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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215  95 RAKLEAILDWHHSNLRRGAATFILNTVLAPSL-GLPSSPQAAKEAEKVLFRSLGLIESMWLKGNaKFLLGNpQLSIADLS 173
Cdd:cd03183     2 RARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFgGTPVSPEKVKKAEENLEESLDLLENKFLKDK-PFLAGD-EISIADLS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002309215 174 LVCEIMQLEVLGDserdRILGPHEKIRSWVQNVKKATSPHFDEVHELIFKM 224
Cdd:cd03183    80 AICEIMQPEAAGY----DVFEGRPKLAAWRKRVKEAGNPLFDEAHKVIYKL 126

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215  95 RAKLEAILDWHHSNLRRGAATFILNTVLAPSL-GLPSSPQAAKEAEKVLFRSLGLIESMWLKGNaKFLLGNpQLSIADLS 173
Cdd:cd03183     2 RARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFgGTPVSPEKVKKAEENLEESLDLLENKFLKDK-PFLAGD-EISIADLS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002309215 174 LVCEIMQLEVLGDserdRILGPHEKIRSWVQNVKKATSPHFDEVHELIFKM 224
Cdd:cd03183    80 AICEIMQPEAAGY----DVFEGRPKLAAWRKRVKEAGNPLFDEAHKVIYKL 126

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215   5 LKVYADRRSQPSRAIIIFCRVNRIDFEEVTVDLFKREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLATVFPGva 84
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPE-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215  85 DHWYPADLFTRAKLEAILDWHHSNLrrGAATFILNTVLAPslglPSSPQAAKEAEKVLFRSLGLIESMWlkGNAKFLLGN 164
Cdd:COG0625    80 PPLLPADPAARARVRQWLAWADGDL--HPALRNLLERLAP----EKDPAAIARARAELARLLAVLEARL--AGGPYLAGD 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1002309215 165 pQLSIADLSLVCEIMQLEVLGDSerdriLGPHEKIRSWVQNVK 207
Cdd:COG0625   152 -RFSIADIALAPVLRRLDRLGLD-----LADYPNLAAWLARLA 188

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002309215   5 LKVYADRRSQPSRAIIIFCRVNRIDFEEVTVDLFKREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLA 77
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIA 75

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215 132 PQAAKEAEKVLFRS------LGLIESMWLKGNAKFLLGNpQLSIADLSLVCEIMQLEVLGDSErdrILGPHEKIRSWVQN 205
Cdd:pfam14497  15 DEKKKAKRRKEFREerlpkfLGYFEKVLNKNGGGYLVGD-KLTYADLALFQVLDGLLYPKAPD---ALDKYPKLKALHER 90

                  ..
gi 1002309215 206 VK 207
Cdd:pfam14497  91 VA 92

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215  95 RAKLEAILDWHHSNLRRGAATFILNTVLAPSL-GLPSSPQAAKEAEKVLFRSLGLIESMWLKGNaKFLLGNpQLSIADLS 173
Cdd:cd03183     2 RARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFgGTPVSPEKVKKAEENLEESLDLLENKFLKDK-PFLAGD-EISIADLS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002309215 174 LVCEIMQLEVLGDserdRILGPHEKIRSWVQNVKKATSPHFDEVHELIFKM 224
Cdd:cd03183    80 AICEIMQPEAAGY----DVFEGRPKLAAWRKRVKEAGNPLFDEAHKVIYKL 126

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215   5 LKVYADRRSQPSRAIIIFCRVNRIDFEEVTVDLFKREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLATVFPGva 84
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPE-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215  85 DHWYPADLFTRAKLEAILDWHHSNLrrGAATFILNTVLAPslglPSSPQAAKEAEKVLFRSLGLIESMWlkGNAKFLLGN 164
Cdd:COG0625    80 PPLLPADPAARARVRQWLAWADGDL--HPALRNLLERLAP----EKDPAAIARARAELARLLAVLEARL--AGGPYLAGD 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1002309215 165 pQLSIADLSLVCEIMQLEVLGDSerdriLGPHEKIRSWVQNVK 207
Cdd:COG0625   152 -RFSIADIALAPVLRRLDRLGLD-----LADYPNLAAWLARLA 188

GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial 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. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002309215   5 LKVYADRRSQPSRAIIIFCRVNRIDFEEVTVDLFKREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLA 77
Cdd:cd03053     2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLA 74

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002309215   5 LKVYADRRSQPSRAIIIFCRVNRIDFEEVTVDLFKREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLA 77
Cdd:cd03045     1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIYLV 73

glutathione transferase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215  28 IDFEEVTVDLFKREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLATVFPgvADHW---YPADLFTRAKLEAILDW 104
Cdd:PRK15113   31 LPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFA--PPAWeriYPADLQARARARQIQAW 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002309215 105 HHSNL---RRGAATfilNTVLAPSLGLPSSPQAAKEAEKvLFRSLGliesMWLKGNAKFLLGnpQLSIADLSL 174
Cdd:PRK15113  109 LRSDLmplREERPT---DVVFAGAKKAPLSEAGKAAAEK-LFAVAE----RLLAPGQPNLFG--EWCIADTDL 171

GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002309215  28 IDFEEVTVDLFKREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLATVFP 81
Cdd:cd03046    23 LPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002309215  28 IDFEEVTVDLFKREHLSPEFKKINPMGQVPAIVD---GRFRLFESHAILRYLA 77
Cdd:cd03048    24 LPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDhngTPLTVFESGAILLYLA 76

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002309215   5 LKVYADRRSQPSRAIIIFCRVNRIDFEEVTVDLFKREHLSPEFKKINPMGQVPAIV--DGRFrLFESHAILRYL 76
Cdd:cd03051     1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLEldDGTV-ITESVAICRYL 73

GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with similarity to GSTs. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1002309215  45 PEFKKINPMGQVPAIVDGRFRLFESHAILRYLA 77
Cdd:cd03047    41 PEFLAMNPNGRVPVLEDGDFVLWESNAILRYLA 73

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002309215   8 YADRRSQPSRAIIIFCRVNRIDFEEVTVDLFKRehlSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLATVFPG 82
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDH---PPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPG 73

GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002309215  28 IDFEEVTVDlfKREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLA 77
Cdd:cd03039    24 VEYEDVRIT--YEEWPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLA 71

GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, with similarity to GSTs. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002309215  28 IDFEEVTVDLFkREHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYLA 77
Cdd:cd03043    25 IPFEEILVPLY-TPDTRARILEFSPTGKVPVLVDGGIVVWDSLAICEYLA 73

putative S-transferase; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002309215  47 FKKINPMGQVPAIVDGR----FRLFESHAILRYLATVFpgvaDHWYPADLFTRAKLEAILDWHHsnlrrGAATFI 117
Cdd:PRK11752   92 FVEINPNSKIPALLDRSgnppIRVFESGAILLYLAEKF----GAFLPKDLAARTETLNWLFWQQ-----GSAPFL 157

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002309215  28 IDFEEVTVDLFkreHLSPEFKKINPMGQVPAIVDGRFRLFESHAILRYL 76
Cdd:cd03059    24 VSVEIIDVDPD---NPPEDLAELNPYGTVPTLVDRDLVLYESRIIMEYL 69

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002309215 146 LGLIESMwLKGNaKFLLGNpQLSIADLSLVCEIMQLEVLG-DserdriLGPHEKIRSWVQNVKK 208
Cdd:cd03177    47 LEFLETF-LEGS-DYVAGD-QLTIADLSLVATVSTLEVVGfD------LSKYPNVAAWYERLKA 101

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309215 132 PQAAKEAEKVLFRS------LGLIESMWLKGNAKFLLGNpQLSIADLSLVCEIMQLEVLGDSErdrILGPHEKIRSWVQN 205
Cdd:pfam14497  15 DEKKKAKRRKEFREerlpkfLGYFEKVLNKNGGGYLVGD-KLTYADLALFQVLDGLLYPKAPD---ALDKYPKLKALHER 90

                  ..
gi 1002309215 206 VK 207
Cdd:pfam14497  91 VA 92