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Conserved domains on  [gi|1731011084|gb|TYJ98888|]
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glutathione S-transferase U9-like [Cucumis melo var. makuwa]

Protein Classification

glutathione S-transferase( domain architecture ID 10122769)

glutathione S-transferase (GST) catalyzes 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; such as plant tau class GSTs that are primarily responsible for herbicide detoxification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 92-220 9.18e-43

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: 140.78  E-value: 9.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  92 PYKRSQVRFWADFVQNQLFDGLLLAMKTEGEAQEKAIKEVKEKLKVVEEQglkslLGEGSPFVNGDELGYLDIGMLTILG 171
Cdd:cd03185     1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEE-----LKGGKPFFGGDTIGYLDIALGSFLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1731011084 172 RYKIYEEFFGMKIMEEEEIPIVFSWLNRLIEHPIAKEGAHPKEKVLGLL 220
Cdd:cd03185    76 WFKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-80 4.57e-39

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: 129.71  E-value: 4.57e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731011084   7 VVLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPVYKKVPVLVHNGRSICESAIIFEYIEEVW 80
Cdd:cd03058     1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 92-220 9.18e-43

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: 140.78  E-value: 9.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  92 PYKRSQVRFWADFVQNQLFDGLLLAMKTEGEAQEKAIKEVKEKLKVVEEQglkslLGEGSPFVNGDELGYLDIGMLTILG 171
Cdd:cd03185     1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEE-----LKGGKPFFGGDTIGYLDIALGSFLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1731011084 172 RYKIYEEFFGMKIMEEEEIPIVFSWLNRLIEHPIAKEGAHPKEKVLGLL 220
Cdd:cd03185    76 WFKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-80 4.57e-39

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: 129.71  E-value: 4.57e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731011084   7 VVLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPVYKKVPVLVHNGRSICESAIIFEYIEEVW 80
Cdd:cd03058     1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-204 3.69e-38

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 131.56  E-value: 3.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFL---NKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEEVWNDngP 85
Cdd:COG0625     4 LYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAERYPE--P 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  86 SLLPQDPYKRSQVRFWADFVQNQLFDGLLLAMK-----TEGEAQEKAIKEVKEKLKVVEEQglkslLGEGsPFVNGDELG 160
Cdd:COG0625    81 PLLPADPAARARVRQWLAWADGDLHPALRNLLErlapeKDPAAIARARAELARLLAVLEAR-----LAGG-PYLAGDRFS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1731011084 161 YLDIGMLTILGRYkiyeEFFGMKImeeEEIPIVFSWLNRLIEHP 204
Cdd:COG0625   155 IADIALAPVLRRL----DRLGLDL---ADYPNLAAWLARLAARP 191
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
9-78 3.62e-19

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 78.42  E-value: 3.62e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPVYkKVPVLVHNGRSICESAIIFEYIEE 78
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLG-KVPVLEDDGGILCESLAIIDYLEE 69
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 9-171 5.12e-13

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 65.51  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPVyKKVPVLV-HNGRSICESAIIFEYIEEVwnDNGPSL 87
Cdd:PRK10357    3 LIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVtEEGECWFDSPIIAEYIELL--NVAPAM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  88 LPQDPYKRSQVRfwadfvQ-NQLFDGLLlamktegeaqEKAIKEVKEKLKVVEEQ-----------------GLKSLLGE 149
Cdd:PRK10357   80 LPRDPLAALRVR------QlEALADGIM----------DAALVSVREQARPAAQQsedellrqrekinrsldALEGYLVD 143

                         170       180
                  ....*....|....*....|..
gi 1731011084 150 GSpfVNGDELGYLDIGMLTILG 171
Cdd:PRK10357  144 GT--LKTDTVNLATIAIACAVG 163
PLN02395 PLN02395
glutathione S-transferase
 7-145 2.25e-11

