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Conserved domains on  [gi|19922528|ref|NP_611324|]
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glutathione S transferase E2 [Drosophila melanogaster]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 11427749)

glutathione S-transferase (GST) family protein may catalyze the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress

CATH:  1.20.1050.10|3.40.30.10
EC:  2.5.1.-
Gene Ontology:  GO:0006749|GO:0005515
PubMed:  11035031
SCOP:  4000976|4000472

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
5-200 4.31e-48

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


:

Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 156.59  E-value: 4.31e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKYANSD 84
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  85 eLYPRDLVLRAQVDQRLFFDASILFMSLRNVSIPYFLRQVSLVPKEKVDNIKDAYGHLENFLGDNPYLTGSQLTIADLCC 164
Cdd:COG0625  82 -LLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIAL 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19922528 165 GATASSLAAV-LDLDElkYPKVAAWFERLSKLPHYEE 200
Cdd:COG0625 161 APVLRRLDRLgLDLAD--YPNLAAWLARLAARPAFQR 195
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
5-200 4.31e-48

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 156.59  E-value: 4.31e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKYANSD 84
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  85 eLYPRDLVLRAQVDQRLFFDASILFMSLRNVSIPYFLRQVSLVPKEKVDNIKDAYGHLENFLGDNPYLTGSQLTIADLCC 164
Cdd:COG0625  82 -LLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIAL 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19922528 165 GATASSLAAV-LDLDElkYPKVAAWFERLSKLPHYEE 200
Cdd:COG0625 161 APVLRRLDRLgLDLAD--YPNLAAWLARLAARPAFQR 195
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 94-209 1.71e-44

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: 144.60  E-value: 1.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQRLFFDASILFMSLRNVSIPYFLRQVSlVPKEKVDNIKDAYGHLENFLGDNPYLTGSQLTIADLCCGATASSLAA 173
Cdd:cd03177   3 RAIVNQRLFFDSGTLYQRLRDYYYPILFGGAE-PPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVSTLEV 81

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19922528 174 VlDLDELKYPKVAAWFERLSKLPHYEEDNLRGLKKY 209
Cdd:cd03177  82 V-GFDLSKYPNVAAWYERLKALPPGEEENGEGAKEL 116
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
7-83 1.14e-14

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 66.48  E-value: 1.14e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922528     7 LYGMDISPPVRACKLTLRALNLDYEYKEMDLlaGDHFkDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKYANS 83
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPP--GDHP-PELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGP 74
PLN02395 PLN02395
glutathione S-transferase
 5-200 5.80e-11

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 59.88  E-value: 5.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528    5 LVLYGMDISPPVRACkLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKY-ANS 83
Cdd:PLN02395   3 LKVYGPAFASPKRAL-VTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYrSQG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   84 DELYPRDLVLRAQVDQRLFFDASILFMSLRNVSIP-YFLRQVSLVPKEKVdnIKDAYGHL-------ENFLGDNPYLTGS 155
Cdd:PLN02395  82 PDLLGKTIEERGQVEQWLDVEATSYHPPLLNLTLHiLFASKMGFPADEKV--IKESEEKLakvldvyEARLSKSKYLAGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19922528  156 QLTIADLCCGATASSLAAVLD----LDELKYpkVAAWFERLSKLPHYEE 200
Cdd:PLN02395 160 FVSLADLAHLPFTEYLVGPIGkaylIKDRKH--VSAWWDDISSRPAWKE 206
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
5-200 4.31e-48

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 156.59  E-value: 4.31e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKYANSD 84
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  85 eLYPRDLVLRAQVDQRLFFDASILFMSLRNVSIPYFLRQVSLVPKEKVDNIKDAYGHLENFLGDNPYLTGSQLTIADLCC 164
Cdd:COG0625  82 -LLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIAL 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19922528 165 GATASSLAAV-LDLDElkYPKVAAWFERLSKLPHYEE 200
Cdd:COG0625 161 APVLRRLDRLgLDLAD--YPNLAAWLARLAARPAFQR 195
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 94-209 1.71e-44

