inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP2 isoform X1 [Arachis hypogaea]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| His_Phos_2 | pfam00328 | Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ... |
375-969 | 3.08e-61 | |||||||||
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: 213.04 E-value: 3.08e-61
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| PPIP5K2_N | pfam18086 | Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain ... |
18-113 | 1.58e-53 | |||||||||
Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain found in the Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (PPIP5K2), EC:2.7.4.24. Structure analysis of human PPIP5K2 indicate that this region forms alpha-beta-alpha domain.PPIP5K2 is one of the mammalian PPIP5K isoforms responsible for synthesis of diphosphoinositol polyphosphates (inositol pyrophosphates; PP-InsPs), regulatory molecules that function at the interface of cell signaling and organizmic homeostasis. : Pssm-ID: 465643 Cd Length: 90 Bit Score: 181.18 E-value: 1.58e-53
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| LysX | COG0189 | Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
87-304 | 4.07e-12 | |||||||||
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis : Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 68.04 E-value: 4.07e-12
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| Name | Accession | Description | Interval | E-value | |||||||||
| His_Phos_2 | pfam00328 | Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ... |
375-969 | 3.08e-61 | |||||||||
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: 213.04 E-value: 3.08e-61
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| PPIP5K2_N | pfam18086 | Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain ... |
18-113 | 1.58e-53 | |||||||||
Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain found in the Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (PPIP5K2), EC:2.7.4.24. Structure analysis of human PPIP5K2 indicate that this region forms alpha-beta-alpha domain.PPIP5K2 is one of the mammalian PPIP5K isoforms responsible for synthesis of diphosphoinositol polyphosphates (inositol pyrophosphates; PP-InsPs), regulatory molecules that function at the interface of cell signaling and organizmic homeostasis. Pssm-ID: 465643 Cd Length: 90 Bit Score: 181.18 E-value: 1.58e-53
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| HP_HAP_like | cd07061 | Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ... |
512-604 | 4.08e-18 | |||||||||
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: 85.12 E-value: 4.08e-18
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| LysX | COG0189 | Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
87-304 | 4.07e-12 | |||||||||
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 68.04 E-value: 4.07e-12
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| Name | Accession | Description | Interval | E-value | |||||||||
| His_Phos_2 | pfam00328 | Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ... |
375-969 | 3.08e-61 | |||||||||
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: 213.04 E-value: 3.08e-61
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| PPIP5K2_N | pfam18086 | Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain ... |
18-113 | 1.58e-53 | |||||||||
Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain found in the Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (PPIP5K2), EC:2.7.4.24. Structure analysis of human PPIP5K2 indicate that this region forms alpha-beta-alpha domain.PPIP5K2 is one of the mammalian PPIP5K isoforms responsible for synthesis of diphosphoinositol polyphosphates (inositol pyrophosphates; PP-InsPs), regulatory molecules that function at the interface of cell signaling and organizmic homeostasis. Pssm-ID: 465643 Cd Length: 90 Bit Score: 181.18 E-value: 1.58e-53
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| HP_HAP_like | cd07061 | Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ... |
512-604 | 4.08e-18 | |||||||||
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: 85.12 E-value: 4.08e-18
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| LysX | COG0189 | Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
87-304 | 4.07e-12 | |||||||||
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 68.04 E-value: 4.07e-12
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| His_Phos_1 | pfam00300 | Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ... |
514-573 | 9.00e-03 | |||||||||
Histidine phosphatase superfamily (branch 1); 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 larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members. Pssm-ID: 459751 [Multi-domain] Cd Length: 194 Bit Score: 38.73 E-value: 9.00e-03
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