FYTPHEADTAKELARV---AQSSGLDFVLSLGDNFYYDGVKDVDDTRFKFsyeqvfshpALMTIPWYLIAGNHDHRGnvs 121
Cdd:COG1409  11 LGAPDGSDTAEVLAAAladINAPRPDFVVVTGDLTDDGEPEEYAAAREIL---------ARLGVPVYVVPGNHDIRA--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 122 aqiAYSSRSERWIYPDLYYELNFKVPHSNtsLTILMTDTVVVcGNTYDGLDPvgpedlaaanKQLAWIEQRLQSTKADFV 201
Cdd:COG1409  79 ---AMAEAYREYFGDLPPGGLYYSFDYGG--VRFIGLDSNVP-GRSSGELGP----------EQLAWLEEELAAAPAKPV 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50539964 202 IVVGHYPIWSIGHHGPTKCLI--SKLRPLLKKYNVSLYLSGHDHsLQFIREDDGSSFVVSGA 261
Cdd:COG1409 143 IVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVH-RYERTRRDGVPYIVAGS 203
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 5-309 2.08e-23

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 99.51  E-value: 2.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964    5 LAFLLISCLqtFSTASQTNQQassLRFVGIGDWGGRPSYpfytphEADTAKELARVAQSSGLDFVLSLGDNFYyDGVKDV 84
Cdd:PTZ00422   8 VLFSLFVLI--FISSYSVKAQ---LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNFP-GGVDGL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964   85 DDTRFKFSYEQVFSHPA-LMTIPWYLIAGNHDHRGNVSAQ----------------IAYSSRSE---RWIYPDLYYEL-- 142
Cdd:PTZ00422  76 NDPKWKHCFENVYSEESgDMQIPFFTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYft 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  143 ---------NFKVPHSNTSLTILMTDTVVVCGNTYDglDPVGPEDLAAANKQLawieqRLQSTKADFVIVVGHYPIWSIG 213
Cdd:PTZ00422 156 hftdtsgpsLLKSGHKDMSVAFIFIDTWILSSSFPY--KKVSERAWQDLKATL-----EYAPKIADYIIVVGDKPIYSSG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  214 HHGPTKCLISKLRPLLKKYNVSLYLSGHDHSLQFIrEDDGSSFVVSGAGveedsSTDHRKS-FPSAWQLFSSpvnqTSGS 292
Cdd:PTZ00422 229 SSKGDSYLSYYLLPLLKDAQVDLYISGYDRNMEVL-TDEGTAHINCGSG-----GNSGRKSiMKNSKSLFYS----EDIG 298

                        330
                 ....*....|....*..
gi 50539964  293 FVYFEVNKSEMLINYLQ 309
Cdd:PTZ00422 299 FCIHELNAEGMVTKFVS 315
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 29-119 2.91e-05

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: 42.59  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964    29 LRFVGIGDWGGRPSYpfytpheADTAKELARVAQSSGLDFVLSLGDNfyydgvkdVDDTRFKFSYEQVFShPALMTIPWY 108
Cdd:pfam00149   1 MRILVIGDLHLPGQL-------DDLLELLKKLLEEGKPDLVLHAGDL--------VDRGPPSEEVLELLE-RLIKYVPVY 64

                          90
                  ....*....|.
gi 50539964   109 LIAGNHDHRGN 119
Cdd:pfam00149  65 LVRGNHDFDYG 75
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 29-312 5.77e-143

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: 405.17  E-value: 5.77e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  29 LRFVGIGDWGGRPSyPFYTPHEADTAKELARVAQSSGLDFVLSLGDNFYYDGVKDVDDTRFKFSYEQVFSHPALMtIPWY 108
Cdd:cd07378   1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQ-VPWY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 109 LIAGNHDHRGNVSAQIAYSSR--SERWIYPDLYYELNFKVPHSNTSLTILMTDTVVVCGNTYDGLD--PVGPEDLAAANK 184
Cdd:cd07378  79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASgqPRGPPNKKLAET 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 185 QLAWIEQRLQSTKADFVIVVGHYPIWSIGHHGPTKCLISKLRPLLKKYNVSLYLSGHDHSLQFIREDDGSSFVVSGAGVE 264
Cdd:cd07378 159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 50539964 265 EDSSTDHRKSFPSAWQLFSSPVNQTSGSFVYFEVNKSEMLINYLQPDG 312
Cdd:cd07378 239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
45-261 1.73e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 107.47  E-value: 1.73e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  45 FYTPHEADTAKELARV---AQSSGLDFVLSLGDNFYYDGVKDVDDTRFKFsyeqvfshpALMTIPWYLIAGNHDHRGnvs 121
Cdd:COG1409  11 LGAPDGSDTAEVLAAAladINAPRPDFVVVTGDLTDDGEPEEYAAAREIL---------ARLGVPVYVVPGNHDIRA--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 122 aqiAYSSRSERWIYPDLYYELNFKVPHSNtsLTILMTDTVVVcGNTYDGLDPvgpedlaaanKQLAWIEQRLQSTKADFV 201
Cdd:COG1409  79 ---AMAEAYREYFGDLPPGGLYYSFDYGG--VRFIGLDSNVP-GRSSGELGP----------EQLAWLEEELAAAPAKPV 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50539964 202 IVVGHYPIWSIGHHGPTKCLI--SKLRPLLKKYNVSLYLSGHDHsLQFIREDDGSSFVVSGA 261
Cdd:COG1409 143 IVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVH-RYERTRRDGVPYIVAGS 203
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 5-309 2.08e-23