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: 144.60  E-value: 1.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQRLFFDASILFMSLRNVSIPYFLRQVSlVPKEKVDNIKDAYGHLENFLGDNPYLTGSQLTIADLCCGATASSLAA 173
Cdd:cd03177   3 RAIVNQRLFFDSGTLYQRLRDYYYPILFGGAE-PPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVSTLEV 81

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19922528 174 VlDLDELKYPKVAAWFERLSKLPHYEEDNLRGLKKY 209
Cdd:cd03177  82 V-GFDLSKYPNVAAWYERLKALPPGEEENGEGAKEL 116
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 5-78 1.11e-36

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: 123.10  E-value: 1.11e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVD 78
Cdd:cd03045   1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIYLVE 74
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 5-76 9.58e-19

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: 76.84  E-value: 9.58e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLLAGDHfkDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYL 76
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQ--EEFLALNPLGKVPVLEDGGLVLTESLAILEYL 70
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 20-76 2.01e-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: 68.37  E-value: 2.01e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19922528  20 KLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYL 76
Cdd:cd03056  16 RLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 4-79 2.62e-15

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: 68.06  E-value: 2.62e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922528   4 KLVLYGMDISPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDK 79
Cdd:cd03053   1 VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAEK 76
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
7-83 1.14e-14

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 66.48  E-value: 1.14e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922528     7 LYGMDISPPVRACKLTLRALNLDYEYKEMDLlaGDHFkDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKYANS 83
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPP--GDHP-PELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGP 74
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 94-200 9.88e-13

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: 62.62  E-value: 9.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQRLFFDAsilfMSLRNVSIPYFLrQVSLVPK--------EKVD----NIKDAYGHLEN-FLGDNPYLTGSQLTIA 160
Cdd:cd03183   2 RARVDEYLAWQH----TNLRLGCAAYFW-QKVLLPLfggtpvspEKVKkaeeNLEESLDLLENkFLKDKPFLAGDEISIA 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19922528 161 DlccgatassLAAVLDLDELK---------YPKVAAWFERLSK--LPHYEE 200
Cdd:cd03183  77 D---------LSAICEIMQPEaagydvfegRPKLAAWRKRVKEagNPLFDE 118
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 25-76 1.79e-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: 60.66  E-value: 1.79e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19922528  25 ALNL---DYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYL 76
Cdd:cd03042  18 ALNLkglDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYL 72
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 5-81 2.26e-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: 60.21  E-value: 2.26e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922528   5 LVLYGmdiSPPVRA--CKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKYA 81
Cdd:cd03046   1 ITLYH---LPRSRSfrILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 26-80 4.19e-12

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: 59.87  E-value: 4.19e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19922528  26 LNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDN---GALIWDSHAIVCYLVDKY 80
Cdd:cd03048  22 LGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDHngtPLTVFESGAILLYLAEKY 79
PLN02395 PLN02395
glutathione S-transferase
 5-200 5.80e-11

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 59.88  E-value: 5.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528    5 LVLYGMDISPPVRACkLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKY-ANS 83
Cdd:PLN02395   3 LKVYGPAFASPKRAL-VTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYrSQG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   84 DELYPRDLVLRAQVDQRLFFDASILFMSLRNVSIP-YFLRQVSLVPKEKVdnIKDAYGHL-------ENFLGDNPYLTGS 155
Cdd:PLN02395  82 PDLLGKTIEERGQVEQWLDVEATSYHPPLLNLTLHiLFASKMGFPADEKV--IKESEEKLakvldvyEARLSKSKYLAGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19922528  156 QLTIADLCCGATASSLAAVLD----LDELKYpkVAAWFERLSKLPHYEE 200
Cdd:PLN02395 160 FVSLADLAHLPFTEYLVGPIGkaylIKDRKH--VSAWWDDISSRPAWKE 206
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
 5-76 7.99e-11

