NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17533789|ref|NP_496864|]
View 

Glutathione S-Transferase [Caenorhabditis elegans]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 10122574)

glutathione S-transferase (GST) family protein may catalyze the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress

CATH:  1.20.1050.10|3.40.30.10
PubMed:  15822171|15607001|11695986|15558583
SCOP:  4000976|4000472

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 4-72 1.26e-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: 104.55  E-value: 1.26e-29
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533789   4 YKFTYFPFRGLGEPVRLLFHLADCPFKDERFSFEEW--GAVKSKSPMGQLPILGVDGLEIPQSAAILRYLA 72
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWpeLDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLA 71
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 83-189 1.37e-24

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: 92.69  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789  83 EDRAWVDAVVDRFKDFFVEFKKFLVAKRGGKSEEEVAKVVSESVvpamESYFKLLNGLLERSKSGFLIGNSITYADLVVV 162
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYFYEPDGEEKKEKKKEFLEEAL----PKFLGKFEKILKKSGGGYFVGDKLTWADLALF 76

                        90       100
                ....*....|....*....|....*...
gi 17533789 163 NNLETLRNFG-FLNASEQPKLTALLEKV 189
Cdd:cd03192  77 DVLDYLLYLLpKDLLEKYPKLKALRERV 104
 
Name Accession Description Interval E-value
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 4-72 1.26e-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: 104.55  E-value: 1.26e-29
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533789   4 YKFTYFPFRGLGEPVRLLFHLADCPFKDERFSFEEW--GAVKSKSPMGQLPILGVDGLEIPQSAAILRYLA 72
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWpeLDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLA 71
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 83-189 1.37e-24

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: 92.69  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789  83 EDRAWVDAVVDRFKDFFVEFKKFLVAKRGGKSEEEVAKVVSESVvpamESYFKLLNGLLERSKSGFLIGNSITYADLVVV 162
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYFYEPDGEEKKEKKKEFLEEAL----PKFLGKFEKILKKSGGGYFVGDKLTWADLALF 76

                        90       100
                ....*....|....*....|....*...
gi 17533789 163 NNLETLRNFG-FLNASEQPKLTALLEKV 189
Cdd:cd03192  77 DVLDYLLYLLpKDLLEKYPKLKALRERV 104
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 96-202 1.49e-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: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789    96 KDFFVEFKKFLVAKRGgKSEEEVAKVVSESVVPAmesYFKLLNGLLERSKSGFLIGNSITYADLVVVNNLETLRNFGFLN 175
Cdd:pfam14497   1 HDLHHPIASSLYYEDE-KKKAKRRKEFREERLPK---FLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPD 76

                          90       100
                  ....*....|....*....|....*...
gi 17533789   176 ASEQ-PKLTALLEKVYSQPGIKEYVSSR 202
Cdd:pfam14497  77 ALDKyPKLKALHERVAARPNIKAYLASR 104
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-197 1.91e-19

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 82.25  E-value: 1.91e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789   4 YKFTYFPFRGLGEPVRLLFHLADCPFKDERFSFEEWG----AVKSKSPMGQLPILGVDGLEIPQSAAILRYLALKFG--- 76
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEqkspEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPepp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789  77 FAGKTPEDRAWVDAVVDRF-KDFFVEFKKFLVAKRGGKSEEEVAKVVSEsvvpaMESYFKLLNGLLerSKSGFLIGNSIT 155
Cdd:COG0625  82 LLPADPAARARVRQWLAWAdGDLHPALRNLLERLAPEKDPAAIARARAE-----LARLLAVLEARL--AGGPYLAGDRFS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17533789 156 YADLVVVNNLETLRNFGFlNASEQPKLTALLEKVYSQPGIKE 197
Cdd:COG0625 155 IADIALAPVLRRLDRLGL-DLADYPNLAAWLARLAARPAFQR 195
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 8-205 1.55e-17

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 77.33  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789    8 YFPFRGLGEPVRLLFHLADCPFKDERF-----SFEEWGAVKSK--SPMGQLPILGVDGLEIPQSAAILRYLALKFGFAGK 80
Cdd:PTZ00057   9 YFDARGKAELIRLIFAYLGIEYTDKRFgengdAFIEFKNFKKEkdTPFEQVPILEMDNIIFAQSQAIVRYLSKKYKICGE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789   81 TPEDRAWVDAVVDRFKDFFVEFKKFLVAKrggksEEEVAKVVSEsvVPAMESYFKllnGLLERSKSGFLIGNSITYADLV 160
Cdd:PTZ00057  89 SELNEFYADMIFCGVQDIHYKFNNTNLFK-----QNETTFLNEE--LPKWSGYFE---NILKKNHCNYFVGDNLTYADLA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17533789  161 VVN---NLET-----LRNFgflnaseqPKLTALLEKVYSQPGIKEYVSSRTAS 205
Cdd:PTZ00057 159 VFNlydDIETkypnsLKNF--------PLLKAHNEFISNLPNIKNYISNRKES 203
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 6-72 6.10e-03

