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Conserved domains on  [gi|1346207|sp|P48774|]
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RecName: Full=Glutathione S-transferase Mu 5; AltName: Full=Fibrous sheath component 2; Short=Fsc2; AltName: Full=GST class-mu 5

Protein Classification

glutathione S-transferase mu( domain architecture ID 10122909)

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

CATH:  1.20.1050.10|3.40.30.10
EC:  2.5.1.18
Gene Ontology:  GO:0004364|GO:0043295|GO:0042178
PubMed:  15822171|15607001|11695986|15558583

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 ...
 95-215 6.25e-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: 201.71  E-value: 6.25e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   95 EEKIRVDIMENQIMDFRMQLVRLCYNSNHENLKPQYLEQLPAQLKQFSLFLGKFTWFAGEKLTFVDFLTYDVLDQNRIFE 174
Cdd:cd03209   1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 1346207  175 PKCLDEFPNLKAFMCRFEALEKIAAFLQSDRFFKMPINNKM 215
Cdd:cd03209  81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 6-87 8.97e-53

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: 164.48  E-value: 8.97e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    6 MVLGYWDIRGLAHAIRMLLEFTDTSYEEKRYICGEAPDYDRSQWLDVKFKLDLDFPNLPYLMDGKNKITQSNAILRYIAR 85
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDAPDYDRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIAR 80


                ..
gi 1346207   86 KH 87
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 ...
 95-215 6.25e-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: 201.71  E-value: 6.25e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   95 EEKIRVDIMENQIMDFRMQLVRLCYNSNHENLKPQYLEQLPAQLKQFSLFLGKFTWFAGEKLTFVDFLTYDVLDQNRIFE 174
Cdd:cd03209   1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 1346207  175 PKCLDEFPNLKAFMCRFEALEKIAAFLQSDRFFKMPINNKM 215
Cdd:cd03209  81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 6-87 8.97e-53

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: 164.48  E-value: 8.97e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    6 MVLGYWDIRGLAHAIRMLLEFTDTSYEEKRYICGEAPDYDRSQWLDVKFKLDLDFPNLPYLMDGKNKITQSNAILRYIAR 85
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDAPDYDRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIAR 80


                ..
gi 1346207   86 KH 87
Cdd:cd03075  81 KH 82
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 107-195 8.05e-23

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: 88.50  E-value: 8.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    107 IMDFRMQLVRLCYNSNHENLKPQYLEQLPAQLKQFSLFLGKF---TWFAGEKLTFVDFLTYDVLDQNRIFEPKCL-DEFP 182
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVDEALEKVARVLSALEEVLkgqTYLVGDKLTLADIALAPALLWLYELDPACLrEKFP 80

                          90
                  ....*....|...
gi 1346207    183 NLKAFMCRFEALE 195
Cdd:pfam00043  81 NLKAWFERVAARP 93
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 6-85 1.07e-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: 82.35  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207      6 MVLGYWDIRG--LAHAIRMLLEFTDTSYEEKRYICGEAPDYDrSQWLDVKFkldldFPNLPYLMDGKNKITQSNAILRYI 83
Cdd:pfam02798   1 MVLTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFGAGPEKS-PELLKLNP-----LGKVPALEDGGKKLTESRAILEYI 74


                  ..
gi 1346207     84 AR 85
Cdd:pfam02798  75 AR 76
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 3-186 2.77e-14

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 68.86  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207     3 SKSMVLGYWDIRGLAHAIRMLLEFTDTSYEEKRYicGEAPDyDRSQWLDVKFKLDLDFPNLPYLMDGKNKITQSNAILRY 82
Cdd:PTZ00057   2 AEEIVLYYFDARGKAELIRLIFAYLGIEYTDKRF--GENGD-AFIEFKNFKKEKDTPFEQVPILEMDNIIFAQSQAIVRY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    83 IARKHNMCGDTEEEKIRVDIMENQIMDFRmqlvrlcYNSNHENLKPQ----YL-EQLPAQLKQFSLFLGK--FTWFAGEK 155
Cdd:PTZ00057  79 LSKKYKICGESELNEFYADMIFCGVQDIH-------YKFNNTNLFKQnettFLnEELPKWSGYFENILKKnhCNYFVGDN 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 1346207   156 LTFVDFLTYDVLDQNRIFEPKCLDEFPNLKA 186
Cdd:PTZ00057 152 LTYADLAVFNLYDDIETKYPNSLKNFPLLKA 182
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
17-205 4.96e-13

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 65.30  E-value: 4.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   17 AHAIRMLLEFTDTSYEEKRYicGEAPDYDRSQWLdvkfkLDLDfPN--LPYLMDGKNKITQSNAILRYIARKH---NMCG 91
Cdd:COG0625  13 SRRVRIALEEKGLPYELVPV--DLAKGEQKSPEF-----LALN-PLgkVPVLVDDGLVLTESLAILEYLAERYpepPLLP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   92 DTEEEKIRV----DIMENQIMDFRMQLVRLCYNSNHENLKPQYLEQLPAQLKQFSLFLGKFTWFAGEKLTFVDFLTYDVL 167
Cdd:COG0625  85 ADPAARARVrqwlAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALAPVL 164