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 99.51  E-value: 2.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964    5 LAFLLISCLqtFSTASQTNQQassLRFVGIGDWGGRPSYpfytphEADTAKELARVAQSSGLDFVLSLGDNFYyDGVKDV 84
Cdd:PTZ00422   8 VLFSLFVLI--FISSYSVKAQ---LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNFP-GGVDGL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964   85 DDTRFKFSYEQVFSHPA-LMTIPWYLIAGNHDHRGNVSAQ----------------IAYSSRSE---RWIYPDLYYEL-- 142
Cdd:PTZ00422  76 NDPKWKHCFENVYSEESgDMQIPFFTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYft 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  143 ---------NFKVPHSNTSLTILMTDTVVVCGNTYDglDPVGPEDLAAANKQLawieqRLQSTKADFVIVVGHYPIWSIG 213
Cdd:PTZ00422 156 hftdtsgpsLLKSGHKDMSVAFIFIDTWILSSSFPY--KKVSERAWQDLKATL-----EYAPKIADYIIVVGDKPIYSSG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  214 HHGPTKCLISKLRPLLKKYNVSLYLSGHDHSLQFIrEDDGSSFVVSGAGveedsSTDHRKS-FPSAWQLFSSpvnqTSGS 292
Cdd:PTZ00422 229 SSKGDSYLSYYLLPLLKDAQVDLYISGYDRNMEVL-TDEGTAHINCGSG-----GNSGRKSiMKNSKSLFYS----EDIG 298

                        330
                 ....*....|....*..
gi 50539964  293 FVYFEVNKSEMLINYLQ 309
Cdd:PTZ00422 299 FCIHELNAEGMVTKFVS 315
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 28-244 4.81e-12

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: 65.40  E-value: 4.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  28 SLRFVGIGDWGgrpsypFYTPHEADTAKELarVAQSSGLDFVLSLGD---NFYYDGVKdVDDTRFKFSyEQVFSHpalmt 104
Cdd:cd00839   4 PLKFAVFGDMG------QNTNNSTNTLDHL--EKELGNYDAIIHVGDiayADGYNNGS-RWDTFMRQI-EPLASY----- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 105 IPWYLIAGNHDHR--GNVSAQIAYSSRSERWIYP-----DLYYELNFKVPHsntsltilmtdTVVVCGNTYdgldpVGPE 177
Cdd:cd00839  69 VPYMVAPGNHEADynGSTSKIKFFMPGRGMPPSPsgsteNLWYSFDVGPVH-----------FISLSTETD-----FLKG 132

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50539964 178 DLAAanKQLAWIEQRLQstKAD-----FVIVVGHYPIWS----IGHHGPTKCLISKLRPLLKKYNVSLYLSGHDHS 244
Cdd:cd00839 133 DNIS--PQYDWLEADLA--KVDrsrtpWIIVMGHRPMYCsnddDADCIEGEKMREALEDLFYKYGVDLVLSGHVHA 204
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 64-264 1.27e-08

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: 54.65  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  64 SGLDFVLSLGDnfYYDGvkDVDDTRFKFSYEQVFSHPALMTIPWYLIAGNHDHRGnvsaqiaYSSRSERWIY-----PDL 138
Cdd:cd07396  45 SNLAFVVQLGD--IIDG--YNAKDRSKEALDAVLSILDRLKGPVHHVLGNHEFYN-------FPREYLNHLKtlngeDAY 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 139 YYELnfkVPHSNtsLTILMTDTVVVCGntydGLDPvgpedlaaanKQLAWIEQRLQSTKA--DFVIVVGHYPIWSigHHG 216
Cdd:cd07396 114 YYSF---SPGPG--FRFLVLDFVKFNG----GIGE----------EQLAWLRNELTSADAngEKVIVLSHLPIYP--EAA 172

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 50539964 217 PTKCLI---SKLRPLLKKY-NVSLYLSGHDHSLQFIREDDGSSFVVSGAGVE 264
Cdd:cd07396 173 DPQCLLwnyEEVLAILESYpCVKACFSGHNHEGGYEQDSHGVHHVTLEGVLE 224
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 107-246 1.50e-08

