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Conserved domains on  [gi|2462492125|ref|XP_054185431|]
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glutathione S-transferase theta-1 isoform X1 [Homo sapiens]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 10122710)

glutathione S-transferase (GST) family protein such as bacterial dichloromethane dehalogenase, which catalyzes the GSH-dependent hydrolytic dehalogenation of dihalomethanes and class theta GSTs that catalyze the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 140-265 2.03e-58

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: 182.80  E-value: 2.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 140 ARARVDEYLAWQHTTLRRSCLRALWHKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVA 219
Cdd:cd03183     1 KRARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTPVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462492125 220 ITELMHPVGAGCQVFEGRPKLATWRQRVEAAvGEDLFQEAHEVILK 265
Cdd:cd03183    81 ICEIMQPEAAGYDVFEGRPKLAAWRKRVKEA-GNPLFDEAHKVIYK 125
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 3-127 2.54e-32

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


:

Pssm-ID: 239348 [Multi-domain]  Cd Length: 76  Bit Score: 114.26  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125   3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGalpvfanqecrlvgrrtvklgpehcreghrpwraqrspptthha 82
Cdd:cd03050     1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKG-------------------------------------------- 36

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462492125  83 glfpgQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKY 127
Cdd:cd03050    37 -----EQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76
 
Name Accession Description Interval E-value
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 140-265 2.03e-58

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: 182.80  E-value: 2.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 140 ARARVDEYLAWQHTTLRRSCLRALWHKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVA 219
Cdd:cd03183     1 KRARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTPVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462492125 220 ITELMHPVGAGCQVFEGRPKLATWRQRVEAAvGEDLFQEAHEVILK 265
Cdd:cd03183    81 ICEIMQPEAAGYDVFEGRPKLAAWRKRVKEA-GNPLFDEAHKVIYK 125
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 3-127 2.54e-32

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


Pssm-ID: 239348 [Multi-domain]  Cd Length: 76  Bit Score: 114.26  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125   3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGalpvfanqecrlvgrrtvklgpehcreghrpwraqrspptthha 82
Cdd:cd03050     1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKG-------------------------------------------- 36

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462492125  83 glfpgQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKY 127
Cdd:cd03050    37 -----EQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
76-249 1.63e-30

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 113.45  E-value: 1.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125  76 PPTTHHAGLFPGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKVPDyWYPQDLQARARVDEYLAWQHTTL 155
Cdd:COG0625    26 PYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP-LLPADPAARARVRQWLAWADGDL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 156 RRSCLRALWHkvmfpvfLGEPVSPQTLAATLAELDVTLQLLEDKfLQNKAFLTGPHISLADLVAITELMHPVGAGCQVfE 235
Cdd:COG0625   105 HPALRNLLER-------LAPEKDPAAIARARAELARLLAVLEAR-LAGGPYLAGDRFSIADIALAPVLRRLDRLGLDL-A 175

                         170
                  ....*....|....
gi 2462492125 236 GRPKLATWRQRVEA 249
Cdd:COG0625   176 DYPNLAAWLARLAA 189
PRK15113 PRK15113
glutathione transferase;
87-187 5.40e-14

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 69.22  E-value: 5.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125  87 GQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKVPDYW--YPQDLQARARVDEYLAWQhttlrRSCLRALw 164
Cdd:PRK15113   43 GEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAPPAWEriYPADLQARARARQIQAWL-----RSDLMPL- 116

                          90       100
                  ....*....|....*....|....*.
gi 2462492125 165 hKVMFP---VFLGEPVSPQTLAATLA 187
Cdd:PRK15113  117 -REERPtdvVFAGAKKAPLSEAGKAA 141
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 86-125 1.12e-08

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.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 51.15  E-value: 1.12e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462492125  86 PGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTR 125
Cdd:pfam02798  37 AGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
PRK11752 PRK11752
putative S-transferase; Provisional
 87-151 5.03e-07

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 49.93  E-value: 5.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462492125  87 GQHLSDAFAQVNPLKKVPALKD--GD--FTLTESVAILLYLTRKYkvpDYWYPQDLQARARVDEYLAWQ 151
Cdd:PRK11752   85 GDQFSSGFVEINPNSKIPALLDrsGNppIRVFESGAILLYLAEKF---GAFLPKDLAARTETLNWLFWQ 150
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 165-249 5.18e-03

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 35.72  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 165 HKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKfLQNKAFLTGPHISLADLVAITEL-MHP-VGAGCqVFEGRPKLAT 242
Cdd:pfam00043   7 QIALLPYVPPEEKKEPEVDEALEKVARVLSALEEV-LKGQTYLVGDKLTLADIALAPALlWLYeLDPAC-LREKFPNLKA 84