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 1346207  168 DQNRIFEPKcLDEFPNLKAFMCRFEALEKIAAFLQSDR 205
Cdd:COG0625 165 RRLDRLGLD-LADYPNLAAWLARLAARPAFQRALAAAE 201
 
Name Accession Description Interval E-value
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 95-215 6.25e-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: 201.71  E-value: 6.25e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   95 EEKIRVDIMENQIMDFRMQLVRLCYNSNHENLKPQYLEQLPAQLKQFSLFLGKFTWFAGEKLTFVDFLTYDVLDQNRIFE 174
Cdd:cd03209   1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 1346207  175 PKCLDEFPNLKAFMCRFEALEKIAAFLQSDRFFKMPINNKM 215
Cdd:cd03209  81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 6-87 8.97e-53

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: 164.48  E-value: 8.97e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    6 MVLGYWDIRGLAHAIRMLLEFTDTSYEEKRYICGEAPDYDRSQWLDVKFKLDLDFPNLPYLMDGKNKITQSNAILRYIAR 85
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDAPDYDRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIAR 80


                ..
gi 1346207   86 KH 87
Cdd:cd03075  81 KH 82
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 6-85 7.02e-28

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: 100.70  E-value: 7.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    6 MVLGYWDIRGLAHAIRMLLEFTDTSYEEKRYicgeapdyDRSQWLDVKFKLDLDFPNLPYLMDGKNKITQSNAILRYIAR 85
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRI--------TYEEWPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLAR 72
GST_C_Pi cd03210
C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione ...
 94-212 5.23e-23

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: 89.68  E-value: 5.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   94 EEEKIRVDIMENQIMDFRMQLVRLCYnSNHENLKPQYLEQLPAQLKQFSLFL---GKFTWFAGEKLTFVDFLTYDVLDQN 170
Cdd:cd03210   1 EKEAALIDMVNDGVEDLRLKYVRMIY-QNYEAGKDDYIKDLPEQLKPFEKLLaknNGKGFIVGDKISFADYNLFDLLDIH 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 1346207  171 RIFEPKCLDEFPNLKAFMCRFEALEKIAAFLQSDRFFKMPIN 212
Cdd:cd03210  80 LVLAPGCLDAFPLLKAFVERLSARPKLKAYLESDAFKNRPIN 121
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 107-195 8.05e-23

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: 88.50  E-value: 8.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    107 IMDFRMQLVRLCYNSNHENLKPQYLEQLPAQLKQFSLFLGKF---TWFAGEKLTFVDFLTYDVLDQNRIFEPKCL-DEFP 182
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVDEALEKVARVLSALEEVLkgqTYLVGDKLTLADIALAPALLWLYELDPACLrEKFP 80

                          90
                  ....*....|...
gi 1346207    183 NLKAFMCRFEALE 195
Cdd:pfam00043  81 NLKAWFERVAARP 93
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 6-85 1.07e-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: 82.35  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207      6 MVLGYWDIRG--LAHAIRMLLEFTDTSYEEKRYICGEAPDYDrSQWLDVKFkldldFPNLPYLMDGKNKITQSNAILRYI 83
Cdd:pfam02798   1 MVLTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFGAGPEKS-PELLKLNP-----LGKVPALEDGGKKLTESRAILEYI 74


                  ..
gi 1346207     84 AR 85
Cdd:pfam02798  75 AR 76
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 108-204 1.61e-18

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 77.60  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    108 MDFRMQLVRLCYNSNHENLKPQ----YLEQLPAQLKQFSLFL--GKFTWFAGEKLTFVDFLTYDVLDQNR-IFEPKCLDE 180
Cdd:pfam14497   1 HDLHHPIASSLYYEDEKKKAKRrkefREERLPKFLGYFEKVLnkNGGGYLVGDKLTYADLALFQVLDGLLyPKAPDALDK 80

                          90       100
                  ....*....|....*....|....
gi 1346207    181 FPNLKAFMCRFEALEKIAAFLQSD 204
Cdd:pfam14497  81 YPKLKALHERVAARPNIKAYLASR 104
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 95-187 7.81e-17

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: 73.04  E-value: 7.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   95 EEKIRVDIMENQIMDFRMQLVRLCYNSNHEN----LKPQYLEQLPAQLKQFSLFLGKFT--WFAGEKLTFVDFLTYDVLD 168
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYFYEPDGEEkkekKKEFLEEALPKFLGKFEKILKKSGggYFVGDKLTWADLALFDVLD 80

