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Conserved domains on  [gi|530362451|ref|XP_005270839|]
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glutathione S-transferase Mu 1 isoform X1 [Homo sapiens]

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 ...
 58-178 3.17e-74

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: 218.66  E-value: 3.17e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  58 EEKIRVDILENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFE 137
Cdd:cd03209    1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530362451 138 PKCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFSKM 178
Cdd:cd03209   81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 1-50 1.16e-30

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: 106.70  E-value: 1.16e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530362451   1 MGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKH 50
Cdd:cd03075   33 LGDAPDYDRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIARKH 82
 
Name Accession Description Interval E-value
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 58-178 3.17e-74

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: 218.66  E-value: 3.17e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  58 EEKIRVDILENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFE 137
Cdd:cd03209    1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530362451 138 PKCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFSKM 178
Cdd:cd03209   81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 1-50 1.16e-30

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: 106.70  E-value: 1.16e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530362451   1 MGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKH 50
Cdd:cd03075   33 LGDAPDYDRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIARKH 82
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 71-158 1.30e-20

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: 81.56  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451   71 MDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEF---LGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCL-DAFPN 146
Cdd:pfam00043   2 MDLRMQIALLPYVPPEEKKEPEVDEALEKVARVLSALeevLKGQTYLVGDKLTLADIALAPALLWLYELDPACLrEKFPN 81

                          90
                  ....*....|..
gi 530362451  147 LKDFISRFEGLE 158
Cdd:pfam00043  82 LKAWFERVAARP 93
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
27-155 1.45e-15

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 71.08  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  27 PYLIDGAHKITQSNAILCYIARKH---NLCGETEEEKIRVDILE---NQTMDNHMQLGMICYNPE-FEKLKPKYLEELPE 99
Cdd:COG0625   54 PVLVDDGLVLTESLAILEYLAERYpepPLLPADPAARARVRQWLawaDGDLHPALRNLLERLAPEkDPAAIARARAELAR 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530362451 100 KLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKcLDAFPNLKDFISRFE 155
Cdd:COG0625  134 LLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLGLD-LADYPNLAAWLARLA 188
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 23-169 1.42e-07

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 49.60  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  23 FPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYnpeFEKLKPKYL-EELPEKL 101
Cdd:PTZ00057  56 FEQVPILEMDNIIFAQSQAIVRYLSKKYKICGESELNEFYADMIFCGVQDIHYKFNNTNL---FKQNETTFLnEELPKWS 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530362451 102 KLYSEFLGKR--PWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPNLK---DFISRFEGLEKISAYMKSSRF 169
Cdd:PTZ00057 133 GYFENILKKNhcNYFVGDNLTYADLAVFNLYDDIETKYPNSLKNFPLLKahnEFISNLPNIKNYISNRKESVY 205
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 1-48 7.00e-07

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: 44.99  E-value: 7.00e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530362451    1 MGDAPDYDrSQWLNEKFklgldFPNLPYLIDGAHKITQSNAILCYIAR 48
Cdd:pfam02798  35 FGAGPEKS-PELLKLNP-----LGKVPALEDGGKKLTESRAILEYIAR 76
 
Name Accession Description Interval E-value
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 58-178 3.17e-74

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: 218.66  E-value: 3.17e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  58 EEKIRVDILENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFE 137
Cdd:cd03209    1 KERIRVDMLEQQAMDLRMGLIRICYSPDFEKLKPDYLEKLPDKLKLFSEFLGDRPWFAGDKITYVDFLLYEALDQHRIFE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530362451 138 PKCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFSKM 178
Cdd:cd03209   81 PDCLDAFPNLKDFLERFEALPKISAYMKSDRFIKWPINGWK 121
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 1-50 1.16e-30

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: 106.70  E-value: 1.16e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530362451   1 MGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKH 50
Cdd:cd03075   33 LGDAPDYDRSQWLNEKFKLGLDFPNLPYYIDGDVKLTQSNAILRYIARKH 82
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 71-158 1.30e-20

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: 81.56  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451   71 MDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEF---LGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCL-DAFPN 146
Cdd:pfam00043   2 MDLRMQIALLPYVPPEEKKEPEVDEALEKVARVLSALeevLKGQTYLVGDKLTLADIALAPALLWLYELDPACLrEKFPN 81

                          90
                  ....*....|..
gi 530362451  147 LKDFISRFEGLE 158
Cdd:pfam00043  82 LKAWFERVAARP 93
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 58-154 7.54e-20