                  ....*..
gi 2462492125 243 WRQRVEA 249
Cdd:pfam00043  85 WFERVAA 91
 
Name Accession Description Interval E-value
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 140-265 2.03e-58

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: 182.80  E-value: 2.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 140 ARARVDEYLAWQHTTLRRSCLRALWHKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVA 219
Cdd:cd03183     1 KRARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTPVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462492125 220 ITELMHPVGAGCQVFEGRPKLATWRQRVEAAvGEDLFQEAHEVILK 265
Cdd:cd03183    81 ICEIMQPEAAGYDVFEGRPKLAAWRKRVKEA-GNPLFDEAHKVIYK 125
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 3-127 2.54e-32

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


Pssm-ID: 239348 [Multi-domain]  Cd Length: 76  Bit Score: 114.26  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125   3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGalpvfanqecrlvgrrtvklgpehcreghrpwraqrspptthha 82
Cdd:cd03050     1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKG-------------------------------------------- 36

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462492125  83 glfpgQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKY 127
Cdd:cd03050    37 -----EQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
76-249 1.63e-30

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 113.45  E-value: 1.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125  76 PPTTHHAGLFPGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKVPDyWYPQDLQARARVDEYLAWQHTTL 155
Cdd:COG0625    26 PYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP-LLPADPAARARVRQWLAWADGDL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 156 RRSCLRALWHkvmfpvfLGEPVSPQTLAATLAELDVTLQLLEDKfLQNKAFLTGPHISLADLVAITELMHPVGAGCQVfE 235
Cdd:COG0625   105 HPALRNLLER-------LAPEKDPAAIARARAELARLLAVLEAR-LAGGPYLAGDRFSIADIALAPVLRRLDRLGLDL-A 175

                         170
                  ....*....|....
gi 2462492125 236 GRPKLATWRQRVEA 249
Cdd:COG0625   176 DYPNLAAWLARLAA 189
PRK15113 PRK15113
glutathione transferase;
87-187 5.40e-14

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 69.22  E-value: 5.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125  87 GQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKVPDYW--YPQDLQARARVDEYLAWQhttlrRSCLRALw 164
Cdd:PRK15113   43 GEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAPPAWEriYPADLQARARARQIQAWL-----RSDLMPL- 116

                          90       100
                  ....*....|....*....|....*.
gi 2462492125 165 hKVMFP---VFLGEPVSPQTLAATLA 187
Cdd:PRK15113  117 -REERPtdvVFAGAKKAPLSEAGKAA 141
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 3-123 1.20e-12

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.


Pssm-ID: 239343 [Multi-domain]  Cd Length: 74  Bit Score: 61.85  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125   3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGalpvfanqecrlvgrrtvklgpehcreghrpwraqrspptthha 82
Cdd:cd03045     1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKG-------------------------------------------- 36

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462492125  83 glfpgQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYL 123
Cdd:cd03045    37 -----EHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIYL 72
PLN02395 PLN02395
glutathione S-transferase
 84-243 1.19e-11

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 62.96  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125  84 LFPGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKV--PDYwYPQDLQARARVDEYLAWQHTTLRRSCLR 161
Cdd:PLN02395   34 LMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYRSqgPDL-LGKTIEERGQVEQWLDVEATSYHPPLLN 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 162 ALWHkVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKaFLTGPHISLADLVAI--TE-LMHPVGAGCQVfEGRP 238
Cdd:PLN02395  113 LTLH-ILFASKMGFPADEKVIKESEEKLAKVLDVYEARLSKSK-YLAGDFVSLADLAHLpfTEyLVGPIGKAYLI-KDRK 189


                  ....*
gi 2462492125 239 KLATW 243
Cdd:PLN02395  190 HVSAW 194
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 84-123 1.35e-11

GST_N family, Class Zeta 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. 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. Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid.


Pssm-ID: 239340 [Multi-domain]  Cd Length: 73  Bit Score: 59.12  E-value: 1.35e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462492125  84 LFPGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYL 123
Cdd:cd03042    33 LLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYL 72
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 86-127 3.12e-11

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.


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 58.28  E-value: 3.12e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462492125  86 PGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKY 127
Cdd:cd03046    34 PGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKY 75
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 3-123 1.61e-10

Glutathione S-transferase (GST) family, N-terminal 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 subfamily, a member of the DsbA family). 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 56.04  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125   3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGAlpvfanqecrlvgrrtvklgpehcreghrpwraqrspptthha 82
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGE------------------------------------------- 37

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462492125  83 glfpgqhlSDAFAQVNPLKKVPALKDGDFTLTESVAILLYL 123
Cdd:cd00570    38 --------QEEFLALNPLGKVPVLEDGGLVLTESLAILEYL 70
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 76-127 1.44e-09

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.