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: 34.59  E-value: 6.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533789     6 FTYFPFRG--LGEPVRLLFHLADCPFKDERFSF-------EEWgavKSKSPMGQLPILGVDGLEIPQSAAILRYLA 72
Cdd:pfam02798   3 LTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFgagpeksPEL---LKLNPLGKVPALEDGGKKLTESRAILEYIA 75
 
Name Accession Description Interval E-value
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 4-72 1.26e-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: 104.55  E-value: 1.26e-29
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533789   4 YKFTYFPFRGLGEPVRLLFHLADCPFKDERFSFEEW--GAVKSKSPMGQLPILGVDGLEIPQSAAILRYLA 72
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWpeLDLKPTLPFGQLPVLEIDGKKLTQSNAILRYLA 71
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 83-189 1.37e-24

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: 92.69  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789  83 EDRAWVDAVVDRFKDFFVEFKKFLVAKRGGKSEEEVAKVVSESVvpamESYFKLLNGLLERSKSGFLIGNSITYADLVVV 162
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYFYEPDGEEKKEKKKEFLEEAL----PKFLGKFEKILKKSGGGYFVGDKLTWADLALF 76

                        90       100
                ....*....|....*....|....*...
gi 17533789 163 NNLETLRNFG-FLNASEQPKLTALLEKV 189
Cdd:cd03192  77 DVLDYLLYLLpKDLLEKYPKLKALRERV 104
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-74 4.27e-22

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: 85.44  E-value: 4.27e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17533789   3 SYKFTYFPFRGLGEPVRLLFHLADCPFKDERFSFEEWG-AVKSKSPMGQLPILGVDGLEIPQSAAILRYLALK 74
Cdd:cd03076   1 PYTLTYFPVRGRAEAIRLLLADQGISWEEERVTYEEWQeSLKPKMLFGQLPCFKDGDLTLVQSNAILRHLGRK 73
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 96-202 1.49e-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: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789    96 KDFFVEFKKFLVAKRGgKSEEEVAKVVSESVVPAmesYFKLLNGLLERSKSGFLIGNSITYADLVVVNNLETLRNFGFLN 175
Cdd:pfam14497   1 HDLHHPIASSLYYEDE-KKKAKRRKEFREERLPK---FLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPD 76

                          90       100
                  ....*....|....*....|....*...
gi 17533789   176 ASEQ-PKLTALLEKVYSQPGIKEYVSSR 202
Cdd:pfam14497  77 ALDKyPKLKALHERVAARPNIKAYLASR 104
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-197 1.91e-19

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 82.25  E-value: 1.91e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789   4 YKFTYFPFRGLGEPVRLLFHLADCPFKDERFSFEEWG----AVKSKSPMGQLPILGVDGLEIPQSAAILRYLALKFG--- 76
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEqkspEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPepp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789  77 FAGKTPEDRAWVDAVVDRF-KDFFVEFKKFLVAKRGGKSEEEVAKVVSEsvvpaMESYFKLLNGLLerSKSGFLIGNSIT 155
Cdd:COG0625  82 LLPADPAARARVRQWLAWAdGDLHPALRNLLERLAPEKDPAAIARARAE-----LARLLAVLEARL--AGGPYLAGDRFS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17533789 156 YADLVVVNNLETLRNFGFlNASEQPKLTALLEKVYSQPGIKE 197
Cdd:COG0625 155 IADIALAPVLRRLDRLGL-DLADYPNLAAWLARLAARPAFQR 195
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 8-205 1.55e-17

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 77.33  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789    8 YFPFRGLGEPVRLLFHLADCPFKDERF-----SFEEWGAVKSK--SPMGQLPILGVDGLEIPQSAAILRYLALKFGFAGK 80
Cdd:PTZ00057   9 YFDARGKAELIRLIFAYLGIEYTDKRFgengdAFIEFKNFKKEkdTPFEQVPILEMDNIIFAQSQAIVRYLSKKYKICGE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789   81 TPEDRAWVDAVVDRFKDFFVEFKKFLVAKrggksEEEVAKVVSEsvVPAMESYFKllnGLLERSKSGFLIGNSITYADLV 160
Cdd:PTZ00057  89 SELNEFYADMIFCGVQDIHYKFNNTNLFK-----QNETTFLNEE--LPKWSGYFE---NILKKNHCNYFVGDNLTYADLA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17533789  161 VVN---NLET-----LRNFgflnaseqPKLTALLEKVYSQPGIKEYVSSRTAS 205
Cdd:PTZ00057 159 VFNlydDIETkypnsLKNF--------PLLKAHNEFISNLPNIKNYISNRKES 203
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 4-72 3.57e-16

