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Conserved domains on  [gi|119580038|gb|EAW59634|]
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glutathione S-transferase theta 1, isoform CRA_f [Homo sapiens]

Protein Classification

GST_N_Theta domain-containing protein( domain architecture ID 10122709)

GST_N_Theta domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
3-66 3.47e-36

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: 3.47e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038  3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03050   1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAE 64
 
Name Accession Description Interval E-value
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
3-66 3.47e-36

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: 3.47e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038  3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03050   1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAE 64
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
3-66 3.72e-15

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 67.23  E-value: 3.72e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038   3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTE 65
PRK15113 PRK15113
glutathione transferase;
3-66 6.04e-11

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 56.12  E-value: 6.04e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119580038   3 LELYLD--LLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:PRK15113   6 ITLYSDahFFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSE 71
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
25-66 5.32e-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: 45.76  E-value: 5.32e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119580038  25 DIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:pfam02798 25 GVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTE 66
 
Name Accession Description Interval E-value
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
3-66 3.47e-36

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: 3.47e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038  3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03050   1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAE 64
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
3-66 4.60e-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: 73.79  E-value: 4.60e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038  3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03045   1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDNGFVLWE 64
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
3-66 2.83e-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: 64.13  E-value: 2.83e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038  3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHlsDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQ--EEFLALNPLGKVPVLEDGGLVLTE 62
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
3-66 3.72e-15

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 67.23  E-value: 3.72e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038   3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTE 65
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
26-66 1.58e-12

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: 57.19  E-value: 1.58e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 119580038 26 IPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03042  24 LDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQ 64
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
3-66 1.61e-12

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: 57.28  E-value: 1.61e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038  3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03053   2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGDLKLFE 65
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
3-66 1.12e-11

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: 54.89  E-value: 1.12e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580038  3 LELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03056   1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAE 64
PRK15113 PRK15113
glutathione transferase;
3-66 6.04e-11

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 56.12  E-value: 6.04e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119580038   3 LELYLD--LLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:PRK15113   6 ITLYSDahFFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSE 71
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
25-66 1.28e-10

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: 52.50  E-value: 1.28e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 119580038 25 DIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03046  22 GLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDLVLTE 63
PLN02395 PLN02395
glutathione S-transferase
1-66 1.70e-09

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 52.17  E-value: 1.70e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119580038   1 MGLELYLDLLSQPCRAVYIFAKKnDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:PLN02395   1 MVLKVYGPAFASPKRALVTLIEK-GVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFE 65
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
25-66 5.32e-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: 45.76  E-value: 5.32e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119580038  25 DIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:pfam02798 25 GVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTE 66
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
25-66 8.73e-08

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: 45.22  E-value: 8.73e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 119580038 25 DIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFT-LTE 66
Cdd:cd03057  22 GLPFELVRVDLRTKTQKGADYLAINPKGQVPALVLDDGEvLTE 64
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
17-77 7.92e-07

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: 42.92  E-value: 7.92e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119580038 17 VYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTltertcrPVPVWMS 77
Cdd:cd03048  15 VSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDHNGT-------PLTVFES 68
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
3-66 9.02e-06

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: 9.02e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119580038  3 LELYlDLLSQPC-RAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALK--DGDFtLTE 66
Cdd:cd03051   1 MKLY-DSPTAPNpRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLEldDGTV-ITE 65
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
5-66 1.96e-05

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 39.13  E-value: 1.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119580038   5 LYLDLLSQPCRAVYIFAKKNDIPFELRIVDLikgQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:pfam13417  1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPP---GDHPPELLAKNPLGKVPVLEDDGGILCE 59
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
13-66 1.84e-04

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: 36.46  E-value: 1.84e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 119580038 13 PCRA--VYIFAKKNDIpfELRIVDLIKGQHL-SDAFAQVNPLKKVPALKDGD-FTLTE 66
Cdd:cd03044   9 NPRSlkILAAAKYNGL--DVEIVDFQPGKENkTPEFLKKFPLGKVPAFEGADgFCLFE 64
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
14-66 9.20e-04

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 34.53  E-value: 9.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119580038  14 CRAVYIFAKKNDIPFELRIVDLiKGQHLSDAFAQVNPLKKVPALKDGD-FTLTE 66
Cdd:pfam13409  5 SHRVRLALEEKGLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVLPDgTVLTD 57
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
21-63 9.95e-04

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: 34.49  E-value: 9.95e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 119580038 21 AKKNDIPFELRIVDLiKGQHLSDAFAQVNPLKKVPALKDGDFT 63
Cdd:cd03043  20 LKAAGIPFEEILVPL-YTPDTRARILEFSPTGKVPVLVDGGIV 61
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
8-66 1.16e-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: 34.61  E-value: 1.16e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 119580038  8 DLLSQPCRAVyiFAKKNdIPFELRIVDLikgQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03059   9 DVYSHRVRIV--LAEKG-VSVEIIDVDP---DNPPEDLAELNPYGTVPTLVDRDLVLYE 61
PLN02473 PLN02473
glutathione S-transferase
13-66 3.41e-03

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 34.96  E-value: 3.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119580038  13 PCRAVYIFAKKnDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:PLN02473  14 PQRVLLCFLEK-GIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGDLKLFE 66
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
43-66 4.87e-03

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: 33.06  E-value: 4.87e-03
                        10        20
                ....*....|....*....|....
gi 119580038 43 DAFAQVNPLKKVPALKDGDFTLTE 66
Cdd:cd03047  41 PEFLAMNPNGRVPVLEDGDFVLWE 64
 
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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