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: 56.17  E-value: 7.99e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYL 76
Cdd:cd03047   1 LTIWGRRSSINVQKVLWLLDELGLPYERIDAGGQFGGLDTPEFLAMNPNGRVPVLEDGDFVLWESNAILRYL 72
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
 94-196 1.15e-10

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: 56.87  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQRLFFDASIL-FMSLRNVSIPYFLRQVSLVPKEKVDN-IKDAYGHLENFLGDNPYLTGSQLTIADLCCGATASSL 171
Cdd:cd03178   2 RAEVLQWLFFQMSGLgPMFGQAGHFLYFAPEKIPYAIERYTDeVKRLYGVLDKRLSDRPYLAGEEYSIADIALYPWTHYA 81

                        90       100
                ....*....|....*....|....*
gi 19922528 172 AAVLDLDELKYPKVAAWFERLSKLP 196
Cdd:cd03178  82 DLGGFADLSEYPNVKRWLERIAARP 106
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 5-78 1.23e-10

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: 55.77  E-value: 1.23e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922528     5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVD 78
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 13-76 5.99e-09

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 51.09  E-value: 5.99e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922528    13 SPPVRACKLTLRALNLDYEYKEMDLLaGDHFKDAFLKKNPQHTVPLLED-NGALIWDSHAIVCYL 76
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLD-PKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYL 65
PLN02473 PLN02473
glutathione S-transferase
 27-200 6.53e-09

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 53.84  E-value: 6.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   27 NLDYEYKEMDLlagdhfkDAFLKKNPQH-------TVPLLEDNGALIWDSHAIVCYLVDKYANS-DELYPRDLVLRAQVD 98
Cdd:PLN02473  25 GIEFEVIHVDL-------DKLEQKKPEHllrqpfgQVPAIEDGDLKLFESRAIARYYATKYADQgTDLLGKTLEHRAIVD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   99 Q-----RLFFDASILFMSLRNVSIPYFLRQ--VSLVP--KEKVDNIKDAYghlENFLGDNPYLTGSQLTIADLCCGATAS 169
Cdd:PLN02473  98 QwveveNNYFYAVALPLVINLVFKPRLGEPcdVALVEelKVKFDKVLDVY---ENRLATNRYLGGDEFTLADLTHMPGMR 174

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19922528  170 SLAAVLDLDELKYPK--VAAWFERLSKLPHYEE 200
Cdd:PLN02473 175 YIMNETSLSGLVTSRenLNRWWNEISARPAWKK 207
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 102-192 1.47e-08

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: 50.96  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528 102 FFDASILFMSLRNVSIPYFLRQVSLVPKEK-VDNIKDAYGHLENFLGDNPYLTGSQLTIADLCCGATASSLAAVLDLDEL 180
Cdd:cd00299   7 WADATLAPPLVRLLYLEKVPLPKDEAAVEAaREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPYYDL 86

                        90
                ....*....|....
gi 19922528 181 --KYPKVAAWFERL 192
Cdd:cd00299  87 ldEYPRLKAWYDRL 100
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 94-200 1.77e-08

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: 51.02  E-value: 1.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQRLFFDASILFMSLrnvsIPYFLRQVSLVP--KEKVD----NIKDAYGHLENFLGDNPYLTGSQLTIADLCCgat 167
Cdd:cd03181   2 AAQVLQWISFANSELLPAA----ATWVLPLLGIAPynKKAVDkakeDLKRALGVLEEHLLTRTYLVGERITLADIFV--- 74

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 19922528 168 ASSL----AAVLDLDELK-YPKVAAWFERLSKLPHYEE 200
Cdd:cd03181  75 ASALlrgfETVLDPEFRKkYPNVTRWFNTVVNQPKFKA 112
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 18-196 2.50e-08