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 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: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 54.68  E-value: 1.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 107 WYLIAGNHDHRGnvsaqiAYSSRSERWIYpdLYYELNFKVPHSNTSLTILMTDTVVVCGNTYDGLDPVGPEDLAAANKQL 186
Cdd:cd07401  80 LFDIRGNHDLFG------IVSFDSQNNYY--RKYSNTGRDHSHSFSSTTRFGNYSFIGFDPTIFPGPKRPFNFFGSLDKK 151

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50539964 187 ---AWIEQRLQSTKADFVIVVGHYPIWSIGHHGPtKCLISKLRPLLKKYNVSLYLSGHDHSLQ 246
Cdd:cd07401 152 lldRLEKELEKSKNSKYTIWFGHYPHSLIISPSA-KSSSKTFKDLLKKYNVTAYLCGHLHPLG 213
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 92-244 2.02e-07

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: 51.12  E-value: 2.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  92 SYEQVFSHPALMTIPWYLIAGNHDHRGNVSAqiayssrserwIYPDLYYELNFKV--PHSNTSLTILMTDTVVVcGNTYD 169
Cdd:cd07402  57 SYERLRELLAPLPAPVYWIPGNHDDRAAMRE-----------ALPEPPYDDNGPVqyVVDFGGWRLILLDTSVP-GVHHG 124

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50539964 170 GLDPvgpedlaaanKQLAWIEQRLQSTKADFVIVVGHYPIWSIG--HHGPTKCLIS-KLRPLLKKY-NVSLYLSGHDHS 244
Cdd:cd07402 125 ELSD----------EQLDWLEAALAEAPDRPTLIFLHHPPFPLGipWMDAIRLRNSqALFAVLARHpQVKAILCGHIHR 193
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 159-258 3.33e-06

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 45.72  E-value: 3.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 159 DTVVVCG-NTYDGLDPVgpedlaaaNKQLAWIEQRLQSTKADFV-----IVVGHYPIWSIGHHGPTKCLI--SKLRPLLK 230
Cdd:cd00838  28 DLVICLGdLVDYGPDPE--------EVELKALRLLLAGIPVYVVpgnhdILVTHGPPYDPLDEGSPGEDPgsEALLELLD 99

                        90       100
                ....*....|....*....|....*...
gi 50539964 231 KYNVSLYLSGHDHSLQFIREDDGSSFVV 258
Cdd:cd00838 100 KYGPDLVLSGHTHVPGRREVDKGGTLVV 127
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 29-119 2.91e-05

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: 42.59  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964    29 LRFVGIGDWGGRPSYpfytpheADTAKELARVAQSSGLDFVLSLGDNfyydgvkdVDDTRFKFSYEQVFShPALMTIPWY 108
Cdd:pfam00149   1 MRILVIGDLHLPGQL-------DDLLELLKKLLEEGKPDLVLHAGDL--------VDRGPPSEEVLELLE-RLIKYVPVY 64

                          90
                  ....*....|.
gi 50539964   109 LIAGNHDHRGN 119
Cdd:pfam00149  65 LVRGNHDFDYG 75
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 201-262 1.84e-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: 40.74  E-value: 1.84e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50539964 201 VIVVGHYPIWSI--GHHGPTKCLISK-LRPLLKKYNVSLYLSGHDHSLQFIREDDGSSFVVSGAG 262
Cdd:cd07400  73 AIVALHHPLLPPpdTGRERNVLLDAGdALKLLKELGVDLVLHGHKHVPAVWNLGLLNGIVVVNAG 137
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
30-252 2.35e-04

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 41.82  E-value: 2.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964  30 RFVGIGDW--GgrpsYPFYTPH-EADTAK---ELARVAQSSGLDFVLSLGDnFYYDGVKDVDDTRFkfsYEQVFSHPALM 103
Cdd:COG0420   2 RFLHTADWhlG----KPLHGASrREDQLAaldRLVDLAIEEKVDAVLIAGD-LFDSANPSPEAVRL---LAEALRRLSEA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539964 104 TIPWYLIAGNHDhrgnvsaqiaysSRSERWIYPDLYYELNFKV--PHSNTSLTILMTDTVVVCgntydGLDPVGPEDLAA 181
Cdd:COG0420  74 GIPVVLIAGNHD------------SPSRLSAGSPLLENLGVHVfgSVEPEPVELEDGLGVAVY-----GLPYLRPSDEEA 136

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50539964 182 ANKQLAWIEQRLqsTKADFVIVVGHYPIWSIGHHGPTKCLISKLRPLLKKyNVSLYLSGHDHSLQFIREDD 252
Cdd:COG0420 137 LRDLLERLPRAL--DPGGPNILLLHGFVAGASGSRDIYVAPVPLSALPAA-GFDYVALGHIHRPQVLGGDP 204
 
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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