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Conserved domains on  [gi|15227086|ref|NP_180507|]
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glutathione S-transferase tau 4 [Arabidopsis thaliana]

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 ...
91-216 7.94e-41

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: 135.77  E-value: 7.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086  91 PYEKAMALFWAKFVDEQVGPVAFMSVAKAEKGVEVAIKEAQELFMFLEKE-VTGKDFFGGKTIGFLDLVAGSMIPFCLAR 169
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEElKGGKPFFGGDTIGYLDIALGSFLGWFKAI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15227086 170 GWEGmGIDMIPEEKFPELNRWIKNLKEIEIVRECIPPREEQIEHMKK 216
Cdd:cd03185  81 EEVG-GVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKA 126
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
8-81 1.15e-37

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: 125.85  E-value: 1.15e-37
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227086   8 VKLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPVYKKVPVLVYKGKILSESHVILEYIDQIW 81
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 ...
91-216 7.94e-41

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: 135.77  E-value: 7.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086  91 PYEKAMALFWAKFVDEQVGPVAFMSVAKAEKGVEVAIKEAQELFMFLEKE-VTGKDFFGGKTIGFLDLVAGSMIPFCLAR 169
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEElKGGKPFFGGDTIGYLDIALGSFLGWFKAI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15227086 170 GWEGmGIDMIPEEKFPELNRWIKNLKEIEIVRECIPPREEQIEHMKK 216
Cdd:cd03185  81 EEVG-GVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKA 126
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
8-81 1.15e-37

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: 125.85  E-value: 1.15e-37
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227086   8 VKLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPVYKKVPVLVYKGKILSESHVILEYIDQIW 81
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-212 1.73e-33

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 119.23  E-value: 1.73e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086   9 KLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIV---NKSPLLLQINPvYKKVPVLVYKGKILSESHVILEYIDQIWKNNP 85
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086  86 ILPQDPYEKAMALFWAKFVDEQVGPVAFMSV-----AKAEKGVEVAIKEAQELFMFLEKEVTGKDFFGGKTIGFLDLVAG 160
Cdd:COG0625  82 LLPADPAARARVRQWLAWADGDLHPALRNLLerlapEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALA 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15227086 161 SMIPFclargWEGMGIDMipeEKFPELNRWIKNLKEIEIVRECIPPREEQIE 212
Cdd:COG0625 162 PVLRR-----LDRLGLDL---ADYPNLAAWLARLAARPAFQRALAAAEPDLA 205
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
10-80 1.16e-16

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 71.87  E-value: 1.16e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227086    10 LLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPVYkKVPVLVYKGKILSESHVILEYIDQI 80
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLG-KVPVLEDDGGILCESLAIIDYLEEL 70
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
9-91 2.11e-10

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 58.19  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086    9 KLLGFWASPFTRRVEMAFKLKGVPYEYleqdiVNKSPLL-----LQINPVyKKVPVLVY-KGKILSESHVILEYIDQIWK 82
Cdd:PRK10357   2 KLIGSYTSPFVRKISILLLEKGITFEF-----VNELPYNadngvAQYNPL-GKVPALVTeEGECWFDSPIIAEYIELLNV 75

                 ....*....
gi 15227086   83 NNPILPQDP 91
Cdd:PRK10357  76 APAMLPRDP 84
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
17-160 1.22e-06

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 48.06  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086   17 PFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPvYKKVPVLVYKGKILSESHVILEYIDQIWKNNPIlpQDPYEKAM 96
Cdd:PLN02817  74 PFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISP-EGKVPVVKLDEKWVADSDVITQALEEKYPDPPL--ATPPEKAS 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227086   97 alfwakfVDEQVGP--VAFMSVAKAEKGVEVAIkeAQELFMFLEKEVTGKDFFGGKTIGFLDLVAG 160
Cdd:PLN02817 151 -------VGSKIFStfIGFLKSKDPGDGTEQAL--LDELTSFDDYIKENGPFINGEKISAADLSLG 207
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
91-216 7.94e-41