                        90       100
                ....*....|....*....|
gi 1346207  169 QNRIFEPKC-LDEFPNLKAF 187
Cdd:cd03192  81 YLLYLLPKDlLEKYPKLKAL 100
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 3-186 2.77e-14

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 68.86  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207     3 SKSMVLGYWDIRGLAHAIRMLLEFTDTSYEEKRYicGEAPDyDRSQWLDVKFKLDLDFPNLPYLMDGKNKITQSNAILRY 82
Cdd:PTZ00057   2 AEEIVLYYFDARGKAELIRLIFAYLGIEYTDKRF--GENGD-AFIEFKNFKKEKDTPFEQVPILEMDNIIFAQSQAIVRY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    83 IARKHNMCGDTEEEKIRVDIMENQIMDFRmqlvrlcYNSNHENLKPQ----YL-EQLPAQLKQFSLFLGK--FTWFAGEK 155
Cdd:PTZ00057  79 LSKKYKICGESELNEFYADMIFCGVQDIH-------YKFNNTNLFKQnettFLnEELPKWSGYFENILKKnhCNYFVGDN 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 1346207   156 LTFVDFLTYDVLDQNRIFEPKCLDEFPNLKA 186
Cdd:PTZ00057 152 LTYADLAVFNLYDDIETKYPNSLKNFPLLKA 182
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
17-205 4.96e-13

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 65.30  E-value: 4.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   17 AHAIRMLLEFTDTSYEEKRYicGEAPDYDRSQWLdvkfkLDLDfPN--LPYLMDGKNKITQSNAILRYIARKH---NMCG 91
Cdd:COG0625  13 SRRVRIALEEKGLPYELVPV--DLAKGEQKSPEF-----LALN-PLgkVPVLVDDGLVLTESLAILEYLAERYpepPLLP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207   92 DTEEEKIRV----DIMENQIMDFRMQLVRLCYNSNHENLKPQYLEQLPAQLKQFSLFLGKFTWFAGEKLTFVDFLTYDVL 167
Cdd:COG0625  85 ADPAARARVrqwlAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALAPVL 164

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 1346207  168 DQNRIFEPKcLDEFPNLKAFMCRFEALEKIAAFLQSDR 205
Cdd:COG0625 165 RRLDRLGLD-LADYPNLAAWLARLAARPAFQRALAAAE 201
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 6-84 6.00e-12

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: 59.12  E-value: 6.00e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1346207    6 MVLGYWDIRGLAHAIRMLLEFTDTSYEEKRYicgeapdyDRSQWLDVKFKLDLDFPNLPYLMDGKNKITQSNAILRYIA 84
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPV--------DLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-86 1.68e-11

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: 58.09  E-value: 1.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    7 VLGYWDIRGLAHAIRMLLEFTDTSYEEKRYicgeapdyDRSQWLDvKFKLDLDFPNLPYLMDGKNKITQSNAILRYIARK 86
Cdd:cd03076   3 TLTYFPVRGRAEAIRLLLADQGISWEEERV--------TYEEWQE-SLKPKMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 123-190 1.24e-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: 42.87  E-value: 1.24e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207  123 HENLKPQYLEQLPAQLKQFSLFLGKFTWFAGEKLTFVDFLTYDVLDQNRIFEPKC--LDEFPNLKAFMCR 190
Cdd:cd00299  30 DEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPYYdlLDEYPRLKAWYDR 99
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-89 7.84e-05

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Alpha subfamily is composed of eukaryotic 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: 239375  Cd Length: 79  Bit Score: 39.82  E-value: 7.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346207    7 VLGYWDIRGLAHAIRMLLEFTDTSYEEKryICGEAPDYDrsqwldvKFKLD--LDFPNLPYL-MDGKnKITQSNAILRYI 83
Cdd:cd03077   3 VLHYFNGRGRMESIRWLLAAAGVEFEEK--FIESAEDLE-------KLKKDgsLMFQQVPMVeIDGM-KLVQTRAILNYI 72


                ....*.
gi 1346207   84 ARKHNM 89
Cdd:cd03077  73 AGKYNL 78
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 123-201 2.75e-04

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 39.15  E-value: 2.75e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1346207  123 HENLKPQYLEQLPAQLKQFSLFLGKFTWFAGEKLTFVDFLTYDVLDQNRIFePKCLDEFPNLKAFMCRFEALEKIAAFL 201
Cdd:cd03188  36 AEEVKAAARERLERRLAYLDAQLAGGPYLLGDQFSVADAYLFVVLRWARAV-GLDLSDWPHLAAYLARVAARPAVQAAL 113
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 132-193 5.45e-03

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 35.35  E-value: 5.45e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346207  132 EQLPAQLKQFSLFLGKFTWFAGEKLTFVDFLTYDVLDQNRIFepKCLDEFPNLKAFMCRFEA 193
Cdd:cd03207  39 GDLDERLAALEAALAGRPYLVGERFSAADLLLASVLRWARAF--GLLPEYPALRAYVARCTA 98
 
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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