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Conserved domains on  [gi|50263046|ref|NP_032208|]
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glutathione S-transferase A2 [Mus musculus]

Protein Classification

glutathione S-transferase alpha( domain architecture ID 10122945)

class-alpha 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_Alpha cd03208
C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione ...
 86-220 6.31e-70

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


:

Pssm-ID: 198317 [Multi-domain]  Cd Length: 135  Bit Score: 209.88  E-value: 6.31e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046  86 MKERALIDMYTEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHLLELLL 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 50263046 166 YVEELDASLLTPFPLLKAFKSRISSLPNVKKFLHPGSQRKPPLDAKQIEEARKVF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 4-82 6.15e-53

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: 165.01  E-value: 6.15e-53
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50263046   4 KPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLVQTRAILNYIATKYDLY 82
Cdd:cd03077   1 KPVLHYFNGRGRMESIRWLLAAAGVEFEEKFIESAEDLEKLKKDGSLMFQQVPMVEIDGMKLVQTRAILNYIAGKYNLY 79
 
Name Accession Description Interval E-value
GST_C_Alpha cd03208
C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione ...
 86-220 6.31e-70

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 198317 [Multi-domain]  Cd Length: 135  Bit Score: 209.88  E-value: 6.31e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046  86 MKERALIDMYTEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHLLELLL 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 50263046 166 YVEELDASLLTPFPLLKAFKSRISSLPNVKKFLHPGSQRKPPLDAKQIEEARKVF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 4-82 6.15e-53

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: 165.01  E-value: 6.15e-53
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50263046   4 KPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLVQTRAILNYIATKYDLY 82
Cdd:cd03077   1 KPVLHYFNGRGRMESIRWLLAAAGVEFEEKFIESAEDLEKLKKDGSLMFQQVPMVEIDGMKLVQTRAILNYIAGKYNLY 79
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 1-198 6.29e-25

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 96.98  E-value: 6.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046    1 MAGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPED----LEKLKKDGNLMFDQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:PTZ00057   1 MAEEIVLYYFDARGKAELIRLIFAYLGIEYTDKRFGENGDafieFKNFKKEKDTPFEQVPILEMDNIIFAQSQAIVRYLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   77 TKYDLYGKDMKERALIDMYTEGILDLTEMIGQLVLCppdQREAKTALAKDRTKnrYLPAFEKVLKSHGQDYLVGNRLTRV 156
Cdd:PTZ00057  81 KKYKICGESELNEFYADMIFCGVQDIHYKFNNTNLF---KQNETTFLNEELPK--WSGYFENILKKNHCNYFVGDNLTYA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 50263046  157 DVHLLELLLYVEELDASLLTPFPLLKAFKSRISSLPNVKKFL 198
Cdd:PTZ00057 156 DLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYI 197
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 5-76 1.54e-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: 81.97  E-value: 1.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50263046     5 PVLHYFNARG--RMECIRWLLAAAGVEFEEKFIQS---PEDLEKLKKDGNLmfDQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:pfam02798   1 MVLTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFgagPEKSPELLKLNPL--GKVPALEDGGKKLTESRAILEYIA 75
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 101-198 9.90e-17

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 72.59  E-value: 9.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   101 DLTEMIGQLVLCPPDQREAK-TALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHL-LELLLYVEELDASLLTPF 178
Cdd:pfam14497   2 DLHHPIASSLYYEDEKKKAKrRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALfQVLDGLLYPKAPDALDKY 81

                          90       100
                  ....*....|....*....|
gi 50263046   179 PLLKAFKSRISSLPNVKKFL 198
Cdd:pfam14497  82 PKLKALHERVAARPNIKAYL 101
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
7-198 6.91e-15

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 70.31  E-value: 6.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   7 LHYFNARGRMECIRWLLAAAGVEFEEKFI------QSPEDLEKLkkdgNLMFdQVPMVEIDGMKLVQTRAILNYIATKYD 80
Cdd:COG0625   4 LYGSPPSPNSRRVRIALEEKGLPYELVPVdlakgeQKSPEFLAL----NPLG-KVPVLVDDGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046  81 ---LYGKDMKERALIDM---YTEGILDltEMIGQLV-LCPPDQREAKTALAKDRTKnRYLPAFEKVLKshGQDYLVGNRL 153
Cdd:COG0625  79 eppLLPADPAARARVRQwlaWADGDLH--PALRNLLeRLAPEKDPAAIARARAELA-RLLAVLEARLA--GGPYLAGDRF 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 50263046 154 TRVDVHLLELLLYVEELDASlLTPFPLLKAFKSRISSLPNVKKFL 198
Cdd:COG0625 154 SIADIALAPVLRRLDRLGLD-LADYPNLAAWLARLAARPAFQRAL 197
PLN02395 PLN02395
glutathione S-transferase
 23-133 3.75e-04