Pssm-ID: 239346 [Multi-domain]  Cd Length: 81  Bit Score: 53.70  E-value: 1.44e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462492125  76 PPTTHHAGLFPGQHLSDAFAQVNPLKKVPALKD---GDFTLTESVAILLYLTRKY 127
Cdd:cd03048    25 PYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDhngTPLTVFESGAILLYLAEKY 79
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 86-125 1.12e-08

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.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 51.15  E-value: 1.12e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462492125  86 PGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTR 125
Cdd:pfam02798  37 AGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 76-123 1.38e-08

GST_N family, unknown subfamily 4; 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.


Pssm-ID: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 50.65  E-value: 1.38e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462492125  76 PPTTHHAGLFPGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYL 123
Cdd:cd03056    25 PYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 84-126 1.65e-08

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.


Pssm-ID: 239351 [Multi-domain]  Cd Length: 76  Bit Score: 50.73  E-value: 1.65e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462492125  84 LFPGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRK 126
Cdd:cd03053    34 LTKGEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAEK 76
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 139-261 4.21e-08

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: 50.61  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 139 QARARVDEYLAWQHTTLRRSCLRalwhkVMFPV-FLGEPVSPQTLAAtlaeLDVTLQLLEdKFLQNKAFLTGPHISLADL 217
Cdd:cd03177     1 KKRAIVNQRLFFDSGTLYQRLRD-----YYYPIlFGGAEPPEEKLDK----LEEALEFLE-TFLEGSDYVAGDQLTIADL 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462492125 218 VAITELMHPVGAGCQvFEGRPKLATWRQRVEAAV-GEDLFQEAHE 261
Cdd:cd03177    71 SLVATVSTLEVVGFD-LSKYPNVAAWYERLKALPpGEEENGEGAK 114
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 92-249 9.39e-08

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 51.22  E-value: 9.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125  92 DAFAQVNPLKKVPALK-DGDFTLTESVAILLYLTRkyKVPDYWY--PQDLQARARVDEYLAWQHTTLrrsclralwHKVM 168
Cdd:PRK10542   41 DDYLAINPKGQVPALLlDDGTLLTEGVAIMQYLAD--SVPDRQLlaPVGSLSRYHTIEWLNYIATEL---------HKGF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 169 FPVFLgePVSPQTLAATL-AELDVTLQLLeDKFLQNKAFLTGPHISLAD--LVAITELMHPVGAGcqvFEGRPKLATWRQ 245
Cdd:PRK10542  110 TPLFR--PDTPEEYKPTVrAQLEKKFQYV-DEALADEQWICGQRFTIADayLFTVLRWAYAVKLN---LEGLEHIAAYMQ 183


                  ....
gi 2462492125 246 RVEA 249
Cdd:PRK10542  184 RVAE 187
PRK11752 PRK11752
putative S-transferase; Provisional
 87-151 5.03e-07

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 49.93  E-value: 5.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462492125  87 GQHLSDAFAQVNPLKKVPALKD--GD--FTLTESVAILLYLTRKYkvpDYWYPQDLQARARVDEYLAWQ 151
Cdd:PRK11752   85 GDQFSSGFVEINPNSKIPALLDrsGNppIRVFESGAILLYLAEKF---GAFLPKDLAARTETLNWLFWQ 150
PLN02473 PLN02473
glutathione S-transferase
 99-217 1.05e-06

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 48.45  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125  99 PLKKVPALKDGDFTLTESVAILLYLTRKYKVPDY-WYPQDLQARARVDEYLAWQhTTLRRSCLRALWHKVMFPVFLGEPV 177
Cdd:PLN02473   50 PFGQVPAIEDGDLKLFESRAIARYYATKYADQGTdLLGKTLEHRAIVDQWVEVE-NNYFYAVALPLVINLVFKPRLGEPC 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462492125 178 SPQTLAATLAELDVTLQLLEDKFLQNKaFLTGPHISLADL 217
Cdd:PLN02473  129 DVALVEELKVKFDKVLDVYENRLATNR-YLGGDEFTLADL 167
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 68-126 1.42e-06

GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression.