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: 135.77  E-value: 7.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086  91 PYEKAMALFWAKFVDEQVGPVAFMSVAKAEKGVEVAIKEAQELFMFLEKE-VTGKDFFGGKTIGFLDLVAGSMIPFCLAR 169
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEElKGGKPFFGGDTIGYLDIALGSFLGWFKAI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15227086 170 GWEGmGIDMIPEEKFPELNRWIKNLKEIEIVRECIPPREEQIEHMKK 216
Cdd:cd03185  81 EEVG-GVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKA 126
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
8-81 1.15e-37

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: 125.85  E-value: 1.15e-37
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227086   8 VKLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPVYKKVPVLVYKGKILSESHVILEYIDQIW 81
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-212 1.73e-33

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 119.23  E-value: 1.73e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086   9 KLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIV---NKSPLLLQINPvYKKVPVLVYKGKILSESHVILEYIDQIWKNNP 85
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNP-LGKVPVLVDDGLVLTESLAILEYLAERYPEPP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086  86 ILPQDPYEKAMALFWAKFVDEQVGPVAFMSV-----AKAEKGVEVAIKEAQELFMFLEKEVTGKDFFGGKTIGFLDLVAG 160
Cdd:COG0625  82 LLPADPAARARVRQWLAWADGDLHPALRNLLerlapEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIALA 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15227086 161 SMIPFclargWEGMGIDMipeEKFPELNRWIKNLKEIEIVRECIPPREEQIE 212
Cdd:COG0625 162 PVLRR-----LDRLGLDL---ADYPNLAAWLARLAARPAFQRALAAAEPDLA 205
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
8-78 3.71e-17

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: 72.99  E-value: 3.71e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227086   8 VKLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPL-LLQINPvYKKVPVLVYKGKILSESHVILEYID 78
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEeFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
10-80 1.16e-16

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 71.87  E-value: 1.16e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227086    10 LLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPVYkKVPVLVYKGKILSESHVILEYIDQI 80
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLG-KVPVLEDDGGILCESLAIIDYLEEL 70
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
15-78 1.20e-14

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 66.11  E-value: 1.20e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227086    15 ASPFTRRVEMAFKLKGVPYEYLEQDI--VNKSPLLLQINPvYKKVPVLV-YKGKILSESHVILEYID 78
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNP-LGTVPVLVlPDGTVLTDSLVILEYLE 66
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
6-79 1.39e-13

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: 63.48  E-value: 1.39e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227086     6 EDVKLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIV---NKSPLLLQINPvYKKVPVLVYKGKILSESHVILEYIDQ 79
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNP-LGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
9-78 1.05e-12

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: 61.05  E-value: 1.05e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227086   9 KLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVN---KSPLLLQINPVyKKVPVLVYKGKILSESHVILEYID 78
Cdd:cd03042   2 ILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKgeqLSPAYRALNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
9-91 2.11e-10

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 58.19  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086    9 KLLGFWASPFTRRVEMAFKLKGVPYEYleqdiVNKSPLL-----LQINPVyKKVPVLVY-KGKILSESHVILEYIDQIWK 82
Cdd:PRK10357   2 KLIGSYTSPFVRKISILLLEKGITFEF-----VNELPYNadngvAQYNPL-GKVPALVTeEGECWFDSPIIAEYIELLNV 75

                 ....*....
gi 15227086   83 NNPILPQDP 91
Cdd:PRK10357  76 APAMLPRDP 84
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
9-76 2.48e-09

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: 52.19  E-value: 2.48e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227086   9 KLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVN---KSPLLLQINPvYKKVPVLVYKGKILSESHVILEY 76
Cdd:cd03056   2 KLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKgetRTPEFLALNP-NGEVPVLELDGRVLAESNAILVY 71
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
17-79 4.52e-09

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: 51.56  E-value: 4.52e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227086  17 PFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPvYKKVPVLVYKGKILSESHVILEYIDQ 79
Cdd:cd03059  10 VYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNP-YGTVPTLVDRDLVLYESRIIMEYLDE 71
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
9-78 7.81e-09

GST_N family, unknown subfamily 3; 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: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 50.72  E-value: 7.81e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227086   9 KLLGFWASPFTR--RVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPVyKKVPVLVYK-GKILSESHVILEYID 78
Cdd:cd03049   2 KLLYSPTSPYVRkvRVAAHETGLGDDVELVLVNPWSDDESLLAVNPL-GKIPALVLDdGEALFDSRVICEYLD 73
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
8-78 2.70e-08

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: 49.57  E-value: 2.70e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227086   8 VKLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIV---NKSPLLLQINPvYKKVPVLVYKGKILSESHVILEYID 78
Cdd:cd03053   2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNP-FGQIPALEDGDLKLFESRAITRYLA 74
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
8-77 4.44e-07

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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 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 aryl or alkyl sulfate esters.


