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Conserved domains on  [gi|294610650|ref|NP_083748|]
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glutathione S-transferase theta-4 [Mus musculus]

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 ...
 92-216 1.54e-41

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: 138.12  E-value: 1.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  92 RARVDEFMAWQHTAIQVPMSKILWIKLIIPMITGEEVPTERLEKTLDEVKRNLQQFEEKFLQDKMFITGDHISLADLVAL 171
Cdd:cd03183    2 RARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTPVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSAI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 294610650 172 VEMMQPMGSNHNVFVS-SKLAEWRMRVELAiGSGLFWEAHERLVKL 216
Cdd:cd03183   82 CEIMQPEAAGYDVFEGrPKLAAWRKRVKEA-GNPLFDEAHKVIYKL 126
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 3-78 3.90e-34

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: 117.34  E-value: 3.90e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKY 78
Cdd:cd03050    1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76
 
Name Accession Description Interval E-value
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 92-216 1.54e-41

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: 138.12  E-value: 1.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  92 RARVDEFMAWQHTAIQVPMSKILWIKLIIPMITGEEVPTERLEKTLDEVKRNLQQFEEKFLQDKMFITGDHISLADLVAL 171
Cdd:cd03183    2 RARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTPVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSAI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 294610650 172 VEMMQPMGSNHNVFVS-SKLAEWRMRVELAiGSGLFWEAHERLVKL 216
Cdd:cd03183   82 CEIMQPEAAGYDVFEGrPKLAAWRKRVKEA-GNPLFDEAHKVIYKL 126
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 3-78 3.90e-34

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: 117.34  E-value: 3.90e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKY 78
Cdd:cd03050    1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
3-198 1.43e-33

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 120.00  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSAPS 82
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  83 hWYPPDLHMRARVDEFMAWQHTAIQVPMSKILWikliipMITGEEVPtERLEKTLDEVKRNLQQFEEKfLQDKMFITGDH 162
Cdd:COG0625   82 -LLPADPAARARVRQWLAWADGDLHPALRNLLE------RLAPEKDP-AAIARARAELARLLAVLEAR-LAGGPYLAGDR 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 294610650 163 ISLAD--LVALVEMMQPMGSNHNVFvsSKLAEWRMRVE 198
Cdd:COG0625  153 FSIADiaLAPVLRRLDRLGLDLADY--PNLAAWLARLA 188
PRK15113 PRK15113
glutathione transferase;
3-101 8.60e-17

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 76.15  E-value: 8.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650   3 LELYMD--LLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSA 80
Cdd:PRK15113   6 ITLYSDahFFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAP 85

                         90       100
                 ....*....|....*....|...
gi 294610650  81 PSHW--YPPDLHMRARVDEFMAW 101
Cdd:PRK15113  86 PAWEriYPADLQARARARQIQAW 108
PLN02395 PLN02395
glutathione S-transferase
 1-182 1.61e-13

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 67.20  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650   1 MGLELYMDLLSAPCRAVYIFARKnGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSA 80
Cdd:PLN02395   1 MVLKVYGPAFASPKRALVTLIEK-GVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  81 PShwypPDL-----HMRARVDEFMAWQHTAIQVPMSKILWIKLIIPM--ITGEEVPTERLEKTLDEVkrnLQQFEEKFLQ 153
Cdd:PLN02395  80 QG----PDLlgktiEERGQVEQWLDVEATSYHPPLLNLTLHILFASKmgFPADEKVIKESEEKLAKV---LDVYEARLSK 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 294610650 154 DKmFITGDHISLADLVALV---EMMQPMGSNH 182
Cdd:PLN02395 153 SK-YLAGDFVSLADLAHLPfteYLVGPIGKAY 183
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
5-82 1.68e-09

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 53.00  E-value: 1.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294610650    5 LYMDLLSAPCRAVYIFARKNGIPFdfQFVDLLKGHHhSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSAPS 82
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPY--EFVPIPPGDH-PPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
 
Name Accession Description Interval E-value
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 92-216 1.54e-41