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: 69.91  E-value: 3.57e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533789   4 YKFTYFPFRGLGEPVRLLFHLADCPFKDERFSFEEWG--AVKSKSPMGQLPILGVDGLEIPQSAAILRYLA 72
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEqeEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 18-72 1.64e-08

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: 49.49  E-value: 1.64e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789  18 VRLLFHLADCPFKDERFSFEEwGAVKS-----KSPMGQLPILGVDGLEIPQSAAILRYLA 72
Cdd:cd03056  15 VRLLLALLGIPYEWVEVDILK-GETRTpeflaLNPNGEVPVLELDGRVLAESNAILVYLA 73
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 8-74 5.99e-08

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: 48.54  E-value: 5.99e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17533789   8 YFPFRGLGEPVRLLFHLADCPFKDER--------FSFEEWGAVKSK--SPMGQLPILGVDGLEIPQSAAILRYLALK 74
Cdd:cd03075   5 YWDIRGLAQPIRLLLEYTGEKYEEKRyelgdapdYDRSQWLNEKFKlgLDFPNLPYYIDGDVKLTQSNAILRYIARK 81
MCP2201-like_sensor cd19411
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
 80-142 9.27e-06

ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.


Pssm-ID: 438629 [Multi-domain]  Cd Length: 138  Bit Score: 43.78  E-value: 9.27e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17533789  80 KTPEDRAWVDAVVDRFKDFFVEFKKFLVAKRGGKSeEEVAKVVSESVVPAMESYFKLLNGLLE 142
Cdd:cd19411  64 TSPEGKALLAAIAEARAAYLAARDKVLELKKAGDR-EEARALLLGELRPAQAAYLAALDALVD 125
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-75 1.40e-05

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


Pssm-ID: 239375  Cd Length: 79  Bit Score: 41.75  E-value: 1.40e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17533789   5 KFTYFPFRGLGEPVRLLFHLADCPFkDERF--SFEEWGAVKSKSPM--GQLPILGVDGLEIPQSAAILRYLALKF 75
Cdd:cd03077   3 VLHYFNGRGRMESIRWLLAAAGVEF-EEKFieSAEDLEKLKKDGSLmfQQVPMVEIDGMKLVQTRAILNYIAGKY 76
GST_C_Pi cd03210
C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione ...
 82-204 4.89e-05

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: 41.53  E-value: 4.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789  82 PEDRAWVDAVVDRFKDFFVEFKKFLVakrggkSEEEVAKvvsESVVPAMESYFKLLNGLLE-RSKSGFLIGNSITYADLv 160
Cdd:cd03210   1 EKEAALIDMVNDGVEDLRLKYVRMIY------QNYEAGK---DDYIKDLPEQLKPFEKLLAkNNGKGFIVGDKISFADY- 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17533789 161 vvNNLETLRNFGFLNAS---EQPKLTALLEKVYSQPGIKEYVSSRTA 204
Cdd:cd03210  71 --NLFDLLDIHLVLAPGcldAFPLLKAFVERLSARPKLKAYLESDAF 115
GST_C_Sigma cd10295
C-terminal, alpha helical domain of Class Sigma Glutathione S-transferases; Glutathione ...
 84-189 9.14e-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: 9.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789  84 DRAWVDAVVDRFKDFfveFKKFLVAKrggKSEEEVAKVVSEsvvpAMESYFKLLNGLLERSKSG--FLIGNSITYADLVV 161
Cdd:cd10295   3 EQCLVDALVDTLDDF---MSCFPWAE---KKQDVKEKMFNE----ALTGPAPHLLKDLDTYLGGreWLVGKSVTWADFYW 72

                        90       100
                ....*....|....*....|....*...
gi 17533789 162 VNNLETLRNFGFLNASEQPKLTALLEKV 189
Cdd:cd10295  73 DTCSTTLLSFKPDLLKNYPRLVALRDKV 100
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 120-197 1.36e-04

C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal 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 Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.