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 51.99  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   18 ACKL----TLRALNLDYEYKEMDLLAG--DHFKDaFLKKNPQHTVP-LLEDNGALIWDSHAIVCYLVDKYANSDELYPRD 90
Cdd:PRK10542   9 ACSLashiTLRESGLDFTLVSVDLAKKrlENGDD-YLAINPKGQVPaLLLDDGTLLTEGVAIMQYLADSVPDRQLLAPVG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   91 LVLRAQVDQRLFFDASIL---FMSLRNVSIP--YFLRQVSLVPKEkvdnikdaYGHLENFLGDNPYLTGSQLTIADlccg 165
Cdd:PRK10542  88 SLSRYHTIEWLNYIATELhkgFTPLFRPDTPeeYKPTVRAQLEKK--------FQYVDEALADEQWICGQRFTIAD---- 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19922528  166 A---TASSLAAVLDLDELKYPKVAAWFERLSKLP 196
Cdd:PRK10542 156 AylfTVLRWAYAVKLNLEGLEHIAAYMQRVAERP 189
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 27-76 4.01e-08

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: 48.83  E-value: 4.01e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 19922528  27 NLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLE-DNGALIWDSHAIVCYL 76
Cdd:cd03051  23 GIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLElDDGTVITESVAICRYL 73
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
 13-196 4.48e-08

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 51.61  E-value: 4.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   13 SPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGAL-------IWDSHAIVCYLVDKyanSDE 85
Cdd:PRK13972   9 TPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPAdggeplsLFESGAILLYLAEK---TGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   86 LYPRDLVLRAQVDQRLFFDASIL---------FMSLRNVSIPYFLRQVSLvpkekvdNIKDAYGHLENFLGDNPYLTGSQ 156
Cdd:PRK13972  86 FLSHETRERAATLQWLFWQVGGLgpmlgqnhhFNHAAPQTIPYAIERYQV-------ETQRLYHVLNKRLENSPWLGGEN 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19922528  157 LTIADLCCGATASSLAAvLDLDELKYPKVAAWFERLSKLP 196
Cdd:PRK13972 159 YSIADIACWPWVNAWTR-QRIDLAMYPAVKNWHERIRSRP 197
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 23-80 1.11e-07

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: 47.53  E-value: 1.11e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19922528  23 LRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLE-DNGALIWDSHAIVCYLVDKY 80
Cdd:cd03057  18 LEELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALVlDDGEVLTESAAILQYLADLH 76
PRK15113 PRK15113
glutathione transferase;
1-99 1.44e-07

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 49.96  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528    1 MSDK-LVLYGMD--ISPPVRACKLTLRALNLDYEYKEMDLLAGDHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLV 77
Cdd:PRK15113   1 MSKPaITLYSDAhfFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLE 80

                         90       100
                 ....*....|....*....|....
gi 19922528   78 DKYANSD--ELYPRDLVLRAQVDQ 99
Cdd:PRK15113  81 ERFAPPAweRIYPADLQARARARQ 104
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
 94-196 2.42e-07

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related 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. 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. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 47.65  E-value: 2.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQRLFFDASIL---------FMSLRNVSIPYFLrqvslvpKEKVDNIKDAYGHLENFLGDNPYLTGSQLTIADLCC 164
Cdd:cd10291   2 RYAVLQWLMWQMGGLgpmqgqahhFKRYAPEKIPYAI-------KRYTNETKRLYGVLDRRLAKSKYLAGDEYSIADIAI 74

                        90       100       110
                ....*....|....*....|....*....|..
gi 19922528 165 GATASSLAAVlDLDELKYPKVAAWFERLSKLP 196
Cdd:cd10291  75 WPWVARHEWQ-GIDLADFPNLKRWFERLAARP 105
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 130-191 2.04e-06

