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Conserved domains on  [gi|232197|sp|P30112|]
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RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme 51; Short=GST51; AltName: Full=Fh51

Protein Classification

glutathione S-transferase mu( domain architecture ID 10221694)

class-mu 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 87-207 2.39e-67

C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1) thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


:

Pssm-ID: 198318 [Multi-domain]  Cd Length: 121  Bit Score: 202.48  E-value: 2.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    87 EERARISMIEGAAMDLRMGFVRVCYNPKFEEVKGDYLKELPTTLKMWSNFLGDRHYLTGSPVSHVDFMVYEALDCIRYLA 166
Cdd:cd03209   1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 232197   167 PQCLEDFPKLKEFKSRIEDLPKIKAYMESEKFIKWPLNSWI 207
Cdd:cd03209  81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 3-79 4.60e-32

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03075:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 82  Bit Score: 111.71  E-value: 4.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     3 AKLGYWKIRGLQQPVRLLLEYLGEEYEEHLYGRDD-----REKWFGDKFNMGLDLPNLPYYIDDKCKLTQSVAIMRYIAD 77
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDapdydRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIAR 80


                ..
gi 232197    78 KH 79
Cdd:cd03075  81 KH 82
 
Name Accession Description Interval E-value
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 87-207 2.39e-67

C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1) thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


Pssm-ID: 198318 [Multi-domain]  Cd Length: 121  Bit Score: 202.48  E-value: 2.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    87 EERARISMIEGAAMDLRMGFVRVCYNPKFEEVKGDYLKELPTTLKMWSNFLGDRHYLTGSPVSHVDFMVYEALDCIRYLA 166
Cdd:cd03209   1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 232197   167 PQCLEDFPKLKEFKSRIEDLPKIKAYMESEKFIKWPLNSWI 207
Cdd:cd03209  81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-79 4.60e-32

GST_N family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1), thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


Pssm-ID: 239373 [Multi-domain]  Cd Length: 82  Bit Score: 111.71  E-value: 4.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     3 AKLGYWKIRGLQQPVRLLLEYLGEEYEEHLYGRDD-----REKWFGDKFNMGLDLPNLPYYIDDKCKLTQSVAIMRYIAD 77
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDapdydRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIAR 80


                ..
gi 232197    78 KH 79
Cdd:cd03075  81 KH 82
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 100-196 3.20e-22

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 86.84  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     100 MDLRMGFVRVCY---NPKFEEVKGDYLKE-LPTTLKMWSNFL--GDRHYLTGSPVSHVDFMVYEALDCIRY-LAPQCLED 172
Cdd:pfam14497   1 HDLHHPIASSLYyedEKKKAKRRKEFREErLPKFLGYFEKVLnkNGGGYLVGDKLTYADLALFQVLDGLLYpKAPDALDK 80

                          90       100
                  ....*....|....*....|....
gi 232197     173 FPKLKEFKSRIEDLPKIKAYMESE 196
Cdd:pfam14497  81 YPKLKALHERVAARPNIKAYLASR 104
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
56-197 3.76e-17

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 76.47  E-value: 3.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    56 PYYIDDKCKLTQSVAIMRYIADKHG---MLGTTPEERARISMIEGAAMDLRMGFVRVCYN----PKFEEVKGDYLKELPT 128
Cdd:COG0625  54 PVLVDDGLVLTESLAILEYLAERYPeppLLPADPAARARVRQWLAWADGDLHPALRNLLErlapEKDPAAIARARAELAR 133

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 232197   129 TLKMWSNFLGDRHYLTGSPVSHVDFMVYEALDCIRYLApQCLEDFPKLKEFKSRIEDLPKIKAYMESEK 197
Cdd:COG0625 134 LLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLG-LDLADYPNLAAWLARLAARPAFQRALAAAE 201
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 65-197 1.43e-08

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 53.06  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     65 LTQSVAIMRYIADKHGMLGTTPEERARISMIEGAAMDLRMGFVRVCYnpkFEEVKGDYLKE-LPTTLKMWSNFLGDRH-- 141
Cdd:PTZ00057  69 FAQSQAIVRYLSKKYKICGESELNEFYADMIFCGVQDIHYKFNNTNL---FKQNETTFLNEeLPKWSGYFENILKKNHcn 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 232197    142 YLTGSPVSHVDFMVYEALDCIRYLAPQCLEDFPKLKEFKSRIEDLPKIKAYMESEK 197
Cdd:PTZ00057 146 YFVGDNLTYADLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYISNRK 201
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 33-77 2.23e-04

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: 38.44  E-value: 2.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 232197      33 YGRDDREKWFGDKFnmgldLPNLPYYIDDKCKLTQSVAIMRYIAD 77
Cdd:pfam02798  37 AGPEKSPELLKLNP-----LGKVPALEDGGKKLTESRAILEYIAR 76
 