Pssm-ID: 239348 [Multi-domain]  Cd Length: 76  Bit Score: 46.08  E-value: 4.44e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227086   8 VKLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVN---KSPLLLQINPvYKKVPVLVYKGKILSESHVILEYI 77
Cdd:cd03050   1 LKLYYDLMSQPSRAVYIFLKLNKIPFEECPIDLRKgeqLTPEFKKINP-FGKVPAIVDGDFTLAESVAILRYL 72
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
17-160 1.22e-06

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 48.06  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086   17 PFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPvYKKVPVLVYKGKILSESHVILEYIDQIWKNNPIlpQDPYEKAM 96
Cdd:PLN02817  74 PFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISP-EGKVPVVKLDEKWVADSDVITQALEEKYPDPPL--ATPPEKAS 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227086   97 alfwakfVDEQVGP--VAFMSVAKAEKGVEVAIkeAQELFMFLEKEVTGKDFFGGKTIGFLDLVAG 160
Cdd:PLN02817 151 -------VGSKIFStfIGFLKSKDPGDGTEQAL--LDELTSFDDYIKENGPFINGEKISAADLSLG 207
sspA PRK09481
stringent starvation protein A; Provisional
18-91 1.68e-06

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 47.01  E-value: 1.68e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227086   18 FTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPvYKKVPVLVYKGKILSESHVILEYIDQIWKNNPILPQDP 91
Cdd:PRK09481  21 YSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPHPPLMPVYP 93
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
17-78 2.35e-06

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: 44.27  E-value: 2.35e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227086  17 PFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPvYKKVPVL-VYKGKILSESHVILEYID 78
Cdd:cd03055  28 PYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNP-QGKVPALeIDEGKVVYESLIICEYLD 89
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
100-194 1.13e-05

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


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 42.87  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086 100 WAKFVDEQVGP-------VAFMSVAKAEKGVEVAIKEAQELFMFLEKEVTGKDFFGGKTIGFLDLVAGSMIpfclaRGWE 172
Cdd:cd00299   4 LEDWADATLAPplvrllyLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVL-----ARLE 78
                        90       100
                ....*....|....*....|..
gi 15227086 173 GMGIDMIPEEKFPELNRWIKNL 194
Cdd:cd00299  79 ALGPYYDLLDEYPRLKAWYDRL 100
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
15-76 2.11e-05

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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: 239343 [Multi-domain]  Cd Length: 74  Bit Score: 41.44  E-value: 2.11e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227086  15 ASPFTRRVEMAFKLKGVPYEYLEQDIVNK---SPLLLQINPVyKKVPVLVYKGKILSESHVILEY 76
Cdd:cd03045   8 GSPPCRAVLLTAKALGLELNLKEVNLMKGehlKPEFLKLNPQ-HTVPTLVDNGFVLWESHAILIY 71
PRK15113 PRK15113
glutathione transferase;
14-97 3.26e-05

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 43.41  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086   14 WASPFTRRVEMAFKLKGVPYEYLEQDIVNKSplllQINPVY------KKVPVLVYKGKILSESHVILEYIDQIW---KNN 84
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFELKTVDLDAGE----HLQPTYqgysltRRVPTLQHDDFELSESSAIAEYLEERFappAWE 89
                         90
                 ....*....|...
gi 15227086   85 PILPQDPYEKAMA 97
Cdd:PRK15113  90 RIYPADLQARARA 102
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
9-78 5.94e-05

