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Conserved domains on  [gi|14719799|pdb|1E6B|A]
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Chain A, GLUTATHIONE S-TRANSFERASE

Protein Classification

maleylacetoacetate isomerase( domain architecture ID 11492162)

maleylacetoacetate isomerase is a bifunctional enzyme that shows maleylacetoacetate isomerase activity using glutathione as a cofactor and minimal glutathione-conjugating activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 10-217 7.37e-102

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


:

Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 293.46  E-value: 7.37e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         10 KLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLK-GDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPP 88
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRdGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         89 LLPRDLHKRAVNYQAMSIVLSGIQPHQNLAVIRYIEEKINVEE--KTAWVNNAITKGFTALEKLLVNCAGKHATGDEIYL 166
Cdd:TIGR01262  81 LLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEeaRNRWYQHWISKGFAALEALLQPHAGRFCVGDTPTL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
1E6B_A        167 ADLFLAPQIHGAInRFQINMEPYPTLAKCYESYNELPAFQNALPEKQPDAP 217
Cdd:TIGR01262 161 ADLCLVPQVYNAE-RFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210
 
Name Accession Description Interval E-value
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 10-217 7.37e-102

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 293.46  E-value: 7.37e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         10 KLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLK-GDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPP 88
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRdGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         89 LLPRDLHKRAVNYQAMSIVLSGIQPHQNLAVIRYIEEKINVEE--KTAWVNNAITKGFTALEKLLVNCAGKHATGDEIYL 166
Cdd:TIGR01262  81 LLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEeaRNRWYQHWISKGFAALEALLQPHAGRFCVGDTPTL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
1E6B_A        167 ADLFLAPQIHGAInRFQINMEPYPTLAKCYESYNELPAFQNALPEKQPDAP 217
Cdd:TIGR01262 161 ADLCLVPQVYNAE-RFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-217 2.23e-64

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 198.20  E-value: 2.23e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPP 88
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A       89 LLPRDLHKRAVNYQAMSIVLSGIQPHQNLAVIRYIEEKInvEEKTAWVNNAITKGFTALEKLLVncAGKHATGDEIYLAD 168
Cdd:COG0625  82 LLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKD--PAAIARARAELARLLAVLEARLA--GGPYLAGDRFSIAD 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1E6B_A      169 LFLAPQIHGAiNRFQINMEPYPTLAKCYESYNELPAFQNALPEKQPDAP 217
Cdd:COG0625 158 IALAPVLRRL-DRLGLDLADYPNLAAWLARLAARPAFQRALAAAEPDLA 205
GST_C_Zeta cd03191
C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione ...
 94-213 2.00e-57

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198300 [Multi-domain]  Cd Length: 121  Bit Score: 177.77  E-value: 2.00e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A       94 LHKRAVNYQAMSIVLSGIQPHQNLAVIRYIEEKINV--EEKTAWVNNAITKGFTALEKLLVNCAGKHATGDEIYLADLFL 171
Cdd:cd03191   1 PKKRARVRAIALIIACDIHPLQNLRVLKYLTEKLGVseEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1E6B_A      172 APQIHGAInRFQINMEPYPTLAKCYESYNELPAFQNALPEKQ 213
Cdd:cd03191  81 VPQVYNAR-RFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 7-82 6.07e-20

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: 80.43  E-value: 6.07e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1E6B_A          7 EKLKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDE 82
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
PLN02395 PLN02395
glutathione S-transferase
 18-114 2.59e-16

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 74.51  E-value: 2.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        18 SCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPE--PPLLPRDLH 95
Cdd:PLN02395  11 ASPKRALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYRSqgPDLLGKTIE 90

                         90
                 ....*....|....*....
1E6B_A        96 KRAVNYQAMSIVLSGIQPH 114
Cdd:PLN02395  91 ERGQVEQWLDVEATSYHPP 109
 
Name Accession Description Interval E-value
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 10-217 7.37e-102

