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Conserved domains on  [gi|672204097|ref|XP_008778822|]
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glutathione S-transferase U17-like [Phoenix dactylifera]

Protein Classification

glutathione S-transferase( domain architecture ID 10122769)

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; such as plant tau class GSTs that are primarily responsible for herbicide detoxification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 167-295 1.49e-62

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


:

Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 193.93  E-value: 1.49e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 167 PYDRALHRFWAHYVDDKWFPSVFASsRAQTEEARAEAVEQVFAGLKLLEEAFQKcskGKGFFGGDTIGYLDIALGCSLGW 246
Cdd:cd03185    1 PYERAQARFWAAYIDDKLFPAGRKV-WAAKGEEQEKAVEEALEALKVLEEELKG---GKPFFGGDTIGYLDIALGSFLGW 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 672204097 247 LKATEKMTGIKFLDEAKTPLLAQWAERFCANDAVRGLMPETDKLVEFAK 295
Cdd:cd03185   77 FKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLK 125
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 82-155 1.06e-43

GST_N family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


:

Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 143.96  E-value: 1.06e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672204097  82 VKLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGVKSELLLESNPVYKKIPVLIHEGKPVCESMIIVQYIDDVW 155
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 167-295 1.49e-62

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 193.93  E-value: 1.49e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 167 PYDRALHRFWAHYVDDKWFPSVFASsRAQTEEARAEAVEQVFAGLKLLEEAFQKcskGKGFFGGDTIGYLDIALGCSLGW 246
Cdd:cd03185    1 PYERAQARFWAAYIDDKLFPAGRKV-WAAKGEEQEKAVEEALEALKVLEEELKG---GKPFFGGDTIGYLDIALGSFLGW 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 672204097 247 LKATEKMTGIKFLDEAKTPLLAQWAERFCANDAVRGLMPETDKLVEFAK 295
Cdd:cd03185   77 FKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLK 125
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 82-155 1.06e-43

GST_N family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 143.96  E-value: 1.06e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672204097  82 VKLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGVKSELLLESNPVYKKIPVLIHEGKPVCESMIIVQYIDDVW 155
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
83-286 6.83e-34

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 123.08  E-value: 6.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  83 KLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGV---KSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYIDDvwAATP 159
Cdd:COG0625    3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAE--RYPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 160 PAILPADPYDRALHRFWAHYVDDKWFPSVFASSR----AQTEEARAEAVEQVFAGLKLLEEAFQkcskGKGFFGGDTIGY 235
Cdd:COG0625   80 PPLLPADPAARARVRQWLAWADGDLHPALRNLLErlapEKDPAAIARARAELARLLAVLEARLA----GGPYLAGDRFSI 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 672204097 236 LDIALGCSLGWLKATEkmtgikfLDEAKTPLLAQWAERFCANDAVRGLMPE 286
Cdd:COG0625  156 ADIALAPVLRRLDRLG-------LDLADYPNLAAWLARLAARPAFQRALAA 199
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 80-153 1.86e-15

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: 70.03  E-value: 1.86e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672204097   80 EDVKLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGV---KSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYIDD 153
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAgpeKSPELLKLNP-LGKVPALEDGGKKLTESRAILEYIAR 76
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 83-247 3.83e-10

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 58.58  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  83 KLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGVKSELLLESNPVyKKIPVLI-HEGKPVCESMIIVQYIDDVWAAtpPA 161
Cdd:PRK10357   2 KLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVtEEGECWFDSPIIAEYIELLNVA--PA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 162 ILPADPYD----RALHRFwAHYVDDKWFPSVFASSRAQTEEARAEAVEQ---VFAGLKLLEEAFQKcskgkGFFGGDTIG 234
Cdd:PRK10357  79 MLPRDPLAalrvRQLEAL-ADGIMDAALVSVREQARPAAQQSEDELLRQrekINRSLDALEGYLVD-----GTLKTDTVN 152

                        170
                 ....*....|...
gi 672204097 235 YLDIALGCSLGWL 247
Cdd:PRK10357 153 LATIAIACAVGYL 165
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 175-276 4.64e-07

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: 47.28  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  175 FWAHYVDDKWFPSVfaSSRAQTEEARAEAVEQVFAGLKLLEEAFqkcsKGKGFFGGDTIGYLDIALGCSLGWLkateKMT 254
Cdd:pfam00043   1 LMDLRMQIALLPYV--PPEEKKEPEVDEALEKVARVLSALEEVL----KGQTYLVGDKLTLADIALAPALLWL----YEL 70