Pssm-ID: 239342 [Multi-domain]  Cd Length: 75  Bit Score: 45.32  E-value: 1.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462492125  68 RPWRAQRSPPTTHHAGL-------FPGQHL-SDAFAQVNPLKKVPALKDGD-FTLTESVAILLYLTRK 126
Cdd:cd03044     8 GNPRSLKILAAAKYNGLdveivdfQPGKENkTPEFLKKFPLGKVPAFEGADgFCLFESNAIAYYVANL 75
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
86-127 3.58e-06

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 44.14  E-value: 3.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462492125  86 PGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKY 127
Cdd:pfam13417  30 PPGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELY 71
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 144-247 4.88e-06

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: 44.41  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 144 VDEYLAWQHTTLRRSCLRALWHKVMFPvflgePVSPQTLAATLAELDVTLQLLEdKFLQNKAFLTGPHISLADLVAITEL 223
Cdd:cd00299     1 VRALEDWADATLAPPLVRLLYLEKVPL-----PKDEAAVEAAREELPALLAALE-QLLAGRPYLAGDQFSLADVALAPVL 74

                          90       100
                  ....*....|....*....|....*.
gi 2462492125 224 MH--PVGAGCQVFEGRPKLATWRQRV 247
Cdd:cd00299    75 ARleALGPYYDLLDEYPRLKAWYDRL 100
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
 92-123 5.63e-06

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.


Pssm-ID: 239345 [Multi-domain]  Cd Length: 73  Bit Score: 43.46  E-value: 5.63e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462492125  92 DAFAQVNPLKKVPALKDGDFTLTESVAILLYL 123
Cdd:cd03047    41 PEFLAMNPNGRVPVLEDGDFVLWESNAILRYL 72
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 84-123 7.14e-06

GST_N family, Class Beta 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. 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.


Pssm-ID: 239355 [Multi-domain]  Cd Length: 77  Bit Score: 43.29  E-value: 7.14e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462492125  84 LFPGQHLSDAFAQVNPLKKVPALKDGDFT-LTESVAILLYL 123
Cdd:cd03057    32 LRTKTQKGADYLAINPKGQVPALVLDDGEvLTESAAILQYL 72
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 139-218 1.04e-05

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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.


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 43.81  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 139 QARARVDEYLAWQHTTLRRSCLRALWHKVMFPvflGEPVSPQTLAATLAELDVTLQLLEDKfLQNKAFLTGPHISLADLV 218
Cdd:cd03180     1 AQRALADRWMDWQTSTLNPAFRYAFWGLVRTP---PEQRDPAAIAASLAACNKLMAILDAQ-LARQAYLAGDRFTLADIA 76
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 87-123 9.71e-05

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.


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 39.97  E-value: 9.71e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462492125  87 GQHLSDAFAQVNPLKKVPALK--DGDFtLTESVAILLYL 123
Cdd:cd03051    36 GEQRSPEFLAKNPAGTVPVLEldDGTV-ITESVAICRYL 73
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 89-123 1.03e-03

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 36.84  E-value: 1.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462492125  89 HLSDAFAQVNPLKKVPALKDGD-FTLTESVAILLYL 123
Cdd:pfam13409  30 DKPPELLALNPLGTVPVLVLPDgTVLTDSLVILEYL 65
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 99-125 1.28e-03

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.


Pssm-ID: 239337 [Multi-domain]  Cd Length: 72  Bit Score: 36.76  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462492125  99 PLKKVPALKDGDFTLTESVAILLYLTR 125
Cdd:cd03039    46 PFGQLPVLEIDGKKLTQSNAILRYLAR 72
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
 92-123 2.38e-03

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.


Pssm-ID: 239341 [Multi-domain]  Cd Length: 73  Bit Score: 36.04  E-value: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462492125  92 DAFAQVNPLKKVPALKDGDFTLTESVAILLYL 123
Cdd:cd03043    41 ARILEFSPTGKVPVLVDGGIVVWDSLAICEYL 72
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 168-226 4.48e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 36.38  E-value: 4.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462492125 168 MFPVFLGEPVSPQTLAATLAELDVTLQLLEdKFLQNKAFLTGPHISLADLVAITELMHP 226
Cdd:cd03181    24 VLPLLGIAPYNKKAVDKAKEDLKRALGVLE-EHLLTRTYLVGERITLADIFVASALLRG 81
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 165-249 5.18e-03

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 35.72  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492125 165 HKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKfLQNKAFLTGPHISLADLVAITEL-MHP-VGAGCqVFEGRPKLAT 242
Cdd:pfam00043   7 QIALLPYVPPEEKKEPEVDEALEKVARVLSALEEV-LKGQTYLVGDKLTLADIALAPALlWLYeLDPAC-LREKFPNLKA 84


                  ....*..
gi 2462492125 243 WRQRVEA 249
Cdd:pfam00043  85 WFERVAA 91
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 102-126 7.90e-03

GST_N family, Class Pi 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. 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. Class Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumours.


Pssm-ID: 239374 [Multi-domain]  Cd Length: 73  Bit Score: 34.60  E-value: 7.90e-03
                          10        20
                  ....*....|....*....|....*
gi 2462492125 102 KVPALKDGDFTLTESVAILLYLTRK 126
Cdd:cd03076    49 QLPCFKDGDLTLVQSNAILRHLGRK 73
 
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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