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 61.03  E-value: 2.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   7 VVLYG-LWASPfvKRVELALKIKGIPFEYVEEDFL---NKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEEVWND 82
Cdd:PLN02395    3 LKVYGpAFASP--KRALVTLIEKGVEFETVPVDLMkgeHKQPEYLALQP-FGVVPVIVDGDYKIFESRAIMRYYAEKYRS 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731011084  83 NGPSLLPQDPYKRSQVRFWADfVQNQLFDGLLLAM--------KTEGEAQEKAIKEVKEK----LKVVEEQGLKS 145
Cdd:PLN02395   80 QGPDLLGKTIEERGQVEQWLD-VEATSYHPPLLNLtlhilfasKMGFPADEKVIKESEEKlakvLDVYEARLSKS 153
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
6-66 3.53e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 35.17  E-value: 3.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731011084   6 KVVLYGLWASPFVKRVELALKIKGIPFEYVEEDflnKSPELLKFnpVYKK-----VPVLVHNGRSI 66
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVD---EDPEAREE--LRERsgrrtVPVIFIGGEHL 61
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 92-220 9.18e-43

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: 140.78  E-value: 9.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  92 PYKRSQVRFWADFVQNQLFDGLLLAMKTEGEAQEKAIKEVKEKLKVVEEQglkslLGEGSPFVNGDELGYLDIGMLTILG 171
Cdd:cd03185     1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEE-----LKGGKPFFGGDTIGYLDIALGSFLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1731011084 172 RYKIYEEFFGMKIMEEEEIPIVFSWLNRLIEHPIAKEGAHPKEKVLGLL 220
Cdd:cd03185    76 WFKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFL 124
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-80 4.57e-39

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: 129.71  E-value: 4.57e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731011084   7 VVLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPVYKKVPVLVHNGRSICESAIIFEYIEEVW 80
Cdd:cd03058     1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-204 3.69e-38

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 131.56  E-value: 3.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFL---NKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEEVWNDngP 85
Cdd:COG0625     4 LYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAERYPE--P 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  86 SLLPQDPYKRSQVRFWADFVQNQLFDGLLLAMK-----TEGEAQEKAIKEVKEKLKVVEEQglkslLGEGsPFVNGDELG 160
Cdd:COG0625    81 PLLPADPAARARVRQWLAWADGDLHPALRNLLErlapeKDPAAIARARAELARLLAVLEAR-----LAGG-PYLAGDRFS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1731011084 161 YLDIGMLTILGRYkiyeEFFGMKImeeEEIPIVFSWLNRLIEHP 204
Cdd:COG0625   155 IADIALAPVLRRL----DRLGLDL---ADYPNLAAWLARLAARP 191
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
9-78 3.62e-19

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 78.42  E-value: 3.62e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPVYkKVPVLVHNGRSICESAIIFEYIEE 78
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLG-KVPVLEDDGGILCESLAIIDYLEE 69
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 7-77 2.16e-18

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: 76.46  E-value: 2.16e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731011084   7 VVLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSP-ELLKFNPvYKKVPVLVHNGRSICESAIIFEYIE 77
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQeEFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 9-78 2.02e-16

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: 71.18  E-value: 2.02e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFL---NKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEE 78
Cdd:pfam02798   5 LYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNP-LGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 14-78 2.42e-15

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 68.04  E-value: 2.42e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731011084  14 ASPFVKRVELALKIKGIPFEYVEEDFL--NKSPELLKFNPvYKKVPVLV-HNGRSICESAIIFEYIEE 78
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLDpkDKPPELLALNP-LGTVPVLVlPDGTVLTDSLVILEYLEE 67
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 9-171 5.12e-13

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 65.51  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPVyKKVPVLV-HNGRSICESAIIFEYIEEVwnDNGPSL 87
Cdd:PRK10357    3 LIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVtEEGECWFDSPIIAEYIELL--NVAPAM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  88 LPQDPYKRSQVRfwadfvQ-NQLFDGLLlamktegeaqEKAIKEVKEKLKVVEEQ-----------------GLKSLLGE 149
Cdd:PRK10357   80 LPRDPLAALRVR------QlEALADGIM----------DAALVSVREQARPAAQQsedellrqrekinrsldALEGYLVD 143