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: 138.12  E-value: 1.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  92 RARVDEFMAWQHTAIQVPMSKILWIKLIIPMITGEEVPTERLEKTLDEVKRNLQQFEEKFLQDKMFITGDHISLADLVAL 171
Cdd:cd03183    2 RARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTPVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSAI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 294610650 172 VEMMQPMGSNHNVFVS-SKLAEWRMRVELAiGSGLFWEAHERLVKL 216
Cdd:cd03183   82 CEIMQPEAAGYDVFEGrPKLAAWRKRVKEA-GNPLFDEAHKVIYKL 126
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 3-78 3.90e-34

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: 117.34  E-value: 3.90e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKY 78
Cdd:cd03050    1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
3-198 1.43e-33

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 120.00  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSAPS 82
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  83 hWYPPDLHMRARVDEFMAWQHTAIQVPMSKILWikliipMITGEEVPtERLEKTLDEVKRNLQQFEEKfLQDKMFITGDH 162
Cdd:COG0625   82 -LLPADPAARARVRQWLAWADGDLHPALRNLLE------RLAPEKDP-AAIARARAELARLLAVLEAR-LAGGPYLAGDR 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 294610650 163 ISLAD--LVALVEMMQPMGSNHNVFvsSKLAEWRMRVE 198
Cdd:COG0625  153 FSIADiaLAPVLRRLDRLGLDLADY--PNLAAWLARLA 188
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 3-75 1.35e-19

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: 79.57  E-value: 1.35e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLC 75
Cdd:cd03045    1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIYLV 73
PRK15113 PRK15113
glutathione transferase;
3-101 8.60e-17

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 76.15  E-value: 8.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650   3 LELYMD--LLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSA 80
Cdd:PRK15113   6 ITLYSDahFFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAP 85

                         90       100
                 ....*....|....*....|...
gi 294610650  81 PSHW--YPPDLHMRARVDEFMAW 101
Cdd:PRK15113  86 PAWEriYPADLQARARARQIQAW 108
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 3-75 2.02e-15

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: 68.75  E-value: 2.02e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHhsKEYIEINPLRKLPSLKDGKFILSESVAILFYLC 75
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQ--EEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 3-74 8.98e-15

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: 66.83  E-value: 8.98e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYL 74
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 25-74 1.08e-13

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: 64.13  E-value: 1.08e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 294610650  25 GIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYL 74
Cdd:cd03042   23 GLDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYL 72
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 3-77 1.40e-13

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: 63.82  E-value: 1.40e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294610650   3 LELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRK 77
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAEK 76
PLN02395 PLN02395
glutathione S-transferase
 1-182 1.61e-13

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 67.20  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650   1 MGLELYMDLLSAPCRAVYIFARKnGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSA 80
Cdd:PLN02395   1 MVLKVYGPAFASPKRALVTLIEK-GVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  81 PShwypPDL-----HMRARVDEFMAWQHTAIQVPMSKILWIKLIIPM--ITGEEVPTERLEKTLDEVkrnLQQFEEKFLQ 153
Cdd:PLN02395  80 QG----PDLlgktiEERGQVEQWLDVEATSYHPPLLNLTLHILFASKmgFPADEKVIKESEEKLAKV---LDVYEARLSK 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 294610650 154 DKmFITGDHISLADLVALV---EMMQPMGSNH 182
Cdd:PLN02395 153 SK-YLAGDFVSLADLAHLPfteYLVGPIGKAY 183
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 25-78 1.68e-12

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: 60.98  E-value: 1.68e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 294610650  25 GIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKY 78
Cdd:cd03046   22 GLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKY 75
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 17-78 1.15e-11

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: 58.71  E-value: 1.15e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294610650  17 VYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKD---GKFILSESVAILFYLCRKY 78
Cdd:cd03048   15 VSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDhngTPLTVFESGAILLYLAEKY 79
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 3-74 2.71e-10

