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Conserved domains on  [gi|568966717|ref|XP_006513304|]
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glutathione S-transferase theta-2 isoform X3 [Mus musculus]

Protein Classification

PRK15113 and GST_C_Theta domain-containing protein( domain architecture ID 10123606)

PRK15113 and GST_C_Theta domain-containing protein

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 ...
 52-177 2.29e-51

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: 161.61  E-value: 2.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  52 ARAQVHEYLGWHADNIRGTFGVLLWTKVLGPLIGVQ-VPQEKVERNRDRMVLVLQQLEDKFLRDRAFLVGQQVTLADLMS 130
Cdd:cd03183    1 KRARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTpVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568966717 131 LEELMQPVALGYNLFEGRPQLTAWRERVEAFlGAELCQEAHSTILSI 177
Cdd:cd03183   81 ICEIMQPEAAGYDVFEGRPKLAAWRKRVKEA-GNPLFDEAHKVIYKL 126
 
Name Accession Description Interval E-value
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 52-177 2.29e-51

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: 161.61  E-value: 2.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  52 ARAQVHEYLGWHADNIRGTFGVLLWTKVLGPLIGVQ-VPQEKVERNRDRMVLVLQQLEDKFLRDRAFLVGQQVTLADLMS 130
Cdd:cd03183    1 KRARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTpVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568966717 131 LEELMQPVALGYNLFEGRPQLTAWRERVEAFlGAELCQEAHSTILSI 177
Cdd:cd03183   81 ICEIMQPEAAGYDVFEGRPKLAAWRKRVKEA-GNPLFDEAHKVIYKL 126
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
28-160 1.18e-12

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 63.76  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  28 STAILIYLSSKYQVAdHWYPADLQARAQVHEYLGWHADNIRGTFGVLLwtKVLGPligvQVPQEKVERNRDRMVLVLQQL 107
Cdd:COG0625   66 SLAILEYLAERYPEP-PLLPADPAARARVRQWLAWADGDLHPALRNLL--ERLAP----EKDPAAIARARAELARLLAVL 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568966717 108 EDKfLRDRAFLVGQQVTLADLMSLEELMQPVALGYNLfEGRPQLTAWRERVEA 160
Cdd:COG0625  139 EAR-LAGGPYLAGDRFSIADIALAPVLRRLDRLGLDL-ADYPNLAAWLARLAA 189
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 89-160 7.80e-08

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: 48.44  E-value: 7.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568966717   89 PQEKVERNRDRMVLVLQQLEDKfLRDRAFLVGQQVTLADLMSLEELMQPVALGYN-LFEGRPQLTAWRERVEA 160
Cdd:pfam00043  20 KEPEVDEALEKVARVLSALEEV-LKGQTYLVGDKLTLADIALAPALLWLYELDPAcLREKFPNLKAWFERVAA 91
PRK11752 PRK11752
putative S-transferase; Provisional
 28-128 1.43e-03

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 38.37  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  28 STAILIYLSSKYqvaDHWYPADLQARAqvhEYLGWhadnirgtfgvLLWTKVLGPLIG-------VQVPqEKVERNRDRM 100
Cdd:PRK11752 118 SGAILLYLAEKF---GAFLPKDLAART---ETLNW-----------LFWQQGSAPFLGggfghfyAYAP-EKIEYAINRF 179

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568966717 101 VL-VLQQLE--DKFLRDRAFLVGQQVTLADL 128
Cdd:PRK11752 180 TMeAKRQLDvlDKQLAEHEYIAGDEYTIADI 210
 
Name Accession Description Interval E-value
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 52-177 2.29e-51

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: 161.61  E-value: 2.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  52 ARAQVHEYLGWHADNIRGTFGVLLWTKVLGPLIGVQ-VPQEKVERNRDRMVLVLQQLEDKFLRDRAFLVGQQVTLADLMS 130
Cdd:cd03183    1 KRARVDEYLAWQHTNLRLGCAAYFWQKVLLPLFGGTpVSPEKVKKAEENLEESLDLLENKFLKDKPFLAGDEISIADLSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568966717 131 LEELMQPVALGYNLFEGRPQLTAWRERVEAFlGAELCQEAHSTILSI 177
Cdd:cd03183   81 ICEIMQPEAAGYDVFEGRPKLAAWRKRVKEA-GNPLFDEAHKVIYKL 126
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
28-160 1.18e-12