Name Accession Description Interval E-value
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 87-207 2.39e-67

C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1) thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


Pssm-ID: 198318 [Multi-domain]  Cd Length: 121  Bit Score: 202.48  E-value: 2.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    87 EERARISMIEGAAMDLRMGFVRVCYNPKFEEVKGDYLKELPTTLKMWSNFLGDRHYLTGSPVSHVDFMVYEALDCIRYLA 166
Cdd:cd03209   1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 232197   167 PQCLEDFPKLKEFKSRIEDLPKIKAYMESEKFIKWPLNSWI 207
Cdd:cd03209  81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-79 4.60e-32

GST_N family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1), thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


Pssm-ID: 239373 [Multi-domain]  Cd Length: 82  Bit Score: 111.71  E-value: 4.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     3 AKLGYWKIRGLQQPVRLLLEYLGEEYEEHLYGRDD-----REKWFGDKFNMGLDLPNLPYYIDDKCKLTQSVAIMRYIAD 77
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDapdydRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIAR 80


                ..
gi 232197    78 KH 79
Cdd:cd03075  81 KH 82
GST_C_Pi cd03210
C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione ...
 86-204 1.74e-25

C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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 tumors.


Pssm-ID: 198319 [Multi-domain]  Cd Length: 126  Bit Score: 96.23  E-value: 1.74e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    86 PEERARISMIEGAAMDLRMGFVRVCYnPKFEEVKGDYLKELPTTLKMWSNFL---GDRHYLTGSPVSHVDFMVYEALDCI 162
Cdd:cd03210   1 EKEAALIDMVNDGVEDLRLKYVRMIY-QNYEAGKDDYIKDLPEQLKPFEKLLaknNGKGFIVGDKISFADYNLFDLLDIH 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 232197   163 RYLAPQCLEDFPKLKEFKSRIEDLPKIKAYMESEKFIKWPLN 204
Cdd:cd03210  80 LVLAPGCLDAFPLLKAFVERLSARPKLKAYLESDAFKNRPIN 121
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 100-196 3.20e-22

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 86.84  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     100 MDLRMGFVRVCY---NPKFEEVKGDYLKE-LPTTLKMWSNFL--GDRHYLTGSPVSHVDFMVYEALDCIRY-LAPQCLED 172
Cdd:pfam14497   1 HDLHHPIASSLYyedEKKKAKRRKEFREErLPKFLGYFEKVLnkNGGGYLVGDKLTYADLALFQVLDGLLYpKAPDALDK 80

                          90       100
                  ....*....|....*....|....
gi 232197     173 FPKLKEFKSRIEDLPKIKAYMESE 196
Cdd:pfam14497  81 YPKLKALHERVAARPNIKAYLASR 104
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
56-197 3.76e-17

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 76.47  E-value: 3.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    56 PYYIDDKCKLTQSVAIMRYIADKHG---MLGTTPEERARISMIEGAAMDLRMGFVRVCYN----PKFEEVKGDYLKELPT 128
Cdd:COG0625  54 PVLVDDGLVLTESLAILEYLAERYPeppLLPADPAARARVRQWLAWADGDLHPALRNLLErlapEKDPAAIARARAELAR 133

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 232197   129 TLKMWSNFLGDRHYLTGSPVSHVDFMVYEALDCIRYLApQCLEDFPKLKEFKSRIEDLPKIKAYMESEK 197
Cdd:COG0625 134 LLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLG-LDLADYPNLAAWLARLAARPAFQRALAAAE 201
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 87-183 1.41e-15

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: 69.57  E-value: 1.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    87 EERARISMIEGAAMDLRMGFVRVCYNP----KFEEVKGDYLKELPTTLKMWSNFLGDRH--YLTGSPVSHVDFMVYEALD 160
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYFYEPdgeeKKEKKKEFLEEALPKFLGKFEKILKKSGggYFVGDKLTWADLALFDVLD 80

                        90       100
                ....*....|....*....|....
gi 232197   161 CIRYLAPQC-LEDFPKLKEFKSRI 183
Cdd:cd03192  81 YLLYLLPKDlLEKYPKLKALRERV 104
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 4-77 7.30e-13

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: 61.41  E-value: 7.30e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 232197     4 KLGYWKIRGLQQPVRLLLEYLGEEYEEHLYGRDDrekWFGDKFNMGLDLPNLPYYIDDKCKLTQSVAIMRYIAD 77
Cdd:cd03039   2 KLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEE---WPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLAR 72
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 100-187 1.92e-10

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 55.75  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     100 MDLRMGFVRVCYNPKFEEVKGDYLKELPTTLKMWSNF---LGDRHYLTGSPVSHVDFMVYEALDCIRYLAPQCL-EDFPK 175
Cdd:pfam00043   2 MDLRMQIALLPYVPPEEKKEPEVDEALEKVARVLSALeevLKGQTYLVGDKLTLADIALAPALLWLYELDPACLrEKFPN 81