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: 55.00  E-value: 2.71e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294610650   3 LELYmDLLSAPC-RAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLK--DGKFIlSESVAILFYL 74
Cdd:cd03051    1 MKLY-DSPTAPNpRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLEldDGTVI-TESVAICRYL 73
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 16-78 1.04e-09

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: 53.31  E-value: 1.04e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294610650  16 AVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSL--KDGKfILSESVAILFYLCRKY 78
Cdd:cd03057   13 APHIALEELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALvlDDGE-VLTESAAILQYLADLH 76
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
5-82 1.68e-09

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 53.00  E-value: 1.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294610650    5 LYMDLLSAPCRAVYIFARKNGIPFdfQFVDLLKGHHhSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSAPS 82
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPY--EFVPIPPGDH-PPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 25-76 1.40e-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: 50.38  E-value: 1.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 294610650   25 GIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCR 76
Cdd:pfam02798  25 GVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
PLN02473 PLN02473
glutathione S-transferase
 1-174 6.91e-08

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 51.53  E-value: 6.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650   1 MGLELYMDLLSA-PCRAVYIFARKnGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYS 79
Cdd:PLN02473   1 MVVKVYGQIKAAnPQRVLLCFLEK-GIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGDLKLFESRAIARYYATKYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  80 -APSHWYPPDLHMRARVDEFMAWQHTAIQVpMSKILWIKLIIPMITGEE---VPTERLEKTLDEVkrnLQQFEEKfLQDK 155
Cdd:PLN02473  80 dQGTDLLGKTLEHRAIVDQWVEVENNYFYA-VALPLVINLVFKPRLGEPcdvALVEELKVKFDKV---LDVYENR-LATN 154

                        170
                 ....*....|....*....
gi 294610650 156 MFITGDHISLADLVALVEM 174
Cdd:PLN02473 155 RYLGGDEFTLADLTHMPGM 173
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 14-77 2.54e-06

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 43.77  E-value: 2.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294610650   14 CRAVYIFARKNGIPFDFQFVDLlKGHHHSKEYIEINPLRKLPSLKDGK-FILSESVAILFYLCRK 77
Cdd:pfam13409   5 SHRVRLALEEKGLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVLPDgTVLTDSLVILEYLEEL 68
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
 38-75 3.67e-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: 3.67e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 294610650  38 GHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLC 75
Cdd:cd03047   36 GGLDTPEFLAMNPNGRVPVLEDGDFVLWESNAILRYLA 73
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 16-167 1.24e-05

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 44.67  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  16 AVYIFARKNGIPFDFQFVDL-LKGHHHSKEYIEINPLRKLPSLK-DGKFILSESVAILFYLCRKYsapshwypPDLHMRA 93
Cdd:PRK10542  13 ASHITLRESGLDFTLVSVDLaKKRLENGDDYLAINPKGQVPALLlDDGTLLTEGVAIMQYLADSV--------PDRQLLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  94 RVDEfMAWQHTaiqvpmskILWIKLIIPMITGEEVPTERlEKTLDEVK-RNLQQFEEKF------LQDKMFITGDHISLA 166
Cdd:PRK10542  85 PVGS-LSRYHT--------IEWLNYIATELHKGFTPLFR-PDTPEEYKpTVRAQLEKKFqyvdeaLADEQWICGQRFTIA 154


                 .
gi 294610650 167 D 167
Cdd:PRK10542 155 D 155
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 121-211 6.05e-05

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: 41.36  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650 121 PMITGEEVPTERLEKTLDEVkrnlqQFEEKFLQDKMFITGDHISLAD--LVALVEMMQPMGSNHNVFvsSKLAEW--RMR 196
Cdd:cd03177   28 ILFGGAEPPEEKLDKLEEAL-----EFLETFLEGSDYVAGDQLTIADlsLVATVSTLEVVGFDLSKY--PNVAAWyeRLK 100

                         90
                 ....*....|....*
gi 294610650 197 VELAiGSGLFWEAHE 211
Cdd:cd03177  101 ALPP-GEEENGEGAK 114
PRK11752 PRK11752
putative S-transferase; Provisional
 28-168 1.30e-03