                         170       180
                  ....*....|....*....|..
gi 1731011084 150 GSpfVNGDELGYLDIGMLTILG 171
Cdd:PRK10357  144 GT--LKTDTVNLATIAIACAVG 163
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 8-77 1.24e-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: 61.05  E-value: 1.24e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731011084   8 VLYGLWASPFVKRVELALKIKGIPFEYVEEDFLN---KSPELLKFNPVyKKVPVLVHNGRSICESAIIFEYIE 77
Cdd:cd03042     2 ILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKgeqLSPAYRALNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 9-75 2.64e-12

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: 60.28  E-value: 2.64e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFLN---KSPELLKFNPvYKKVPVLVHNGRSICESAIIFEY 75
Cdd:cd03056     3 LYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKgetRTPEFLALNP-NGEVPVLELDGRVLAESNAILVY 71
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 6-78 7.59e-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: 59.20  E-value: 7.59e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731011084   6 KVVLYGLWASPFVKRVELALKIKGIPFEYVEEDFL---NKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEE 78
Cdd:cd03053     1 VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNP-FGQIPALEDGDLKLFESRAITRYLAE 75
PLN02395 PLN02395
glutathione S-transferase
 7-145 2.25e-11

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 61.03  E-value: 2.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   7 VVLYG-LWASPfvKRVELALKIKGIPFEYVEEDFL---NKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEEVWND 82
Cdd:PLN02395    3 LKVYGpAFASP--KRALVTLIEKGVEFETVPVDLMkgeHKQPEYLALQP-FGVVPVIVDGDYKIFESRAIMRYYAEKYRS 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731011084  83 NGPSLLPQDPYKRSQVRFWADfVQNQLFDGLLLAM--------KTEGEAQEKAIKEVKEK----LKVVEEQGLKS 145
Cdd:PLN02395   80 QGPDLLGKTIEERGQVEQWLD-VEATSYHPPLLNLtlhilfasKMGFPADEKVIKESEEKlakvLDVYEARLSKS 153
PRK15113 PRK15113
glutathione transferase;
7-99 1.75e-10

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 58.82  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   7 VVLYG--LWASPFVKRVELALKIKGIPFEYV----------EEDFLNKSPEllkfnpvyKKVPVLVHNGRSICESAIIFE 74
Cdd:PRK15113    6 ITLYSdaHFFSPYVMSAFVALQEKGLPFELKtvdldagehlQPTYQGYSLT--------RRVPTLQHDDFELSESSAIAE 77

                          90       100
                  ....*....|....*....|....*.
gi 1731011084  75 YIEEVWNDNG-PSLLPQDPYKRSQVR 99
Cdd:PRK15113   78 YLEERFAPPAwERIYPADLQARARAR 103
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 7-75 3.41e-10

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: 54.53  E-value: 3.41e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731011084   7 VVLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNK---SPELLKFNPVyKKVPVLVHNGRSICESAIIFEY 75
Cdd:cd03045     1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKGehlKPEFLKLNPQ-HTVPTLVDNGFVLWESHAILIY 71
sspA PRK09481
stringent starvation protein A; Provisional
 20-172 6.06e-09

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 54.33  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  20 RVELALKIKGIPFEYVEEDflNKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEEVWNDngPSLLPQDPYKRSQVR 99
Cdd:PRK09481   26 RIVLAEKGVSVEIEQVEKD--NLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPH--PPLMPVYPVARGESR 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731011084 100 FWADFVQNQLFDGLLLAMKTEGEAQEKAIKEVKEKLkvveeQGLKSLLGEgSPFVNGDELGYLDIGMLTILGR 172
Cdd:PRK09481  101 LMMHRIEKDWYSLMNKIVNGSASEADAARKQLREEL-----LAIAPVFGE-KPYFMSEEFSLVDCYLAPLLWR 167
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 9-77 6.62e-09