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 40.23  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   23 LAAAGVEFEekfiQSPEDLEKLK-KDGNLM----FDQVPMVEIDGMKLVQTRAILNYIATKY-----DLYGKDMKERALI 92
Cdd:PLN02395  20 LIEKGVEFE----TVPVDLMKGEhKQPEYLalqpFGVVPVIVDGDYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQV 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50263046   93 DMYTE--------GILDLT--EMIGQLVLCPPDQR---EAKTALAK-------DRTKNRYL 133
Cdd:PLN02395  96 EQWLDveatsyhpPLLNLTlhILFASKMGFPADEKvikESEEKLAKvldvyeaRLSKSKYL 156
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
18-66 1.48e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 36.33  E-value: 1.48e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 50263046  18 CIR--WLLAAAGVEFEEKFI-QSPEDLEKLKKDGNLMfdQVPMVEIDGMKLV 66
Cdd:COG0695  13 CARakRLLDEKGIPYEEIDVdEDPEAREELRERSGRR--TVPVIFIGGEHLG 62
 
Name Accession Description Interval E-value
GST_C_Alpha cd03208
C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione ...
 86-220 6.31e-70

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 198317 [Multi-domain]  Cd Length: 135  Bit Score: 209.88  E-value: 6.31e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046  86 MKERALIDMYTEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHLLELLL 165
Cdd:cd03208   1 LKERALIDMYVEGTADLMEMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQLLEAIL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 50263046 166 YVEELDASLLTPFPLLKAFKSRISSLPNVKKFLHPGSQRKPPLDAKQIEEARKVF 220
Cdd:cd03208  81 MVEELDPSILSDFPLLQAFKTRISNIPTIKKFLQPGSKRKPPPDEKYVETVRKVF 135
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 4-82 6.15e-53

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: 165.01  E-value: 6.15e-53
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50263046   4 KPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLVQTRAILNYIATKYDLY 82
Cdd:cd03077   1 KPVLHYFNGRGRMESIRWLLAAAGVEFEEKFIESAEDLEKLKKDGSLMFQQVPMVEIDGMKLVQTRAILNYIAGKYNLY 79
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 5-76 4.89e-29

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: 103.78  E-value: 4.89e-29
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50263046   5 PVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKdGNLMFDQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPELDLK-PTLPFGQLPVLEIDGKKLTQSNAILRYLA 71
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 1-198 6.29e-25

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 96.98  E-value: 6.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046    1 MAGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPED----LEKLKKDGNLMFDQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:PTZ00057   1 MAEEIVLYYFDARGKAELIRLIFAYLGIEYTDKRFGENGDafieFKNFKKEKDTPFEQVPILEMDNIIFAQSQAIVRYLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   77 TKYDLYGKDMKERALIDMYTEGILDLTEMIGQLVLCppdQREAKTALAKDRTKnrYLPAFEKVLKSHGQDYLVGNRLTRV 156
Cdd:PTZ00057  81 KKYKICGESELNEFYADMIFCGVQDIHYKFNNTNLF---KQNETTFLNEELPK--WSGYFENILKKNHCNYFVGDNLTYA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 50263046  157 DVHLLELLLYVEELDASLLTPFPLLKAFKSRISSLPNVKKFL 198
Cdd:PTZ00057 156 DLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYI 197
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 5-76 1.54e-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: 81.97  E-value: 1.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50263046     5 PVLHYFNARG--RMECIRWLLAAAGVEFEEKFIQS---PEDLEKLKKDGNLmfDQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:pfam02798   1 MVLTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFgagPEKSPELLKLNPL--GKVPALEDGGKKLTESRAILEYIA 75
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 101-198 9.90e-17

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 72.59  E-value: 9.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   101 DLTEMIGQLVLCPPDQREAK-TALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHL-LELLLYVEELDASLLTPF 178
Cdd:pfam14497   2 DLHHPIASSLYYEDEKKKAKrRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALfQVLDGLLYPKAPDALDKY 81

                          90       100
                  ....*....|....*....|
gi 50263046   179 PLLKAFKSRISSLPNVKKFL 198
Cdd:pfam14497  82 PKLKALHERVAARPNIKAYL 101
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 99-192 5.03e-15

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: 67.70  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046    99 ILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKshGQDYLVGNRLTRVDVHLLELLLYVEELD-ASLLTP 177
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVDEALEKVARVLSALEEVLK--GQTYLVGDKLTLADIALAPALLWLYELDpACLREK 78