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 293.46  E-value: 7.37e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         10 KLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLK-GDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPP 88
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRdGEQRSPEFLALNPQGLVPTLDIDGEVLTQSLAIIEYLEETYPDPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         89 LLPRDLHKRAVNYQAMSIVLSGIQPHQNLAVIRYIEEKINVEE--KTAWVNNAITKGFTALEKLLVNCAGKHATGDEIYL 166
Cdd:TIGR01262  81 LLPADPIKRARVRALALLIACDIHPLNNLRVLQYLREKLGVEEeaRNRWYQHWISKGFAALEALLQPHAGRFCVGDTPTL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
1E6B_A        167 ADLFLAPQIHGAInRFQINMEPYPTLAKCYESYNELPAFQNALPEKQPDAP 217
Cdd:TIGR01262 161 ADLCLVPQVYNAE-RFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-217 2.23e-64

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 198.20  E-value: 2.23e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPP 88
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A       89 LLPRDLHKRAVNYQAMSIVLSGIQPHQNLAVIRYIEEKInvEEKTAWVNNAITKGFTALEKLLVncAGKHATGDEIYLAD 168
Cdd:COG0625  82 LLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKD--PAAIARARAELARLLAVLEARLA--GGPYLAGDRFSIAD 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1E6B_A      169 LFLAPQIHGAiNRFQINMEPYPTLAKCYESYNELPAFQNALPEKQPDAP 217
Cdd:COG0625 158 IALAPVLRRL-DRLGLDLADYPNLAAWLARLAARPAFQRALAAAEPDLA 205
GST_C_Zeta cd03191
C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione ...
 94-213 2.00e-57

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198300 [Multi-domain]  Cd Length: 121  Bit Score: 177.77  E-value: 2.00e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A       94 LHKRAVNYQAMSIVLSGIQPHQNLAVIRYIEEKINV--EEKTAWVNNAITKGFTALEKLLVNCAGKHATGDEIYLADLFL 171
Cdd:cd03191   1 PKKRARVRAIALIIACDIHPLQNLRVLKYLTEKLGVseEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1E6B_A      172 APQIHGAInRFQINMEPYPTLAKCYESYNELPAFQNALPEKQ 213
Cdd:cd03191  81 VPQVYNAR-RFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 9-81 7.39e-44

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: 141.55  E-value: 7.39e-44
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLD 81
Cdd:cd03042   1 MILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYLD 73
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 9-81 1.57e-27

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: 99.57  E-value: 1.57e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDsdFKKINPMGTVPALVDGDVVINDSFAIIMYLD 81
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEE--FLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 9-85 2.39e-22

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: 86.40  E-value: 2.39e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1E6B_A        9 LKLYsYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYP 85
Cdd:cd03046   1 ITLY-HLPRSRSFRILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 8-83 3.15e-21

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: 83.47  E-value: 3.15e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1E6B_A        8 KLKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEK 83
Cdd:cd03053   1 VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAEK 76
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 7-82 6.07e-20

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: 80.43  E-value: 6.07e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1E6B_A          7 EKLKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDE 82
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 9-85 6.47e-20

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: 80.28  E-value: 6.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        9 LKLYSyWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVD---GDVVINDSFAIIMYLDEKYP 85
Cdd:cd03048   2 ITLYT-HGTPNGFKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDhngTPLTVFESGAILLYLAEKYD 80
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 17-83 1.41e-19

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 79.21  E-value: 1.41e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1E6B_A         17 SSCAHRVRIALALKGLDYEYIPVNlLKGDQFDSDFKKINPMGTVPALVDGD-VVINDSFAIIMYLDEK 83
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVD-LDPKDKPPELLALNPLGTVPVLVLPDgTVLTDSLVILEYLEEL 68
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 9-80 1.49e-19

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: 79.16  E-value: 1.49e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYL 80
Cdd:cd03056   1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
11-88 6.91e-19

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 77.27  E-value: 6.91e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1E6B_A         11 LYSYWRSSCAHRVRIALALKGLDYEYIPVNLlkGDQFDSdFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPP 88
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPP--GDHPPE-LLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 9-80 1.82e-18

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: 76.49  E-value: 1.82e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYL 80
Cdd:cd03045   1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIYL 72
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 9-81 1.36e-17

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: 73.87  E-value: 1.36e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALV-DGDVVINDSFAIIMYLD 81
Cdd:cd03051   1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLElDDGTVITESVAICRYLE 74
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 9-85 3.61e-17

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: 72.95  E-value: 3.61e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1E6B_A        9 LKLYsYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGD-VVINDSFAIIMYLDEKYP 85
Cdd:cd03057   1 MKLY-YSPGACSLAPHIALEELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALVLDDgEVLTESAAILQYLADLHP 77
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 9-84 2.36e-16