                          90       100
                  ....*....|....*....|..
gi 672204097  255 GIKFLDEaKTPLLAQWAERFCA 276
Cdd:pfam00043  71 DPACLRE-KFPNLKAWFERVAA 91
sspA PRK09481
stringent starvation protein A; Provisional
 95-209 6.44e-06

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 46.24  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  95 RTRTALNLKGVDYEFLEEVFGVKSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYIDDVWaatP-PAILPADPYDRALH 173
Cdd:PRK09481  24 QVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERF---PhPPLMPVYPVARGES 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 672204097 174 RFWAHYVDDKWFP---SVFASSRAQTEEARAEAVEQVFA 209
Cdd:PRK09481 100 RLMMHRIEKDWYSlmnKIVNGSASEADAARKQLREELLA 138
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 167-295 1.49e-62

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 193.93  E-value: 1.49e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 167 PYDRALHRFWAHYVDDKWFPSVFASsRAQTEEARAEAVEQVFAGLKLLEEAFQKcskGKGFFGGDTIGYLDIALGCSLGW 246
Cdd:cd03185    1 PYERAQARFWAAYIDDKLFPAGRKV-WAAKGEEQEKAVEEALEALKVLEEELKG---GKPFFGGDTIGYLDIALGSFLGW 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 672204097 247 LKATEKMTGIKFLDEAKTPLLAQWAERFCANDAVRGLMPETDKLVEFAK 295
Cdd:cd03185   77 FKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLK 125
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 82-155 1.06e-43

GST_N family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 143.96  E-value: 1.06e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672204097  82 VKLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGVKSELLLESNPVYKKIPVLIHEGKPVCESMIIVQYIDDVW 155
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
83-286 6.83e-34

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 123.08  E-value: 6.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  83 KLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGV---KSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYIDDvwAATP 159
Cdd:COG0625    3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAE--RYPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 160 PAILPADPYDRALHRFWAHYVDDKWFPSVFASSR----AQTEEARAEAVEQVFAGLKLLEEAFQkcskGKGFFGGDTIGY 235
Cdd:COG0625   80 PPLLPADPAARARVRQWLAWADGDLHPALRNLLErlapEKDPAAIARARAELARLLAVLEARLA----GGPYLAGDRFSI 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 672204097 236 LDIALGCSLGWLKATEkmtgikfLDEAKTPLLAQWAERFCANDAVRGLMPE 286
Cdd:COG0625  156 ADIALAPVLRRLDRLG-------LDLADYPNLAAWLARLAARPAFQRALAA 199
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 80-153 1.86e-15

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: 70.03  E-value: 1.86e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672204097   80 EDVKLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGV---KSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYIDD 153
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAgpeKSPELLKLNP-LGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 82-152 7.34e-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: 65.29  E-value: 7.34e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672204097  82 VKLLGRWASPLVMRTRTALNLKGVDYEFLE-EVFGVKSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYID 152
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPvDLGEGEQEEFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
84-153 5.00e-13

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 63.40  E-value: 5.00e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097   84 LLGRWASPLVMRTRTALNLKGVDYEFLEEVFGVKSELLLESNPVYkKIPVLIHEGKPVCESMIIVQYIDD 153
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLG-KVPVLEDDGGILCESLAIIDYLEE 69
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 83-247 3.83e-10

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 58.58  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  83 KLLGRWASPLVMRTRTALNLKGVDYEFLEEVFGVKSELLLESNPVyKKIPVLI-HEGKPVCESMIIVQYIDDVWAAtpPA 161
Cdd:PRK10357   2 KLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVtEEGECWFDSPIIAEYIELLNVA--PA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 162 ILPADPYD----RALHRFwAHYVDDKWFPSVFASSRAQTEEARAEAVEQ---VFAGLKLLEEAFQKcskgkGFFGGDTIG 234
Cdd:PRK10357  79 MLPRDPLAalrvRQLEAL-ADGIMDAALVSVREQARPAAQQSEDELLRQrekINRSLDALEGYLVD-----GTLKTDTVN 152

                        170
                 ....*....|...
gi 672204097 235 YLDIALGCSLGWL 247
Cdd:PRK10357 153 LATIAIACAVGYL 165
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 89-153 2.36e-08