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 43.85  E-value: 2.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922528   130 EKVDNIKDAYGHLENFLGDNPYLTGSQLTIADLCCGATASSLAAV---LDLDElKYPKVAAWFER 191
Cdd:pfam13410   4 RAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAypgLDLRE-GYPRLRAWLER 67
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 94-198 2.62e-06

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: 44.96  E-value: 2.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQRLFFDASILFMSLRNVSIPYFlRQvslvPKEKVDNIKDAYGH---------LENFLGDNPYLTGSQLTIADLCC 164
Cdd:cd03180   3 RALADRWMDWQTSTLNPAFRYAFWGLV-RT----PPEQRDPAAIAASLaacnklmaiLDAQLARQAYLAGDRFTLADIAL 77

                        90       100       110
                ....*....|....*....|....*....|....
gi 19922528 165 GATASSLAAvLDLDELKYPKVAAWFERLSKLPHY 198
Cdd:cd03180  78 GCSVYRWLE-LPIERPALPHLERWYARLSQRPAF 110
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-76 5.14e-06

GST_N family, Class Omega 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 Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


Pssm-ID: 239353 [Multi-domain]  Cd Length: 89  Bit Score: 43.50  E-value: 5.14e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922528   3 DKLVLYGMDISPPVRACKLTLRALNLDYEYKEMDLlagDHFKDAFLKKNPQHTVPLLE-DNGALIWDSHAIVCYL 76
Cdd:cd03055  17 GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININL---KDKPDWFLEKNPQGKVPALEiDEGKVVYESLIICEYL 88
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 101-196 5.93e-06

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: 43.44  E-value: 5.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528 101 LFFDASILFMSLRNvsipyFLRQVSLVPKEKVDNIKDAYG-------HLENFLGDNPYLTGSQLTIADLCCGATASSLAA 173
Cdd:cd03207   5 LFFAAGTVEPPLLN-----KALGRFFEPPWGEPAIAAAYGdlderlaALEAALAGRPYLVGERFSAADLLLASVLRWARA 79

                        90       100
                ....*....|....*....|...
gi 19922528 174 VLDLDElkYPKVAAWFERLSKLP 196
Cdd:cd03207  80 FGLLPE--YPALRAYVARCTARP 100
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
 21-76 7.39e-06

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: 42.58  E-value: 7.39e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19922528  21 LTLRALNLDYEYKEMDLLAGDhFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYL 76
Cdd:cd03043  18 LLLKAAGIPFEEILVPLYTPD-TRARILEFSPTGKVPVLVDGGIVVWDSLAICEYL 72
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 94-196 8.00e-06

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: 43.39  E-value: 8.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQRLFFDASIL---FMSLRNVSIPYFLRQVSLVpKEKV-DNIKDAYGHLENFLGDNPYLTGSQLTIADLCCgATAS 169
Cdd:cd03188   3 RARLLEWLNFIASELhkaFGPLFYPARWADDALAEEV-KAAArERLERRLAYLDAQLAGGPYLLGDQFSVADAYL-FVVL 80

                        90       100
                ....*....|....*....|....*..
gi 19922528 170 SLAAVLDLDELKYPKVAAWFERLSKLP 196
Cdd:cd03188  81 RWARAVGLDLSDWPHLAAYLARVAARP 107
GST_C_6 cd03205
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ...
 135-200 1.66e-05

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.


Pssm-ID: 198314 [Multi-domain]  Cd Length: 109  Bit Score: 42.57  E-value: 1.66e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922528 135 IKDAYGHLENFLGDnpyLTGSQLTIADLccgatasSLAAVLD-LD----ELK----YPKVAAWFERLSKLPHYEE 200
Cdd:cd03205  42 IERALDALEAELGD---LPGGRLTLGDI-------AVACALGyLDfrfpELDwragHPALAAWFARFEARPSFQA 106
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-76 2.13e-05