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: 70.73  E-value: 2.36e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKY 84
Cdd:cd03050   1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76
PLN02395 PLN02395
glutathione S-transferase
 18-114 2.59e-16

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 74.51  E-value: 2.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        18 SCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPE--PPLLPRDLH 95
Cdd:PLN02395  11 ASPKRALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYRSqgPDLLGKTIE 90

                         90
                 ....*....|....*....
1E6B_A        96 KRAVNYQAMSIVLSGIQPH 114
Cdd:PLN02395  91 ERGQVEQWLDVEATSYHPP 109
PRK15113 PRK15113
glutathione transferase;
9-98 9.63e-16

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 72.68  E-value: 9.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         9 LKLYS--YWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPE 86
Cdd:PRK15113   6 ITLYSdaHFFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAP 85

                         90
                 ....*....|....*
1E6B_A        87 PP---LLPRDLHKRA 98
Cdd:PRK15113  86 PAwerIYPADLQARA 100
sspA PRK09481
stringent starvation protein A; Provisional
 20-91 2.85e-15

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 71.66  E-value: 2.85e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1E6B_A        20 AHRVRIALALKGLDYEyipVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPPLLP 91
Cdd:PRK09481  22 SHQVRIVLAEKGVSVE---IEQVEKDNLPQDLIDLNPYQSVPTLVDRELTLYESRIIMEYLDERFPHPPLMP 90
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 9-84 1.21e-13

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: 63.50  E-value: 1.21e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLlkgDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKY 84
Cdd:cd03059   1 MTLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDP---DNPPEDLAELNPYGTVPTLVDRDLVLYESRIIMEYLDERF 73
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 9-82 4.16e-13

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: 62.30  E-value: 4.16e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNL-LKGDQfdsdFKKINPM-GTVPALVDGDVVINDSFAIIMYLDE 82
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLgNKSEL----LLASNPVhKKIPVLLHNGKPICESLIIVEYIDE 72
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 22-85 4.40e-12

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: 59.67  E-value: 4.40e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A       22 RVRIALALKGLDYEYIPVNL-----LKGDQFDSDFKkinpmgTVPALVDGD-VVINDSFAIIMYLDEKYP 85
Cdd:cd03038  21 KTRLALNHKGLEYKTVPVEFpdippILGELTSGGFY------TVPVIVDGSgEVIGDSFAIAEYLEEAYP 84
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
 20-213 1.29e-11

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 61.63  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        20 AHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGD-------VVINDSFAIIMYLDEKypEPPLLPR 92
Cdd:PRK13972  12 GHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAEK--TGLFLSH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        93 DLHKRAVNYQAMSIVLSGIQP---------HQNLAVIRYIEEKINVEEKtawvnnaitKGFTALEKLLVNcaGKHATGDE 163
Cdd:PRK13972  90 ETRERAATLQWLFWQVGGLGPmlgqnhhfnHAAPQTIPYAIERYQVETQ---------RLYHVLNKRLEN--SPWLGGEN 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
1E6B_A       164 IYLADLFLAPQIHgAINRFQINMEPYPTLAKCYESYNELPAFQNALPEKQ 213
Cdd:PRK13972 159 YSIADIACWPWVN-AWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQ 207
PRK11752 PRK11752
putative S-transferase; Provisional
 25-98 2.12e-11

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 61.48  E-value: 2.12e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1E6B_A        25 IALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVD--GD--VVINDSFAIIMYLDEKYPEppLLPRDLHKRA 98
Cdd:PRK11752  66 LALGVKGAEYDAWLIRIGEGDQFSSGFVEINPNSKIPALLDrsGNppIRVFESGAILLYLAEKFGA--FLPKDLAART 141
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
 10-80 1.53e-10

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: 55.30  E-value: 1.53e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1E6B_A       10 KLYSYWrsscAHRVRIALALKGLDYEYIPVNLLKGDQFDsDFKKINPMGTVPALVDGDVVINDSFAIIMYL 80
Cdd:cd03043   7 KNYSSW----SLRPWLLLKAAGIPFEEILVPLYTPDTRA-RILEFSPTGKVPVLVDGGIVVWDSLAICEYL 72
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 20-80 5.65e-10

GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 239337 [Multi-domain]  Cd Length: 72  Bit Score: 53.71  E-value: 5.65e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1E6B_A       20 AHRVRIALALKGLDYEYIPVNllKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYL 80
Cdd:cd03039  12 GEPIRLLLADAGVEYEDVRIT--YEEWPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYL 70
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
 9-80 1.84e-08

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: 49.62  E-value: 1.84e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVnllkGDQF----DSDFKKINPMGTVPALVDGDVVINDSFAIIMYL 80
Cdd:cd03047   1 LTIWGRRSSINVQKVLWLLDELGLPYERIDA----GGQFggldTPEFLAMNPNGRVPVLEDGDFVLWESNAILRYL 72
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 6-81 5.25e-08

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: 48.89  E-value: 5.25e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1E6B_A        6 EEKLKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLL-KGDQFdsdFKKiNPMGTVPAL-VDGDVVINDSFAIIMYLD 81
Cdd:cd03055  16 PGIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKdKPDWF---LEK-NPQGKVPALeIDEGKVVYESLIICEYLD 89
PLN02473 PLN02473
glutathione S-transferase
 9-99 7.28e-08

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 51.14  E-value: 7.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPE-- 86
Cdd:PLN02473   3 VKVYGQIKAANPQRVLLCFLEKGIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGDLKLFESRAIARYYATKYADqg 82

                         90
                 ....*....|...
1E6B_A        87 PPLLPRDLHKRAV 99
Cdd:PLN02473  83 TDLLGKTLEHRAI 95
GST_N_GDAP1 cd03052
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ...
 9-81 2.16e-07

GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal TRX-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains. It does not exhibit GST activity using standard substrates.


Pssm-ID: 239350 [Multi-domain]  Cd Length: 73  Bit Score: 46.77  E-value: 2.16e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLD 81
Cdd:cd03052   1 LVLYHWTQSFSSQKVRLVIAEKGLRCEEYDVSLPLSEHNEPWFMRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 8-81 2.25e-06

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: 44.17  E-value: 2.25e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1E6B_A        8 KLkLYSYwRSSCAHRVRIALALKGL--DYEYIPVNLLKGDqfdSDFKKINPMGTVPALV-DGDVVINDSFAIIMYLD 81
Cdd:cd03049   2 KL-LYSP-TSPYVRKVRVAAHETGLgdDVELVLVNPWSDD---ESLLAVNPLGKIPALVlDDGEALFDSRVICEYLD 73
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 21-89 2.67e-06

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 46.91  E-value: 2.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1E6B_A        21 HRVRIALALKGLDYEYIPVNLLKGDQFdsdFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPPL 89
Cdd:PLN02817  77 QRVLLTLEEKHLPYDMKLVDLTNKPEW---FLKISPEGKVPVVKLDEKWVADSDVITQALEEKYPDPPL 142
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 9-172 3.18e-06

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 46.25  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         9 LKLYSYWRSSCAHRVRIALALKGLDYEYipVNLLKGDQfDSDFKKINPMGTVPALV--DGDVVInDSFAIIMYLDEKYPE 86
Cdd:PRK10357   1 MKLIGSYTSPFVRKISILLLEKGITFEF--VNELPYNA-DNGVAQYNPLGKVPALVteEGECWF-DSPIIAEYIELLNVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        87 PPLLPRD----LHKRAVNYQA---MSIVLSGIQPHQNLAVIRYIEEKINVEEKtawvnnaITKGFTALEKLLVNcaGKHA 159
Cdd:PRK10357  77 PAMLPRDplaaLRVRQLEALAdgiMDAALVSVREQARPAAQQSEDELLRQREK-------INRSLDALEGYLVD--GTLK 147

                        170
                 ....*....|...
1E6B_A       160 TgDEIYLADLFLA 172
Cdd:PRK10357 148 T-DTVNLATIAIA 159
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 9-91 5.81e-06

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 45.44  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         9 LKLYsYWRSSCAHRVRIALALKGLDYEYIPVNLLK-----GDqfdsDFKKINPMGTVPALV-DGDVVINDSFAIIMYLDE 82
Cdd:PRK10542   1 MKLF-YKPGACSLASHITLRESGLDFTLVSVDLAKkrlenGD----DYLAINPKGQVPALLlDDGTLLTEGVAIMQYLAD 75