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 39.14  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  28 FDFQFVDLLKGHHHSKEYIEINPLRKLPSLKD----GKFILSESVAILFYLCRKYsapSHWYPPDLHMRARVDEFMAWQH 103
Cdd:PRK11752  75 YDAWLIRIGEGDQFSSGFVEINPNSKIPALLDrsgnPPIRVFESGAILLYLAEKF---GAFLPKDLAARTETLNWLFWQQ 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294610650 104 TAiqvpmskilwikliIPMITG------EEVPtERLEKTLD----EVKRNLQQFeEKFLQDKMFITGDHISLADL 168
Cdd:PRK11752 152 GS--------------APFLGGgfghfyAYAP-EKIEYAINrftmEAKRQLDVL-DKQLAEHEYIAGDEYTIADI 210
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 42-77 2.24e-03

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: 35.69  E-value: 2.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 294610650  42 SKEYIEINPLRKLPSLK--DGkFILSESVAILFYLCRK 77
Cdd:cd03044   39 TPEFLKKFPLGKVPAFEgaDG-FCLFESNAIAYYVANL 75
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 8-78 2.91e-03

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.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 35.38  E-value: 2.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294610650   8 DLLSAPCRAVyiFARKnGIPFDFQFVDLlkgHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKY 78
Cdd:cd03059    9 DVYSHRVRIV--LAEK-GVSVEIIDVDP---DNPPEDLAELNPYGTVPTLVDRDLVLYESRIIMEYLDERF 73
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 92-169 4.38e-03

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: 35.72  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  92 RARVDEFMAWQHTAIQVPMSKILWIKLIIPmitgeevPTERlekTLDEVKRNLQQFEEKF------LQDKMFITGDHISL 165
Cdd:cd03180    3 RALADRWMDWQTSTLNPAFRYAFWGLVRTP-------PEQR---DPAAIAASLAACNKLMaildaqLARQAYLAGDRFTL 72


                 ....
gi 294610650 166 ADLV 169
Cdd:cd03180   73 ADIA 76
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 50-76 6.17e-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: 34.45  E-value: 6.17e-03
                         10        20
                 ....*....|....*....|....*..
gi 294610650  50 PLRKLPSLKDGKFILSESVAILFYLCR 76
Cdd:cd03039   46 PFGQLPVLEIDGKKLTQSNAILRYLAR 72
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
 7-168 7.40e-03

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 36.59  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650   7 MDLLSAPC---RAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGK-------FILSESVAILFYLCR 76
Cdd:PRK13972   2 IDLYFAPTpngHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  77 KYSApshWYPPDLHMRARVDEFMAWQHTAIQVPMSKILWIKLIIPM-----ITGEEVPTERLEKTLDevkrnlqqfeeKF 151
Cdd:PRK13972  82 KTGL---FLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQtipyaIERYQVETQRLYHVLN-----------KR 147

                        170
                 ....*....|....*..
gi 294610650 152 LQDKMFITGDHISLADL 168
Cdd:PRK13972 148 LENSPWLGGENYSIADI 164
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
 21-74 8.28e-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: 34.11  E-value: 8.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 294610650  21 ARKNGIPFDFQFVDLLKG------HHHSkeyieinPLRKLPSLKDGKFILSESVAILFYL 74
Cdd:cd03043   20 LKAAGIPFEEILVPLYTPdtrariLEFS-------PTGKVPVLVDGGIVVWDSLAICEYL 72
GST_N_Metaxin cd03054
GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a ...
 10-74 9.96e-03

GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities.


Pssm-ID: 239352 [Multi-domain]  Cd Length: 72  Bit Score: 34.13  E-value: 9.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294610650  10 LSAPCRAVYIFARKNGIPFDFQFVDLLkghhhskeyiEINPLRKLPSLKDGKFILSESVAILFYL 74
Cdd:cd03054   15 LSPECLKVETYLRMAGIPYEVVFSSNP----------WRSPTGKLPFLELNGEKIADSEKIIEYL 69
 
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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