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Conserved domains on  [gi|1064303047|sp|F1NPQ2|]
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RecName: Full=Multiple inositol polyphosphate phosphatase 1; AltName: Full=2,3-bisphosphoglycerate 3-phosphatase; Short=2,3-BPG phosphatase; AltName: Full=Band 17; AltName: Full=Histidine phosphatase of the endoplasmic reticulum 1; Short=HiPER1; Flags: Precursor

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 ...
62-399 2.42e-47

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: 162.93  E-value: 2.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047  62 QLRAVLRHGTRYPtagqirrlaelhgrlrraaapscpaaaalaawpmwyeeslDRLAPRGRRDMEHLARRLAARFPALF- 140
Cdd:cd07061     4 QVQVLSRHGDRYP----------------------------------------GELTPFGRQQAFELGRYFRQRYGELLl 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 141 ---AARRRLALASSSKHRCLQSGAAFRRGLGPSLSLG--ADETEIEvndalmrffdhcdkfvafvEDNDTAMyqvnafke 215
Cdd:cd07061    44 lhsYNRSDLYIRSSDSQRTLQSAQAFLAGLFPPDGWQpiAVHTIPE-------------------EEDDVSN-------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 216 gpemrkvlekvasalclpaselnadlvqvAFLTCSYELAIKNVTSPWCSLFSEEDAKVLEYLNDLKQYWKRGYGYDINSR 295
Cdd:cd07061    97 -----------------------------LFDLCAYETVAKGYSAPFCDLFTEEEWVKLEYLNDLKFYYGYGPGNPLARA 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 296 SSCILFQDIFQQLDKAVDESrSSKPISSPLIVQVGHAETLQPLLALMGYFKDAEPLQAnnyirQAHRKFRSGRIVPYAAN 375
Cdd:cd07061   148 QGSPLLNELLARLTNGPSGS-QTFPLDRKLYLYFSHDTTILPLLTALGLFDFAEPLPP-----DFLRGFSESDYPPFAAR 221
                         330       340
                  ....*....|....*....|....
gi 1064303047 376 LVFVLYHCEQktsKEEYQVQMLLN 399
Cdd:cd07061   222 LVFELWRCPG---DGESYVRVLVN 242
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
62-399 2.42e-47

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: 162.93  E-value: 2.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047  62 QLRAVLRHGTRYPtagqirrlaelhgrlrraaapscpaaaalaawpmwyeeslDRLAPRGRRDMEHLARRLAARFPALF- 140
Cdd:cd07061     4 QVQVLSRHGDRYP----------------------------------------GELTPFGRQQAFELGRYFRQRYGELLl 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 141 ---AARRRLALASSSKHRCLQSGAAFRRGLGPSLSLG--ADETEIEvndalmrffdhcdkfvafvEDNDTAMyqvnafke 215
Cdd:cd07061    44 lhsYNRSDLYIRSSDSQRTLQSAQAFLAGLFPPDGWQpiAVHTIPE-------------------EEDDVSN-------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 216 gpemrkvlekvasalclpaselnadlvqvAFLTCSYELAIKNVTSPWCSLFSEEDAKVLEYLNDLKQYWKRGYGYDINSR 295
Cdd:cd07061    97 -----------------------------LFDLCAYETVAKGYSAPFCDLFTEEEWVKLEYLNDLKFYYGYGPGNPLARA 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 296 SSCILFQDIFQQLDKAVDESrSSKPISSPLIVQVGHAETLQPLLALMGYFKDAEPLQAnnyirQAHRKFRSGRIVPYAAN 375
Cdd:cd07061   148 QGSPLLNELLARLTNGPSGS-QTFPLDRKLYLYFSHDTTILPLLTALGLFDFAEPLPP-----DFLRGFSESDYPPFAAR 221
                         330       340
                  ....*....|....*....|....
gi 1064303047 376 LVFVLYHCEQktsKEEYQVQMLLN 399
Cdd:cd07061   222 LVFELWRCPG---DGESYVRVLVN 242
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
62-399 1.45e-45

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: 161.81  E-value: 1.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047  62 QLRAVLRHGTRYPTAG---QIRRLAELHGRLRRAAAPSCPAAAALAAWPMWYEESLDRLAPRGRRDMEHLARRLAARFPA 138
Cdd:pfam00328   4 QVQVVSRHGDRTPTQKfkkSYESLIFKILSLAGSLEGKLSFPGDYRYFKLQYTLGWGGLTPSGRVQAENLGRYFRQRYVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 139 LFA----ARRRLALASSSKHRCLQSGAAFRRGLGPSLSLGA---------------DETEIEVNDALMRFFDHCDKFVAF 199
Cdd:pfam00328  84 GLLrdgyNAKDIYIRASSEGRVIASAQAFAEGLFGPEGEDVdkdllddsnvakvtiDEDKKALANNLTAGYCSCPAFEWP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 200 VEDNDTAMYQVNAFKegPEMRKVLEKVASALCLPASELNADLVQVAFLTCSYELAIKNvTSPWCSLFSEEDAKVLEYLND 279
Cdd:pfam00328 164 LQLLKQVDEALDYYL--PVFLEPIAKRLEQLCPGETNLTADDVWALLFLCFFETNKAD-LSPFCDLFTEEDALHNEYLLD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 280 LKQYWKR-GYGYDINSRSSCILFQDIFQQL-DKAVDESRSSKPISSPLIVQVGHAETLQPLLALMGYFKDAEPLQAnnyi 357
Cdd:pfam00328 241 LEEYYGLaGIGNELKKTIGGPLLNELLARLtNDLVCTQEATFPLDAKLYLYFTHDTTIYSLLSALGLFDDLPPLSS---- 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1064303047 358 RQAHRKFRSGRIVPYAANLVFVLYHCEQKtsKEEYQVQMLLN 399
Cdd:pfam00328 317 LRVLDGYSASGEVPYGARLVFELYECSSE--KDSRYVRLLLN 356
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
115-186 6.32e-04