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 49.94  E-value: 2.36e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672204097   89 ASPLVMRTRTALNLKGVDYE--FLEEVFGVKSELLLESNPvYKKIPVLIHE-GKPVCESMIIVQYIDD 153
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEieLVDLDPKDKPPELLALNP-LGTVPVLVLPdGTVLTDSLVILEYLEE 67
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 83-152 2.72e-08

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: 49.88  E-value: 2.72e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672204097  83 KLLGRWASPLVMRTRTALNLKGVDYEFLeEVFGVKSELLLES----NPVyKKIPVLIHEGKPVCESMIIVQYID 152
Cdd:cd03042    2 ILYSYFRSSASYRVRIALNLKGLDYEYV-PVNLLKGEQLSPAyralNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 173-273 4.98e-08

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


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 50.19  E-value: 4.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 173 HRFWAHYVDDKWFPSVFASSRAQT------EEARAEAVEQVFAGLKLLEEAFQkcskGKGFFGGDTIGYLDIALGCSLGW 246
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLEKvplpkdEAAVEAAREELPALLAALEQLLA----GRPYLAGDQFSLADVALAPVLAR 76

                         90       100
                 ....*....|....*....|....*..
gi 672204097 247 LkateKMTGIKFLDEAKTPLLAQWAER 273
Cdd:cd00299   77 L----EALGPYYDLLDEYPRLKAWYDR 99
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 175-276 4.64e-07

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: 47.28  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  175 FWAHYVDDKWFPSVfaSSRAQTEEARAEAVEQVFAGLKLLEEAFqkcsKGKGFFGGDTIGYLDIALGCSLGWLkateKMT 254
Cdd:pfam00043   1 LMDLRMQIALLPYV--PPEEKKEPEVDEALEKVARVLSALEEVL----KGQTYLVGDKLTLADIALAPALLWL----YEL 70

                          90       100
                  ....*....|....*....|..
gi 672204097  255 GIKFLDEaKTPLLAQWAERFCA 276
Cdd:pfam00043  71 DPACLRE-KFPNLKAWFERVAA 91
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 199-273 5.05e-07

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 46.16  E-value: 5.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672204097  199 ARAEAVEQVFAGLKLLEEAFqkcsKGKGFFGGDTIGYLDIALGCSLGWLKATEKMtgikFLDEAKTPLLAQWAER 273
Cdd:pfam13410   1 ALERAREQLRAALDALEARL----ADGPGLLGDRPTLADIALAPVLARLDAAYPG----LDLREGYPRLRAWLER 67
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 82-153 1.34e-06

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: 45.33  E-value: 1.34e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672204097  82 VKLLGRWASPLVMRTRTALNLKGVDYEFLE-EVFGV--KSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYIDD 153
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPvDLTKGehKSPEHLARNP-FGQIPALEDGDLKLFESRAITRYLAE 75
sspA PRK09481
stringent starvation protein A; Provisional
 95-209 6.44e-06

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 46.24  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  95 RTRTALNLKGVDYEFLEEVFGVKSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYIDDVWaatP-PAILPADPYDRALH 173
Cdd:PRK09481  24 QVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERF---PhPPLMPVYPVARGES 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 672204097 174 RFWAHYVDDKWFP---SVFASSRAQTEEARAEAVEQVFA 209
Cdd:PRK09481 100 RLMMHRIEKDWYSlmnKIVNGSASEADAARKQLREELLA 138
PRK15113 PRK15113
glutathione transferase;
87-240 1.31e-05

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 45.34  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097  87 RWASPLVMRTRTALNLKGVDYEF----------LEEVFGVKSelllesnpVYKKIPVLIHEGKPVCESMIIVQYIDDVWA 156
Cdd:PRK15113  13 HFFSPYVMSAFVALQEKGLPFELktvdldagehLQPTYQGYS--------LTRRVPTLQHDDFELSESSAIAEYLEERFA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 157 ATP-PAILPADPYDRALHR-FWAhyvddkWFPS-------------VFASSRAQ--TEEARAEAVEQVFAGLKLLEEAfq 219
Cdd:PRK15113  85 PPAwERIYPADLQARARARqIQA------WLRSdlmplreerptdvVFAGAKKAplSEAGKAAAEKLFAVAERLLAPG-- 156

                        170       180
                 ....*....|....*....|.
gi 672204097 220 kcskGKGFFGGDTIGYLDIAL 240
Cdd:PRK15113 157 ----QPNLFGEWCIADTDLAL 173
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 95-153 2.38e-05