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 63.76  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  28 STAILIYLSSKYQVAdHWYPADLQARAQVHEYLGWHADNIRGTFGVLLwtKVLGPligvQVPQEKVERNRDRMVLVLQQL 107
Cdd:COG0625   66 SLAILEYLAERYPEP-PLLPADPAARARVRQWLAWADGDLHPALRNLL--ERLAP----EKDPAAIARARAELARLLAVL 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568966717 108 EDKfLRDRAFLVGQQVTLADLMSLEELMQPVALGYNLfEGRPQLTAWRERVEA 160
Cdd:COG0625  139 EAR-LAGGPYLAGDRFSIADIALAPVLRRLDRLGLDL-ADYPNLAAWLARLAA 189
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 89-160 7.80e-08

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: 48.44  E-value: 7.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568966717   89 PQEKVERNRDRMVLVLQQLEDKfLRDRAFLVGQQVTLADLMSLEELMQPVALGYN-LFEGRPQLTAWRERVEA 160
Cdd:pfam00043  20 KEPEVDEALEKVARVLSALEEV-LKGQTYLVGDKLTLADIALAPALLWLYELDPAcLREKFPNLKAWFERVAA 91
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 56-158 6.83e-07

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: 45.95  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  56 VHEYLGWHADNIRGTFGVLLWTKVLGPligvQVPQEKVERNRDRMVLVLQQLEdKFLRDRAFLVGQQVTLADLM--SLEE 133
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLEKVPL----PKDEAAVEAAREELPALLAALE-QLLAGRPYLAGDQFSLADVAlaPVLA 75

                         90       100
                 ....*....|....*....|....*
gi 568966717 134 LMQPVALGYNLFEGRPQLTAWRERV 158
Cdd:cd00299   76 RLEALGPYYDLLDEYPRLKAWYDRL 100
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 79-171 1.45e-06

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: 45.60  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  79 VLGPLI--GVQVPQEKVERnrdrmvlVLQQLE--DKFLRDRAFLVGQQVTLADLMSLEELMQPVALGYNLfEGRPQLTAW 154
Cdd:cd03177   24 YYYPILfgGAEPPEEKLDK-------LEEALEflETFLEGSDYVAGDQLTIADLSLVATVSTLEVVGFDL-SKYPNVAAW 95

                         90
                 ....*....|....*...
gi 568966717 155 RERVEAFL-GAELCQEAH 171
Cdd:cd03177   96 YERLKALPpGEEENGEGA 113
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 69-160 2.33e-05

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other 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. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 41.90  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  69 GTFGVLLWTKVLGPLIGVQVPQEKVERNRDRMVLVLQQLEDKfLRDRAFLVGQQVTLADLMSLEELMQPVALGynLFEGR 148
Cdd:cd03207   10 GTVEPPLLNKALGRFFEPPWGEPAIAAAYGDLDERLAALEAA-LAGRPYLVGERFSAADLLLASVLRWARAFG--LLPEY 86

                         90
                 ....*....|..
gi 568966717 149 PQLTAWRERVEA 160
Cdd:cd03207   87 PALRAYVARCTA 98
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 77-160 5.72e-05

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces 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 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. 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: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 41.15  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  77 TKVLGPLIGVQVPqEKVERNRDRmVLVLQQLEDKFLRDRAFLVGQQVTLADLMSLEELMQPVALGYNLFEGRPQLTAWRE 156
Cdd:cd03182   31 TPGLKPDREVQVP-EWGERNKKR-VIDFLPVLDKRLAESPYVAGDRFSIADITAFVALDFAKNLKLPVPEELTALRRWYE 108


                 ....
gi 568966717 157 RVEA 160
Cdd:cd03182  109 RMAA 112
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 52-129 6.02e-05

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: 41.01  E-value: 6.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568966717  52 ARAQVHEYLGWHADNIrgtfgVLLWTKVLGPLIGV-QVPQEKVERNRDRMVLVLQQLEdKFLRDRAFLVGQQVTLADLM 129
Cdd:cd03181    1 EAAQVLQWISFANSEL-----LPAAATWVLPLLGIaPYNKKAVDKAKEDLKRALGVLE-EHLLTRTYLVGERITLADIF 73
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 104-160 7.67e-04