GST_N family, Class Tau 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 41.49  E-value: 2.13e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLlagDHFKDAFLKKNPQH-TVPLLEDNGALIWDSHAIVCYL 76
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDL---GNKSELLLASNPVHkKIPVLLHNGKPICESLIIVEYI 70
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 139-211 5.11e-05

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 41.00  E-value: 5.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   139 YGHLENFL--GDNPYLTGSQLTIADLccgatasSLAAVLDLDEL--------KYPKVAAWFERLSKLPhyeednlrGLKK 208
Cdd:pfam14497  35 LGYFEKVLnkNGGGYLVGDKLTYADL-------ALFQVLDGLLYpkapdaldKYPKLKALHERVAARP--------NIKA 99


                  ...
gi 19922528   209 YIN 211
Cdd:pfam14497 100 YLA 102
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 127-196 6.74e-05

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: 40.35  E-value: 6.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922528   127 VPKEKVDNIKDAYGHLENFLGDNPYLTGSQLTIADLC-CGATASSLAAVLDLDELKYPKVAAWFERLSKLP 196
Cdd:pfam00043  23 EVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIAlAPALLWLYELDPACLREKFPNLKAWFERVAARP 93
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 94-191 1.09e-04

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: 40.30  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  94 RAQVDQrlFFDAsilFMSLRNVSIPYFLRQVSLVPKEK----VDNIKDAY-GHLENFLGDN--PYLTGSQLTIADLCC-G 165
Cdd:cd03192   3 EARVDA--IVDT---IADLRAEFAPYFYEPDGEEKKEKkkefLEEALPKFlGKFEKILKKSggGYFVGDKLTWADLALfD 77

                        90       100
                ....*....|....*....|....*.
gi 19922528 166 ATASSLAAVLDLDELKYPKVAAWFER 191
Cdd:cd03192  78 VLDYLLYLLPKDLLEKYPKLKALRER 103
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 107-196 1.39e-04

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 40.37  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528 107 ILFMSLRNvSIPYFLRQVSLVPKEKVD------NIKDAYGHLENFLGDNPYLTGSQLTIADLCCGATASSLAAVLDLDEl 180
Cdd:cd03189  30 LVFGKIGE-APPPFFRPISRKIADKPLqafinpELKRHLDFLEDHLAKHPYFAGDELTAADIMMSFPLEAALARGPLLE- 107

                        90
                ....*....|....*.
gi 19922528 181 KYPKVAAWFERLSKLP 196
Cdd:cd03189 108 QYPNIAAYLERIEARP 123
GST_C_7 cd03206
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ...
 142-198 2.22e-04

C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized 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: 198315 [Multi-domain]  Cd Length: 100  Bit Score: 39.13  E-value: 2.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19922528 142 LENFLGDNPYLTGSQLTIADLCCGA-TASSLAAVLDLDElkYPKVAAWFERLSKLPHY 198
Cdd:cd03206  45 LDQHLAGRDWLAGDRPTIADVACYPyIALAPEGGVSLEP--YPAIRAWLARVEALPGF 100
GST_C_Ure2p cd10293
C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione ...
 95-196 2.82e-04

C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Ure2p subfamily; composed of the Saccharomyces cerevisiae Ure2p and related fungal 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. 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: 198326 [Multi-domain]  Cd Length: 117  Bit Score: 39.33  E-value: 2.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528  95 AQVDQRLFFDASilfmslrnVSIPYFLRQV--SLVPKEKV--------DNIKDAYGHLENFLGD--NPYLTGSQLTIADL 162
Cdd:cd10293   3 YQAKQWLFFQAS--------GQGPYWGQAGwfNVFHAEKVpsaierytNEIRRVLGVLETALAEryRVWLVGDKFTIADL 74

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 19922528 163 CCGATASSLAAVL----DLDELKYPKVAAWFERLSKLP 196
Cdd:cd10293  75 AFVPWNNVVDMIFidpeLDIKKEFPHVYKWLKRMLARP 112
GST_N_Metaxin_like cd03080
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ...
 10-80 3.46e-04

GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, predominantly uncharacterized, with similarity to metaxins and GSTs. 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. One characterized member of this subgroup is a novel GST from Rhodococcus with toluene o-monooxygenase and gamma-glutamylcysteine synthetase activities. Also members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system.