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 41.55  E-value: 2.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672204097  95 RTRTALNLKGVDYEFLEEVFGVKSELLLESNPvYKKIPVLIHEGKPVCESMIIVQYIDD 153
Cdd:cd03059   14 RVRIVLAEKGVSVEIIDVDPDNPPEDLAELNP-YGTVPTLVDRDLVLYESRIIMEYLDE 71
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 184-281 3.38e-05

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


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 42.23  E-value: 3.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 184 WFPSVFASSRAQtEEARAEAVEQVFAGLKLLEEAFQkcskGKGFFGGDTIGYLDIALGCSLGWLKATEkmtgikfLDEAK 263
Cdd:cd03188   25 FYPARWADDALA-EEVKAAARERLERRLAYLDAQLA----GGPYLLGDQFSVADAYLFVVLRWARAVG-------LDLSD 92

                         90
                 ....*....|....*...
gi 672204097 264 TPLLAQWAERFCANDAVR 281
Cdd:cd03188   93 WPHLAAYLARVAARPAVQ 110
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 185-295 7.78e-05

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


Pssm-ID: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 41.54  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 185 FPSVFASSRAQTEeARAEAVEQVFAGLKLLEEAFQKcsKGKGFFGGDTIGYLD--IALGCS-LGWLKatekMTGIKFLDE 261
Cdd:cd03184   16 VPSAFYKFLRSGE-DRKGLKEELRSALENLEEELAK--RGTPFFGGNSPGMVDymIWPWFErLEALK----LLDGYELCL 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 672204097 262 AKTPLLAQWAERFCANDAVRGLMPETDKLVEFAK 295
Cdd:cd03184   89 DRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLN 122
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 91-152 9.25e-05

GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


Pssm-ID: 239353 [Multi-domain]  Cd Length: 89  Bit Score: 40.41  E-value: 9.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672204097  91 PLVMRTRTALNLKGVDYEFLEEVFGVKSELLLESNPvYKKIPVL-IHEGKPVCESMIIVQYID 152
Cdd:cd03055   28 PYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNP-QGKVPALeIDEGKVVYESLIICEYLD 89
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 90-153 1.80e-04

GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF.


Pssm-ID: 239336 [Multi-domain]  Cd Length: 84  Bit Score: 39.64  E-value: 1.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672204097  90 SPLVMRTRTALNLKGVDY--EFLEevF-GVKSELLLESNPVYKKIPVLIH-EGKPVCESMIIVQYIDD 153
Cdd:cd03038   16 SPNVWKTRLALNHKGLEYktVPVE--FpDIPPILGELTSGGFYTVPVIVDgSGEVIGDSFAIAEYLEE 81
GST_C_6 cd03205
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ...
 205-285 6.95e-04

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.


Pssm-ID: 198314 [Multi-domain]  Cd Length: 109  Bit Score: 38.34  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 205 EQVFAGLKLLEEAFqkcskGKGFFGGDTIGylDIALGCSLGWLkaTEKMTGIKflDEAKTPLLAQWAERFCANDAVRGLM 284
Cdd:cd03205   40 GKIERALDALEAEL-----GDLPGGRLTLG--DIAVACALGYL--DFRFPELD--WRAGHPALAAWFARFEARPSFQATP 108


                 .
gi 672204097 285 P 285
Cdd:cd03205  109 P 109
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 94-151 1.04e-03

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: 37.10  E-value: 1.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672204097  94 MRTRTALNLKGVDYEfLEEVF----GVKSELLLESNPVyKKIPVLIHEGKPVCESMIIVQYI 151
Cdd:cd03046   12 FRILWLLEELGLPYE-LVLYDrgpgEQAPPEYLAINPL-GKVPVLVDGDLVLTESAAIILYL 71
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 183-273 5.06e-03

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


Pssm-ID: 198292 [Multi-domain]  Cd Length: 126  Bit Score: 36.42  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672204097 183 KWFPSVFASSRAQTEEArAEAVEQVFAGLKLLEEAFQKcskGKGFFGGDTIGYLDIALGCSLgwlkatEKMTGIKFLDEA 262
Cdd:cd03183   27 KVLLPLFGGTPVSPEKV-KKAEENLEESLDLLENKFLK---DKPFLAGDEISIADLSAICEI------MQPEAAGYDVFE 96

                         90
                 ....*....|.
gi 672204097 263 KTPLLAQWAER 273
Cdd:cd03183   97 GRPKLAAWRKR 107
 
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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