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 37.54  E-value: 7.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568966717  104 LQQLEdKFLRDRA--FLVGQQVTLADLM---SLEELMQPVALgyNLFEGRPQLTAWRERVEA 160
Cdd:pfam14497  35 LGYFE-KVLNKNGggYLVGDKLTYADLAlfqVLDGLLYPKAP--DALDKYPKLKALHERVAA 93
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 52-160 8.41e-04

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 37.61  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  52 ARAQVHEYLGWHADNIRGTFGVLLWTkvlGPLIGVQVPQEKVERNRDRMVLVLQQLEDKfLRDRAFLVGQQVTLADLMSL 131
Cdd:cd03188    2 ERARLLEWLNFIASELHKAFGPLFYP---ARWADDALAEEVKAAARERLERRLAYLDAQ-LAGGPYLLGDQFSVADAYLF 77

                         90       100
                 ....*....|....*....|....*....
gi 568966717 132 EELMQPVALGYNLfEGRPQLTAWRERVEA 160
Cdd:cd03188   78 VVLRWARAVGLDL-SDWPHLAAYLARVAA 105
GST_C_Phi cd03187
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione ...
 74-160 1.11e-03

C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau 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: 198296 [Multi-domain]  Cd Length: 118  Bit Score: 37.59  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  74 LLWTKVLGPLIGVQVPQEKVERNRDRMVLVLQQLEDKfLRDRAFLVGQQVTLADLMSLEELMQPVALGYN-LFEGRPQLT 152
Cdd:cd03187   24 LVFELVFKPMLGLKTDEAVVEENEAKLKKVLDVYEAR-LSKSKYLAGDSFTLADLSHLPNLHYLMATPSKkLFDSRPHVK 102


                 ....*...
gi 568966717 153 AWRERVEA 160
Cdd:cd03187  103 AWWEDISA 110
PRK11752 PRK11752
putative S-transferase; Provisional
 28-128 1.43e-03

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 38.37  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  28 STAILIYLSSKYqvaDHWYPADLQARAqvhEYLGWhadnirgtfgvLLWTKVLGPLIG-------VQVPqEKVERNRDRM 100
Cdd:PRK11752 118 SGAILLYLAEKF---GAFLPKDLAART---ETLNW-----------LFWQQGSAPFLGggfghfyAYAP-EKIEYAINRF 179

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568966717 101 VL-VLQQLE--DKFLRDRAFLVGQQVTLADL 128
Cdd:PRK11752 180 TMeAKRQLDvlDKQLAEHEYIAGDEYTIADI 210
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 91-158 2.21e-03

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, 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. Members also include 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: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 36.45  E-value: 2.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568966717  91 EKVERNRDRMV----LVLQQLEdKFL--RDRAFLVGQQVTLADLMSLEELMQP-VALGYNLFEGRPQLTAWRERV 158
Cdd:cd03192   31 EKKEKKKEFLEealpKFLGKFE-KILkkSGGGYFVGDKLTWADLALFDVLDYLlYLLPKDLLEKYPKLKALRERV 104
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
 52-160 2.96e-03

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. 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 thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-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. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. 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. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198288 [Multi-domain]  Cd Length: 110  Bit Score: 36.07  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966717  52 ARAQVHEYLGWHADNIRGTFGVLLWTKVLGPligVQVPQEkVERNRDRMVLVLQQLeDKFLRDRAFLVGQQVTLADLMSL 131
Cdd:cd03178    1 ERAEVLQWLFFQMSGLGPMFGQAGHFLYFAP---EKIPYA-IERYTDEVKRLYGVL-DKRLSDRPYLAGEEYSIADIALY 75

                         90       100
                 ....*....|....*....|....*....
gi 568966717 132 EELMQPVALGYNLFEGRPQLTAWRERVEA 160
Cdd:cd03178   76 PWTHYADLGGFADLSEYPNVKRWLERIAA 104
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 93-157 7.33e-03

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 33.83  E-value: 7.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568966717   93 VERNRDRMVLVLQQLEDkFLRDRAFLVGQQVTLADLM--SLEELMQPVALGYNLFEGRPQLTAWRER 157
Cdd:pfam13410   2 LERAREQLRAALDALEA-RLADGPGLLGDRPTLADIAlaPVLARLDAAYPGLDLREGYPRLRAWLER 67
 
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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