GST_N family, unknown subfamily 3; 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: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 51.11  E-value: 6.62e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731011084   9 LYGLWASPFVKRVELAL--KIKGIPFEYVEEDFLNKSPELLKFNPVyKKVPVLVHN-GRSICESAIIFEYIE 77
Cdd:cd03049     3 LLYSPTSPYVRKVRVAAheTGLGDDVELVLVNPWSDDESLLAVNPL-GKIPALVLDdGEALFDSRVICEYLD 73
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 20-78 2.28e-08

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: 49.81  E-value: 2.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731011084  20 RVELALKIKGIPFEYVEEDFLN---KSPELLKFNPVyKKVPVLVHNGRSICESAIIFEYIEE 78
Cdd:cd03046    13 RILWLLEELGLPYELVLYDRGPgeqAPPEYLAINPL-GKVPVLVDGDLVLTESAAIILYLAE 73
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 8-78 2.77e-08

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: 49.25  E-value: 2.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731011084   8 VLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEE 78
Cdd:cd03059     2 TLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNP-YGTVPTLVDRDLVLYESRIIMEYLDE 71
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 16-174 1.06e-07

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 51.15  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  16 PFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEEVWNDngPSlLPQDPYKR 95
Cdd:PLN02817   74 PFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISP-EGKVPVVKLDEKWVADSDVITQALEEKYPD--PP-LATPPEKA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  96 SqvrfwadfVQNQLFDGLL--LAMKTEGEAQEKAIKEvkeklkvvEEQGLKSLLGEGSPFVNGDELGYLDIG-------M 166
Cdd:PLN02817  150 S--------VGSKIFSTFIgfLKSKDPGDGTEQALLD--------ELTSFDDYIKENGPFINGEKISAADLSlgpklyhL 213


                  ....*...
gi 1731011084 167 LTILGRYK 174
Cdd:PLN02817  214 EIALGHYK 221
GST_N_Metaxin_like cd03080
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ...
 7-78 1.38e-07

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: 47.62  E-value: 1.38e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731011084   7 VVLYGLW-------ASPFVKRVELALKIKGIPFEYVEEDFLNKSPEllkfnpvyKKVPVLVHNGRSICESAIIFEYIEE 78
Cdd:cd03080     2 ITLYQFPrafgvpsLSPFCLKVETFLRMAGIPYENKFGGLAKRSPK--------GKLPFIELNGEKIADSELIIDHLEE 72
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-77 2.43e-07

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: 47.35  E-value: 2.43e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731011084   3 EENKVVLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPvYKKVPVLVHN-GRSICESAIIFEYIE 77
Cdd:cd03055    15 VPGIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNP-QGKVPALEIDeGKVVYESLIICEYLD 89
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 9-77 2.67e-07

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: 46.91  E-value: 2.67e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFL---NKSPELLKFNPvYKKVPVLV-HNGRSICESAIIFEYIE 77
Cdd:cd03051     3 LYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAageQRSPEFLAKNP-AGTVPVLElDDGTVITESVAICRYLE 74
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 9-78 5.36e-06

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: 43.30  E-value: 5.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731011084   9 LYGlWASPFVKRVELALKIKGIPFEYVEEDFL---NKSPELLKFNPvYKKVPVLV---HNGRSICESAIIFEYIEE 78
Cdd:cd03048     4 LYT-HGTPNGFKVSIMLEELGLPYEIHPVDISkgeQKKPEFLKINP-NGRIPAIVdhnGTPLTVFESGAILLYLAE 77
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 15-78 8.44e-06

GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF.


Pssm-ID: 239336 [Multi-domain]  Cd Length: 84  Bit Score: 42.72  E-value: 8.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731011084  15 SPFVKRVELALKIKGIPFEYVEEDFLNKSPEL-LKFNPVYKKVPVLVH-NGRSICESAIIFEYIEE 78
Cdd:cd03038    16 SPNVWKTRLALNHKGLEYKTVPVEFPDIPPILgELTSGGFYTVPVIVDgSGEVIGDSFAIAEYLEE 81
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 8-69 8.59e-06

GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega 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. 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. Like Omega enzymes, proteins in this subfamily 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.