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: 39.97  E-value: 5.94e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227086   9 KLLGFWASPFTRRVEMAFKLKGVPYEYLEQDIV---NKSPLLLQINPvYKKVPVLVY-KGKILSESHVILEYID 78
Cdd:cd03051   2 KLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAageQRSPEFLAKNP-AGTVPVLELdDGTVITESVAICRYLE 74
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
13-77 6.70e-05

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


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 40.18  E-value: 6.70e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086  13 FWASPFTR--RVEMAFKLKGVPYE---YLEQDIVNKSPLLLQINPVyKKVPVLVYKGKILSESHVILEYI 77
Cdd:cd03046   3 LYHLPRSRsfRILWLLEELGLPYElvlYDRGPGEQAPPEYLAINPL-GKVPVLVDGDLVLTESAAIILYL 71
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
126-216 2.58e-04

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


Pssm-ID: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 39.61  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086 126 AIKEAQELFMFLEKEVT--GKDFFGGKTIGFLDLvagSMIPFCLARGWEGM-GIDMIPEEKFPELNRWIKNLKEIEIVRE 202
Cdd:cd03184  33 LKEELRSALENLEEELAkrGTPFFGGNSPGMVDY---MIWPWFERLEALKLlDGYELCLDRFPKLKKWMAAMKQDPAVKA 109
                        90
                ....*....|....
gi 15227086 203 CIPPREEQIEHMKK 216
Cdd:cd03184 110 FYTDPETHAEFLNS 123
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
13-76 1.54e-03

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes.


Pssm-ID: 239346 [Multi-domain]  Cd Length: 81  Bit Score: 36.37  E-value: 1.54e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227086  13 FWASPFTRRVEMAFKLKGVPYEYLEQDI---VNKSPLLLQINPvYKKVPVLV---YKGKILSESHVILEY 76
Cdd:cd03048   6 THGTPNGFKVSIMLEELGLPYEIHPVDIskgEQKKPEFLKINP-NGRIPAIVdhnGTPLTVFESGAILLY 74
GST_N_Metaxin_like cd03080
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ...
15-79 1.62e-03

GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, predominantly uncharacterized, with similarity to metaxins and GSTs. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. One characterized member of this subgroup is a novel GST from Rhodococcus with toluene o-monooxygenase and gamma-glutamylcysteine synthetase activities. Also members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system.


Pssm-ID: 239378 [Multi-domain]  Cd Length: 75  Bit Score: 36.06  E-value: 1.62e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227086  15 ASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPlllqinpvYKKVPVLVYKGKILSESHVILEYIDQ 79
Cdd:cd03080  16 LSPFCLKVETFLRMAGIPYENKFGGLAKRSP--------KGKLPFIELNGEKIADSELIIDHLEE 72
GST_N_Metaxin cd03054
GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a ...
15-79 2.92e-03

GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities.


Pssm-ID: 239352 [Multi-domain]  Cd Length: 72  Bit Score: 35.28  E-value: 2.92e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227086  15 ASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPLllqinpvyKKVPVLVYKGKILSESHVILEYIDQ 79
Cdd:cd03054  15 LSPECLKVETYLRMAGIPYEVVFSSNPWRSPT--------GKLPFLELNGEKIADSEKIIEYLKK 71
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
10-70 4.76e-03

GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega 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. 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. Like Omega enzymes, proteins in this subfamily 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.


Pssm-ID: 239358 [Multi-domain]  Cd Length: 71  Bit Score: 34.64  E-value: 4.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227086  10 LLGFWASPFTRRVEMAFKLKGVPYEYLEQDIVNKSPLLLQINPvYKKVPVLVYK-GKILSES 70
Cdd:cd03060   3 LYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASP-KGTVPVLVLGnGTVIEES 63
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
16-78 5.17e-03

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: 35.01  E-value: 5.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227086  16 SPFTRRVEMAFKLKGVPY--EYLE-QDIVNKSPLLlqINPVYKKVPVLVY-KGKILSESHVILEYID 78
Cdd:cd03038  16 SPNVWKTRLALNHKGLEYktVPVEfPDIPPILGEL--TSGGFYTVPVIVDgSGEVIGDSFAIAEYLE 80
 
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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