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: 79.97  E-value: 7.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  58 EEKIRVDILENQTMDNHMQLGMICYNPE----FEKLKPKYLEELPEKLKLYSEFLGK--RPWFAGNKITFVDFLVYDVLD 131
Cdd:cd03192    1 EEEARVDAIVDTIADLRAEFAPYFYEPDgeekKEKKKEFLEEALPKFLGKFEKILKKsgGGYFVGDKLTWADLALFDVLD 80

                         90       100
                 ....*....|....*....|....
gi 530362451 132 LHRIFEPKC-LDAFPNLKDFISRF 154
Cdd:cd03192   81 YLLYLLPKDlLEKYPKLKALRERV 104
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 71-166 1.08e-19

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 79.52  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451   71 MDNHMQLGMICY---NPEFEKLKPKYLEE-LPEKLKLYSEFL--GKRPWFAGNKITFVDFLVYDVLD-LHRIFEPKCLDA 143
Cdd:pfam14497   1 HDLHHPIASSLYyedEKKKAKRRKEFREErLPKFLGYFEKVLnkNGGGYLVGDKLTYADLALFQVLDgLLYPKAPDALDK 80

                          90       100
                  ....*....|....*....|...
gi 530362451  144 FPNLKDFISRFEGLEKISAYMKS 166
Cdd:pfam14497  81 YPKLKALHERVAARPNIKAYLAS 103
GST_C_Pi cd03210
C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione ...
 57-174 2.23e-18

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: 76.59  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  57 EEEKIRVDILENQTMDNHMQLGMICYnPEFEKLKPKYLEELPEKLKLYSEFL---GKRPWFAGNKITFVDFLVYDVLDLH 133
Cdd:cd03210    1 EKEAALIDMVNDGVEDLRLKYVRMIY-QNYEAGKDDYIKDLPEQLKPFEKLLaknNGKGFIVGDKISFADYNLFDLLDIH 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530362451 134 RIFEPKCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPV 174
Cdd:cd03210   80 LVLAPGCLDAFPLLKAFVERLSARPKLKAYLESDAFKNRPI 120
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
27-155 1.45e-15

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 71.08  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  27 PYLIDGAHKITQSNAILCYIARKH---NLCGETEEEKIRVDILE---NQTMDNHMQLGMICYNPE-FEKLKPKYLEELPE 99
Cdd:COG0625   54 PVLVDDGLVLTESLAILEYLAERYpepPLLPADPAARARVRQWLawaDGDLHPALRNLLERLAPEkDPAAIARARAELAR 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530362451 100 KLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKcLDAFPNLKDFISRFE 155
Cdd:COG0625  134 LLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLGLD-LADYPNLAAWLARLA 188
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 7-48 1.85e-12

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: 59.48  E-value: 1.85e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530362451   7 YDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIAR 48
Cdd:cd03039   31 ITYEEWPELDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLAR 72
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 84-153 1.67e-08

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


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 50.19  E-value: 1.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530362451  84 PEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKC--LDAFPNLKDFISR 153
Cdd:cd00299   28 PKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGPYYdlLDEYPRLKAWYDR 99
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 23-169 1.42e-07

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 49.60  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  23 FPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYnpeFEKLKPKYL-EELPEKL 101
Cdd:PTZ00057  56 FEQVPILEMDNIIFAQSQAIVRYLSKKYKICGESELNEFYADMIFCGVQDIHYKFNNTNL---FKQNETTFLnEELPKWS 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530362451 102 KLYSEFLGKR--PWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPNLK---DFISRFEGLEKISAYMKSSRF 169
Cdd:PTZ00057 133 GYFENILKKNhcNYFVGDNLTYADLAVFNLYDDIETKYPNSLKNFPLLKahnEFISNLPNIKNYISNRKESVY 205
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 1-48 7.00e-07

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: 44.99  E-value: 7.00e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530362451    1 MGDAPDYDrSQWLNEKFklgldFPNLPYLIDGAHKITQSNAILCYIAR 48
Cdd:pfam02798  35 FGAGPEKS-PELLKLNP-----LGKVPALEDGGKKLTESRAILEYIAR 76
PLN02395 PLN02395
glutathione S-transferase
 23-144 2.31e-05