Pssm-ID: 239378 [Multi-domain]  Cd Length: 75  Bit Score: 37.99  E-value: 3.46e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922528  10 MDISPPVRACKLTLRALNLDYEykemdllagdHFKDAFLKKNPQHTVPLLEDNGALIWDSHAIVCYLVDKY 80
Cdd:cd03080  14 PSLSPFCLKVETFLRMAGIPYE----------NKFGGLAKRSPKGKLPFIELNGEKIADSELIIDHLEEKY 74
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 129-196 7.72e-04

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 38.31  E-value: 7.72e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922528 129 KEKVDNIKDAYGHLEN-FLGDNPYLTGSQLTIADLCCGATASSLAA------VLDLDELKYPKVAAWFERLSKLP 196
Cdd:cd03185  34 EKAVEEALEALKVLEEeLKGGKPFFGGDTIGYLDIALGSFLGWFKAieevggVKLLDEEKFPLLAAWAERFLERE 108
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 5-80 9.76e-04

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized 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. 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: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 36.94  E-value: 9.76e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKemDLLAGDHFKDAFLKKNPQHTVPLLED--NGALIWDSHAIVCYLVDKY 80
Cdd:cd03041   2 LELYEFEGSPFCRLVREVLTELELDVILY--PCPKGSPKRDKFLEKGGKVQVPYLVDpnTGVQMFESADIVKYLFKTY 77
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 1-211 9.94e-04

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 38.81  E-value: 9.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528    1 MSDKLVLYGMDISPPVRACKLTLRALNLDYEYKEMDLlAGDHFKD----AFLKKNPQHTVPLLEDNGALIWDSHAIVCYL 76
Cdd:PTZ00057   1 MAEEIVLYYFDARGKAELIRLIFAYLGIEYTDKRFGE-NGDAFIEfknfKKEKDTPFEQVPILEMDNIIFAQSQAIVRYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922528   77 VDKYANSDElyprdlvlrAQVDQrlfFDASILFMSLRNvsIPYFLRQVSLVPKEKV----DNIKDAYGHLENFLGDN--P 150
Cdd:PTZ00057  80 SKKYKICGE---------SELNE---FYADMIFCGVQD--IHYKFNNTNLFKQNETtflnEELPKWSGYFENILKKNhcN 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922528  151 YLTGSQLTIADLccgatasSLAAVLDLDELKYPKVAAWFERLSKlpHYE-EDNLRGLKKYIN 211
Cdd:PTZ00057 146 YFVGDNLTYADL-------AVFNLYDDIETKYPNSLKNFPLLKA--HNEfISNLPNIKNYIS 198
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 5-77 1.39e-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: 36.46  E-value: 1.39e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922528   5 LVLYGMDISPPVRACKLTLRALNLDYEYKEMDLlAGDHFKDAFLKKNPQHTVPLLE-DNGALIWDSHAIVCYLV 77
Cdd:cd03044   1 GTLYTYPGNPRSLKILAAAKYNGLDVEIVDFQP-GKENKTPEFLKKFPLGKVPAFEgADGFCLFESNAIAYYVA 73
GST_C_GluProRS_N cd10309
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ...
 133-195 7.16e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198342 [Multi-domain]  Cd Length: 81  Bit Score: 34.60  E-value: 7.16e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922528 133 DNIKDAYGHLENFLGDNPYLTGSQLTIADLCCGATASSLAAVLDLDElKYPKVAAWFERLSKL 195
Cdd:cd10309  20 QDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGEWLASKE-KYVNVTRWFKFISSQ 81
 
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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