Pssm-ID: 198287 [Multi-domain]  Cd Length: 117  Bit Score: 39.82  E-value: 1.36e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533789 120 KVVSESVVPAMESYFKLLNGLLERSKsgFLIGNSITYADLVVVNNLETLRNFGFlNASEQPKLTALLEKVYSQPGIKE 197
Cdd:cd03177  33 AEPPEEKLDKLEEALEFLETFLEGSD--YVAGDQLTIADLSLVATVSTLEVVGF-DLSKYPNVAAWYERLKALPPGEE 107
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 46-76 1.39e-04

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: 39.02  E-value: 1.39e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 17533789  46 SPMGQLPILGVDGLEIPQSAAILRYLALKFG 76
Cdd:cd03046  46 NPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
PLN02473 PLN02473
glutathione S-transferase
 45-159 2.58e-04

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 40.36  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789   45 KSPMGQLPILGVDGLEIPQSAAILRYLALKFG-----FAGKTPEDRAWVDAVVDRFKDFFVEFKKFLVAKR--GGKSEEE 117
Cdd:PLN02473  48 RQPFGQVPAIEDGDLKLFESRAIARYYATKYAdqgtdLLGKTLEHRAIVDQWVEVENNYFYAVALPLVINLvfKPRLGEP 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17533789  118 VAKVVSESVVPAMESYFKLLNGLLERSKsgFLIGNSITYADL 159
Cdd:PLN02473 128 CDVALVEELKVKFDKVLDVYENRLATNR--YLGGDEFTLADL 167
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 47-71 2.88e-04

GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid.


Pssm-ID: 239340 [Multi-domain]  Cd Length: 73  Bit Score: 37.93  E-value: 2.88e-04
                        10        20
                ....*....|....*....|....*
gi 17533789  47 PMGQLPILGVDGLEIPQSAAILRYL 71
Cdd:cd03042  48 PQGLVPTLVIDGLVLTQSLAIIEYL 72
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 102-189 6.57e-04

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: 38.35  E-value: 6.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789 102 FKKFLVAKRGGK--SEEEVAKVVSEsvvpaMESYFKLL-NGLLERSKsgFLIGNSITYADLVVVNNLETLRNFGFLNASE 178
Cdd:cd03183  25 WQKVLLPLFGGTpvSPEKVKKAEEN-----LEESLDLLeNKFLKDKP--FLAGDEISIADLSAICEIMQPEAAGYDVFEG 97

                        90
                ....*....|.
gi 17533789 179 QPKLTALLEKV 189
Cdd:cd03183  98 RPKLAAWRKRV 108
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 41-71 1.37e-03

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 36.12  E-value: 1.37e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 17533789  41 AVKSKSPMGQLPILGV-DGLEIPQSAAILRYL 71
Cdd:cd03051  42 EFLAKNPAGTVPVLELdDGTVITESVAICRYL 73
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 95-193 4.77e-03

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: 34.95  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789    95 FKDFFVEFKKFLVAKRGGKSEEEVAKVVsesvvPAMESYFKLLNGLLerSKSGFLIGNSITYADLVVVNNLETLRNFGF- 173
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVDEAL-----EKVARVLSALEEVL--KGQTYLVGDKLTLADIALAPALLWLYELDPa 73

                          90       100
                  ....*....|....*....|
gi 17533789   174 LNASEQPKLTALLEKVYSQP 193
Cdd:pfam00043  74 CLREKFPNLKAWFERVAARP 93
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 6-72 6.10e-03

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: 34.59  E-value: 6.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533789     6 FTYFPFRG--LGEPVRLLFHLADCPFKDERFSF-------EEWgavKSKSPMGQLPILGVDGLEIPQSAAILRYLA 72
Cdd:pfam02798   3 LTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFgagpeksPEL---LKLNPLGKVPALEDGGKKLTESRAILEYIA 75
PLN02395 PLN02395
glutathione S-transferase
 47-159 8.83e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 35.99  E-value: 8.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533789   47 PMGQLPILgVDG-LEIPQSAAILRYLALKF-----GFAGKTPEDRAWVDAVVDrfkdffVEFKKF------------LVA 108
Cdd:PLN02395  49 PFGVVPVI-VDGdYKIFESRAIMRYYAEKYrsqgpDLLGKTIEERGQVEQWLD------VEATSYhppllnltlhilFAS 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17533789  109 KRGGKSEEEVAKVVSESVVPAMESYFKLLngllerSKSGFLIGNSITYADL 159
Cdd:PLN02395 122 KMGFPADEKVIKESEEKLAKVLDVYEARL------SKSKYLAGDFVSLADL 166
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH