NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17533209|ref|NP_495776|]
View 

ACid Phosphatase family [Caenorhabditis elegans]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
79-371 4.01e-19

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: 85.89  E-value: 4.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209  79 LLFTQVIFRHGARAPgnekqtdtkffprdyGQLTDQGYNHSFMMGRFLKKRYVDTGFLSSFvKPNEMEWRSRDINRCLST 158
Cdd:cd07061   2 LEQVQVLSRHGDRYP---------------GELTPFGRQQAFELGRYFRQRYGELLLLHSY-NRSDLYIRSSDSQRTLQS 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209 159 ASTVAAGMFktENQIWLTVPIVTNLGINDVLLNLpIRGCNFTRNSRIKQCPKtekvnrdemyavlyecmggnhsifqeik 238
Cdd:cd07061  66 AQAFLAGLF--PPDGWQPIAVHTIPEEEDDVSNL-FDLCAYETVAKGYSAPF---------------------------- 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209 239 iddCDRYINEyrnhvpvpEFvrdnfktISEEYLKVRNFQ--NGIGNrKMIKARFGFLVHTLLENLVNAWKHHLARIKSLK 316
Cdd:cd07061 115 ---CDLFTEE--------EW-------VKLEYLNDLKFYygYGPGN-PLARAQGSPLLNELLARLTNGPSGSQTFPLDRK 175
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533209 317 FKVYSSQDWLLGGVLDAFGVLDHIQSKSKEEPN---------YNTMIIMELW--KKNGKPIVKFYY 371
Cdd:cd07061 176 LYLYFSHDTTILPLLTALGLFDFAEPLPPDFLRgfsesdyppFAARLVFELWrcPGDGESYVRVLV 241
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
79-371 4.01e-19

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: 85.89  E-value: 4.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209  79 LLFTQVIFRHGARAPgnekqtdtkffprdyGQLTDQGYNHSFMMGRFLKKRYVDTGFLSSFvKPNEMEWRSRDINRCLST 158
Cdd:cd07061   2 LEQVQVLSRHGDRYP---------------GELTPFGRQQAFELGRYFRQRYGELLLLHSY-NRSDLYIRSSDSQRTLQS 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209 159 ASTVAAGMFktENQIWLTVPIVTNLGINDVLLNLpIRGCNFTRNSRIKQCPKtekvnrdemyavlyecmggnhsifqeik 238
Cdd:cd07061  66 AQAFLAGLF--PPDGWQPIAVHTIPEEEDDVSNL-FDLCAYETVAKGYSAPF---------------------------- 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209 239 iddCDRYINEyrnhvpvpEFvrdnfktISEEYLKVRNFQ--NGIGNrKMIKARFGFLVHTLLENLVNAWKHHLARIKSLK 316
Cdd:cd07061 115 ---CDLFTEE--------EW-------VKLEYLNDLKFYygYGPGN-PLARAQGSPLLNELLARLTNGPSGSQTFPLDRK 175
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533209 317 FKVYSSQDWLLGGVLDAFGVLDHIQSKSKEEPN---------YNTMIIMELW--KKNGKPIVKFYY 371
Cdd:cd07061 176 LYLYFSHDTTILPLLTALGLFDFAEPLPPDFLRgfsesdyppFAARLVFELWrcPGDGESYVRVLV 241
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
79-371 1.52e-08

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: 56.26  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209    79 LLFTQVIFRHGARAP--GNEKQ-TDTKF--------------FPRDY-----------GQLTDQGYNHSFMMGRFLKKRY 130
Cdd:pfam00328   2 LEQVQVVSRHGDRTPtqKFKKSyESLIFkilslagslegklsFPGDYryfklqytlgwGGLTPSGRVQAENLGRYFRQRY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209   131 VdTGFLSSFVKPNEMEWRSRDINRCLSTASTVAAGMFKTENQI-------WLTVPIVTNLGINDVLLNLPIRG---C-NF 199
Cdd:pfam00328  82 V-GGLLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFGPEGEDvdkdlldDSNVAKVTIDEDKKALANNLTAGycsCpAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209   200 TRNSRIKQ------------------------CPKTEKVNRDEMYAVLYECmggnhsiFQEIKIDD----CDRYiNEYrn 251
Cdd:pfam00328 161 EWPLQLLKqvdealdyylpvflepiakrleqlCPGETNLTADDVWALLFLC-------FFETNKADlspfCDLF-TEE-- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209   252 hvpvpEFVRDNFKTISEEYLKVRnfqnGIGNrKMIKARFGFLVHTLLENLVNAWKHHLARIKSLKFKV--YSSQDWLLGG 329
Cdd:pfam00328 231 -----DALHNEYLLDLEEYYGLA----GIGN-ELKKTIGGPLLNELLARLTNDLVCTQEATFPLDAKLylYFTHDTTIYS 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17533209   330 VLDAFGVLDHIQSKSKE----------EPNYNTMIIMELWK---KNGKPIVKFYY 371
Cdd:pfam00328 301 LLSALGLFDDLPPLSSLrvldgysasgEVPYGARLVFELYEcssEKDSRYVRLLL 355
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
79-371 4.01e-19