Pssm-ID: 239358 [Multi-domain]  Cd Length: 71  Bit Score: 42.35  E-value: 8.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731011084   8 VLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPELLKFNPvYKKVPVLV-HNGRSICES 69
Cdd:cd03060     2 ILYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASP-KGTVPVLVlGNGTVIEES 63
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 9-76 1.68e-05

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: 41.84  E-value: 1.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731011084   9 LYGLWASPFVKRVELALKIKGIPFEYVEEDFLN---KSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYI 76
Cdd:cd03050     3 LYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKgeqLTPEFKKINP-FGKVPAIVDGDFTLAESVAILRYL 72
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
 20-76 1.70e-05

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: 41.81  E-value: 1.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1731011084  20 RVELALKIKGIPFEYVEEDFLNKS--PELLKFNPVyKKVPVLVHNGRSICESAIIFEYI 76
Cdd:cd03043    15 RPWLLLKAAGIPFEEILVPLYTPDtrARILEFSPT-GKVPVLVDGGIVVWDSLAICEYL 72
GST_N_Metaxin cd03054
GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a ...
 14-78 4.97e-05

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


Pssm-ID: 239352 [Multi-domain]  Cd Length: 72  Bit Score: 40.29  E-value: 4.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731011084  14 ASPFVKRVELALKIKGIPFEYVEEDFLNKSPEllkfnpvyKKVPVLVHNGRSICESAIIFEYIEE 78
Cdd:cd03054    15 LSPECLKVETYLRMAGIPYEVVFSSNPWRSPT--------GKLPFLELNGEKIADSEKIIEYLKK 71
PLN02473 PLN02473
glutathione S-transferase
 7-117 2.96e-04

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 40.74  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084   7 VVLYGLWASPFVKRVELALKIKGIPFEYVEED---FLNKSPELLKFNPvYKKVPVLVHNGRSICESAIIFEYIEEVWNDN 83
Cdd:PLN02473    3 VKVYGQIKAANPQRVLLCFLEKGIEFEVIHVDldkLEQKKPEHLLRQP-FGQVPAIEDGDLKLFESRAIARYYATKYADQ 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1731011084  84 GPSLLPQDPYKRSQVRFWADfVQNQLFDGLLLAM 117
Cdd:PLN02473   82 GTDLLGKTLEHRAIVDQWVE-VENNYFYAVALPL 114
GST_N_4 pfam17172
Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.
 16-114 1.91e-03

Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.


Pssm-ID: 465370 [Multi-domain]  Cd Length: 97  Bit Score: 36.40  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731011084  16 PFVKRVELALKIKGIPFEYVEEDFLNKSPEllkfnpvyKKVPVLVHNGRSICESAIIFEYIEEVWNDNGPSLLPQDpykR 95
Cdd:pfam17172   1 PFCLKVETYLRMAGIPYEVEPSSNPSASPK--------GKLPFIELNGDLIADSEFIIEFLKEKGVDLDAGLSPEQ---K 69

                          90
                  ....*....|....*....
gi 1731011084  96 SQVRFWADFVQNQLFDGLL 114
Cdd:pfam17172  70 ADARALKALVEEHLYWALL 88
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
6-66 3.53e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 35.17  E-value: 3.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731011084   6 KVVLYGLWASPFVKRVELALKIKGIPFEYVEEDflnKSPELLKFnpVYKK-----VPVLVHNGRSI 66
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVD---EDPEAREE--LRERsgrrtVPVIFIGGEHL 61
GST_N_mPGES2 cd03040
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ...
 6-64 5.10e-03

GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated, and a C-terminal soluble domain with a GST-like structure.


Pssm-ID: 239338  Cd Length: 77  Bit Score: 35.08  E-value: 5.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1731011084   6 KVVLYGLWASPFVKRVELALKIKGIPFEYVEEDFLNKSPelLKFNpVYKKVPVLVHNGR 64
Cdd:cd03040     1 KITLYQYKTCPFCCKVRAFLDYHGIPYEVVEVNPVSRKE--IKWS-SYKKVPILRVESG 56
 
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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