                          90
                  ....*....|..
gi 232197     176 LKEFKSRIEDLP 187
Cdd:pfam00043  82 LKAWFERVAARP 93
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 65-197 1.43e-08

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 53.06  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     65 LTQSVAIMRYIADKHGMLGTTPEERARISMIEGAAMDLRMGFVRVCYnpkFEEVKGDYLKE-LPTTLKMWSNFLGDRH-- 141
Cdd:PTZ00057  69 FAQSQAIVRYLSKKYKICGESELNEFYADMIFCGVQDIHYKFNNTNL---FKQNETTFLNEeLPKWSGYFENILKKNHcn 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 232197    142 YLTGSPVSHVDFMVYEALDCIRYLAPQCLEDFPKLKEFKSRIEDLPKIKAYMESEK 197
Cdd:PTZ00057 146 YFVGDNLTYADLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYISNRK 201
GST_C_Alpha cd03208
C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione ...
 86-194 3.10e-08

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha 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 class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 198317 [Multi-domain]  Cd Length: 135  Bit Score: 50.79  E-value: 3.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    86 PEERARISMIEGAAMDL-RMGFVRVCYNPKFEEVKGDYLKELPTT--LKMWSNFLGD--RHYLTGSPVSHVDFMVYEALD 160
Cdd:cd03208   1 LKERALIDMYVEGTADLmEMIMMLPFLPPEEKEAKLALIKEKAKNryFPVFEKVLKDhgQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 232197   161 CIRYLAPQCLEDFPKLKEFKSRIEDLPKIKAYME 194
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQ 114
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 88-199 3.42e-06

C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is the subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from the aryl or alkyl sulfate esters.


Pssm-ID: 198292 [Multi-domain]  Cd Length: 126  Bit Score: 44.90  E-value: 3.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197    88 ERARISM-IEGAAMDLRMG----FVRVCYNPKF-------EEVKgDYLKELPTTLKMWSN-FLGDRHYLTGSPVSHVDFM 154
Cdd:cd03183   1 KRARVDEyLAWQHTNLRLGcaayFWQKVLLPLFggtpvspEKVK-KAEENLEESLDLLENkFLKDKPFLAGDEISIADLS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 232197   155 VYEALDCIRYLAPQCLEDFPKLKEFKSRIEDLPKiKAYMESEKFI 199
Cdd:cd03183  80 AICEIMQPEAAGYDVFEGRPKLAAWRKRVKEAGN-PLFDEAHKVI 123
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 103-183 1.59e-05

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 42.49  E-value: 1.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197   103 RMGFVRVCYNPKFEEVKGDYLKELPTTLKMWSNFLGDRHYLTGSPVSHVDFMVYEALDCIRYLAPQC--LEDFPKLKEFK 180
Cdd:cd00299  18 RLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPYYdlLDEYPRLKAWY 97


                ...
gi 232197   181 SRI 183
Cdd:cd00299  98 DRL 100
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 33-77 2.23e-04

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: 38.44  E-value: 2.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 232197      33 YGRDDREKWFGDKFnmgldLPNLPYYIDDKCKLTQSVAIMRYIAD 77
Cdd:pfam02798  37 AGPEKSPELLKLNP-----LGKVPALEDGGKKLTESRAILEYIAR 76
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 59-199 3.14e-03

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 37.35  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     59 IDDKCKLTQSVAIMRYIADK--HGMLGTTPEERARISMIEG---AAMDLRMGFVRVcYNPKF-EEVKGDYLKELPTTLKM 132
Cdd:PRK10542  57 LDDGTLLTEGVAIMQYLADSvpDRQLLAPVGSLSRYHTIEWlnyIATELHKGFTPL-FRPDTpEEYKPTVRAQLEKKFQY 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 232197    133 WSNFLGDRHYLTGSPVSHVDFMVYEALDCIRYLAPQcLEDFPKLKEFKSRIEDLPKIKAYMESEKFI 199
Cdd:PRK10542 136 VDEALADEQWICGQRFTIADAYLFTVLRWAYAVKLN-LEGLEHIAAYMQRVAERPAVAAALKAEGLK 201
PLN02395 PLN02395
glutathione S-transferase
 55-152 6.93e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 36.38  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232197     55 LPYYIDDKCKLTQSVAIMRYIADKH-----GMLGTTPEERARISM---IEGA-------AMDLRMGFVRVCYNPKFEEVK 119
Cdd:PLN02395  53 VPVIVDGDYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQVEQwldVEATsyhppllNLTLHILFASKMGFPADEKVI 132

                         90       100       110
                 ....*....|....*....|....*....|...
gi 232197    120 GDYLKELPTTLKMWSNFLGDRHYLTGSPVSHVD 152
Cdd:PLN02395 133 KESEEKLAKVLDVYEARLSKSKYLAGDFVSLAD 165
 
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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