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Conserved domains on  [gi|523498731|ref|NP_057445|]
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lysophosphatidic acid phosphatase type 6 isoform 1 [Homo sapiens]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10162533)

histidine phosphatase family protein contains a conserved His residue that is transiently phosphorylated during the catalytic cycle

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
49-379 5.88e-39

Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.


:

Pssm-ID: 132717 [Multi-domain]  Cd Length: 242  Bit Score: 140.20  E-value: 5.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  49 KLKMVQVVFRHGARSPlkplpleeqvewnpqllevppqtqfdytvtnlaggpkpyspydsqyhettlkggmfaGQLTKVG 128
Cdd:cd07061    1 ELEQVQVLSRHGDRYP---------------------------------------------------------GELTPFG 23
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 129 MQQMFALGERLRKNYVEDIPFlsPTFNPQEVFIRSTNIFRNLESTRCLLAGLFQCQKEGPIIIHTDEADSEvlypnyqsc 208
Cdd:cd07061   24 RQQAFELGRYFRQRYGELLLL--HSYNRSDLYIRSSDSQRTLQSAQAFLAGLFPPDGWQPIAVHTIPEEED--------- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 209 wslrqrtrgrrqtaslqpgisedlkkvkdrmgiDSSDKVDFFilldnvAAEQAHNLPSCPMLKRFarmIEQRAVDTS-LY 287
Cdd:cd07061   93 ---------------------------------DVSNLFDLC------AYETVAKGYSAPFCDLF---TEEEWVKLEyLN 130
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 288 ILPKEDRESLQMAVG-----PFLHILESNLLKAMDSATAPDKIRKLYLYAAHDVTFIPLLMTLGIFD------------- 349
Cdd:cd07061  131 DLKFYYGYGPGNPLAraqgsPLLNELLARLTNGPSGSQTFPLDRKLYLYFSHDTTILPLLTALGLFDfaeplppdflrgf 210
                        330       340       350
                 ....*....|....*....|....*....|..
gi 523498731 350 --HKWPPFAVDLTMELYQHLESKEWFVQLYYH 379
Cdd:cd07061  211 seSDYPPFAARLVFELWRCPGDGESYVRVLVN 242
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
49-379 5.88e-39

Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.


Pssm-ID: 132717 [Multi-domain]  Cd Length: 242  Bit Score: 140.20  E-value: 5.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  49 KLKMVQVVFRHGARSPlkplpleeqvewnpqllevppqtqfdytvtnlaggpkpyspydsqyhettlkggmfaGQLTKVG 128
Cdd:cd07061    1 ELEQVQVLSRHGDRYP---------------------------------------------------------GELTPFG 23
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 129 MQQMFALGERLRKNYVEDIPFlsPTFNPQEVFIRSTNIFRNLESTRCLLAGLFQCQKEGPIIIHTDEADSEvlypnyqsc 208
Cdd:cd07061   24 RQQAFELGRYFRQRYGELLLL--HSYNRSDLYIRSSDSQRTLQSAQAFLAGLFPPDGWQPIAVHTIPEEED--------- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 209 wslrqrtrgrrqtaslqpgisedlkkvkdrmgiDSSDKVDFFilldnvAAEQAHNLPSCPMLKRFarmIEQRAVDTS-LY 287
Cdd:cd07061   93 ---------------------------------DVSNLFDLC------AYETVAKGYSAPFCDLF---TEEEWVKLEyLN 130
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 288 ILPKEDRESLQMAVG-----PFLHILESNLLKAMDSATAPDKIRKLYLYAAHDVTFIPLLMTLGIFD------------- 349
Cdd:cd07061  131 DLKFYYGYGPGNPLAraqgsPLLNELLARLTNGPSGSQTFPLDRKLYLYFSHDTTILPLLTALGLFDfaeplppdflrgf 210
                        330       340       350
                 ....*....|....*....|....*....|..
gi 523498731 350 --HKWPPFAVDLTMELYQHLESKEWFVQLYYH 379
Cdd:cd07061  211 seSDYPPFAARLVFELWRCPGDGESYVRVLVN 242
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
49-379 4.65e-26

Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 108.26  E-value: 4.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731   49 KLKMVQVVFRHGARSPLKPLPLEEQVEWNPQLLevppqtqfdytvtnLAGGPKPYSPYDSQYHETTLKGGMFAGQLTKVG 128
Cdd:pfam00328   1 ELEQVQVVSRHGDRTPTQKFKKSYESLIFKILS--------------LAGSLEGKLSFPGDYRYFKLQYTLGWGGLTPSG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  129 MQQMFALGERLRKNYVEDipFLSPTFNPQEVFIRSTNIFRNLESTRCLLAGLF------------QCQKEGPIIIHTDE- 195
Cdd:pfam00328  67 RVQAENLGRYFRQRYVGG--LLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFgpegedvdkdllDDSNVAKVTIDEDKk 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  196 ADSEVLYPNYQSC----WSLRQRTRGRRQTASLQPGISEDL-KKVKDRM-GIDSSDKVDFFILLDNVAAEQ--AHNLPSC 267
Cdd:pfam00328 145 ALANNLTAGYCSCpafeWPLQLLKQVDEALDYYLPVFLEPIaKRLEQLCpGETNLTADDVWALLFLCFFETnkADLSPFC 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  268 PMLKR-FARMIEQRAVDTSLYILPK-EDRESLQMAvGPFLHilesNLLKAMDSATAPDKI------RKLYLYAAHDVTFI 339
Cdd:pfam00328 225 DLFTEeDALHNEYLLDLEEYYGLAGiGNELKKTIG-GPLLN----ELLARLTNDLVCTQEatfpldAKLYLYFTHDTTIY 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 523498731  340 PLLMTLGIFD----------------HKWPPFAVDLTMELYQHL-ESKEWFVQLYYH 379
Cdd:pfam00328 300 SLLSALGLFDdlpplsslrvldgysaSGEVPYGARLVFELYECSsEKDSRYVRLLLN 356
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
49-379 5.88e-39

Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.


Pssm-ID: 132717 [Multi-domain]  Cd Length: 242  Bit Score: 140.20  E-value: 5.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  49 KLKMVQVVFRHGARSPlkplpleeqvewnpqllevppqtqfdytvtnlaggpkpyspydsqyhettlkggmfaGQLTKVG 128
Cdd:cd07061    1 ELEQVQVLSRHGDRYP---------------------------------------------------------GELTPFG 23
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 129 MQQMFALGERLRKNYVEDIPFlsPTFNPQEVFIRSTNIFRNLESTRCLLAGLFQCQKEGPIIIHTDEADSEvlypnyqsc 208
Cdd:cd07061   24 RQQAFELGRYFRQRYGELLLL--HSYNRSDLYIRSSDSQRTLQSAQAFLAGLFPPDGWQPIAVHTIPEEED--------- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 209 wslrqrtrgrrqtaslqpgisedlkkvkdrmgiDSSDKVDFFilldnvAAEQAHNLPSCPMLKRFarmIEQRAVDTS-LY 287
Cdd:cd07061   93 ---------------------------------DVSNLFDLC------AYETVAKGYSAPFCDLF---TEEEWVKLEyLN 130
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731 288 ILPKEDRESLQMAVG-----PFLHILESNLLKAMDSATAPDKIRKLYLYAAHDVTFIPLLMTLGIFD------------- 349
Cdd:cd07061  131 DLKFYYGYGPGNPLAraqgsPLLNELLARLTNGPSGSQTFPLDRKLYLYFSHDTTILPLLTALGLFDfaeplppdflrgf 210
                        330       340       350
                 ....*....|....*....|....*....|..
gi 523498731 350 --HKWPPFAVDLTMELYQHLESKEWFVQLYYH 379
Cdd:cd07061  211 seSDYPPFAARLVFELWRCPGDGESYVRVLVN 242
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
49-379 4.65e-26

Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 108.26  E-value: 4.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731   49 KLKMVQVVFRHGARSPLKPLPLEEQVEWNPQLLevppqtqfdytvtnLAGGPKPYSPYDSQYHETTLKGGMFAGQLTKVG 128
Cdd:pfam00328   1 ELEQVQVVSRHGDRTPTQKFKKSYESLIFKILS--------------LAGSLEGKLSFPGDYRYFKLQYTLGWGGLTPSG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  129 MQQMFALGERLRKNYVEDipFLSPTFNPQEVFIRSTNIFRNLESTRCLLAGLF------------QCQKEGPIIIHTDE- 195
Cdd:pfam00328  67 RVQAENLGRYFRQRYVGG--LLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFgpegedvdkdllDDSNVAKVTIDEDKk 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  196 ADSEVLYPNYQSC----WSLRQRTRGRRQTASLQPGISEDL-KKVKDRM-GIDSSDKVDFFILLDNVAAEQ--AHNLPSC 267
Cdd:pfam00328 145 ALANNLTAGYCSCpafeWPLQLLKQVDEALDYYLPVFLEPIaKRLEQLCpGETNLTADDVWALLFLCFFETnkADLSPFC 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523498731  268 PMLKR-FARMIEQRAVDTSLYILPK-EDRESLQMAvGPFLHilesNLLKAMDSATAPDKI------RKLYLYAAHDVTFI 339
Cdd:pfam00328 225 DLFTEeDALHNEYLLDLEEYYGLAGiGNELKKTIG-GPLLN----ELLARLTNDLVCTQEatfpldAKLYLYFTHDTTIY 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 523498731  340 PLLMTLGIFD----------------HKWPPFAVDLTMELYQHL-ESKEWFVQLYYH 379
Cdd:pfam00328 300 SLLSALGLFDdlpplsslrvldgysaSGEVPYGARLVFELYECSsEKDSRYVRLLLN 356
 
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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