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 43.31  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  23 FPNLPYLIDGAHKITQSNAILCYIARKH-----NLCGETEEEKIRVD-ILENQTMDNHMQLGMICYN---------PEFE 87
Cdd:PLN02395  50 FGVVPVIVDGDYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQVEqWLDVEATSYHPPLLNLTLHilfaskmgfPADE 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530362451  88 KLKPKYLEELPEKLKLYSEFLGKRPWFAGN--------KITFVDFLVYDVLDLHRIFEPKCLDAF 144
Cdd:PLN02395 130 KVIKESEEKLAKVLDVYEARLSKSKYLAGDfvsladlaHLPFTEYLVGPIGKAYLIKDRKHVSAW 194
GST_C_Sigma cd10295
C-terminal, alpha helical domain of Class Sigma Glutathione S-transferases; Glutathione ...
 57-147 6.43e-05

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


Pssm-ID: 198328 [Multi-domain]  Cd Length: 100  Bit Score: 40.17  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  57 EEEKIRVDILENqTMDNHMQLgMICYNPEFEKLKPKYLEEL----PEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDL 132
Cdd:cd10295    1 ELEQCLVDALVD-TLDDFMSC-FPWAEKKQDVKEKMFNEALtgpaPHLLKDLDTYLGGREWLVGKSVTWADFYWDTCSTT 78

                         90
                 ....*....|....*
gi 530362451 133 HRIFEPKCLDAFPNL 147
Cdd:cd10295   79 LLSFKPDLLKNYPRL 93
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 6-47 1.16e-04

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: 38.71  E-value: 1.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530362451   6 DYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIA 47
Cdd:cd00570   30 PVDLGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 94-153 1.94e-04

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 39.61  E-value: 1.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530362451  94 LEELPEKLKLYSEFLGKR--PWFAGNKITFVDFLVY------DVLDLHRIFEPkCLDAFPNLKDFISR 153
Cdd:cd03184   34 KEELRSALENLEEELAKRgtPFFGGNSPGMVDYMIWpwferlEALKLLDGYEL-CLDRFPKLKKWMAA 100
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 87-153 2.68e-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: 38.77  E-value: 2.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530362451  87 EKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFePKCLDAFPNLKDFISR 153
Cdd:cd03188   37 EEVKAAARERLERRLAYLDAQLAGGPYLLGDQFSVADAYLFVVLRWARAV-GLDLSDWPHLAAYLAR 102
GST_C_Metaxin cd03193
C-terminal, alpha helical domain of Metaxin and related proteins; Glutathione S-transferase ...
 93-154 5.57e-04

C-terminal, alpha helical domain of Metaxin and related proteins; Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken, and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities. Other members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system.


Pssm-ID: 198302 [Multi-domain]  Cd Length: 88  Bit Score: 37.22  E-value: 5.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  93 YLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVldLHRIFEPKC--------LDAFPNLKDFISRF 154
Cdd:cd03193   20 IYELALEDLEALSTLLGDKKFLFGDKPTSVDATVFAH--LASILYPPEdspllrvlVASSPNLVEYCERI 87
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 75-153 7.05e-04

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: 37.27  E-value: 7.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530362451  75 MQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFepKCLDAFPNLKDFISR 153
Cdd:cd03207   19 KALGRFFEPPWGEPAIAAAYGDLDERLAALEAALAGRPYLVGERFSAADLLLASVLRWARAF--GLLPEYPALRAYVAR 95
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 8-49 2.88e-03

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: 34.98  E-value: 2.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530362451   8 DRSQWLnEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARK 49
Cdd:cd03076   33 TYEEWQ-ESLKPKMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 87-165 4.14e-03

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: 35.65  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362451  87 EKLKpKYLEELPEKLK-LYSEFLGKRPWFAGNKITFVDFLVYdvldlHRIFEPKCLDafpnlkdfISRFEGLEKISAYMK 165
Cdd:cd03183   41 EKVK-KAEENLEESLDlLENKFLKDKPFLAGDEISIADLSAI-----CEIMQPEAAG--------YDVFEGRPKLAAWRK 106
GST_C_6 pfam17171
Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.
 105-153 9.64e-03

Glutathione S-transferase, C-terminal domain; This domain is closely related to PF00043.


Pssm-ID: 465369  Cd Length: 64  Bit Score: 33.28  E-value: 9.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530362451  105 SEFLGKRPWFAGNKITFVD--------FLVYDVLDLHRIFEpkCLDAFPNLKDFISR 153
Cdd:pfam17171   9 SERLGDKPFFFGDKPTSLDalvfghlaLILYTPLPSPALRI--HLKEYPNLVAYCER 63
 
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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