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 40.24  E-value: 6.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1064303047 115 DR-LAPRGRRDMEHLARRLAARFPALfaarrRLALASSSKhRCLQSGAAFRRGLGpslslgaDETEIEVNDAL 186
Cdd:COG2062    20 DRpLTERGRRQARAMARWLAALGLKP-----DRILSSPAL-RARQTAEILAEALG-------LPPKVEVEDEL 79
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
62-399 2.42e-47

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: 162.93  E-value: 2.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047  62 QLRAVLRHGTRYPtagqirrlaelhgrlrraaapscpaaaalaawpmwyeeslDRLAPRGRRDMEHLARRLAARFPALF- 140
Cdd:cd07061     4 QVQVLSRHGDRYP----------------------------------------GELTPFGRQQAFELGRYFRQRYGELLl 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 141 ---AARRRLALASSSKHRCLQSGAAFRRGLGPSLSLG--ADETEIEvndalmrffdhcdkfvafvEDNDTAMyqvnafke 215
Cdd:cd07061    44 lhsYNRSDLYIRSSDSQRTLQSAQAFLAGLFPPDGWQpiAVHTIPE-------------------EEDDVSN-------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 216 gpemrkvlekvasalclpaselnadlvqvAFLTCSYELAIKNVTSPWCSLFSEEDAKVLEYLNDLKQYWKRGYGYDINSR 295
Cdd:cd07061    97 -----------------------------LFDLCAYETVAKGYSAPFCDLFTEEEWVKLEYLNDLKFYYGYGPGNPLARA 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 296 SSCILFQDIFQQLDKAVDESrSSKPISSPLIVQVGHAETLQPLLALMGYFKDAEPLQAnnyirQAHRKFRSGRIVPYAAN 375
Cdd:cd07061   148 QGSPLLNELLARLTNGPSGS-QTFPLDRKLYLYFSHDTTILPLLTALGLFDFAEPLPP-----DFLRGFSESDYPPFAAR 221
                         330       340
                  ....*....|....*....|....
gi 1064303047 376 LVFVLYHCEQktsKEEYQVQMLLN 399
Cdd:cd07061   222 LVFELWRCPG---DGESYVRVLVN 242
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
62-399 1.45e-45

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: 161.81  E-value: 1.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047  62 QLRAVLRHGTRYPTAG---QIRRLAELHGRLRRAAAPSCPAAAALAAWPMWYEESLDRLAPRGRRDMEHLARRLAARFPA 138
Cdd:pfam00328   4 QVQVVSRHGDRTPTQKfkkSYESLIFKILSLAGSLEGKLSFPGDYRYFKLQYTLGWGGLTPSGRVQAENLGRYFRQRYVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 139 LFA----ARRRLALASSSKHRCLQSGAAFRRGLGPSLSLGA---------------DETEIEVNDALMRFFDHCDKFVAF 199
Cdd:pfam00328  84 GLLrdgyNAKDIYIRASSEGRVIASAQAFAEGLFGPEGEDVdkdllddsnvakvtiDEDKKALANNLTAGYCSCPAFEWP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 200 VEDNDTAMYQVNAFKegPEMRKVLEKVASALCLPASELNADLVQVAFLTCSYELAIKNvTSPWCSLFSEEDAKVLEYLND 279
Cdd:pfam00328 164 LQLLKQVDEALDYYL--PVFLEPIAKRLEQLCPGETNLTADDVWALLFLCFFETNKAD-LSPFCDLFTEEDALHNEYLLD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064303047 280 LKQYWKR-GYGYDINSRSSCILFQDIFQQL-DKAVDESRSSKPISSPLIVQVGHAETLQPLLALMGYFKDAEPLQAnnyi 357
Cdd:pfam00328 241 LEEYYGLaGIGNELKKTIGGPLLNELLARLtNDLVCTQEATFPLDAKLYLYFTHDTTIYSLLSALGLFDDLPPLSS---- 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1064303047 358 RQAHRKFRSGRIVPYAANLVFVLYHCEQKtsKEEYQVQMLLN 399
Cdd:pfam00328 317 LRVLDGYSASGEVPYGARLVFELYECSSE--KDSRYVRLLLN 356
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
115-186 6.32e-04

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 40.24  E-value: 6.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1064303047 115 DR-LAPRGRRDMEHLARRLAARFPALfaarrRLALASSSKhRCLQSGAAFRRGLGpslslgaDETEIEVNDAL 186
Cdd:COG2062    20 DRpLTERGRRQARAMARWLAALGLKP-----DRILSSPAL-RARQTAEILAEALG-------LPPKVEVEDEL 79
 
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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