                 ....*....
1E6B_A        83 KYPEPPLLP 91
Cdd:PRK10542  76 SVPDRQLLA 84
PLN02378 PLN02378
glutathione S-transferase DHAR1
 20-89 5.85e-06

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 45.47  E-value: 5.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        20 AHRVRIALALKGLDYEYIPVNLLKGDQfdsDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPPL 89
Cdd:PLN02378  23 SQRALLTLEEKSLTYKIHLINLSDKPQ---WFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEKYPDPPL 89
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 114-203 4.19e-05

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 41.39  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        114 HQNLAVIRYIE-EKINVEEKTAWVNNAITKGFTALEKLLVNCAGKHATGDEIYLADLFLAPQIHGAINRFQIN-MEPYPT 191
Cdd:pfam14497   4 HHPIASSLYYEdEKKKAKRRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPDaLDKYPK 83

                          90
                  ....*....|..
1E6B_A        192 LAKCYESYNELP 203
Cdd:pfam14497  84 LKALHERVAARP 95
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 9-80 6.44e-05

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: 39.93  E-value: 6.44e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEyIPVNLLKGDQFDSDFKKINPMGTVPALVDGD-VVINDSFAIIMYL 80
Cdd:cd03044   1 GTLYTYPGNPRSLKILAAAKYNGLDVE-IVDFQPGKENKTPEFLKKFPLGKVPAFEGADgFCLFESNAIAYYV 72
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 9-84 7.39e-05

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: 40.03  E-value: 7.39e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1E6B_A        9 LKLYSYWRSSCAHRVRIALALKGLDYEYIPVNllKGDQFDSDFKKINPMGTVPALVDGD--VVINDSFAIIMYLDEKY 84
Cdd:cd03041   2 LELYEFEGSPFCRLVREVLTELELDVILYPCP--KGSPKRDKFLEKGGKVQVPYLVDPNtgVQMFESADIVKYLFKTY 77
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 11-79 5.68e-04

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: 37.34  E-value: 5.68e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A       11 LYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGdqfDSDFKKINPMGTVPALV-DGDVVINDSFAIIMY 79
Cdd:cd03060   3 LYSFRRCPYAMRARMALLLAGITVELREVELKNK---PAEMLAASPKGTVPVLVlGNGTVIEESLDIMRW 69
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 23-83 7.04e-04

GST_N family, Class Pi 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 Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumours.


Pssm-ID: 239374 [Multi-domain]  Cd Length: 73  Bit Score: 36.91  E-value: 7.04e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1E6B_A       23 VRIALALKGLDYEYIPVNLlkgDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEK 83
Cdd:cd03076  16 IRLLLADQGISWEEERVTY---EEWQESLKPKMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 117-197 9.39e-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: 37.60  E-value: 9.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A      117 LAVIRYIEEKINVEEKTAWV-NNAITKGFTALEKLLVNCAGKHATGDEIYLADLFLAPQIHGAINRFQINM-EPYPTLAK 194
Cdd:cd03192  20 FAPYFYEPDGEEKKEKKKEFlEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLALFDVLDYLLYLLPKDLlEKYPKLKA 99


                ...
1E6B_A      195 CYE 197
Cdd:cd03192 100 LRE 102
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 7-213 3.16e-03

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 37.27  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A         7 EKLKLYSYWRSSCAHRVRIALALKGLDY--EYIPVNllkGDQFDS--DFKK--INPMGTVPALVDGDVVINDSFAIIMYL 80
Cdd:PTZ00057   3 EEIVLYYFDARGKAELIRLIFAYLGIEYtdKRFGEN---GDAFIEfkNFKKekDTPFEQVPILEMDNIIFAQSQAIVRYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1E6B_A        81 DEKYpeppllpRDLHKRAVNYQAMSIVLSGIQPhqnlavIRYIEEKINV--EEKTAWVNNAITKGFTALEKLLVNCAGKH 158
Cdd:PTZ00057  80 SKKY-------KICGESELNEFYADMIFCGVQD------IHYKFNNTNLfkQNETTFLNEELPKWSGYFENILKKNHCNY 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
1E6B_A       159 ATGDEIYLADLFLAPQIHGAINRFQINMEPYPTLAKCYESYNELPAFQNALPEKQ 213
Cdd:PTZ00057 147 FVGDNLTYADLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYISNRK 201
 
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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