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Conserved domains on  [gi|699964219|ref|NP_001289421|]
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lysosomal acid phosphatase isoform 6 [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 ...
 16-143 3.36e-17

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: 77.80  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219  16 VWNVYDTLFCEQTHGLRLPPWA---SPQTMQRLSRLKDFSFRFLFGIYQqaEKARLQGGVLLAQIRKNLTLMATTSQLP- 91
Cdd:cd07061   94 VSNLFDLCAYETVAKGYSAPFCdlfTEEEWVKLEYLNDLKFYYGYGPGN--PLARAQGSPLLNELLARLTNGPSGSQTFp 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 699964219  92 ---KLLVYSAHDTTLVALQMALDVYN---------------GEQAPYASCHIFELYQ-EDSGNFSVEMYFR 143
Cdd:cd07061  172 ldrKLYLYFSHDTTILPLLTALGLFDfaeplppdflrgfseSDYPPFAARLVFELWRcPGDGESYVRVLVN 242
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
 16-143 3.36e-17

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: 77.80  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219  16 VWNVYDTLFCEQTHGLRLPPWA---SPQTMQRLSRLKDFSFRFLFGIYQqaEKARLQGGVLLAQIRKNLTLMATTSQLP- 91
Cdd:cd07061   94 VSNLFDLCAYETVAKGYSAPFCdlfTEEEWVKLEYLNDLKFYYGYGPGN--PLARAQGSPLLNELLARLTNGPSGSQTFp 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 699964219  92 ---KLLVYSAHDTTLVALQMALDVYN---------------GEQAPYASCHIFELYQ-EDSGNFSVEMYFR 143
Cdd:cd07061  172 ldrKLYLYFSHDTTILPLLTALGLFDfaeplppdflrgfseSDYPPFAARLVFELWRcPGDGESYVRVLVN 242
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 6-143 1.48e-12

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: 65.89  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219    6 TGLTDLTLETVWNVYDTLFCEQ--THGLRLPPWASPQTMQRLSRLKDFSFRF-LFGIYQqaEKARLQGGV----LLAQIR 78
Cdd:pfam00328 194 PGETNLTADDVWALLFLCFFETnkADLSPFCDLFTEEDALHNEYLLDLEEYYgLAGIGN--ELKKTIGGPllneLLARLT 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219   79 KNLTLMATTSQLP--KLLVYSAHDTTLVALQMALDVYNGEQ----------------APYASCHIFELYQ--EDSGNFSV 138
Cdd:pfam00328 272 NDLVCTQEATFPLdaKLYLYFTHDTTIYSLLSALGLFDDLPplsslrvldgysasgeVPYGARLVFELYEcsSEKDSRYV 351


                  ....*
gi 699964219  139 EMYFR 143
Cdd:pfam00328 352 RLLLN 356
PRK10173 PRK10173
glucose-1-phosphatase/inositol phosphatase; Provisional
 38-170 3.52e-03

glucose-1-phosphatase/inositol phosphatase; Provisional


Pssm-ID: 182284  Cd Length: 413  Bit Score: 38.16  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219  38 SPQTMQRLSRLKDFSFRFLFGiyqQAEKARLQGGVLLAQIRKNLTLMATTSqlPKLLVYSAHDTTLVALQMALDV--YN- 114
Cdd:PRK10173 255 TDQQWKVLSKLKNGYQDSLFT---SPEVARNVAKPLVKYIDKALVTDRASA--PKVTVLVGHDSNIASLLTALDFkpYQl 329

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 699964219 115 ---GEQAPYASCHIFELYQEDSGN---FSVEMYF------RNE---SDKAPwP----LSLPGCP----HRCPLQDFLRL 170
Cdd:PRK10173 330 hdqYERTPIGGKIVFQRWHDSKANrdlMKIEYVYqsaeqlRNAdalTLQAP-PqrvtLELKGCPidanGFCPMDKFDSV 407
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
 16-143 3.36e-17

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: 77.80  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219  16 VWNVYDTLFCEQTHGLRLPPWA---SPQTMQRLSRLKDFSFRFLFGIYQqaEKARLQGGVLLAQIRKNLTLMATTSQLP- 91
Cdd:cd07061   94 VSNLFDLCAYETVAKGYSAPFCdlfTEEEWVKLEYLNDLKFYYGYGPGN--PLARAQGSPLLNELLARLTNGPSGSQTFp 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 699964219  92 ---KLLVYSAHDTTLVALQMALDVYN---------------GEQAPYASCHIFELYQ-EDSGNFSVEMYFR 143
Cdd:cd07061  172 ldrKLYLYFSHDTTILPLLTALGLFDfaeplppdflrgfseSDYPPFAARLVFELWRcPGDGESYVRVLVN 242
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 6-143 1.48e-12

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: 65.89  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219    6 TGLTDLTLETVWNVYDTLFCEQ--THGLRLPPWASPQTMQRLSRLKDFSFRF-LFGIYQqaEKARLQGGV----LLAQIR 78
Cdd:pfam00328 194 PGETNLTADDVWALLFLCFFETnkADLSPFCDLFTEEDALHNEYLLDLEEYYgLAGIGN--ELKKTIGGPllneLLARLT 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219   79 KNLTLMATTSQLP--KLLVYSAHDTTLVALQMALDVYNGEQ----------------APYASCHIFELYQ--EDSGNFSV 138
Cdd:pfam00328 272 NDLVCTQEATFPLdaKLYLYFTHDTTIYSLLSALGLFDDLPplsslrvldgysasgeVPYGARLVFELYEcsSEKDSRYV 351


                  ....*
gi 699964219  139 EMYFR 143
Cdd:pfam00328 352 RLLLN 356
PRK10173 PRK10173
glucose-1-phosphatase/inositol phosphatase; Provisional
 38-170 3.52e-03

glucose-1-phosphatase/inositol phosphatase; Provisional


Pssm-ID: 182284  Cd Length: 413  Bit Score: 38.16  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964219  38 SPQTMQRLSRLKDFSFRFLFGiyqQAEKARLQGGVLLAQIRKNLTLMATTSqlPKLLVYSAHDTTLVALQMALDV--YN- 114
Cdd:PRK10173 255 TDQQWKVLSKLKNGYQDSLFT---SPEVARNVAKPLVKYIDKALVTDRASA--PKVTVLVGHDSNIASLLTALDFkpYQl 329

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 699964219 115 ---GEQAPYASCHIFELYQEDSGN---FSVEMYF------RNE---SDKAPwP----LSLPGCP----HRCPLQDFLRL 170
Cdd:PRK10173 330 hdqYERTPIGGKIVFQRWHDSKANrdlMKIEYVYqsaeqlRNAdalTLQAP-PqrvtLELKGCPidanGFCPMDKFDSV 407
 
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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