                          90
                  ....*....|....*
gi 50263046   178 FPLLKAFKSRISSLP 192
Cdd:pfam00043  79 FPNLKAWFERVAARP 93
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
7-198 6.91e-15

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 70.31  E-value: 6.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   7 LHYFNARGRMECIRWLLAAAGVEFEEKFI------QSPEDLEKLkkdgNLMFdQVPMVEIDGMKLVQTRAILNYIATKYD 80
Cdd:COG0625   4 LYGSPPSPNSRRVRIALEEKGLPYELVPVdlakgeQKSPEFLAL----NPLG-KVPVLVDDGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046  81 ---LYGKDMKERALIDM---YTEGILDltEMIGQLV-LCPPDQREAKTALAKDRTKnRYLPAFEKVLKshGQDYLVGNRL 153
Cdd:COG0625  79 eppLLPADPAARARVRQwlaWADGDLH--PALRNLLeRLAPEKDPAAIARARAELA-RLLAVLEARLA--GGPYLAGDRF 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 50263046 154 TRVDVHLLELLLYVEELDASlLTPFPLLKAFKSRISSLPNVKKFL 198
Cdd:COG0625 154 SIADIALAPVLRRLDRLGLD-LADYPNLAAWLARLAARPAFQRAL 197
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 5-76 4.84e-14

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: 64.52  E-value: 4.84e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50263046   5 PVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLmFDQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 88-188 2.76e-12

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: 61.10  E-value: 2.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046  88 ERALIDMYTEGILDLTEMIGQLVLcPPDQREAKTALAKDR--TKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHLLELLL 165
Cdd:cd03192   2 EEARVDAIVDTIADLRAEFAPYFY-EPDGEEKKEKKKEFLeeALPKFLGKFEKILKKSGGGYFVGDKLTWADLALFDVLD 80

                        90       100
                ....*....|....*....|....
gi 50263046 166 YVEELDAS-LLTPFPLLKAFKSRI 188
Cdd:cd03192  81 YLLYLLPKdLLEKYPKLKALRERV 104
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 4-78 4.70e-12

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: 59.25  E-value: 4.70e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50263046   4 KPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKdgNLMFDQVPMVEIDGMKLVQTRAILNYIATK 78
Cdd:cd03076   1 PYTLTYFPVRGRAEAIRLLLADQGISWEEERVTYEEWQESLKP--KMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73
GST_C_Pi cd03210
C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione ...
 87-211 5.29e-11

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: 58.10  E-value: 5.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046  87 KERALIDMYTEGILDL----TEMIGQlvlcppDQREAKTALAKDrtknryLPA----FEKVLKSH-GQDYLVGNRLTRVD 157
Cdd:cd03210   2 KEAALIDMVNDGVEDLrlkyVRMIYQ------NYEAGKDDYIKD------LPEqlkpFEKLLAKNnGKGFIVGDKISFAD 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 50263046 158 VHLLELLLYVEELDASLLTPFPLLKAFKSRISSLPNVKKFLHPGSQRKPPLDAK 211
Cdd:cd03210  70 YNLFDLLDIHLVLAPGCLDAFPLLKAFVERLSARPKLKAYLESDAFKNRPINGN 123
PLN02473 PLN02473
glutathione S-transferase
 27-198 2.75e-08

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 52.30  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   27 GVEFEEKFIqspeDLEKL--KKDGNLM---FDQVPMVEIDGMKLVQTRAILNYIATKY-----DLYGKDMKERALIDMYT 96
Cdd:PLN02473  25 GIEFEVIHV----DLDKLeqKKPEHLLrqpFGQVPAIEDGDLKLFESRAIARYYATKYadqgtDLLGKTLEHRAIVDQWV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   97 EGILDLTEMIGQ-----LVLCPPDQREAKTALAKD-RTK-NRYLPAFEKVLKSHgqDYLVGNRLTRVDV-HLLELLLYVE 168
Cdd:PLN02473 101 EVENNYFYAVALplvinLVFKPRLGEPCDVALVEElKVKfDKVLDVYENRLATN--RYLGGDEFTLADLtHMPGMRYIMN 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50263046  169 ELDAS-LLTPFPLLKAFKSRISSLPNVKKFL 198
Cdd:PLN02473 179 ETSLSgLVTSRENLNRWWNEISARPAWKKLM 209
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 87-198 8.44e-07

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: 46.47  E-value: 8.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046  87 KERALIDMYTEGILDLteMIGQLVLC-PPDQREAKTALAKDRTKNryLPAFEKVLKSHgqDYLVGNRLTRVDVHLLELLL 165
Cdd:cd03209   1 KERIRVDMLEQQAMDL--RMGLIRICySPDFEKLKPDYLEKLPDK--LKLFSEFLGDR--PWFAGDKITYVDFLLYEALD 74