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: 85.89  E-value: 4.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209  79 LLFTQVIFRHGARAPgnekqtdtkffprdyGQLTDQGYNHSFMMGRFLKKRYVDTGFLSSFvKPNEMEWRSRDINRCLST 158
Cdd:cd07061   2 LEQVQVLSRHGDRYP---------------GELTPFGRQQAFELGRYFRQRYGELLLLHSY-NRSDLYIRSSDSQRTLQS 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209 159 ASTVAAGMFktENQIWLTVPIVTNLGINDVLLNLpIRGCNFTRNSRIKQCPKtekvnrdemyavlyecmggnhsifqeik 238
Cdd:cd07061  66 AQAFLAGLF--PPDGWQPIAVHTIPEEEDDVSNL-FDLCAYETVAKGYSAPF---------------------------- 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209 239 iddCDRYINEyrnhvpvpEFvrdnfktISEEYLKVRNFQ--NGIGNrKMIKARFGFLVHTLLENLVNAWKHHLARIKSLK 316
Cdd:cd07061 115 ---CDLFTEE--------EW-------VKLEYLNDLKFYygYGPGN-PLARAQGSPLLNELLARLTNGPSGSQTFPLDRK 175
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533209 317 FKVYSSQDWLLGGVLDAFGVLDHIQSKSKEEPN---------YNTMIIMELW--KKNGKPIVKFYY 371
Cdd:cd07061 176 LYLYFSHDTTILPLLTALGLFDFAEPLPPDFLRgfsesdyppFAARLVFELWrcPGDGESYVRVLV 241
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
79-371 1.52e-08

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: 56.26  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209    79 LLFTQVIFRHGARAP--GNEKQ-TDTKF--------------FPRDY-----------GQLTDQGYNHSFMMGRFLKKRY 130
Cdd:pfam00328   2 LEQVQVVSRHGDRTPtqKFKKSyESLIFkilslagslegklsFPGDYryfklqytlgwGGLTPSGRVQAENLGRYFRQRY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209   131 VdTGFLSSFVKPNEMEWRSRDINRCLSTASTVAAGMFKTENQI-------WLTVPIVTNLGINDVLLNLPIRG---C-NF 199
Cdd:pfam00328  82 V-GGLLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFGPEGEDvdkdlldDSNVAKVTIDEDKKALANNLTAGycsCpAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209   200 TRNSRIKQ------------------------CPKTEKVNRDEMYAVLYECmggnhsiFQEIKIDD----CDRYiNEYrn 251
Cdd:pfam00328 161 EWPLQLLKqvdealdyylpvflepiakrleqlCPGETNLTADDVWALLFLC-------FFETNKADlspfCDLF-TEE-- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533209   252 hvpvpEFVRDNFKTISEEYLKVRnfqnGIGNrKMIKARFGFLVHTLLENLVNAWKHHLARIKSLKFKV--YSSQDWLLGG 329
Cdd:pfam00328 231 -----DALHNEYLLDLEEYYGLA----GIGN-ELKKTIGGPLLNELLARLTNDLVCTQEATFPLDAKLylYFTHDTTIYS 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17533209   330 VLDAFGVLDHIQSKSKE----------EPNYNTMIIMELWK---KNGKPIVKFYY 371
Cdd:pfam00328 301 LLSALGLFDDLPPLSSLrvldgysasgEVPYGARLVFELYEcssEKDSRYVRLLL 355
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH