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Conserved domains on  [gi|665410591|ref|NP_001287119|]
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uncharacterized protein Dmel_CG9449, isoform J [Drosophila melanogaster]

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 ...
 35-156 6.62e-22

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: 88.20  E-value: 6.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410591  35 TLELLHVVFRHGPRTPadtyprdpyvnetyypfgwGQITNNGKRELFNIGTWLRKRYGK-FLAPNYSPDSVHAQATGVPR 113
Cdd:cd07061    1 ELEQVQVLSRHGDRYP-------------------GELTPFGRQQAFELGRYFRQRYGElLLLHSYNRSDLYIRSSDSQR 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 665410591 114 THMTMQTVLAAFFPPKGtdmewnsrfnWQPIPVFSQELNEDTV 156
Cdd:cd07061   62 TLQSAQAFLAGLFPPDG----------WQPIAVHTIPEEEDDV 94
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
 35-156 6.62e-22

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: 88.20  E-value: 6.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410591  35 TLELLHVVFRHGPRTPadtyprdpyvnetyypfgwGQITNNGKRELFNIGTWLRKRYGK-FLAPNYSPDSVHAQATGVPR 113
Cdd:cd07061    1 ELEQVQVLSRHGDRYP-------------------GELTPFGRQQAFELGRYFRQRYGElLLLHSYNRSDLYIRSSDSQR 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 665410591 114 THMTMQTVLAAFFPPKGtdmewnsrfnWQPIPVFSQELNEDTV 156
Cdd:cd07061   62 TLQSAQAFLAGLFPPDG----------WQPIAVHTIPEEEDDV 94
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 35-146 6.79e-13

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: 65.12  E-value: 6.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410591   35 TLELLHVVFRHGPRTP------------------------ADTYPRDPYVNETYYPFGWGQITNNGKRELFNIGTWLRKR 90
Cdd:pfam00328   1 ELEQVQVVSRHGDRTPtqkfkksyeslifkilslagslegKLSFPGDYRYFKLQYTLGWGGLTPSGRVQAENLGRYFRQR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665410591   91 Y-GKFLAPNYSPDSVHAQATGVPRTHMTMQTVLAAFFPPKGTDmEWNSRFNWQPIPV 146
Cdd:pfam00328  81 YvGGLLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFGPEGED-VDKDLLDDSNVAK 136
 
Name Accession Description Interval E-value
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
 35-156 6.62e-22

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: 88.20  E-value: 6.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410591  35 TLELLHVVFRHGPRTPadtyprdpyvnetyypfgwGQITNNGKRELFNIGTWLRKRYGK-FLAPNYSPDSVHAQATGVPR 113
Cdd:cd07061    1 ELEQVQVLSRHGDRYP-------------------GELTPFGRQQAFELGRYFRQRYGElLLLHSYNRSDLYIRSSDSQR 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 665410591 114 THMTMQTVLAAFFPPKGtdmewnsrfnWQPIPVFSQELNEDTV 156
Cdd:cd07061   62 TLQSAQAFLAGLFPPDG----------WQPIAVHTIPEEEDDV 94
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 35-146 6.79e-13

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: 65.12  E-value: 6.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410591   35 TLELLHVVFRHGPRTP------------------------ADTYPRDPYVNETYYPFGWGQITNNGKRELFNIGTWLRKR 90
Cdd:pfam00328   1 ELEQVQVVSRHGDRTPtqkfkksyeslifkilslagslegKLSFPGDYRYFKLQYTLGWGGLTPSGRVQAENLGRYFRQR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665410591   91 Y-GKFLAPNYSPDSVHAQATGVPRTHMTMQTVLAAFFPPKGTDmEWNSRFNWQPIPV 146
Cdd:pfam00328  81 YvGGLLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFGPEGED-VDKDLLDDSNVAK 136
 
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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