unnamed protein product [Arabidopsis thaliana]
Protein Classification
glutathione S-transferase family protein( domain architecture ID 11418207)
glutathione S-transferase family protein similar to Saccharomyces cerevisiae glutathione S-transferase omega-like proteins and Escherichia coli glutathionyl-hydroquinone reductase
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ECM4 | COG0435 | Glutathionyl-hydroquinone reductase [Energy production and conversion]; |
11-321 | 4.80e-161 | |||||
Glutathionyl-hydroquinone reductase [Energy production and conversion]; : Pssm-ID: 440204 [Multi-domain] Cd Length: 321 Bit Score: 453.05 E-value: 4.80e-161
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| Name | Accession | Description | Interval | E-value | |||||
| ECM4 | COG0435 | Glutathionyl-hydroquinone reductase [Energy production and conversion]; |
11-321 | 4.80e-161 | |||||
Glutathionyl-hydroquinone reductase [Energy production and conversion]; Pssm-ID: 440204 [Multi-domain] Cd Length: 321 Bit Score: 453.05 E-value: 4.80e-161
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| GST_C_Omega_like | cd03190 | C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ... |
166-307 | 1.63e-71 | |||||
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast. Pssm-ID: 198299 [Multi-domain] Cd Length: 142 Bit Score: 218.98 E-value: 1.63e-71
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| GST_C_2 | pfam13410 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
204-262 | 1.39e-08 | |||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 433185 [Multi-domain] Cd Length: 67 Bit Score: 50.78 E-value: 1.39e-08
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| Name | Accession | Description | Interval | E-value | |||||
| ECM4 | COG0435 | Glutathionyl-hydroquinone reductase [Energy production and conversion]; |
11-321 | 4.80e-161 | |||||
Glutathionyl-hydroquinone reductase [Energy production and conversion]; Pssm-ID: 440204 [Multi-domain] Cd Length: 321 Bit Score: 453.05 E-value: 4.80e-161
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| GST_C_Omega_like | cd03190 | C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ... |
166-307 | 1.63e-71 | |||||
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast. Pssm-ID: 198299 [Multi-domain] Cd Length: 142 Bit Score: 218.98 E-value: 1.63e-71
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| GST_C_2 | pfam13410 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
204-262 | 1.39e-08 | |||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 433185 [Multi-domain] Cd Length: 67 Bit Score: 50.78 E-value: 1.39e-08
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| GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
45-151 | 1.01e-05 | |||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 42.62 E-value: 1.01e-05
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| GST_C_family | cd00299 | C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ... |
170-263 | 7.52e-04 | |||||
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases. Pssm-ID: 198286 [Multi-domain] Cd Length: 100 Bit Score: 38.25 E-value: 7.52e-04
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| GST_C_YfcG_like | cd10291 | C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ... |
198-244 | 1.47e-03 | |||||
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified. Pssm-ID: 198324 [Multi-domain] Cd Length: 110 Bit Score: 37.63 E-value: 1.47e-03
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| GST_C_Delta_Epsilon | cd03177 | C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
204-240 | 1.55e-03 | |||||
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress. Pssm-ID: 198287 [Multi-domain] Cd Length: 117 Bit Score: 37.90 E-value: 1.55e-03
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| GST_C_Theta | cd03183 | C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ... |
170-234 | 3.77e-03 | |||||
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is the subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from the aryl or alkyl sulfate esters. Pssm-ID: 198292 [Multi-domain] Cd Length: 126 Bit Score: 36.81 E-value: 3.77e-03
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| Blast search parameters | ||||
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