                        90       100       110
                ....*....|....*....|....*....|...
gi 50263046 166 YVEELDASLLTPFPLLKAFKSRISSLPNVKKFL 198
Cdd:cd03209  75 QHRIFEPDCLDAFPNLKDFLERFEALPKISAYM 107
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-79 1.93e-06

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: 44.30  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   5 PVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPE-----------DLEKLKKDgnlmFDQVPMVEIDGMKLVQTRAILN 73
Cdd:cd03075   1 PTLGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDapdydrsqwlnEKFKLGLD----FPNLPYYIDGDVKLTQSNAILR 76


                ....*.
gi 50263046  74 YIATKY 79
Cdd:cd03075  77 YIARKH 82
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 5-80 6.22e-05

GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 40.18  E-value: 6.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   5 PVLHYFNaRGRMECIRWLLAAAGVEFEEKFI------QSPEDLEKLKKDGnlmfdQVPMVEIDGMKLVQTRAILNYIATK 78
Cdd:cd03046   1 ITLYHLP-RSRSFRILWLLEELGLPYELVLYdrgpgeQAPPEYLAINPLG-----KVPVLVDGDLVLTESAAIILYLAEK 74


                ..
gi 50263046  79 YD 80
Cdd:cd03046  75 YG 76
PLN02395 PLN02395
glutathione S-transferase
 23-133 3.75e-04

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 40.23  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50263046   23 LAAAGVEFEekfiQSPEDLEKLK-KDGNLM----FDQVPMVEIDGMKLVQTRAILNYIATKY-----DLYGKDMKERALI 92
Cdd:PLN02395  20 LIEKGVEFE----TVPVDLMKGEhKQPEYLalqpFGVVPVIVDGDYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQV 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50263046   93 DMYTE--------GILDLT--EMIGQLVLCPPDQR---EAKTALAK-------DRTKNRYL 133
Cdd:PLN02395  96 EQWLDveatsyhpPLLNLTlhILFASKMGFPADEKvikESEEKLAKvldvyeaRLSKSKYL 156
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 19-76 8.02e-04

GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 36.78  E-value: 8.02e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50263046  19 IRWLLAAAGVEFEEKFI-------QSPEDLEKLKkdgnlmFDQVPMVEIDGMKLVQTRAILNYIA 76
Cdd:cd03056  15 VRLLLALLGIPYEWVEVdilkgetRTPEFLALNP------NGEVPVLELDGRVLAESNAILVYLA 73
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
18-66 1.48e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 36.33  E-value: 1.48e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 50263046  18 CIR--WLLAAAGVEFEEKFI-QSPEDLEKLKKDGNLMfdQVPMVEIDGMKLV 66
Cdd:COG0695  13 CARakRLLDEKGIPYEEIDVdEDPEAREELRERSGRR--TVPVIFIGGEHLG 62
AcetylCoA_hyd_C pfam13336
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
 55-93 2.99e-03

Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 433126 [Multi-domain]  Cd Length: 154  Bit Score: 37.03  E-value: 2.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 50263046    55 VPMVEiDGMKLVQTRAILNYIATKY---DLYGKDMKERA--LID 93
Cdd:pfam13336  98 VPMLS-PGAHVTTTRHDVDYVVTEYgiaDLRGKSLRERAeaLIS 140
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 23-78 3.51e-03

GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.


Pssm-ID: 239351 [Multi-domain]  Cd Length: 76  Bit Score: 35.32  E-value: 3.51e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50263046  23 LAAAGVEFEEKFI-------QSPEDLEKLKkdgnlmFDQVPMVEIDGMKLVQTRAILNYIATK 78
Cdd:cd03053  20 LEEKGVDYELVPVdltkgehKSPEHLARNP------FGQIPALEDGDLKLFESRAITRYLAEK 76
GST_C_Ure2p cd10293
C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione ...
 130-196 7.17e-03

C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Ure2p subfamily; composed of the Saccharomyces cerevisiae Ure2p and related fungal proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198326 [Multi-domain]  Cd Length: 117  Bit Score: 35.10  E-value: 7.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50263046 130 NRYLPAFEKVLKSHGQDYLVGNRLTRVDVH----LLELLLYVEELDASLLTPFPLLKAFKSRISSLPNVKK 196
Cdd:cd10293  46 RRVLGVLETALAERYRVWLVGDKFTIADLAfvpwNNVVDMIFIDPELDIKKEFPHVYKWLKRMLARPAVKK 116
 
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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